|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
37-739 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 809.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 37 REALPAVCSVLVPTAPPLLRAWVVGLSRAAVLWLGARGVLGAAVGsgsesaglgGWLAALQPAAAALGLALPGLALFREL 116
Cdd:TIGR00958 21 RDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAG---------GLLAAVKPLVAALCLATPSLSSLRAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 117 RSWRAPRDSDSPRLLHWGSrldvFALSYLAALSAAALWHKLSGLWAP-----GRRGGSGDAVRRLLGCLGSEMRRLPLLL 191
Cdd:TIGR00958 92 AFWEALDPAVRVALGLWSW----FVWSYGAALPAAALWAVLSSAGASekeaeQGQSETADLLFRLLGLSGRDWPWLISAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 192 ALLVLSSLGEMAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQ 271
Cdd:TIGR00958 168 VFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 272 ETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQV 351
Cdd:TIGR00958 248 DLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 352 LATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGG 431
Cdd:TIGR00958 328 LSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 432 QLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRIPRCPASGVLTSLNLEGLVQFQDVSFA 511
Cdd:TIGR00958 408 QLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFS 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 512 YPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLF 591
Cdd:TIGR00958 488 YPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLF 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 592 GRSFRENIAYGLVQKPtMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:TIGR00958 568 SGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 672 ALDAnsqlRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTM 739
Cdd:TIGR00958 647 ALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
200-478 |
2.18e-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: 424.58 E-value: 2.18e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 200 GEMAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQN 279
Cdd:cd18589 11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 280 QTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTS 359
Cdd:cd18589 91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 360 LAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTI 439
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 548923797 440 SSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
201-745 |
1.56e-130 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 224055 [Multi-domain] Cd Length: 567 Bit Score: 399.11 E-value: 1.56e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 201 EMAIPFFTGHLTDWILQDetASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQ 280
Cdd:COG1132 30 SLLLPLLIGRIIDALLAD--LGELLELLLLLLLLALLGGVLRALQSYLGSRLGQKIVADLRRDLFEKLLRLPLSFFDKAK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 281 TGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSL 360
Cdd:COG1132 108 SGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLLFSLSWRLALILLLILPLLALVLSLLARKSRKLSRRVREAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 361 AESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTIS 440
Cdd:COG1132 188 GELNARLLESLSGIRVIKAFGAEDRELKRFEEANEELRRANLRASRLEALLAPLMLLLSSLGTVLVLALGGFLVLSGSLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 441 SGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRIPRcPASGVLTSLNLEGLVQFQDVSFAYPNHPdvPV 520
Cdd:COG1132 268 VGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAERLFELLDEEPE-VEDPPDPLKDTIGSIEFENVSFSYPGKK--PV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIA 600
Cdd:COG1132 345 LKDISFSIEPGEKVAIVGPSGSGKSTLIKLLLRLYDPTSGEILIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 601 YGLvQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLR 680
Cdd:COG1132 425 LGR-PDATDEEIEEALKLANAHEFIANLPDGYDTIVGERGVNLSGGQRQRLAIARALLRNPPILILDEATSALDTETEAL 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 681 VKQLLYKSPERrfRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQAPGG 745
Cdd:COG1132 504 IQDALKKLLKG--RTTLIIAHRLSTIKNADRIIVLDNGRIVERGTHEELLAKGGLYARLYQAQGG 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
492-720 |
1.35e-120 |
|
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: 360.63 E-value: 1.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 492 GVLTSLNLEGLVQFQDVSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQ 571
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 572 YEHRYLHTQVAAVRQEPQLFGRSFRENIAYGLVQKPtMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAV 651
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHCLSLLEQADQILFLEGGTI 720
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
202-741 |
1.53e-103 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 225183 [Multi-domain] Cd Length: 709 Bit Score: 333.04 E-value: 1.53e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLgDGVYNSIMG-RVHSQVQGEVFQAVLRQETEFFQQNQ 280
Cdd:COG2274 171 LATPLFSQIVIDKVLPDASRSTLTVLAIGLLLAALFEALLRLL-RTYLIAHLGkRLDLELSGRFFRHLLRLPLSYFEKRS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 281 TGAITSRVTED-------TSTLSESLSEklslllwyLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLpekLGRWHQVLA 353
Cdd:COG2274 250 VGEIISRVRELeqireflTGSILTLIID--------LLFALIFLAVMFLYSWKLTLIVLAAIPLNVLI---TLIFQPLLR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 354 TQVQTSLAESSQVA---IEVLSAMPTVRSFANEeceaQKFSQKLQKMNTLHQKEALAYAV-NLWITSISGMLLK---VGI 426
Cdd:COG2274 319 RKTRKLIEESAEQQsflVETIKGIETVKALAAE----PRFRSQWDNRLAKQVNIGFKTEKlALILNTIKSLLQQlssVLI 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 427 LYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRIP-RCPASGVLTSLNLEGLVQF 505
Cdd:COG2274 395 LWFGAILVLEGELTLGQLVAFNMLAGYFISPITRLSQLWTDFQQAKVALERLGDILDTPPeQEGDKTLIHLPKLQGEIEF 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 506 QDVSFAYPNHpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVR 585
Cdd:COG2274 475 ENVSFRYGPD-DPPVLEDLSLEIPPGEKVAIVGRSGSGKSTLLKLLLGLYKPQQGRILLDGVDLNDIDLASLRRQVGYVL 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 586 QEPQLFGRSFRENIAYGLVQkPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLI 665
Cdd:COG2274 554 QDPFLFSGSIRENIALGNPE-ATDEEIIEAAQLAGAHEFIENLPMGYDTPVGEGGANLSGGQRQRLALARALLSKPKILL 632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 666 LDDATSALDANSQLRVKQLLykSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQ 741
Cdd:COG2274 633 LDEATSALDPETEAIILQNL--LQILQGRTVIIIAHRLSTIRSADRIIVLDQGKIVEQGSHEELLAQGGLYARLYQ 706
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
219-734 |
6.88e-102 |
|
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: 324.73 E-value: 6.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 219 ETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSES 298
Cdd:TIGR02204 52 DSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 299 LSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVR 378
Cdd:TIGR02204 132 IGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 379 SFANEECEAQKFSQKLQKMNTLHQKEALAYAvnlWITSISGMLL---KVGILYIGGQLVTNGTISSGSLVTFILYQIQFT 455
Cdd:TIGR02204 212 AFGHEDAERSRFGGAVEKAYEAARQRIRTRA---LLTAIVIVLVfgaIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 456 SAVEALFSTYPSVQKAVGSSKEIFEYLGRIP--RCPASGVLTSLNLEGLVQFQDVSFAYPNHPDVPVLQALTFTLRPGEV 533
Cdd:TIGR02204 289 GSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGET 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 534 IALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGLVQKpTMEEVI 613
Cdd:TIGR02204 369 VALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDA-TDEEVE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 614 AAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERrf 693
Cdd:TIGR02204 448 AAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKG-- 525
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 548923797 694 RSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRG 734
Cdd:TIGR02204 526 RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGG 566
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
503-742 |
7.73e-95 |
|
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: 294.45 E-value: 7.73e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVA 582
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGRSFRENIAYGLvQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPR 662
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGK-PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 663 VLILDDATSALDANSQLRVKQLLYKSpeRRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQA 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 ... |
243-734 |
3.48e-94 |
|
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: 304.33 E-value: 3.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 243 FLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLllwyLVR-GLCLLGL-- 319
Cdd:TIGR02203 72 FVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIV----LVReTLTVIGLfi 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 320 -MLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMN 398
Cdd:TIGR02203 148 vLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 399 TLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 479 FEYLGRIPRcPASGVLTSLNLEGLVQFQDVSFAYPNHpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPT 558
Cdd:TIGR02203 308 FTLLDSPPE-KDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 559 KGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGE 638
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 639 AGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLykspER--RFRSVLLITHCLSLLEQADQILFLE 716
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL----ERlmQGRTTLVIAHRLSTIEKADRIVVMD 541
|
490
....*....|....*...
gi 548923797 717 GGTICEAGTYRQLMERRG 734
Cdd:TIGR02203 542 DGRIVERGTHNELLARNG 559
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
200-478 |
4.70e-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: 260.17 E-value: 4.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 200 GEMAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQN 279
Cdd:cd18572 11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 280 QTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTS 359
Cdd:cd18572 91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 360 LAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTI 439
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 548923797 440 SSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18572 251 SAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
503-739 |
2.02e-78 |
|
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: 251.38 E-value: 2.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPDvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVA 582
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGRSFRENIAYGlvqKP--TMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG---RPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTM 739
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
501-734 |
3.33e-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: 250.61 E-value: 3.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 501 GLVQFQDVSFAYpnHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQ 580
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFGRSFRENIAYGlVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSpeRRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRG 734
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
231-741 |
1.87e-75 |
|
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: 257.75 E-value: 1.87e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 231 MSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEdTSTLSESLSEKLSLLLWYL 310
Cdd:TIGR01846 185 MLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSALTVVLDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 311 VRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLG-RWHQVLATQVQTSlAESSQVAIEVLSAMPTVRSFANEECEAQK 389
Cdd:TIGR01846 264 LFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGpILRKRVEDKFERS-AAATSFLVESVTGIETIKATATEPQFQNR 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 390 FSQKLQKMNTLHQKealAYAVNLWITSISGMLLKVG---ILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYP 466
Cdd:TIGR01846 343 WDRQLAAYVAASFR---VTNLGNIAGQAIELIQKLTfaiLLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 467 SVQKAVGSskeiFEYLGRI---PRCPASGVLTSL-NLEGLVQFQDVSFAYpnHPDVP-VLQALTFTLRPGEVIALVGRNG 541
Cdd:TIGR01846 420 DFQQTGIA----LERLGDIlnsPTEPRSAGLAALpELRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSG 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 542 SGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGLVQKPtMEEVIAAAMVSGA 621
Cdd:TIGR01846 494 SGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAP-FEHVIHAAKLAGA 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 622 HSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPerRFRSVLLITH 701
Cdd:TIGR01846 573 HDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC--RGRTVIIIAH 650
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 548923797 702 CLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQ 741
Cdd:TIGR01846 651 RLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQ 690
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
254-736 |
3.64e-74 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 251.48 E-value: 3.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 254 GRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLllwyLVRG----LCLLGLMLWESLSLTM 329
Cdd:PRK11176 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT----VVREgasiIGLFIMMFYYSWQLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 330 VTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYA 409
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 410 VNLWITSISGMLLKVGILYIGG-----QLVTNGTISsgslVTFilyqiqftSAVEALFSTYPSV-------QKAVGSSKE 477
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASfpsvmDTLTAGTIT----VVF--------SSMIALMRPLKSLtnvnaqfQRGMAACQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 478 IFEYLGRIPRcPASGVLTSLNLEGLVQFQDVSFAYPNHpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQP 557
Cdd:PRK11176 318 LFAILDLEQE-KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 558 TKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVG 637
Cdd:PRK11176 396 DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 638 EAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSpeRRFRSVLLITHCLSLLEQADQILFLEG 717
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILVVED 553
|
490
....*....|....*....
gi 548923797 718 GTICEAGTYRQLMERRGCF 736
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVY 572
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
200-478 |
4.03e-73 |
|
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: 239.38 E-value: 4.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 200 GEMAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQN 279
Cdd:cd18557 11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 280 QTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTS 359
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 360 LAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTI 439
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 548923797 440 SSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
503-741 |
2.00e-72 |
|
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: 235.46 E-value: 2.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYpnHPDVP-VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQV 581
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFGRSFRENIAYGlVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 662 RVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQ 741
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
503-742 |
7.47e-70 |
|
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: 228.65 E-value: 7.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYpnHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVA 582
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGRSFRENIAYGLVqKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPR 662
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRP-DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 663 VLILDDATSALDANSQlrvkQLLYKSPERRF--RSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMM 740
Cdd:cd03253 158 ILLLDEATSALDTHTE----REIQAALRDVSkgRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
..
gi 548923797 741 QA 742
Cdd:cd03253 234 KA 235
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
501-720 |
3.56e-69 |
|
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: 226.32 E-value: 3.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 501 GLVQFQDVSFAYPNHPdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQ 580
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFGRSFRENIAYGLvQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA-PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHCLSLLEQADQILFLEGGTI 720
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
200-478 |
6.34e-69 |
|
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: 228.35 E-value: 6.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 200 GEMAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQN 279
Cdd:cd18784 11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 280 QTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTS 359
Cdd:cd18784 91 KTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 360 LAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTI 439
Cdd:cd18784 171 LAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 548923797 440 SSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18784 251 SGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
414-744 |
4.30e-67 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 232.54 E-value: 4.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 414 ITSISGMLLKVGILYIGGQLVTNGTISSGSLVTFILYQI-------QFTSAVEALFSTYPSVQkavgsskEIFEYLGRIP 486
Cdd:PRK13657 245 LNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATlligrldQVVAFINQVFMAAPKLE-------EFFEVEDAVP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 487 RCPASGVLTSL-NLEGLVQFQDVSFAYPNHPdvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLD 565
Cdd:PRK13657 318 DVRDPPGAIDLgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILID 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 566 GEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGlvqKP--TMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQL 643
Cdd:PRK13657 396 GTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG---RPdaTDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 644 SGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLykSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEA 723
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL--DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVES 550
|
330 340
....*....|....*....|.
gi 548923797 724 GTYRQLMERRGCFWTMMQAPG 744
Cdd:PRK13657 551 GSFDELVARGGRFAALLRAQG 571
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
503-718 |
2.34e-66 |
|
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: 216.87 E-value: 2.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVA 582
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGRSFRENIayglvqkptmeeviaaamvsgahsfiselpqgydtevgeagsqLSGGQRQAVALARALIRKPR 662
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 663 VLILDDATSALDANSQLRVKQLLYKspERRFRSVLLITHCLSLLEQADQILFLEGG 718
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRA--LAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
314-742 |
2.78e-64 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227321 [Multi-domain] Cd Length: 559 Bit Score: 224.06 E-value: 2.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 314 LCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKF--- 390
Cdd:COG4988 129 LLILIAIFFFNWAAALILLITAPLIPLFMILVGLAAKDASEKQFSALARLSGHFLDRLRGLETLRAFGRTEATEERIrkd 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 391 SQKLQK--MNTLhqKEA-LAYAVNLWITSISGMLlkvGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPS 467
Cdd:COG4988 209 SEDFRKatMSVL--RIAfLSSAVLEFFAYLSIAL---VAVYIGFRLLGEGDLTLFAGLFVLILAPEFFQPLRDLGSFFHA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 468 VQKAVGSSKEIFEYLGRIPRCPASGV--LTSLNLEGLVQFQDVSFAYPNHPdvPVLQALTFTLRPGEVIALVGRNGSGKS 545
Cdd:COG4988 284 AAAGEAAADKLFTLLESPVATPGSGEkaEVANEPPIEISLENLSFRYPDGK--PALSDLNLTIKAGQLTALVGASGAGKS 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 546 TVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGLVQKpTMEEVIAAAMVSGAHSFI 625
Cdd:COG4988 362 TLLNLLLGFLAPTQGEIRVNGIDLRDLSPEAWRKQISWVSQNPYLFAGTIRENILLARPDA-SDEEIIAALDQAGLLEFV 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 626 sELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHCLSL 705
Cdd:COG4988 441 -PKPDGLDTVIGEGGAGLSGGQAQRLALARALLSPASLLLLDEPTAHLDAETEQIILQALQELAKQ--KTVLVITHRLED 517
|
410 420 430
....*....|....*....|....*....|....*..
gi 548923797 706 LEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQA 742
Cdd:COG4988 518 AADADRIVVLDNGRLVEQGTHEELSEKQGLYANLLKQ 554
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
263-739 |
5.57e-62 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227590 [Multi-domain] Cd Length: 497 Bit Score: 216.07 E-value: 5.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 263 EVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWE-SLSLTMVTVVTLPLLFLL 341
Cdd:COG5265 20 VTFFHLHSLSLRFHLERRTGGLSRAIERGTKGIETILRWILFNILPTLVEISLVAVILWRVyGWWFALTTLVTVILYLLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 342 PEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKmntlHQKEALAYAVNL-WITSISGM 420
Cdd:COG5265 100 TVIVSDWRTDFRRLMNNADSDANAKAIDSLLNFETVKYFGNEEYEAVRYDHALET----YEKAAIKVHVSLlVLNFGQTA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 421 LLKVG---ILYIGGQLVTNGTISSGSLVtfILYQIQFTSAVEALF--STYPSVQKAVGSSK---EIFEYLGRIPRCPASG 492
Cdd:COG5265 176 IFSTGlrvMMTMSALGVEEGQLTVGDLV--NVNALLFQLSIPLNFlgFSYREIRQALTDMEkmfDLLDVEAEVSDAPDAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 493 VLTSLNLeGLVQFQDVSFAYpnHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQY 572
Cdd:COG5265 254 PLWPVRL-GAVAFINVSFAY--DPRRPILNGISFTIPLGKTVAIVGESGAGKSTILRLLFRFYDVNSGSITIDGQDIRDV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 573 EHRYLHTQVAAVRQEPQLFGRSFRENIAYGlVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVA 652
Cdd:COG5265 331 TQQSLRRAIGIVPQDTVLFNDTIAYNIKYG-RPDATAEEVGAAAEAAQIHDFIQSLPEGYDTGVGERGLKLSGGEKQRVA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDANS----QLRVKQLlykspeRRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQ 728
Cdd:COG5265 410 IARTILKNPPILILDEATSALDTHTeqaiQAALREV------SAGRTTLVIAHRLSTIIDADEIIVLDNGRIVERGTHEE 483
|
490
....*....|....
gi 548923797 729 LMERRGCF---WTM 739
Cdd:COG5265 484 LLAAGGLYaemWRR 497
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
310-741 |
1.13e-59 |
|
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: 227320 [Multi-domain] Cd Length: 573 Bit Score: 211.80 E-value: 1.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 310 LVRGLCLLGLMLWESLSLTM-VTVVTLPLLFLlpeklgRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQ 388
Cdd:COG4987 149 VTIGLSFFSIPLALLLGLILlLLLLIIPTLFY------RAGRKFGAHLAQGRAALRSQFTDWVQGQAELLIFGAEDAYRT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 389 KFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPS- 467
Cdd:COG4987 223 ALEATEASWLKAQRKQARFTGLSDAILLLIAGLLVIGLLLWMAAQVGAGALAQPGAALALLVIFAALEAFEPLAPGAFQh 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 468 VQKAVGSSKEIFEYLGRIP--RCPASGVLTSlnlEGLVQFQDVSFAYPNhPDVPVLQALTFTLRPGEVIALVGRNGSGKS 545
Cdd:COG4987 303 LGQVIASARRLNDILDQKPevTFPDEQTATT---GQALELRNVSFTYPG-QQTKALKNFNLTLAQGEKVAILGRSGSGKS 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 546 TVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIaygLVQKP--TMEEVIAAAMVSGAHS 623
Cdd:COG4987 379 TLLQLLAGAWDPQQGSITLNGVEIASLDEQALRETISVLTQRVHLFSGTLRDNL---RLANPdaSDEELWAALQQVGLEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 624 FISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYkspER-RFRSVLLITHC 702
Cdd:COG4987 456 LLESAPDGLNTWLGEGGRRLSGGERRRLALARALLHDAPLWLLDEPTEGLDPITERQVLALLF---EHaEGKTLLMVTHR 532
|
410 420 430
....*....|....*....|....*....|....*....
gi 548923797 703 LSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQ 741
Cdd:COG4987 533 LRGLERMDRIIVLDNGKIIEEGTHAELLANNGRYKRLYQ 571
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
275-736 |
2.78e-58 |
|
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: 210.75 E-value: 2.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 275 FFQQNQTGAITSRVTEDTSTLSESLSEKLSLL--LWYLVrglcLLGLML-WESLSLTMVTVVTLPLLFLLPEKLGRWHQV 351
Cdd:TIGR01193 246 FFSTRRTGEIVSRFTDASSIIDALASTILSLFldMWILV----IVGLFLvRQNMLLFLLSLLSIPVYAVIIILFKRTFNK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 352 LATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQK----FSQKLQKMNTLHQKEALAYAvnlwITSISGMLLKVGIL 427
Cdd:TIGR01193 322 LNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKADQGQQA----IKAVTKLILNVVIL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 428 YIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRIPRCPASGVLTSL-NLEGLVQFQ 506
Cdd:TIGR01193 398 WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELnNLNGDIVIN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 507 DVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQ 586
Cdd:TIGR01193 478 DVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 587 EPQLFGRSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLIL 666
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 667 DDATSALDANSQLRVKQLLYKSPErrfRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCF 736
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFY 702
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
238-741 |
3.54e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 208.03 E-value: 3.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 238 SAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLllwyLVRGLCLL 317
Cdd:PRK10790 78 AAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVAT----VLRSAALI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 318 GLMLWESLSL----TMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEeceaQKFSQK 393
Cdd:PRK10790 154 GAMLVAMFSLdwrmALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQ----ARFGER 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 394 LQKMNTLHqkealaYAVNLWITSISGMLLK-----------VGILYIGGqLVTNGTISSGSLVTFILYQIQFTSAVEALF 462
Cdd:PRK10790 230 MGEASRSH------YMARMQTLRLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFISYLGRLNEPLIELT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 463 STYPSVQKAVGSSKEIFEYLGRiPR---CPASGVLTSlnleGLVQFQDVSFAYpnHPDVPVLQALTFTLRPGEVIALVGR 539
Cdd:PRK10790 303 TQQSMLQQAVVAGERVFELMDG-PRqqyGNDDRPLQS----GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGH 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 540 NGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGlvqKPTMEEVI--AAAM 617
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG---RDISEEQVwqALET 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 618 VSGAhSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLykSPERRFRSVL 697
Cdd:PRK10790 453 VQLA-ELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL--AAVREHTTLV 529
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 548923797 698 LITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQ 741
Cdd:PRK10790 530 VIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
211-715 |
1.79e-55 |
|
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: 199.05 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 211 LTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTE 290
Cdd:TIGR02857 30 VDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 291 DTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEV 370
Cdd:TIGR02857 110 GVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 371 LSAMPTVRSFANEECEAQ---KFSQKLQK--MNTLhqKEA-LAYAVNLWITSISGMLLKVgilYIGGQLVTNGTISSGSL 444
Cdd:TIGR02857 190 LRGLPTLKLFGRAKAQAAairRSSEEYRErtMRVL--RIAfLSSAVLELFATLSVALVAV---YIGFRLLAGDLDLATGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 445 VTFILYQiQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRIPR-CPASGVLTSLNLEGLVqFQDVSFAYPNHPdvPVLQA 523
Cdd:TIGR02857 265 FVLLLAP-EFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRpLAGKAPVTAAPASSLE-FSGVSVAYPGRR--PALRP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 524 LTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGl 603
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 604 vqKP--TMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRV 681
Cdd:TIGR02857 420 --RPdaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
490 500 510
....*....|....*....|....*....|....
gi 548923797 682 KQLLYKSPERrfRSVLLITHCLSLLEQADQILFL 715
Cdd:TIGR02857 498 LEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
270-739 |
4.93e-52 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 190.31 E-value: 4.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 270 RQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWE-SLSLTMVTVVTLPLLFLLPEKLG-R 347
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGdQ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 348 WHQ--VLATQVQTSLAESSQvaiEVLSAMPTVRSFANEECEAQKFSQKLQKmntlhqkealAYAVNLWITSISG-----M 420
Cdd:PRK10789 161 LHErfKLAQAAFSSLNDRTQ---ESLTSIRMIKAFGLEDRQSALFAADAED----------TGKKNMRVARIDArfdptI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 421 LLKVGI---LYIGGQ--LVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRIPRCpASGVLT 495
Cdd:PRK10789 228 YIAIGManlLAIGGGswMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVV-KDGSEP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 496 SLNLEGLVQFQDVSFAYPNHpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHR 575
Cdd:PRK10789 307 VPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 576 YLHTQVAAVRQEPQLFGRSFRENIAYGlvqKP--TMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVAL 653
Cdd:PRK10789 386 SWRSRLAVVSQTPFLFSDTVANNIALG---RPdaTQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 654 ARALIRKPRVLILDDATSALDANSQLRVKQLLykSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERR 733
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
....*.
gi 548923797 734 GCFWTM 739
Cdd:PRK10789 541 GWYRDM 546
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
358-730 |
1.80e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 187.94 E-value: 1.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 358 TSLAESSQVAIEVLSAMPTVRSfaneeceaqkfsqkLQKM-NTLHQK----EALAYAVNLWITSISG---MLLKVGILYI 429
Cdd:TIGR01842 180 NNLADSALRNAEVIEAMGMMGN--------------LTKRwGRFHSKylsaQSAASDRAGMLSNLSKyfrIVLQSLVLGL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 430 GGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRIPrcPASGVLTSLNLEGLVQFQDVS 509
Cdd:TIGR01842 246 GAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYP--SRDPAMPLPEPEGHLSVENVT 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 510 FAYPNhPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQ 589
Cdd:TIGR01842 324 IVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 590 LFGRSFRENIAYgLVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:TIGR01842 403 LFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEP 481
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 670 TSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLM 730
Cdd:TIGR01842 482 NSNLDEEGEQALANAI-KALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
327-720 |
2.53e-50 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 226969 [Multi-domain] Cd Length: 580 Bit Score: 185.56 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 327 LTMVTVVTLPLLFLLPEKLGRWHQVLATQV---QTSLAESSQVAIEVLSAMPTVRSFAneeceaqkfsQKLQKMNTLHQK 403
Cdd:COG4618 164 IALAGAIILVVLALLNERATRKPLKEASEAsirANQLADATLRNAEVIEAMGMLGNLA----------KRWGRFNAAYLS 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 404 E-ALAYAVNLWITSISG---MLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIF 479
Cdd:COG4618 234 AqERASDRNGAFGALSRalrMALQSAVLGLGAWLVIKGEITPGMMIAGSILSGRALAPIDLAIANWKQFVAARQSYKRLN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 480 EYLGRIPrcPASGVLTSLNLEGLVQFQDVSFAYPNHPdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTK 559
Cdd:COG4618 314 ELLAELP--AAAERMPLPAPQGALSVERLTAAPPGQK-KPILKGISFALQAGEALGIIGPSGSGKSTLARLLVGIWPPTS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 560 GQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYgLVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEA 639
Cdd:COG4618 391 GSVRLDGADLRQWDREQLGRHIGYLPQDVELFDGTIAENIAR-FGEEADPEKVIEAARLAGVHELILRLPQGYDTRIGEG 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 640 GSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQADQILFLEGGT 719
Cdd:COG4618 470 GATLSGGQRQRIALARALYGDPFLVVLDEPNSNLDSEGEAALAAAI-LAAKARGGTVVVIAHRPSALASVDKILVLQDGR 548
|
.
gi 548923797 720 I 720
Cdd:COG4618 549 I 549
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
501-725 |
7.55e-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: 174.22 E-value: 7.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 501 GLVQFQDVSFAYPNHPDvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQ 580
Cdd:cd03244 1 GDIEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFGRSFRENIA-YGLVqkpTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLDpFGEY---SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 660 KPRVLILDDATSALDANSQLRVKQLLYKspERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGT 725
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
200-458 |
1.87e-49 |
|
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: 395537 [Multi-domain] Cd Length: 274 Bit Score: 174.75 E-value: 1.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 200 GEMAIPFFTGHLTDWILQ--DETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQ 277
Cdd:pfam00664 14 ISPAFPLVLGRILDVLLPdgDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 278 QNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQ 357
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQALATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 358 TSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNG 437
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
|
250 260
....*....|....*....|.
gi 548923797 438 TISSGSLVTFILYQIQFTSAV 458
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
515-746 |
4.70e-48 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 179.27 E-value: 4.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 515 HPDVPVLQALTFTLRPGEVIALVGRNGSGKST-VAALLQNLyqPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGR 593
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSlLNALLGFL--PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIAYGlvqKPTM--EEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:PRK11174 438 TLRDNVLLG---NPDAsdEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 672 ALDANSQLRVKQLLYKSPERrfRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQAPGGS 746
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
200-478 |
1.49e-47 |
|
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: 170.21 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 200 GEMAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQN 279
Cdd:cd18590 11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 280 QTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTS 359
Cdd:cd18590 91 KTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 360 LAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTI 439
Cdd:cd18590 171 IAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 548923797 440 SSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18590 251 TTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
500-741 |
1.48e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 171.93 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 500 EGLVQFQDVSFAYPNHPDvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHT 579
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGRSFRENIAYGLvQKPTMEEVIAAAMVSGAHSFIsELPQGYDTEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK11160 415 AISVVSQRVHLFSATLRDNLLLAA-PNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 660 KPRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTM 739
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
..
gi 548923797 740 MQ 741
Cdd:PRK11160 571 KQ 572
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
255-703 |
3.27e-44 |
|
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: 167.15 E-value: 3.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 255 RVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLC---LLGLMLWESLSL---- 327
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAavaAIAVLSVPAALIlaag 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 328 TMVTVVTLPLLFLLpekLGRWHQVLATQVQTSLAessQVAIEVLSAMPTVRSF-ANEECEAQKFSQKLQkMNTLHQKEAL 406
Cdd:TIGR02868 163 LLLAGFVAPLVSLR---AARAAEQALARLRGELA---AQLTDALDGAAELVASgALPAALAQVEEADRE-LTRAERRAAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 407 AYAVNLWITSISGMLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRIP 486
Cdd:TIGR02868 236 ATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 487 RCPASGV---LTSLNLEGLVQFQDVSFAYPnhPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLL 563
Cdd:TIGR02868 316 PVAEGSApaaGAVGLGKPTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 564 LDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGlvqKP--TMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGS 641
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA---RPdaTDEELWAALERVGLADWLRALPDGLDTVLGEGGA 470
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 642 QLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHCL 703
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
521-671 |
1.41e-43 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide as in CFTR, or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 153.96 E-value: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGR-SFRENI 599
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 600 AYGLvqkpTMEEVIAAAMVSGAHSFISELPQGY--DTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
502-724 |
2.24e-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: 156.51 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPD-VPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHRYL 577
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 578 HTQVAAVRQEPQL-------FGRSFRE--NIAYGLVQKPTMEEVIAAAM--VSGAHSFISELPQgydtevgeagsQLSGG 646
Cdd:cd03257 81 RKEIQMVFQDPMSslnprmtIGEQIAEplRIHGKLSKKEARKEAVLLLLvgVGLPEEVLNRYPH-----------ELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 647 QRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAG 724
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
504-719 |
2.01e-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: 153.01 E-value: 2.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 504 QFQDVSFAYPNHpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAA 583
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 584 VRQEP--QLFGRSFRENIAYGLVQ----KPTMEEVIAAAM-VSGAHSFISELPQgydtevgeagsQLSGGQRQAVALARA 656
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlglpEEEIEERVEEALeLVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 657 LIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFrSVLLITHCLSLL-EQADQILFLEGGT 719
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
503-719 |
2.36e-41 |
|
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: 149.93 E-value: 2.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYP--NHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTV-AALLQNLyQPTKGQLlldgeplpqyehrYLHT 579
Cdd:cd03250 1 ISVEDASFTWDsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGRSFRENIAYGLVQKPTM-EEVI-AAAMVSGahsfISELPQGYDTEVGEAGSQLSGGQRQAVALARAL 657
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPFDEERyEKVIkACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 658 IRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGT 719
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
502-732 |
3.58e-41 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 224047 [Multi-domain] Cd Length: 235 Bit Score: 150.48 E-value: 3.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL-PQYEHRYLHTQ 580
Cdd:COG1122 3 MIEAENLSFRYPG--RKAALKDVSLEIEKGERVLLIGPNGSGKSTLLKLLNGLLKPTSGEVLVDGLDTsSEKSLLELRQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEP--QLFGRSFRENIAYGLVQKPT----MEEVIAAAMV-SGAHSFISELPQgydtevgeagsQLSGGQRQAVAL 653
Cdd:COG1122 81 VGLVFQNPddQLFGPTVEDEVAFGLENLGLpreeIEERVAEALElVGLEELLDRPPF-----------NLSGGQKQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 654 ARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLMER 732
Cdd:COG1122 150 AGVLAMGPEILLLDEPTAGLDPKGRRELLELLKKLKEEGGKTIIIVTHDLELVLEyADRVVVLDDGKILADGDPAEIFND 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
502-734 |
3.74e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 224054 [Multi-domain] Cd Length: 293 Bit Score: 152.46 E-value: 3.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHtQV 581
Cdd:COG1131 4 VIEVRNLTKKYGG--DKTALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVKEPAKVRR-RI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFGR-SFRENI-----AYGLVQKPTMEEVIAAamvsgahsfISELpqGYDTEVGEAGSQLSGGQRQAVALAR 655
Cdd:COG1131 81 GYVPQEPSLYPElTVRENLeffarLYGLSKEEAEERIEEL---------LELF--GLEDKANKKVRTLSGGMKQRLSIAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 656 ALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLMERRG 734
Cdd:COG1131 150 ALLHDPELLILDEPTSGLDPESRREIWELLRELAKEGGVTILLSTHILEEAEElCDRVIILNDGKIIAEGTPEELKEKFG 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
207-730 |
4.11e-40 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 159.42 E-value: 4.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 207 FTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEflgdGVYNSIMG-RVHSQVQGEVFQAVLRQETEFFQQ--NQTGA 283
Cdd:PTZ00265 851 YVSTLFDFANLEANSNKYSLYILVIAIAMFISETLK----NYYNNVIGeKVEKTMKRRLFENILYQEISFFDQdkHAPGL 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 284 ITSRVTEDTSTLSESLSEKLSLLLWYLVrgLCLLGLMLWESLSLTMVTVVTLPL-----LFLLPEKLGRWHQVLATQVQT 358
Cdd:PTZ00265 927 LSAHINRDVHLLKTGLVNNIVIFTHFIV--LFLVSMVMSFYFCPIVAAVLTGTYfifmrVFAIRARLTANKDVEKKEINQ 1004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 359 S------------LAESSQVAIEVLSAMPTVRSFANEE--C----EAQKFSQKLQKMNTLhqkealayaVN--LWITSIS 418
Cdd:PTZ00265 1005 PgtvfaynsddeiFKDPSFLIQEAFYNMNTVIIYGLEDyfCnlieKAIDYSNKGQKRKTL---------VNsmLWGFSQS 1075
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 419 GMLLKVGILY-IGGQLVTNGTISSG----SLVTFIlyqiqFT-SAVEALFSTYPSVQKAVGSSKEIFEYLGRIPRCPASG 492
Cdd:PTZ00265 1076 AQLFINSFAYwFGSFLIRRGTILVDdfmkSLFTFL-----FTgSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRD 1150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 493 -----VLTSLNLEGLVQFQDVSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQ----------- 556
Cdd:PTZ00265 1151 nggirIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkn 1230
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 557 -------------------------------------------PTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGR 593
Cdd:PTZ00265 1231 ehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNM 1310
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIAYGLvQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSAL 673
Cdd:PTZ00265 1311 SIYENIKFGK-EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 674 DANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEG----GTICEA-GTYRQLM 730
Cdd:PTZ00265 1390 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELL 1451
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
222-715 |
1.25e-39 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 158.27 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 222 SAFTRNITLMSILTTTSavLEFLGDGVYNSimGRVHSQVQGevfqAVLRQETEFF-QQNQTGAITSRVTEDTSTLSesls 300
Cdd:PTZ00265 117 SSFCMDVVTTKILKTLK--LEFLKSVFYQD--GQFHDNNPG----SKLTSDLDFYlEQVNAGIGTKFITIFTYASA---- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 301 eklslllwylvrglcLLGLMLW---ESLSLTMVTVVTLPLLFLL------PEKLGRWHQVLATQVQTSLAESSQVAIEvl 371
Cdd:PTZ00265 185 ---------------FLGLYIWslfKNARLTLCITCVFPLIYICgvicnkKVKINKKTSLLYNNNTMSIIEEALVGIR-- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 372 sampTVRSFANEECEAQKF--SQKLQKMNTLHQKealaYAVNLWITSISGMLL---KVGILYiGGQLV--------TNGT 438
Cdd:PTZ00265 248 ----TVVSYCGEKTILKKFnlSEKLYSKYILKAN----FMESLHIGMINGFILasyAFGFWY-GTRIIisdlsnqqPNND 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 439 ISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRIPRCPASGVLTSLNLEGLVQFQDVSFAYPNHPDV 518
Cdd:PTZ00265 319 FHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLL-DGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRE 597
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 598 NIAYGLVQKPTME--------------------------------------------------------EVIAAAMVSGA 621
Cdd:PTZ00265 479 NIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLI 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 622 HSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITH 701
Cdd:PTZ00265 559 HDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
570
....*....|....
gi 548923797 702 CLSLLEQADQILFL 715
Cdd:PTZ00265 639 RLSTIRYANTIFVL 652
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
202-475 |
3.78e-39 |
|
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: 146.51 E-value: 3.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQDETASAF-----TRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFF 276
Cdd:cd18573 13 MSVPFAIGKLIDVASKESGDIEIfglslKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 277 QQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQV 356
Cdd:cd18573 93 DKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 357 QTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTN 436
Cdd:cd18573 173 QDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVAS 252
|
250 260 270
....*....|....*....|....*....|....*....
gi 548923797 437 GTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSS 475
Cdd:cd18573 253 GELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGAS 291
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
503-724 |
6.31e-39 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 142.07 E-value: 6.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRyLHTQVA 582
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGRSFRENIayglvqkptmeeviaaamvsgahsfiselpqgydtevgeaGSQLSGGQRQAVALARALIRKPR 662
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 663 VLILDDATSALDANSQLRVKQLLYKspERRFRSVLLITHCLSLLEQADQILFLEGGTICEAG 724
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
504-720 |
1.35e-38 |
|
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: 140.81 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 504 QFQDVSFAYPNHpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAA 583
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 584 VRQEPQLFGRSFRENIayglvqkptmeeviaaamvsgahsfiselpqgydtevgeagsqLSGGQRQAVALARALIRKPRV 663
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 664 LILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQADQILFLEGGTI 720
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
503-732 |
1.76e-38 |
|
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: 143.72 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDG-EPLPQYEHRYLHTQV 581
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEP--QLFGRSFRENIAYGL----VQKPTMEEVI--AAAMVsGAHSFISELPQgydtevgeagsQLSGGQRQAVAL 653
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLenlgVPREEMRKRVdeALKLV-GMEDFRDREPH-----------LLSGGQKQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 654 ARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMER 732
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
502-730 |
1.86e-38 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 224045 [Multi-domain] Cd Length: 258 Bit Score: 143.47 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQV 581
Cdd:COG1120 2 MLEVENLSFGYGGKP---ILDDLSFSIPKGEITGILGPNGSGKSTLLKCLAGLLKPKSGEVLLDGKDIASLSPKELAKKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQL-FGRSFRENIAYG------LVQKPT---MEEVIAAAMVSGAHSFIselpqgyDTEVGEagsqLSGGQRQAV 651
Cdd:COG1120 79 AYVPQSPSApFGLTVYELVLLGryphlgLFGRPSkedEEIVEEALELLGLEHLA-------DRPVDE----LSGGERQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSL-LEQADQILFLEGGTICEAGTYRQLM 730
Cdd:COG1120 148 LIARALAQETPILLLDEPTSHLDIAHQIEVLELLRDLNREKGLTVVMVLHDLNLaARYADHLILLKDGKIVAQGTPEEVL 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
201-478 |
4.91e-38 |
|
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: 143.46 E-value: 4.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 201 EMAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQ 280
Cdd:cd07346 15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 281 TGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSL 360
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 361 AESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTIS 440
Cdd:cd07346 175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLT 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 548923797 441 SGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd07346 255 IGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
503-720 |
1.05e-37 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 140.30 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPN-HPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQyehryLHTQV 581
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFG-RSFRENIAYGL-VQKPTMEEVIAAAMvsgahSFISElpqgydteVGEAG------SQLSGGQRQAVAL 653
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLeLQGVPKAEARERAE-----ELLEL--------VGLSGfenaypHQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 654 ARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHclSLLEQ---ADQILFLEG--GTI 720
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTH--DIDEAvflADRVVVLSArpGRI 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
506-724 |
5.03e-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: 136.80 E-value: 5.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 506 QDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVr 585
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 586 qePQLfgrsfreniayglvqkptMEEVIAAAMvsgAHSFISELpqgydtevgeagsqlSGGQRQAVALARALIRKPRVLI 665
Cdd:cd03214 79 --PQA------------------LELLGLAHL---ADRPFNEL---------------SGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 666 LDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSL-LEQADQILFLEGGTICEAG 724
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
502-732 |
1.70e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 224049 [Multi-domain] Cd Length: 252 Bit Score: 137.78 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPDV-PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHT- 579
Cdd:COG1124 3 LLSVRNLSIVYGGGKFAfHALNNVSLEIERGETLGIVGESGSGKSTLARLLAGLEKPSSGSILLDGKPLAPKKRAKAFYr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEP-------QLFGRSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFISELPqgydtevgeagSQLSGGQRQAVA 652
Cdd:COG1124 83 PVQMVFQDPysslnprRTVGRILSEPLRPHGLSKSQQRIAELLDQVGLPPSFLDRRP-----------HELSGGQRQRIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLME 731
Cdd:COG1124 152 IARALIPEPKLLILDEPTSALDVSVQAQILNLLLELKKERGLTYLFISHDLALVEHmCDRIAVMDNGQIVEIGPTEELLS 231
|
.
gi 548923797 732 R 732
Cdd:COG1124 232 H 232
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
202-478 |
8.23e-36 |
|
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: 137.00 E-value: 8.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQDETASAFTRNITLmsilttTSAVLEFLGDGVYNSIMG------------RVHSQVQGEVFQAVL 269
Cdd:cd18780 13 LALPYFFGQVIDAVTNHSGSGGEEALRAL------NQAVLILLGVVLIGSIATflrswlftlageRVVARLRKRLFSAII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 270 RQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWH 349
Cdd:cd18780 87 AQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 350 QVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYI 429
Cdd:cd18780 167 RKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWY 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 548923797 430 GGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18780 247 GGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
502-729 |
1.05e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 224058 [Multi-domain] Cd Length: 339 Bit Score: 138.15 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPN--HPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHRY 576
Cdd:COG1135 1 MIELENVSKTFGQtgTGTVTALDDVSLEIPKGEIFGIIGYSGAGKSTLLRLINLLERPTSGSVFVDGQdltALSEAELRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 LHTQVAAVRQEPQLFG-RSFRENIAYGL-VQKPTMEEViaAAMVSGAHSF--ISELPQGYDtevgeagSQLSGGQRQAVA 652
Cdd:COG1135 81 LRQKIGMIFQHFNLLSsRTVFENVAFPLeLAGVPKAEI--KQRVAELLELvgLSDKADRYP-------AQLSGGQKQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 653 LARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:COG1135 152 IARALANNPKILLCDEATSALDPETTQSILELLKDINRELGLTIVLITHEMEVVKRiCDRVAVLDQGRLVEEGTVSEV 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
264-744 |
1.82e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 145.12 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 264 VFQAVLRQETEFFQQNQTGAITSRVTEDTSTL---SESLSEKLSLLLWYLVRGLCLLGLMlwESLSLTMVtvvtLPLLFL 340
Cdd:PLN03232 989 MLNSILRAPMLFFHTNPTGRVINRFSKDIGDIdrnVANLMNMFMNQLWQLLSTFALIGTV--STISLWAI----MPLLIL 1062
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 341 LPEKLgRWHQVLATQVQ--TSLAESSQVAI--EVLSAMPTVRSFaneeceaqKFSQKLQKMNTLHQKEALAYAV-----N 411
Cdd:PLN03232 1063 FYAAY-LYYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY--------KAYDRMAKINGKSMDNNIRFTLantssN 1133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 412 LWIT----SISGMLL-KVGILYIGGQLVTNGTISSGSLVTFIL-YQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYLGRI 485
Cdd:PLN03232 1134 RWLTirleTLGGVMIwLTATFAVLRNGNAENQAGFASTMGLLLsYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLP 1213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 486 PRCPA----SGVLTSLNLEGLVQFQDVSFAY-PNHPdvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKG 560
Cdd:PLN03232 1214 SEATAiienNRPVSGWPSRGSIKFEDVHLRYrPGLP--PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKG 1291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 561 QLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENI-AYGLVQKPTMEEVIAAAMVSGAhsfISELPQGYDTEVGEA 639
Cdd:PLN03232 1292 RIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDADLWEALERAHIKDV---IDRNPFGLDAEVSEG 1368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 640 GSQLSGGQRQAVALARALIRKPRVLILDDATSALDansqLRVKQLLYKSPERRFRS--VLLITHCLSLLEQADQILFLEG 717
Cdd:PLN03232 1369 GENFSVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIQRTIREEFKSctMLVIAHRLNTIIDCDKILVLSS 1444
|
490 500
....*....|....*....|....*...
gi 548923797 718 GTICEAGTYRQLMERRG-CFWTMMQAPG 744
Cdd:PLN03232 1445 GQVLEYDSPQELLSRDTsAFFRMVHSTG 1472
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
504-719 |
4.03e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 130.44 E-value: 4.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 504 QFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAA 583
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 584 VrqepqlfgrsfreniayglvqkptmeeviaaamvsgahsfiselpqgydtevgeagSQLSGGQRQAVALARALIRKPRV 663
Cdd:cd00267 78 V--------------------------------------------------------PQLSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 664 LILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCLSLLEQA-DQILFLEGGT 719
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
503-720 |
5.29e-35 |
|
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: 130.60 E-value: 5.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHtQVA 582
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGR-SFRENIayglvqkptmeeviaaamvsgahsfiselpqgydtevgeagsQLSGGQRQAVALARALIRKP 661
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 662 RVLILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCLSLLEQ-ADQILFLEGGTI 720
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
502-722 |
9.74e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224059 [Multi-domain] Cd Length: 226 Bit Score: 131.86 E-value: 9.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPN-HPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHT- 579
Cdd:COG1136 1 MIELKNVSKIYGLgGEKVEALKDVNLEIEAGEFVAIVGPSGSGKSTLLNLLGGLDKPTSGEVLINGKDLTKLSEKELAKl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 ---QVAAVRQEPQLFGR-SFRENIAYGLV-----QKPTMEEVIAAAMVSG-AHSFISELPqgydtevgeagSQLSGGQRQ 649
Cdd:COG1136 81 rrkKIGFVFQNFNLLPDlTVLENVELPLLiagksAGRRKRAAEELLEVLGlEDRLLKKKP-----------SELSGGQQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 650 AVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICE 722
Cdd:COG1136 150 RVAIARALINNPKIILADEPTGNLDSKTAKEVLELLRELNKERGKTIIMVTHDPELAKYADRVIELKDGKIEE 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
503-724 |
1.15e-34 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 131.10 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEP---LPQYEHRylht 579
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgVPPERRN---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 qVAAVRQEPQLF-GRSFRENIAYGLVQKPTMEEVI------AAAMVsGAHSFISELPqgydtevgeagSQLSGGQRQAVA 652
Cdd:cd03259 74 -IGMVFQDYALFpHLTVAENIAFGLKLRGVPKAEIrarvreLLELV-GLEGLLNRYP-----------HELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 653 LARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAG 724
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
263-744 |
1.16e-34 |
|
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: 142.39 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 263 EVFQAVLRQETEFFQQNQTGAITSRVTEDTST--LSESLSEKLSLLLWYLVRGLCLLGLmlwesLSLTMVTVVTLPL--L 338
Cdd:TIGR00957 1043 DLLHNKLRSPMSFFERTPSGNLVNRFSKELDTvdSMIPPVIKMFMGSLFNVIGALIVIL-----LATPIAAVIIPPLglL 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 339 FLLPEKLgrwhqVLATQVQTSLAES-SQVAI-----EVLSAMPTVRSFAneecEAQKFSQKLQKMNTLHQKEALAYAV-N 411
Cdd:TIGR00957 1118 YFFVQRF-----YVASSRQLKRLESvSRSPVyshfnETLLGVSVIRAFE----EQERFIHQSDLKVDENQKAYYPSIVaN 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 412 LWitsisgmlLKVGILYIGGQLV---------TNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEIFEYL 482
Cdd:TIGR00957 1189 RW--------LAVRLECVGNCIVlfaalfaviSRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYS 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 483 GRIPRCP----ASGVLTSLNLEGLVQFQDVSFAYPNHPDVpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPT 558
Cdd:TIGR00957 1261 ETEKEAPwqiqETAPPSGWPPRGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA 1339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 559 KGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENI-AYGlvqKPTMEEVIAAAMVSGAHSFISELPQGYDTEVG 637
Cdd:TIGR00957 1340 EGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS---QYSDEEVWWALELAHLKTFVSALPDKLDHECA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 638 EAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDansqLRVKQLLYKSPERRFR--SVLLITHCLSLLEQADQILFL 715
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD----LETDNLIQSTIRTQFEdcTVLTIAHRLNTIMDYTRVIVL 1492
|
490 500
....*....|....*....|....*....
gi 548923797 716 EGGTICEAGTYRQLMERRGCFWTMMQAPG 744
Cdd:TIGR00957 1493 DKGEVAEFGAPSNLLQQRGIFYSMAKDAG 1521
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
503-720 |
1.66e-34 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein; 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. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. 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: 131.07 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYP-NHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHR----YL 577
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 578 HTQVAAVRQEPQLFGR-SFRENIAYGL----VQKPTMEEVIAAAMvsgahsfiselpqgydTEVGEAG------SQLSGG 646
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLllagVPKKERRERAEELL----------------ERVGLGDrlnhypSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 647 QRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTI 720
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
502-701 |
5.55e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 224041 [Multi-domain] Cd Length: 248 Bit Score: 130.37 E-value: 5.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYehrylHTQV 581
Cdd:COG1116 3 LLEIEGVSKSFGG---VEVLEDINLSVEKGEFVAILGPSGCGKSTLLRLIAGLEKPTSGEVLLDGRPVTGP-----GPDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFG-RSFRENIAYGLVQ----KPTMEEVIAA--AMVsGAHSFISELPqgydtevgeagSQLSGGQRQAVALA 654
Cdd:COG1116 75 GYVFQEDALLPwLTVLDNVALGLELrgksKAEARERAKEllELV-GLAGFEDKYP-----------HQLSGGMRQRVAIA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 548923797 655 RALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITH 701
Cdd:COG1116 143 RALATRPKLLLLDEPFGALDALTREELQDELLRLWEETRKTVLLVTH 189
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
507-720 |
9.93e-34 |
|
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: 128.14 E-value: 9.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 507 DVSFAYPNHPDVpvLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRylhTQVAAVRQ 586
Cdd:cd03226 4 NISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 587 EP--QLFGRSFRENIAYGLVQKPTMEEVIAAAMVS-GAHSFISELPQgydtevgeagsQLSGGQRQAVALARALIRKPRV 663
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDlDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 664 LILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLL-EQADQILFLEGGTI 720
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELI-RELAAQGKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
503-725 |
1.58e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.73 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVA 582
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEP--QLFGRSFRENIAYGL----VQKPTMEEVIA-AAMVSGAHSFISELPQgydtevgeagsQLSGGQRQAVALAR 655
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLenkkVPPKKMKDIIDdLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 656 ALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGT 725
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase components [Amino acid transport ... |
501-732 |
2.81e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase components [Amino acid transport and metabolism];
Pssm-ID: 226361 [Multi-domain] Cd Length: 352 Bit Score: 131.25 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 501 GLVQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEP---LPQYEHRyl 577
Cdd:COG3842 4 PALEIRNVSKSFG---DFTAVDDISLDIKKGEFVTLLGPSGCGKTTLLRMIAGFEQPSSGEILLDGEDitdVPPEKRP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 578 htqVAAVRQEPQLFG-RSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFIsELPQGYDTEVgeagSQLSGGQRQAVALARA 656
Cdd:COG3842 79 ---IGMVFQSYALFPhMTVEENVAFGLKVRKKLKKAEIKARVEEALELV-GLEGFADRKP----HQLSGGQQQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 657 LIRKPRVLILDDATSALDAN--SQLRVKQllyKSPERRFR-SVLLITH----CLSLleqADQILFLEGGTICEAGTYRQL 729
Cdd:COG3842 151 LVPEPKVLLLDEPLSALDAKlrEQMRKEL---KELQRELGiTFVYVTHdqeeALAM---SDRIAVMNDGRIEQVGTPEEI 224
|
...
gi 548923797 730 MER 732
Cdd:COG3842 225 YER 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
503-729 |
3.40e-33 |
|
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: 127.68 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLY-----QPTKGQLLLDGEPL--PQYEHR 575
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 576 YLHTQVAAVRQEPQLFGRSFRENIAYGL----VQKPTMEEVIAAAMVSGAhsfiselpqGYDTEVGE--AGSQLSGGQRQ 649
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLrlhgIKLKEELDERVEEALRKA---------ALWDEVKDrlHALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 650 AVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSpeRRFRSVLLITHclsLLEQA----DQILFLEGGTICEAGT 725
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTH---NMQQAarvaDRTAFLLNGRLVEFGP 223
|
....
gi 548923797 726 YRQL 729
Cdd:cd03260 224 TEQI 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
498-732 |
6.06e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 498 NLEGLVQFQDVSFAYPNHPDvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYL 577
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 578 HTQVAAVRQEP--QLFGRSFRENIAYGL----VQKPTM-EEVIAAAMVSGAHSFISELPqgydtevgeagSQLSGGQRQA 650
Cdd:PRK13635 80 RRQVGMVFQNPdnQFVGATVQDDVAFGLenigVPREEMvERVDQALRQVGMEDFLNREP-----------HRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 651 VALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLM 730
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
..
gi 548923797 731 ER 732
Cdd:PRK13635 229 KS 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
484-732 |
1.54e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 224048 [Multi-domain] Cd Length: 539 Bit Score: 132.70 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 484 RIPRCPASGVLTSLNLEGLVQFQDVSFAYPNHPD--------VPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLY 555
Cdd:COG1123 262 GDEKIIRLPRRGPLRAEPLLSVRNLSKRYGSRKGlfvrergeVKAVDDVSFDLREGETLGLVGESGSGKSTLARILAGLL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 556 QPTKGQLLLDGEPLPQYEHRY--LHTQVAAVRQEPQLF---GRSFRENIA-----YGLVQKPTMEEVIAAAM--VSGAHS 623
Cdd:COG1123 342 PPSSGSIIFDGQDLDLTGGELrrLRRRIQMVFQDPYSSlnpRMTVGDILAeplriHGGGSGAERRARVAELLelVGLPPE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 624 FISELPqgydtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCL 703
Cdd:COG1123 422 FLDRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPVSALDVSVQAQVLNLLKDLQEELGLTYLFISHDL 490
|
250 260 270
....*....|....*....|....*....|
gi 548923797 704 SLLEQ-ADQILFLEGGTICEAGTYRQLMER 732
Cdd:COG1123 491 AVVRYiADRVAVMYDGRIVEEGPTEKVFEN 520
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
503-719 |
1.80e-32 |
|
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: 123.84 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYE--HRYLHTQ 580
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLF-GRSFRENIAYGLvqkptmeeviaaamvsgahsfiselpqgydtevgeagsqlSGGQRQAVALARALIR 659
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALGL----------------------------------------SGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 660 KPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGT 719
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
502-729 |
2.81e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 224051 [Multi-domain] Cd Length: 240 Bit Score: 125.31 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEH-RYLHTQ 580
Cdd:COG1126 2 MIEIKNLSKSFG---DKEVLKGISLSVEKGEVVVIIGPSGSGKSTLLRCLNGLEEPDSGSITVDGEDVGDKKDiLKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFG-RSFRENIAYGL--VQKPTMEEVIAAAMvsgahsfiSELpqgydTEVGEAG------SQLSGGQRQAV 651
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPvkVKKLSKAEAREKAL--------ELL-----EKVGLADkadaypAQLSGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:COG1126 146 AIARALAMDPKVMLFDEPTSALDPELVGEVLDVM-KDLAEEGMTMIIVTHEMGFAREvADRVIFMDQGKIIEEGPPEEF 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
502-729 |
4.29e-32 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 124.62 E-value: 4.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHP-DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHRYL 577
Cdd:cd03258 1 MIELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 578 HTQVAAVRQEPQLF-GRSFRENIAYGL-VQKPTMEEVIAAamvsgahsfISELPQgydtEVGEAG------SQLSGGQRQ 649
Cdd:cd03258 81 RRRIGMIFQHFNLLsSRTVFENVALPLeIAGVPKAEIEER---------VLELLE----LVGLEDkadaypAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 650 AVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQ 728
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
.
gi 548923797 729 L 729
Cdd:cd03258 228 V 228
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
202-478 |
9.47e-32 |
|
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: 125.29 E-value: 9.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGdgVYN-SIMG-RVHSQVQGEVFQAVLRQETEFFQQN 279
Cdd:cd18576 13 LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFR--IYLfARVGeRVVADLRKDLYRHLQRLPLSFFHER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 280 QTGAITSRVTEDTSTLSESLSEKLSLllwyLVRGLCLL----GLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQ 355
Cdd:cd18576 91 RVGELTSRLSNDVTQIQDTLTTTLAE----FLRQILTLiggvVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 356 VQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYA--VNLWITSISGMLlkVGILYIGGQL 433
Cdd:cd18576 167 VQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRAlfSSFIIFLLFGAI--VAVLWYGGRL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 548923797 434 VTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18576 245 VLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
503-732 |
3.83e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 123.37 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQP---TKGQLLLDGEPLPQYEHRYLHT 579
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEP--QLFGRSFRENIAYGL----VQKPTMEEVIAAAMVS-GAHSFISELPQgydtevgeagsQLSGGQRQAVA 652
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLenraVPRPEMIKIVRDVLADvGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMER 732
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
502-721 |
3.88e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 224046 [Multi-domain] Cd Length: 254 Bit Score: 122.34 E-value: 3.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRylhTQV 581
Cdd:COG1121 4 MIEVENLTVSYGNRP---VLEDISLSVEKGEITALIGPNGAGKSTLLKAILGLLKPSSGEIKIFGKPVRKRRKR---LRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQL---FGRSFRENIAYGLVQKPTM---------EEVIAAAMVSGAHSFIselpqgyDTEVGEagsqLSGGQRQ 649
Cdd:COG1121 78 GYVPQKSSVdrsFPITVKDVVLLGRYGKKGWfrrlnkkdkEKVDEALERVGMEDLR-------DRQIGE----LSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 650 AVALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTIC 721
Cdd:COG1121 147 RVLLARALAQNPDLLLLDEPFTGVDVAGQKEIYDLL-KELRQEGKTVLMVTHDLGLVMAyFDRVICLNRHLIA 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
503-732 |
4.41e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 226359 [Multi-domain] Cd Length: 338 Bit Score: 124.68 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNhpdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQY--EHRylhtQ 580
Cdd:COG3839 4 LELKNVRKSFGS---FEVLKDVNLDIEDGEFVVLLGPSGCGKSTLLRMIAGLEEPTSGEILIDGRDVTDLppEKR----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFGR-SFRENIAYGLVQKPTMEEVIA-----AAMVSGAHSFISELPqgydtevgeagSQLSGGQRQAVALA 654
Cdd:COG3839 77 IAMVFQNYALYPHmTVYENIAFGLKLRGVPKAEIDkrvkeVAKLLGLEHLLNRKP-----------LQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 655 RALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITH----CLSLleqADQILFLEGGTICEAGTYRQLM 730
Cdd:COG3839 146 RALVRKPKVFLLDEPLSNLDAKLRVLMRSEIKKLHERLGTTTIYVTHdqveAMTL---ADRIVVMNDGRIQQVGTPLELY 222
|
..
gi 548923797 731 ER 732
Cdd:COG3839 223 ER 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
501-725 |
1.95e-30 |
|
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: 119.05 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 501 GLVQFQDVSFAY-PNHPdvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHT 579
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGRSFRENI-AYGlvqKPTMEEVIAAAMVSgahsfiselpqgydtevgEAGSQLSGGQRQAVALARALI 658
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFD---EYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 659 RKPRVLILDDATSALDANSQLRVKQLLYKspERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGT 725
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
503-729 |
2.21e-30 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 119.53 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLP---QYEHRYLHT 579
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGR-SFRENIAYGLVQKPTM-EEVIAA------AMVsGAHSFISELPqgydtevgeagSQLSGGQRQAV 651
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLsEEEIREivleklEAV-GLRGAEDLYP-----------AELSGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCL-SLLEQADQILFLEGGTICEAGTYRQL 729
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
502-712 |
3.39e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 224053 [Multi-domain] Cd Length: 500 Bit Score: 125.32 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRylHTQ- 580
Cdd:COG1129 8 LLELRGISKSFG---GVKALDGVSLTVRPGEVHALLGENGAGKSTLMKILSGVYPPDSGEILIDGKPVAFSSPR--DALa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 --VAAVRQEPQLFGR-SFRENI--------AYGLVQKPTMEEVIAAAMvsgAHSFISELPqgyDTEVGEagsqLSGGQRQ 649
Cdd:COG1129 83 agIATVHQELSLVPNlSVAENIflgreptrRFGLIDRKAMRRRARELL---ARLGLDIDP---DTLVGD----LSIAQRQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 650 AVALARALIRKPRVLILDDATSALDANSQLRVKQLLykspeRRFR----SVLLITHCLS-LLEQADQI 712
Cdd:COG1129 153 MVEIARALSFDARVLILDEPTAALTVKETERLFDLI-----RRLKaqgvAIIYISHRLDeVFEIADRI 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
516-725 |
5.53e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 224043 [Multi-domain] Cd Length: 345 Bit Score: 121.69 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 516 PDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHT-QVAAVRQEPQLFGR- 593
Cdd:COG1118 13 GAFGALDDISLDIKSGELVALLGPSGAGKSTLLRIIAGLETPDAGRIRLNGRVLFDVSNLAVRDrKVGFVFQHYALFPHm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIAYGL-VQKPTMEEVIAAAMVSGAHSFI--SELPQGYDtevgeagSQLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:COG1118 93 TVADNIAFGLkVRKERPSEAEIRARVEELLRLVqlEGLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDEPF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 671 SALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAGT 725
Cdd:COG1118 166 GALDAKVRKELRRWLRKLHDRLGVTTVFVTHDQEeALELADRVVVLNQGRIEQVGP 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
504-721 |
6.19e-30 |
|
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: 117.63 E-value: 6.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 504 QFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRylhtqVAA 583
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 584 VrqePQLFG--RSF----RENIAYGLV---------QKPTMEEVIAA----AMVSGAHSFISElpqgydtevgeagsqLS 644
Cdd:cd03235 73 V---PQRRSidRDFpisvRDVVLMGLYghkglfrrlSKADKAKVDEAlervGLSELADRQIGE---------------LS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCL-SLLEQADQILFLEGGTIC 721
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDLgLVLEYFDRVLLLNRTVVA 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
500-732 |
9.15e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 224048 [Multi-domain] Cd Length: 539 Bit Score: 124.61 E-value: 9.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 500 EGLVQFQDVSFAYPNHPD-VPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNL----YQPTKGQLLLDGEP---LPQ 571
Cdd:COG1123 3 SPLLEVENLTVEFATDGGrVPAVRDVSFEVEPGEILGIVGESGSGKSTLALALMGLlpegGRITSGEVILDGRDllgLSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 572 YEHRYLH-TQVAAVRQEP-QLF------GRSFRENIA--YGLVQKPTMEEVIAA-AMVSGAHSF-ISELPQgydtevgea 639
Cdd:COG1123 83 REMRKLRgKRIAMIFQDPmTSLnpvmtiGDQIREALRlhGKGSRAEARKRAVELlEQVGLPDPErRDRYPH--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 640 gsQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGG 718
Cdd:COG1123 154 --QLSGGMRQRVMIAMALALKPKLLIADEPTTALDVTTQAQILDLLKDLQRELGMAVLFITHDLGVVAElADRVVVMYKG 231
|
250
....*....|....
gi 548923797 719 TICEAGTYRQLMER 732
Cdd:COG1123 232 EIVETGPTEEILSN 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
501-746 |
1.16e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 126.78 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 501 GLVQFQDVSFAY-PNHPdvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHT 579
Cdd:PLN03130 1236 GSIKFEDVVLRYrPELP--PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGRSFRENIayglvqKPTMEEVIAAAMVS--GAH--SFISELPQGYDTEVGEAGSQLSGGQRQAVALAR 655
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLWESleRAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 656 ALIRKPRVLILDDATSALDansqLRVKQLLYKSPERRFRS--VLLITHCLSLLEQADQILFLEGGTICEAGTYRQL-MER 732
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVD----VRTDALIQKTIREEFKSctMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNE 1463
|
250
....*....|....
gi 548923797 733 RGCFWTMMQAPGGS 746
Cdd:PLN03130 1464 GSAFSKMVQSTGAA 1477
|
|
| FetA |
COG4619 |
ABC-type iron transport system FetAB, ATPase component [Inorganic ion transport and metabolism] ... |
502-701 |
1.89e-29 |
|
ABC-type iron transport system FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226970 [Multi-domain] Cd Length: 223 Bit Score: 116.50 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAypnHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQV 581
Cdd:COG4619 3 LLELKQVGYL---AGDAKILNNISLSVRAGEFIAITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDVSTLKPEAYRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFGRSFRENIAY-GLVQKPTMEEVIAAAMVSGAhsfisELPqgyDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:COG4619 80 SYCAQTPALFGDTVEDNLIFpWQIRNRRPDRAAALDLLARF-----ALP---DSILTKNITELSGGEKQRIALIRNLQFM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITH 701
Cdd:COG4619 152 PKILLLDEITSALDESNKRNIEEMIHRYVREQNVAVLWITH 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
503-720 |
2.49e-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: 116.09 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQ--YEHRYLHTQ 580
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFG-RSFRENIAYGL--VQKPTMEEVIAAAMvsgahsfiselpqGYDTEVGEAG------SQLSGGQRQAV 651
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPikVKGMSKAEAEERAL-------------ELLEKVGLADkadaypAQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 652 ALARALIRKPRVLILDDATSALD---ANSQLRVKQLLYKSPerrfRSVLLITHCLSL-LEQADQILFLEGGTI 720
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEG----MTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
502-722 |
2.49e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.87 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPN------HPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQY--- 572
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 573 EHRYLHTQVAAVRQEP-------QLFGRSFRENIAYGLVQKPTMEEVIAAAM---VSGAHSFISELPQgydtevgeagsQ 642
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSisavnprKTVREIIREPLRHLLSLDKAERLARASEMlraVDLDDSVLDKRPP-----------Q 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 643 LSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTIC 721
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
|
.
gi 548923797 722 E 722
Cdd:PRK10419 232 E 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
504-720 |
7.96e-29 |
|
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: 115.36 E-value: 7.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 504 QFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHT---Q 580
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFGR-SFRENIAYGLVqkptmeeviaaamvsGAHSFISELPQGYDTE-----------VGEAG------SQ 642
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRL---------------GRRSTWRSLFGLFPKEekqralaalerVGLLDkayqraDQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 643 LSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSL-LEQADQILFLEGGTI 720
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRI 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
499-732 |
2.33e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.21 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 499 LEGLVQFQDVSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLH 578
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 579 TQVAAVRQEP--QLFGRSFRENIAYGLVQK----PTMEE-VIAAAMVSGAHSFISELPqgydtevgeagSQLSGGQRQAV 651
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKgiphEEMKErVNEALELVGMQDFKEREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLME 731
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
.
gi 548923797 732 R 732
Cdd:PRK13650 230 R 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
497-729 |
2.57e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 226967 [Multi-domain] Cd Length: 268 Bit Score: 114.62 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 497 LNLEGLVQFQDVSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQyehry 576
Cdd:COG4608 5 LEVKNLKKYFPVGKGFGKKRYVKAVDGVSFSIKEGETLGLVGESGCGKSTLGRLILGLEEPTSGEILFEGKDITK----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 lhtqvaavrqepqlFGRSFRENIAYGLVQKptmeeviaaamVSGAHSFISELPqgydtevgeagSQLSGGQRQAVALARA 656
Cdd:COG4608 80 --------------LSKEERRERVLELLEK-----------VGLPEEFLYRYP-----------HELSGGQRQRIGIARA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 657 LIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:COG4608 124 LALNPKLIVADEPVSALDVSVQAQILNLLKDLQEELGLTYLFISHDLSVVRYiSDRIAVMYLGKIVEIGPTEEV 197
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
203-478 |
2.91e-28 |
|
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: 115.27 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 203 AIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGdgVY--NSIMGRVHSQVQGEVFQAVLRQETEFFQQNQ 280
Cdd:cd18575 14 ALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR--FYlvSWLGERVVADLRKAVFAHLLRLSPSFFETTR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 281 TGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSL 360
Cdd:cd18575 92 TGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 361 AESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTIS 440
Cdd:cd18575 172 ADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMS 251
|
250 260 270
....*....|....*....|....*....|....*...
gi 548923797 441 SGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18575 252 AGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
516-720 |
3.25e-28 |
|
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: 110.98 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 516 PDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPqyehrylhtqvaavrqepqlfGRSF 595
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------FASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 596 RENIAYGLvqkptmeeviaaAMVsgahsfiselpqgydtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDA 675
Cdd:cd03216 70 RDARRAGI------------AMV----------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 548923797 676 NSQLRVKQLLykspeRRFR----SVLLITHCLS-LLEQADQILFLEGGTI 720
Cdd:cd03216 116 AEVERLFKVI-----RRLRaqgvAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| FtsE |
COG2884 |
ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome ... |
502-720 |
4.89e-28 |
|
ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225438 [Multi-domain] Cd Length: 223 Bit Score: 112.69 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHR---YLH 578
Cdd:COG2884 1 MIRFENVSKAYPGGR--EALRDVSFHIPKGEFVFLTGPSGAGKSTLLKLIYGEERPTRGKILVNGHDLSRLKGReipFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 579 TQVAAVRQEPQLF-GRSFRENIAYGL----VQKPTMEEVIAAA--MVSGAHSfISELPqgydtevgeagSQLSGGQRQAV 651
Cdd:COG2884 79 RQIGVVFQDFRLLpDRTVYENVALPLrvigKPPREIRRRVSEVldLVGLKHK-ARALP-----------SQLSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPeRRFRSVLLITHCLSLLEQADQ-ILFLEGGTI 720
Cdd:COG2884 147 AIARAIVNQPAVLLADEPTGNLDPDLSWEIMRLFEEIN-RLGTTVLMATHDLELVNRMRHrVLALEDGRL 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
526-724 |
6.50e-28 |
|
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: 112.00 E-value: 6.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 526 FTLR-----PGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL----------PQYEHrylhtqVAAVRQEPQL 590
Cdd:cd03297 13 FTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinlpPQQRK------IGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 591 FGR-SFRENIAYGLVQKPTMEEVIAAAMVSGAHSfISELPQGYDtevgeagSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:cd03297 87 FPHlNVRENLAFGLKRKRNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 670 TSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAG 724
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
503-725 |
8.64e-28 |
|
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: 112.43 E-value: 8.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNhpdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRylHTQVA 582
Cdd:cd03296 3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGR-SFRENIAYGLVQKPTMEEVIAAAMVSGAHSFI-----SELPQGYDtevgeagSQLSGGQRQAVALARA 656
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 657 LIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAGT 725
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
502-725 |
8.82e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.54 E-value: 8.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDG----EPLPQYEHRYL 577
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 578 htqVAAVRQEP--QLFGRSFRENIAYG---LVQKPT--MEEVIAAAMVSGAHSFISELPQgydtevgeagsQLSGGQRQA 650
Cdd:PRK13644 79 ---VGIVFQNPetQFVGRTVEEDLAFGpenLCLPPIeiRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQC 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 651 VALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGT 725
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERI-KKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
503-730 |
2.13e-27 |
|
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: 111.24 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVA 582
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLF-GRSFRENIayGLVqkPTMEEVIAAAMVSGAHSFISEL---PQGYdteVGEAGSQLSGGQRQAVALARALI 658
Cdd:cd03295 79 YVIQQIGLFpHMTVEENI--ALV--PKLLKWPKEKIRERADELLALVgldPAEF---ADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 659 RKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITH------CLslleqADQILFLEGGTICEAGTYRQLM 730
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHdideafRL-----ADRIAIMKNGEIVQVGTPDEIL 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
502-749 |
4.25e-27 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 226641 [Multi-domain] Cd Length: 534 Bit Score: 116.22 E-value: 4.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAY-PNHPDVPVLQALTFTLRPGEVIALVGRNGSGKS-TVAALLQNLYQPT----KGQLLLDGEPL---PQY 572
Cdd:COG4172 6 LLSIRNLSVAFhQEGGTVEAVKGISFDIEAGETLALVGESGSGKSvTALSILGLLPSPAaahpSGSILFDGEDLlaaSER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 573 EHRYLH-TQVAAVRQEP-------QLFGRSFRENIA--YGLVQKPTMEEVIAAAMVSG---AHSFISELPQgydtevgea 639
Cdd:COG4172 86 QLRGVRgNKIGMIFQEPmtslnplHTIGKQLAEVLRlhRGLSRAAARARALELLELVGipePEKRLDAYPH--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 640 gsQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFR-SVLLITHCLSLLEQ-ADQILFLEG 717
Cdd:COG4172 157 --ELSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLL-KELQAELGmAILFITHDLGIVRKfADRVYVMQH 233
|
250 260 270
....*....|....*....|....*....|....*
gi 548923797 718 GTICEAGTYRQLMERRGCFWTMMQA---PGGSGVP 749
Cdd:COG4172 234 GEIVETGTTETLFAAPQHPYTRKLLaaePSGDPPP 268
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
485-742 |
5.14e-27 |
|
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: 110.77 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 485 IPRCPASGVLtslNLEGLVQFQDVSFAYPNHPDvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLL 564
Cdd:cd03288 5 ISGSSNSGLV---GLGGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 565 DGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFRENIayGLVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLS 644
Cdd:cd03288 81 DGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 645 GGQRQAVALARALIRKPRVLILDDATSALDansqLRVKQLLYKSPERRF--RSVLLITHCLSLLEQADQILFLEGGTICE 722
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASID----MATENILQKVVMTAFadRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
250 260
....*....|....*....|.
gi 548923797 723 AGTYRQLM-ERRGCFWTMMQA 742
Cdd:cd03288 235 CDTPENLLaQEDGVFASLVRT 255
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
498-725 |
5.43e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 498 NLEGLVQFQDVSFAYpnHPDVP-VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRY 576
Cdd:PRK13648 3 DKNSIIVFKNVSFQY--QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 LHTQVAAVRQEP--QLFGRSFRENIAYGL----VQKPTMEEVIAAAmvsgahsfISELPQgYDTEVGEAGSqLSGGQRQA 650
Cdd:PRK13648 81 LRKHIGIVFQNPdnQFVGSIVKYDVAFGLenhaVPYDEMHRRVSEA--------LKQVDM-LERADYEPNA-LSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 651 VALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGT 725
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
519-725 |
8.55e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.86 E-value: 8.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQL-FGRSFRE 597
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 598 NIAYGL-----VQKPTmEEVIAAAMvsgahsfiselpqgydTEVGEAG------SQLSGGQRQAVALARALIR------K 660
Cdd:PRK13548 96 VVAMGRaphglSRAED-DALVAAAL----------------AQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGT 725
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGT 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
203-478 |
1.02e-26 |
|
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: 110.60 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 203 AIPFFTGHLTDwilQDETASAFTRNITLMSILTTTSAVLEFLGdgvyNSIMGRVHSQV----QGEVFQAVLRQETEFFQQ 278
Cdd:cd18551 17 AQPLLVKNLID---ALSAGGSSGGLLALLVALFLLQAVLSALS----SYLLGRTGERVvldlRRRLWRRLLRLPVSFFDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 279 NQTGAITSRVTEDTSTLSESLSEKLSLllwyLVRGLCLL----GLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLAT 354
Cdd:cd18551 90 RRSGDLVSRVTNDTTLLRELITSGLPQ----LVTGVLTVvgavVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 355 QVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLV 434
Cdd:cd18551 166 RAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 548923797 435 TNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18551 246 ASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
502-723 |
1.05e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 108.65 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQV 581
Cdd:PRK10247 7 LLQLQNVGYLAG---DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFGRSFRENIAYG-LVQKPTMEEviaAAMVSGAHSFisELPqgyDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPwQIRNQQPDP---AIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLE--GGTICEA 723
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQphAGEMQEA 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
499-729 |
1.28e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.18 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 499 LEGLVQFQDVSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLH 578
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 579 TQVAAVRQEP--QLFGRSFRENIAYGLV-QKPTMEEVIA----AAMVSGAHSFISELPqgydtevgeagSQLSGGQRQAV 651
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnQGIPREEMIKrvdeALLAVNMLDFKTREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQL 729
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
502-729 |
2.52e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.01 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpQYEHRYL---H 578
Cdd:PRK13639 1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 579 TQVAAVRQEP--QLFGRSFRENIAYGL---------VQKPTMEEVIAAAMvsgahsfiselpQGYDTevgEAGSQLSGGQ 647
Cdd:PRK13639 78 KTVGIVFQNPddQLFAPTVEEDVAFGPlnlglskeeVEKRVKEALKAVGM------------EGFEN---KPPHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 648 RQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFrSVLLITHCLSLLE-QADQILFLEGGTICEAGTY 726
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGI-TIIISTHDVDLVPvYADKVYVMSDGKIIKEGTP 221
|
...
gi 548923797 727 RQL 729
Cdd:PRK13639 222 KEV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
502-724 |
2.75e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 226641 [Multi-domain] Cd Length: 534 Bit Score: 113.91 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHP--------DVPVLQALTFTLRPGEVIALVGRNGSGKSTVA-ALLQNLyqPTKGQLLLDGEPLPQY 572
Cdd:COG4172 276 LLEVEDLRVWFPIKGgflrrtvdHLRAVDGISLTLRRGQTLGLVGESGSGKSTLGlALLRLI--PSQGEIRFDGQDIDGL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 573 ---EHRYLHTQVAAVRQEPqlFG-----RSFRENIAYGL-VQKPTM-----EEVIAAAMVsgahsfiselpqgydtEVGE 638
Cdd:COG4172 354 srkEMRPLRRRMQVVFQDP--YGslsprMTVGQIIEEGLrVHEPKLsaaerDQRVIEALE----------------EVGL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 639 AGSQL-------SGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-AD 710
Cdd:COG4172 416 DPATRnryphefSGGQRQRIAIARALILKPELILLDEPTSALDRSVQAQVLDLLRDLQQKHGLSYLFISHDLAVVRAlCH 495
|
250
....*....|....
gi 548923797 711 QILFLEGGTICEAG 724
Cdd:COG4172 496 RVIVMRDGKIVEQG 509
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
517-729 |
3.24e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 223521 [Multi-domain] Cd Length: 316 Bit Score: 109.97 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVA-ALLQNLYQP----TKGQLLLDGEPL----PQYEHRYLHTQVAAVRQE 587
Cdd:COG0444 17 VVKAVDGVSFELKKGEILGIVGESGSGKSVLAkAIMGLLPKPnariVGGEILFDGKDLlslsEKELRKIRGKEIAMIFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 588 PQL-------FGRSFRENIAY---GLVQKPTMEEVIAAA-MV--SGAHSFISELPqgydtevgeagSQLSGGQRQAVALA 654
Cdd:COG0444 97 PMTslnpvmtIGDQIAEVLRLhgkGLSKKEAKERAIELLeLVgiPDPERRLKSYP-----------HELSGGMRQRVMIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 655 RALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:COG0444 166 MALALNPKLLIADEPTTALDVTVQAQILDLLKELQREKGTALILITHDLGVVAEiADRVAVMYAGRIVEEGPVEEI 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
502-732 |
3.74e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.81 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQY--EHRYLHT 579
Cdd:PRK09452 14 LVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 qvaaVRQEPQLFGR-SFRENIAYGLVQKPTMEEVI------AAAMVSGAHsFISELPQgydtevgeagsQLSGGQRQAVA 652
Cdd:PRK09452 91 ----VFQSYALFPHmTVFENVAFGLRMQKTPAAEItprvmeALRMVQLEE-FAQRKPH-----------QLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDAnsQLRVK-QLLYKSPERRFR-SVLLITH----CLSLleqADQILFLEGGTICEAGTY 726
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDY--KLRKQmQNELKALQRKLGiTFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTP 229
|
....*.
gi 548923797 727 RQLMER 732
Cdd:PRK09452 230 REIYEE 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
517-736 |
4.15e-26 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 115.43 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKST-VAALLQNLYQptkgqllLDGeplpqyeHRYLHTQVAAVRQEPQLFGRSF 595
Cdd:TIGR00957 650 LPPTLNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEMDK-------VEG-------HVHMKGSVAYVPQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 596 RENIAYG-LVQKPTMEEVI-AAAMVSGahsfISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSAL 673
Cdd:TIGR00957 716 RENILFGkALNEKYYQQVLeACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 674 DANsqlrVKQLLYKS---PERRF--RSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCF 736
Cdd:TIGR00957 792 DAH----VGKHIFEHvigPEGVLknKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component [Coenzyme transport and metabolism]; |
507-734 |
4.75e-26 |
|
ABC-type thiamine transport system, ATPase component [Coenzyme transport and metabolism];
Pssm-ID: 226360 [Multi-domain] Cd Length: 231 Bit Score: 107.05 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 507 DVSFAYpNHpdvpvlQALTFTLR--PGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEP---LPQYEHrylhtQV 581
Cdd:COG3840 6 DVRFSY-GH------LPMRFDLTvpAGEIVAILGPSGAGKSTLLNLIAGFETPASGEILINGVDhtaSPPAER-----PV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFGR-SFRENIAYGLvqKPTM-------EEVIAAAMVSGAHSFISELPqgydtevgeagSQLSGGQRQAVAL 653
Cdd:COG3840 74 SMLFQENNLFAHlTVAQNIGLGL--SPGLklnaeqrEKVEAAAAQVGLAGFLKRLP-----------GELSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 654 ARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAGTYRQLMER 732
Cdd:COG3840 141 ARCLVREQPILLLDEPFSALDPALRAEMLALVSQLCDERKMTLLMVTHHPEdAARIADRVVFLDNGRIAAQGSTQELLSG 220
|
..
gi 548923797 733 RG 734
Cdd:COG3840 221 KA 222
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
502-725 |
7.66e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 224050 [Multi-domain] Cd Length: 309 Bit Score: 108.54 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQV 581
Cdd:COG1125 1 MIEFENVSKRYGNKK---AVDDVNLTIEEGEFLVLIGPSGSGKTTTLKMINRLIEPTSGEILIDGEDISDLDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLF-GRSFRENIAYGLVQKPTMEEVIAAAmvsgahsfISELPQGYDTEVGEAG----SQLSGGQRQAVALARA 656
Cdd:COG1125 78 GYVIQQIGLFpHLTVAENIATVPKLLGWDKERIKKR--------ADELLDLVGLDPSEYAdrypHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 657 LIRKPRVLILDDATSALDANSQLRVkQLLYKSPERRF-RSVLLITHCLS-LLEQADQILFLEGGTICEAGT 725
Cdd:COG1125 150 LAADPPILLMDEPFGALDPITRKQL-QEEIKELQKELgKTIVFVTHDIDeALKLADRIAVMDAGEIVQYDT 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
518-731 |
9.59e-26 |
|
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: 107.34 E-value: 9.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 518 VPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHtqvaAVRQEP-----QLFG 592
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELR----ELRRKKismvfQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 593 ----RSFRENIAYGL-VQKPTMEEVIAAAMVS----GAHSFISELPqgydtevgeagSQLSGGQRQAVALARALIRKPRV 663
Cdd:cd03294 113 llphRTVLENVAFGLeVQGVPRAEREERAAEAlelvGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 664 LILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAGTYRQLME 731
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
203-478 |
1.32e-25 |
|
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: 107.51 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 203 AIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTG 282
Cdd:cd18552 17 ALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 283 AITSRVTEDTSTLSESLSEKLSLllwyLVRG----LCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQT 358
Cdd:cd18552 97 DLISRITNDVNQVQNALTSALTV----LVRDpltvIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 359 SLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGT 438
Cdd:cd18552 173 SMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 548923797 439 ISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18552 253 LTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
503-724 |
1.55e-25 |
|
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: 105.03 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNhpdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHrylht 579
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKDR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGR-SFRENIAYGLVQKPTMEEVIAAAMVSGAHSF-ISELPQGYDtevgeagSQLSGGQRQAVALARAL 657
Cdd:cd03301 73 DIAMVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELLqIEHLLDRKP-------KQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 658 IRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITH----CLSLleqADQILFLEGGTICEAG 724
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHdqveAMTM---ADRIAVMNDGQIQQIG 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
369-744 |
2.37e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 112.91 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 369 EVLSAMPTVRSFANEeceaQKFSQKLQKMN----TLHQKEALAYAVNLWITSISGMLLKV---GIL-YIGGQLVTNGTIS 440
Cdd:PLN03130 484 EVLAAMDTVKCYAWE----NSFQSKVQTVRddelSWFRKAQLLSAFNSFILNSIPVLVTVvsfGVFtLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 441 SGSLVT------FILYQIqFTSAVEALFStypsvqkaVGSSKEIFEYLGRI--PRCPASGVLTSLNLEglvqfqDVSFAY 512
Cdd:PLN03130 560 SLSLFAvlrfplFMLPNL-ITQAVNANVS--------LKRLEELLLAEERVllPNPPLEPGLPAISIK------NGYFSW 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 513 PNHPDVPVLQALTFTLRPGEVIALVGRNGSGK-STVAALLQNLYQPTKGQLLLDGeplpqyehrylhtQVAAVRQEPQLF 591
Cdd:PLN03130 625 DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG-------------TVAYVPQVSWIF 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 592 GRSFRENIAYGLVQKPTMEEviAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:PLN03130 692 NATVRDNILFGSPFDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 672 ALDANSQLRVKQLLYKSpERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQAPG 744
Cdd:PLN03130 770 ALDAHVGRQVFDKCIKD-ELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAG 841
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
503-732 |
3.75e-25 |
|
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: 104.63 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEP---LPQYEHrylht 579
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHKR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGR-SFRENIAYGLVQKPTMEEVIAAAmVSGAHSFI--SELPQGYDtevgeagSQLSGGQRQAVALARA 656
Cdd:cd03300 73 PVNTVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKER-VAEALDLVqlEGYANRKP-------SQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 657 LIRKPRVLILDDATSALDAnsQLRVK-QLLYKSPERRFR-SVLLITH----CLSLleqADQILFLEGGTICEAGTYRQLM 730
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDL--KLRKDmQLELKRLQKELGiTFVFVTHdqeeALTM---SDRIAVMNKGKIQQIGTPEEIY 219
|
..
gi 548923797 731 ER 732
Cdd:cd03300 220 EE 221
|
|
| MlaF |
COG1127 |
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF ... |
502-729 |
1.11e-24 |
|
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224052 [Multi-domain] Cd Length: 263 Bit Score: 103.83 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQ------YEHR 575
Cdd:COG1127 8 LIEVRGVTKSFGDRV---ILDGVDLDVPRGEILAILGGSGSGKSTLLRLILGLLRPDKGEILIDGEDIPQlseeelYEIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 576 ylhTQVAAVRQEPQLFGR-SFRENIAYGLVQ-----KPTMEEVIAA--AMVsgahsfiselpqGYDTEVGEA-GSQLSGG 646
Cdd:COG1127 85 ---KRMGVLFQQGALFSSlTVFENVAFPLREhtklpESLIRELVLMklELV------------GLRGAAADLyPSELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 647 QRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLykspeRRFRS-----VLLITHCL-SLLEQADQILFLEGGTI 720
Cdd:COG1127 150 MRKRVALARAIALDPELLFLDEPTSGLDPISAGVIDELI-----RELNDalgltVIMVTHDLdSLLTIADRVAVLADGKV 224
|
....*....
gi 548923797 721 CEAGTYRQL 729
Cdd:COG1127 225 IAEGTPEEL 233
|
|
| ABC_FtsE_transporter |
cd03292 |
ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic ... |
503-707 |
1.18e-24 |
|
ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic nucleotide-binding protein that binds FtsX to form a heterodimeric ATP-binding cassette (ABC)-type transporter that associates with the bacterial inner membrane. The FtsE/X transporter is thought to be involved in cell division and is important for assembly or stability of the septal ring.
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 102.49 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHR---YLHT 579
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLF-GRSFRENIAYGL--VQKPTME---EVIAAAMVSGAHSFISELPqgydtevgeagSQLSGGQRQAVAL 653
Cdd:cd03292 79 KIGVVFQDFRLLpDRNVYENVAFALevTGVPPREirkRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 548923797 654 ARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLE 707
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVD 200
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
202-478 |
1.28e-24 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 104.86 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPF--FTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRV-HSQVQG---EVFQAVLRQETEF 275
Cdd:cd18577 18 MTIVFgdLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITgERQARRirkRYLKALLRQDIAW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 276 FQQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQ 355
Cdd:cd18577 98 FDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 356 VQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVT 435
Cdd:cd18577 178 EQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVR 257
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 548923797 436 NGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18577 258 DGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
520-729 |
1.34e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.64 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVA-ALLQNLyqPTKGQLLLDGEPLPQYEHRYL---HTQVAAVRQEPQ--LFGR 593
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNssLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 -SFRENIAYGL-VQKPTM------EEVIAAAMVSGAHSfisELPQGYDTEvgeagsqLSGGQRQAVALARALIRKPRVLI 665
Cdd:PRK15134 379 lNVLQIIEEGLrVHQPTLsaaqreQQVIAVMEEVGLDP---ETRHRYPAE-------FSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 666 LDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
497-731 |
1.42e-24 |
|
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: 102.51 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 497 LNLEGLVQFqdvsfaypnHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPqyeHRY 576
Cdd:cd03224 1 LEVENLNAG---------YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT---GLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 LHTQVAA----VRQEPQLFGR-SFRENI---AYGLVQ---KPTMEEVIAAamvsgahsFiSELPQGYDTEVGeagsQLSG 645
Cdd:cd03224 69 PHERARAgigyVPEGRRIFPElTVEENLllgAYARRRakrKARLERVYEL--------F-PRLKERRKQLAG----TLSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 646 GQRQAVALARALIRKPRVLILDDATSALdanSQLRVKQLLYKSpeRRFR----SVLLITHCLSL-LEQADQILFLEGGTI 720
Cdd:cd03224 136 GEQQMLAIARALMSRPKLLLLDEPSEGL---APKIVEEIFEAI--RELRdegvTILLVEQNARFaLEIADRAYVLERGRV 210
|
250
....*....|.
gi 548923797 721 CEAGTYRQLME 731
Cdd:cd03224 211 VLEGTAAELLA 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
502-733 |
1.51e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 223562 [Multi-domain] Cd Length: 530 Bit Score: 108.49 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGeplpqyehrylHTQV 581
Cdd:COG0488 3 MITLENLSLAYGDRP---LLENVSLTLNPGERIGLVGRNGAGKSTLLKILAGELEPDSGEVTRPK-----------GLRV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLF-GRSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFISELP---------QGYDTE--VGEAG--------- 640
Cdd:COG0488 69 GYLSQEPPLDpEKTVLDYVIEGFGELRELLAELEEAYALLADPDDELLAelealleelDGWTLEarAEEALlglgfpded 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 641 ---SQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLykspeRRFR-SVLLITHCLSLLEQ-ADQILFL 715
Cdd:COG0488 149 rpvSSLSGGWRRRVALARALLEEPDLLLLDEPTNHLDLESIEWLEDYL-----KRYPgTVIVVSHDRYFLDNvATHILEL 223
|
250
....*....|....*....
gi 548923797 716 EGGTI-CEAGTYRQLMERR 733
Cdd:COG0488 224 DRGKLtPYKGNYSSYLEQK 242
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
502-732 |
2.07e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.48 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL--PQYEHRYLHT 579
Cdd:PRK09493 1 MIEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGR-SFRENIAYGLVQkptmeevIAAAMVSGAHSFISELPqgydTEVGEAG------SQLSGGQRQAVA 652
Cdd:PRK09493 78 EAGMVFQQFYLFPHlTALENVMFGPLR-------VRGASKEEAEKQARELL----AKVGLAErahhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDANSQ---LRVKQLLYKSPerrfRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQ 728
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRhevLKVMQDLAEEG----MTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
....
gi 548923797 729 LMER 732
Cdd:PRK09493 223 LIKN 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ... |
502-732 |
3.09e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 223487 [Multi-domain] Cd Length: 237 Bit Score: 102.16 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYE-HRYLHTQ 580
Cdd:COG0410 3 MLEVENLSAGYGK---IQALRGVSLEVERGEIVALLGRNGAGKTTLLKTIMGLVRPRSGRIIFDGEDITGLPpHERARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFGR-SFRENIAYGLVQKPTMEEviAAAMVSGAHSFISELPQGYDTEVGeagsQLSGGQRQAVALARALIR 659
Cdd:COG0410 80 IAYVPEGRRIFPRlTVEENLLLGAYARRDKEA--QERDLEEVYELFPRLKERRNQRAG----TLSGGEQQMLAIARALMS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 660 KPRVLILDDATSAL---------DANSQLRVKQLLyksperrfrSVLLITHCLSL-LEQADQILFLEGGTICEAGTYRQL 729
Cdd:COG0410 154 RPKLLLLDEPSEGLapkiveeifEAIKELRKEGGM---------TILLVEQNARFaLEIADRGYVLENGRIVLSGTAAEL 224
|
...
gi 548923797 730 MER 732
Cdd:COG0410 225 LAD 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
520-732 |
6.50e-24 |
|
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: 100.87 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHRylhtqVAAVRQEPQLFGR-SF 595
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRD-----ISYVPQNYALFPHmTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 596 RENIAYGLVQKPTM-----EEVIAAAMVSGahsfISELPQGYDTevgeagsQLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:cd03299 89 YKNIAYGLKKRKVDkkeieRKVLEIAEMLG----IDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 671 SALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAGTYRQLMER 732
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
520-725 |
6.59e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226929 [Multi-domain] Cd Length: 259 Bit Score: 101.66 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQL-FGRSFREN 598
Cdd:COG4559 16 LLDGVSLDLRPGEVLAILGPNGAGKSTLLKALSGELSPDSGEVTLNGVPLNSWPPEELARHRAVLPQNSSLaFPFTVQEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 IAYGLV------QKPTMEEVIAAAM----VSG-AHSFISElpqgydtevgeagsqLSGGQRQAVALARAL------IRKP 661
Cdd:COG4559 96 VQMGRIphrsgrEPEEDERIAAQALaatdLSGlAGRDYRT---------------LSGGEQQRVQLARVLaqlwppVPSG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 662 RVLILDDATSALDANSQLRVKQLLYKSPERRFrSVLLITHCLSLLEQ-ADQILFLEGGTICEAGT 725
Cdd:COG4559 161 RWLFLDEPTSALDIAHQHHTLRLARQLAREGG-AVLAVLHDLNLAAQyADRIVLLHQGRVIASGS 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
502-734 |
6.63e-24 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 226927 [Multi-domain] Cd Length: 245 Bit Score: 101.34 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPnhPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHtQV 581
Cdd:COG4555 1 MLEVTDLTKSYG--SKVQAVRDVSFEAEEGEITGLLGENGAGKTTLLRMIATLLIPDSGKVTIDGVDTVRDPSFVRR-KI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFGR-SFRENIAY-----GLVQKPT---MEEVIAAAmvsgahsfisELPQGYDTEVGEagsqLSGGQRQAVA 652
Cdd:COG4555 78 GVLFGERGLYARlTARENLKYfarlnGLSRKEIkarIAELSKRL----------QLLEYLDRRVGE----FSTGMKQKVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLME 731
Cdd:COG4555 144 IARALVHDPSILVLDEPTSGLDIRTRRKFHDFI-KQLKNEGRAVIFSSHIMQEVEAlCDRVIVLHKGEVVLEGSIEALDA 222
|
...
gi 548923797 732 RRG 734
Cdd:COG4555 223 RTV 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
518-722 |
1.24e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 226647 [Multi-domain] Cd Length: 228 Bit Score: 100.17 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 518 VPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpqyeHRYLHTQVAAVRQEPQLF-GRSFR 596
Cdd:COG4181 23 LSILKGVELVVKRGETVAIVGPSGSGKSTLLAVLAGLDDPSSGEVRLLGQPL----HKLDEDARAALRARHVGFvFQSFH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 597 --------ENIAYGLVqkptMEEVIAAAMVSGAHSFISELpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:COG4181 99 lipnltalENVALPLE----LRGESSADSRAGAKALLEAV--GLGKRLTHYPAQLSGGEQQRVALARAFAGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 548923797 669 ATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICE 722
Cdd:COG4181 173 PTGNLDRATGDKIADLLFALNRERGTTLVLVTHDPQLAARCDRQLRLRSGRLVE 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
503-729 |
1.26e-23 |
|
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: 99.89 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNhPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGeplpqyehRYLHTQVA 582
Cdd:cd03263 1 LQIRNLTKTYKK-GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--------YSIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQE----PQ---LFGR-SFRENIAY-----GLVQKPTMEEVIAAAMVSGahsfiseLPQGYDTEVGeagsQLSGGQRQ 649
Cdd:cd03263 72 AARQSlgycPQfdaLFDElTVREHLRFyarlkGLPKSEIKEEVELLLRVLG-------LTDKANKRAR----TLSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 650 AVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKspERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQ 728
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQE 218
|
.
gi 548923797 729 L 729
Cdd:cd03263 219 L 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
503-732 |
1.37e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 224042 [Multi-domain] Cd Length: 253 Bit Score: 100.69 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTvaaLLQNL--------YQPTKGQLLLDGEPLpqYEH 574
Cdd:COG1117 8 IEVRDLNLYYGDKH---ALKDINLDIPKNKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEVLLDGKNI--YDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 575 RY----LHTQVAAVRQEPQLFGRSFRENIAYGL----VQKPTMEEVIAAAMvSGAHSFiselpqgydTEV----GEAGSQ 642
Cdd:COG1117 80 KVdvveLRRRVGMVFQKPNPFPMSIYDNVAYGLrlhgIKDKELDEIVESSL-KKAALW---------DEVkdrlHKSALG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 643 LSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHclsLLEQA----DQILFLEGG 718
Cdd:COG1117 150 LSGGQQQRLCIARALAVKPEVLLMDEPTSALDPISTLKIEELITELKKK--YTIVIVTH---NMQQAarvsDYTAFFYLG 224
|
250
....*....|....
gi 548923797 719 TICEAGTYRQLMER 732
Cdd:COG1117 225 ELVEFGPTDKIFTN 238
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
501-748 |
1.45e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 107.17 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 501 GLVQFQDVSFAYpnHPDVP-VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHT 579
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGRSFRENIAYGLVQKPtmEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 660 KPRVLIL-DDATS----ALDANSQLRVKQLLYKsperrfRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQL-MERR 733
Cdd:PTZ00243 1463 KGSGFILmDEATAnidpALDRQIQATVMSAFSA------YTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQ 1536
|
250
....*....|....*
gi 548923797 734 GCFWTMMQAPGGSGV 748
Cdd:PTZ00243 1537 SIFHSMVEALGRSEA 1551
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
255-744 |
2.38e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 106.60 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 255 RVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLllWYLVRGLCLLGLMLWESLSL-----TM 329
Cdd:PLN03232 371 RLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGL--WSAPFRIIVSMVLLYQQLGVaslfgSL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 330 VTVVTLPLLFLLPEKLGRwhqvLATQVQTSLAESSQVAIEVLSAMPTVRSFANEeceaQKFSQKLQKMN----TLHQKEA 405
Cdd:PLN03232 449 ILFLLIPLQTLIVRKMRK----LTKEGLQWTDKRVGIINEILASMDTVKCYAWE----KSFESRIQGIRneelSWFRKAQ 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 406 LAYAVNLWI---TSISGMLLKVGI-LYIGGQLVTNGTISSGSLVTFILYQIqftSAVEALFSTYPSVQKAVGSSKEIFEY 481
Cdd:PLN03232 521 LLSAFNSFIlnsIPVVVTLVSFGVfVLLGGDLTPARAFTSLSLFAVLRSPL---NMLPNLLSQVVNANVSLQRIEELLLS 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 482 LGRI--------PRCPAsgvltslnleglVQFQDVSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGK-STVAALLQ 552
Cdd:PLN03232 598 EERIlaqnpplqPGAPA------------ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 553 NLYQPTKGQLLLDGeplpqyehrylhtQVAAVRQEPQLFGRSFRENIAYGLVQKPtmEEVIAAAMVSGAHSFISELPqGY 632
Cdd:PLN03232 666 ELSHAETSSVVIRG-------------SVAYVPQVSWIFNATVRENILFGSDFES--ERYWRAIDVTALQHDLDLLP-GR 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 633 D-TEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSpERRFRSVLLITHCLSLLEQADQ 711
Cdd:PLN03232 730 DlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKD-ELKGKTRVLVTNQLHFLPLMDR 808
|
490 500 510
....*....|....*....|....*....|...
gi 548923797 712 ILFLEGGTICEAGTYRQLMERRGCFWTMMQAPG 744
Cdd:PLN03232 809 IILVSEGMIKEEGTFAELSKSGSLFKKLMENAG 841
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
502-732 |
3.96e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQV 581
Cdd:PRK13652 3 LIETRDLCYSYSG--SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEP--QLFGRSFRENIAYGLVQKPTMEEVIAAAMVSGAHSF-ISELPQgydtevgEAGSQLSGGQRQAVALARALI 658
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLgLEELRD-------RVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 659 RKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLL-EQADQILFLEGGTICEAGTYRQLMER 732
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
503-720 |
5.35e-23 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226164 [Multi-domain] Cd Length: 258 Bit Score: 98.86 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHRYLHT 579
Cdd:COG3638 4 IEVKNLSKTYPG--GHQALKDVNLEINQGEMVAIIGPSGAGKSTLLRSLNGLVDPTSGEILFNGVqitKLKGKELRKLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGRSF-RENIAYGLV-QKPTMeeviaaamvsgaHSFISELP-----QGYD--TEVG------EAGSQLS 644
Cdd:COG3638 82 DIGMIFQQFNLVPRLSvLENVLLGRLgYTSTW------------RSLFGLFSkedkaQALDalERVGildkayQRASTLS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSL-LEQADQILFLEGGTI 720
Cdd:COG3638 150 GGQQQRVAIARALVQQPKIILADEPVASLDPESAKKVMDILKDINQEDGITVIVNLHQVDLaKKYADRIIGLKAGRI 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms]; |
524-730 |
5.97e-23 |
|
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];
Pssm-ID: 226637 [Multi-domain] Cd Length: 267 Bit Score: 99.13 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 524 LTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQlfgRSF--RENIAY 601
Cdd:COG4167 32 VSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEILINDHPLHFGDYSFRSKRIRMIFQDPN---TSLnpRLRIGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 602 gLVQKP-----TMEEVIAAAMVSGAHSFISELPQGYDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDAN 676
Cdd:COG4167 109 -ILDFPlrlntDLEPEQRRKQIFETLRMVGLLPDHANYYP----HMLAPGQKQRVALARALILRPKIIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 677 SQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLM 730
Cdd:COG4167 184 MRSQLINLMLELQEKQGISYIYVTQHIGMIKHiSDQVLVMHEGEVVERGSTADVL 238
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
508-718 |
6.72e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226905 [Multi-domain] Cd Length: 259 Bit Score: 98.67 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 508 VSFAYPNHPdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL--PQYEHrylhtqvAAVR 585
Cdd:COG4525 9 LSLSYEGKP-RSALEDVSLTIASGELVVVLGPSGCGKTTLLNLIAGFVTPSRGSIQLNGRRIegPGAER-------GVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 586 QEPQLFG-RSFRENIAYGL----VQKPTMEEvIAAAMVSgahsfiselpqgydtEVGEAGS------QLSGGQRQAVALA 654
Cdd:COG4525 81 QNEALLPwLNVIDNVAFGLqlrgIEKAQRRE-IAHQMLA---------------LVGLEGAehkyiwQLSGGMRQRVGIA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 655 RALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCL-SLLEQADQILFLEGG 718
Cdd:COG4525 145 RALAVEPQLLLLDEPFGALDALTREQMQELLLDLWQETGKQVLLITHDIeEALFLATRLVVLSPG 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
525-712 |
1.18e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.35 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 525 TFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPlpqyehrylHTQVAAVR-------QEPQLFGR-SFR 596
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---------HTTTPPSRrpvsmlfQENNLFSHlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 597 ENIAYGL--------VQKPTMEEvIAAAMvsGAHSFISELPqgydtevgeagSQLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:PRK10771 90 QNIGLGLnpglklnaAQREKLHA-IARQM--GIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 548923797 669 ATSALDANSQLRVKQLLYKSPERRFRSVLLITHClslLEQADQI 712
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVCQERQLTLLMVSHS---LEDAARI 196
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ... |
520-728 |
1.21e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 223488 [Multi-domain] Cd Length: 250 Bit Score: 97.64 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYE-HRYLHTQVAAVRQEPQLF-GRSFRE 597
Cdd:COG0411 19 AVNDVSLEVRPGEIVGLIGPNGAGKTTLFNLITGFYKPSSGTVIFRGRDITGLPpHRIARLGIARTFQITRLFpGLTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 598 NIAYGLVQKPT-------------MEEVIAAAMvsgahsFISE---LPQGYDTEVGEagsqLSGGQRQAVALARALIRKP 661
Cdd:COG0411 99 NVAVGAHARLGlsgllgrprarkeEREARERAR------ELLEfvgLGELADRPAGN----LSYGQQRRLEIARALATQP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 662 RVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQ 728
Cdd:COG0411 169 KLLLLDEPAAGLNPEETEELAELIRELRDRGGVTILLIEHDMKLVMGlADRIVVLNYGEVIAEGTPEE 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
519-720 |
1.55e-22 |
|
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: 95.70 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALL--QNLYQPTKGQLLLDGEPLPQYEHRYlhtQVAAVRQEPQLFGR-SF 595
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRK---IIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 596 RENIAYglvqkptmeeviAAAMvsgahsfiselpqgydtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDA 675
Cdd:cd03213 100 RETLMF------------AAKL-----------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 548923797 676 NSQLRVKQLLykspeRRF----RSVLLITHCLS--LLEQADQILFLEGGTI 720
Cdd:cd03213 145 SSALQVMSLL-----RRLadtgRTIICSIHQPSseIFELFDKLLLLSQGRV 190
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
504-731 |
1.64e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.94 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 504 QFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAA 583
Cdd:PRK10575 13 ALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 584 VRQE-PQLFGRSFRENIA------------YGLVQKPTMEEVIAaamVSGAHSFISELPqgydtevgeagSQLSGGQRQA 650
Cdd:PRK10575 90 LPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAIS---LVGLKPLAHRLV-----------DSLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 651 VALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
..
gi 548923797 730 ME 731
Cdd:PRK10575 236 MR 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
520-729 |
2.00e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQL-----LLDG-EPLPQYEH--RYLHTQVAAVRQEPQLF 591
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 592 -GRSFRENIAYG--LVQKPTMEEVIAAAmvsgahsfiSELPqgydTEVGEAGSQ------LSGGQRQAVALARALIRKPR 662
Cdd:PRK11264 98 pHRTVLENIIEGpvIVKGEPKEEATARA---------RELL----AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 663 VLILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCLSLL-EQADQILFLEGGTICEAGTYRQL 729
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
520-720 |
2.11e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.06 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpqyehrylhtqvAAVRQEPQLFGRSFR--- 596
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL------------AEAREDTRLMFQDARllp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 597 -----ENIAYGLVQ--KPTMEEVIAAAmvsgahsfiselpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:PRK11247 95 wkkviDNVGLGLKGqwRDAALQALAAV--------------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 548923797 670 TSALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTI 720
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
504-725 |
2.64e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224057 [Multi-domain] Cd Length: 249 Bit Score: 96.53 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 504 QFQDVSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEhrylhtqvAA 583
Cdd:COG1134 26 RLKGLAKGGRKVAEFWALKDISFEIYKGERVGIIGHNGAGKSTLLKLIAGIYKPTSGKVKVTGKVAPLIE--------LG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 584 VRQEPQLFGrsfRENI-AYGLVqkPTMEEVIAAAMVSGAHSFiselpqgydTEVGEAGSQ----LSGGQRQAVALARALI 658
Cdd:COG1134 98 AGFDPELTG---RENIyLRGLI--LGLTRKEIDEKVDEIIEF---------AELGDFIDQpvktYSSGMYARLAFSVATH 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 659 RKPRVLILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCLSLLEQA-DQILFLEGGTICEAGT 725
Cdd:COG1134 164 VEPDILLLDEVLAVGDAAFQEKCLERLNELVEKN-KTIVLVSHDLGAIKQYcDRAIWLEHGQIRMEGS 230
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
202-450 |
3.16e-22 |
|
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: 97.48 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWI-LQDETASAFTRNITLMSILTTTSAVLEFLGdgvYNSIMG---RVHSQVQGEVFQAVLRQETEFFQ 277
Cdd:cd18541 16 LLIPRIIGRAIDALtAGTLTASQLLRYALLILLLALLIGIFRFLW---RYLIFGasrRIEYDLRNDLFAHLLTLSPSFYQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 278 QNQTGAITSRVTEDTSTLSESLSEKLSlllwYLVRGLCL----LGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLA 353
Cdd:cd18541 93 KNRTGDLMARATNDLNAVRMALGPGIL----YLVDALFLgvlvLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 354 TQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFsqklQKMNTLHQKEALAYA-VNLWITSISGMLLKVG---ILYI 429
Cdd:cd18541 169 RKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERF----DKLNEEYVEKNLRLArVDALFFPLIGLLIGLSfliVLWY 244
|
250 260
....*....|....*....|.
gi 548923797 430 GGQLVTNGTISSGSLVTFILY 450
Cdd:cd18541 245 GGRLVIRGTITLGDLVAFNSY 265
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
520-731 |
9.73e-22 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 226961 [Multi-domain] Cd Length: 256 Bit Score: 95.18 E-value: 9.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE-------------PLPQYEHRYLHTQVAAVRQ 586
Cdd:COG4598 21 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSAGSIRVNGEeirlkrdkdgqlkPADKRQLQRLRTRLGMVFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 587 EPQLFG-RSFRENIAYGLVQ--KPTMEEVIAAAMVSGAHSFISELPQGYDtevgeagSQLSGGQRQAVALARALIRKPRV 663
Cdd:COG4598 101 HFNLWShMTVLENVIEAPVHvlGVSKAEAIERAEKYLAKVGIAEKADAYP-------AHLSGGQQQRVAIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 664 LILDDATSALD---ANSQLRVKQLLykspERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLME 731
Cdd:COG4598 174 MLFDEPTSALDpelVGEVLKVMQDL----AEEGRTMVVVTHEMGFARDvSSHVIFLHQGKIEEEGPPEQVFG 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
518-725 |
1.18e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 95.24 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 518 VPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEP--------- 588
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 589 --QLFGRSFRENIAyglVQKPTMEEVIAAA--MVSGAHSFISELPQgydtevgeagsQLSGGQRQAVALARALIRKPRVL 664
Cdd:PRK15112 106 isQILDFPLRLNTD---LEPEQREKQIIETlrQVGLLPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 665 ILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGT 725
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
516-719 |
1.22e-21 |
|
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: 93.93 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 516 PDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLL----LDGEPLPQYEHRYLHTQVAAVRQEPQLF 591
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 592 GRSFRENIAYGL-VQKPTMEEVIAAAMVsgaHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:cd03290 92 NATVEENITFGSpFNKQRYKAVTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 548923797 671 SALDAN-SQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGT 719
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
503-725 |
1.29e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.79 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNH-PDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLhtqV 581
Cdd:PRK11153 2 IELKNISKVFPQGgRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKEL---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLF-------GRSFRENIAYGLVQKPTMEEVIAA------AMVSgahsfISELPQGYDtevgeagSQLSGGQR 648
Cdd:PRK11153 79 KARRQIGMIFqhfnllsSRTVFDNVALPLELAGTPKAEIKArvtellELVG-----LSDKADRYP-------AQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 649 QAVALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFR-SVLLITHCLSLLEQ-ADQILFLEGGTICEAGT 725
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELL-KDINRELGlTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
503-724 |
2.12e-21 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 92.94 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAY---PNHPDVPVLQaltftlrpGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEP---LPQYEHry 576
Cdd:cd03298 1 VRLDKIRFSYgeqPMHFDLTFAQ--------GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvtaAPPADR-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 lhtQVAAVRQEPQLFGR-SFRENIAYGL--------VQKPTMEeVIAAAMvsGAHSFISELPQgydtevgeagsQLSGGQ 647
Cdd:cd03298 71 ---PVSMLFQENNLFAHlTVEQNVGLGLspglkltaEDRQAIE-VALARV--GLAGLEKRLPG-----------ELSGGE 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 648 RQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAG 724
Cdd:cd03298 134 RQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
507-724 |
2.29e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 507 DVSFAypnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQ 586
Cdd:PRK09536 10 SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 587 EPQL-FGRSFRENIAYGLV--------QKPTMEEVIAAAMVSGahsfiselpqGYDTEVGEAGSQLSGGQRQAVALARAL 657
Cdd:PRK09536 85 DTSLsFEFDVRQVVEMGRTphrsrfdtWTETDRAAVERAMERT----------GVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 658 IRKPRVLILDDATSALDANSQLRVKQLLykspeRRF----RSVLLITHCLSLLEQ-ADQILFLEGGTICEAG 724
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELV-----RRLvddgKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
502-725 |
2.96e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.80 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAY-PNHPDVP-VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQL----LLDGEPLPQYEHR 575
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 576 YLHTQVAAVRQEP--QLFGRSFRENIAYGL----VQKPTMEEVIAAA--MVSGAHSFISELPqgydtevgeagSQLSGGQ 647
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPqnfgIPKEKAEKIAAEKleMVGLADEFWEKSP-----------FELSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 648 RQAVALARALIRKPRVLILDDATSALDANSQLRVKQlLYKSPERRFRSVLLITHCL-SLLEQADQILFLEGGTICEAGT 725
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGT 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
524-701 |
4.22e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.06 E-value: 4.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 524 LTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL---PQYEHrylhtQVAAVRQEPQLFGR-SFRENI 599
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvPPYQR-----PINMMFQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 600 AYGLVQKPTMEEVIAA---AMVSGAH--SFISELPQgydtevgeagsQLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:PRK11607 113 AFGLKQDKLPKAEIASrvnEMLGLVHmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190
....*....|....*....|....*....|.
gi 548923797 675 AN----SQLRVKQLLykspERRFRSVLLITH 701
Cdd:PRK11607 182 KKlrdrMQLEVVDIL----ERVGVTCVMVTH 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
503-735 |
4.71e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.28 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQyEHRYLHTQVA 582
Cdd:PRK13536 42 IDLAGVSKSYG---DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQ----EPQ--------LFGRSFReniayglVQKPTMEEVIAAAMVsgahsfISELPQGYDTEVgeagSQLSGGQRQA 650
Cdd:PRK13536 118 VVPQfdnlDLEftvrenllVFGRYFG-------MSTREIEAVIPSLLE------FARLESKADARV----SDLSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 651 VALARALIRKPRVLILDDATSALDANSQL----RVKQLLykspeRRFRSVLLITHCLSLLEQ-ADQILFLEGG-TICEAG 724
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHliweRLRSLL-----ARGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGR 255
|
250
....*....|.
gi 548923797 725 TYRQLMERRGC 735
Cdd:PRK13536 256 PHALIDEHIGC 266
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
525-725 |
4.84e-21 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 226643 [Multi-domain] Cd Length: 386 Bit Score: 95.91 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 525 TFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHRYLHT-QVAAVRQEPQLF-GRSFRENI 599
Cdd:COG4175 48 SLDVEEGEIFVIMGLSGSGKSTLVRLLNRLIEPTRGEILVDGKdiaKLSAAELRELRRkKISMVFQSFALLpHRTVLENV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 600 AYGL----VQKPTMEEVIAAAM-VSGAHSFISELPqgydtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:COG4175 128 AFGLevqgVPKAEREERALEALeLVGLEGYADKYP-----------NELSGGMQQRVGLARALANDPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 548923797 675 ANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAGT 725
Cdd:COG4175 197 PLIRTEMQDELLELQAKLKKTIVFITHDLDeALRIGDRIAIMKDGEIVQVGT 248
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
520-728 |
7.22e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.79 E-value: 7.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpqyEHRYLHTQ-VAAVRQEPQLFGR-SFRE 597
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRdICMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 598 NIAYGL-VQKPTMEEVI-----AAAMVSGAhsfiselpqGY-DTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:PRK11432 98 NVGYGLkMLGVPKEERKqrvkeALELVDLA---------GFeDRYV----DQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 671 SALDANsqLR------VKQLlykspERRFR-SVLLITHclsllEQA------DQILFLEGGTICEAGT----YRQ 728
Cdd:PRK11432 165 SNLDAN--LRrsmrekIREL-----QQQFNiTSLYVTH-----DQSeafavsDTVIVMNKGKIMQIGSpqelYRQ 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
505-729 |
7.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.55 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 505 FQDVSFAY-PNHP-------DVPVlqaltfTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLdGEPLPQYEHRY 576
Cdd:PRK13634 5 FQKVEHRYqYKTPferralyDVNV------SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 -----LHTQVAAVRQ--EPQLFGRSFRENIAYGLVQ--------KPTMEEVIAaaMVSGAHSFISELPqgYDtevgeags 641
Cdd:PRK13634 78 kklkpLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgvseedaKQKAREMIE--LVGLPEELLARSP--FE-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 642 qLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTI 720
Cdd:PRK13634 146 -LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTV 224
|
....*....
gi 548923797 721 CEAGTYRQL 729
Cdd:PRK13634 225 FLQGTPREI 233
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
203-478 |
8.34e-21 |
|
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: 93.62 E-value: 8.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 203 AIPFFTGHLTDWILQDETA------SAFTRNITLMSILTTTSAVLEFLgdgvYNSIMGRVhsqVQGEVFQavLRQETE-- 274
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGgggvdfSGLLRILLLLLGLYLLSALFSYL----QNRLMARV---SQRTVYD--LRKDLFek 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 275 -------FFQQNQTGAITSRVTEDTSTLSESLSEKLSLllwyLVRGLCL----LGLMLWESLSLTMVTVVTLPLLFLLPE 343
Cdd:cd18547 88 lqrlplsYFDTHSHGDIMSRVTNDVDNISQALSQSLTQ----LISSILTivgtLIMMLYISPLLTLIVLVTVPLSLLVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 344 KLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQK-EALAYAVNLWITSISGMLL 422
Cdd:cd18547 164 FIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKaQFYSGLLMPIMNFINNLGY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 423 kVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18547 244 -VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
503-719 |
8.60e-21 |
|
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: 89.04 E-value: 8.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGeplpqyehrylhtqva 582
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 avrqepqlfgrsfRENIAYglvqkptmeeviaaamvsgahsFiselpqgydtevgeagSQLSGGQRQAVALARALIRKPR 662
Cdd:cd03221 62 -------------TVKIGY----------------------F----------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 663 VLILDDATSALDANSQLRVKQLLYKSPerrfRSVLLITHCLSLLEQ-ADQILFLEGGT 719
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ... |
509-734 |
8.89e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 226952 [Multi-domain] Cd Length: 325 Bit Score: 93.99 E-value: 8.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 509 SFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGeplpqyehrylhtqvaavrQEP 588
Cdd:COG4586 28 HFFHRKERSIEAVQDISFEIPKGEIVGFLGANGAGKSTTLKMLTGLLLPTSGKVRVNG-------------------KDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 589 QLFGRSFRENIAYGLVQKPTMEEVIAA----------AMVSGAH-----SFISELpQGYDTEVGEAGSQLSGGQRQAVAL 653
Cdd:COG4586 89 FRRREEYLRSIGLVMGQKLQLWWDLPAldslevlkliYEIPDDEfaerlDFLTEI-LDLEGFLKWPVRKLSLGQRMRAEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 654 ARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLMER 732
Cdd:COG4586 168 AAALLHPPKVLFLDEPTVGLDVNAQANIREFLKEYNEERQATVLLTTHIFDDIATlCDRVLLIDQGQLVFDGTLAQLQEQ 247
|
..
gi 548923797 733 RG 734
Cdd:COG4586 248 FG 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
502-729 |
9.87e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 9.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL----PQYEHR-- 575
Cdd:PRK15439 11 LLCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPAKAHQlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 576 -YLhtqvaaVRQEPQLF-GRSFRENIAYGLVQKPTMEEVIAAamvsgahsFISELPQGYDTEVgEAGSqLSGGQRQAVAL 653
Cdd:PRK15439 88 iYL------VPQEPLLFpNLSVKENILFGLPKRQASMQKMKQ--------LLAALGCQLDLDS-SAGS-LEVADRQIVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 654 ARALIRKPRVLILDDATSALDA--NSQL--RVKQLLYKSperrfRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQ 728
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPaeTERLfsRIRELLAQG-----VGIVFISHKLPEIRQlADRISVMRDGTIALSGKTAD 226
|
.
gi 548923797 729 L 729
Cdd:PRK15439 227 L 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
507-734 |
1.01e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 507 DVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpQYEHR---YLHTQVAA 583
Cdd:PRK13638 6 DLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 584 VRQEP--QLFGRSFRENIAYGLVQKPTMEEVIaAAMVSGAHSFISelPQGYDTEVGEAgsqLSGGQRQAVALARALIRKP 661
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEI-TRRVDEALTLVD--AQHFRHQPIQC---LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 662 RVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLL-EQADQILFLEGGTICEAG------TYRQLMERRG 734
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAII-RRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
239-487 |
1.40e-20 |
|
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: 93.29 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 239 AVLEFLGDGVYNSIMGRVhSQ-----VQGEVFQAVLRQETEFFQQ--NQTGAITSRVTEDTStlseslseklslllwyLV 311
Cdd:cd18578 62 AIVAGIAYFLQGYLFGIA-GErltrrLRKLAFRAILRQDIAWFDDpeNSTGALTSRLSTDAS----------------DV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 312 RGLC--LLGLMLwESLS---------------LTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAM 374
Cdd:cd18578 125 RGLVgdRLGLIL-QAIVtlvagliiafvygwkLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 375 PTVRSFANEECEAQKFSQKLQKMNTLHQKEA--------LAYAVNLWITSIsgmllkvgILYIGGQLVTNGTISSGS-LV 445
Cdd:cd18578 204 RTVASLTLEDYFLEKYEEALEEPLKKGLRRAlisglgfgLSQSLTFFAYAL--------AFWYGGRLVANGEYTFEQfFI 275
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 548923797 446 TFILyqIQFTS-AVEALFSTYPSVQKAVGSSKEIFEYLGRIPR 487
Cdd:cd18578 276 VFMA--LIFGAqSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
510-724 |
1.43e-20 |
|
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: 91.05 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 510 FAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEhrylhtqvAAVRQEPQ 589
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG--------LGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 590 LFGrsfRENI-----AYGLVQK--PTMEEVIAAamvsgahsfISELPQGYDTEVGEagsqLSGGQRQAVALARALIRKPR 662
Cdd:cd03220 99 LTG---RENIylngrLLGLSRKeiDEKIDEIIE---------FSELGDFIDLPVKT----YSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 663 VLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAG 724
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRL-RELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
202-450 |
1.45e-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: 92.49 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGdGVYNSIMG-RVHSQVQGEVFQAVLRQETEFFQQNQ 280
Cdd:cd18542 16 LLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQ-GYLAEKASqKVAYDLRNDLYDHLQRLSFSFHDKAR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 281 TGAITSRVTEDTSTLSESLSEKLSLllwyLVRGLCLLG----LMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQV 356
Cdd:cd18542 95 TGDLMSRCTSDVDTIRRFLAFGLVE----LVRAVLLFIgaliIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 357 QTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTN 436
Cdd:cd18542 171 REQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVIN 250
|
250
....*....|....
gi 548923797 437 GTISSGSLVTFILY 450
Cdd:cd18542 251 GEITLGELVAFISY 264
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
520-729 |
1.61e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRylHTQVAAVRQEPQLFGR-SFREN 598
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 IAYGLVQKPTMEEVIAAA----------MVSGAHsfiseLPQGYDtevgeagSQLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:PRK10851 95 IAFGLTVLPRRERPNAAAikakvtqlleMVQLAH-----LADRYP-------AQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 669 ATSALDAN--SQLR--VKQLlykSPERRFRSVlLITHCL-SLLEQADQILFLEGGTICEAGTYRQL 729
Cdd:PRK10851 163 PFGALDAQvrKELRrwLRQL---HEELKFTSV-FVTHDQeEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
201-478 |
2.19e-20 |
|
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: 92.19 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 201 EMAIPFFTGHLTDWILQDETASAFTRN-ITLMSILTTTSAVLEFLGdGVYNSIMGRVHSQV----QGEVFQAVLRQETEF 275
Cdd:cd18563 15 GLVPPYLTKILIDDVLIQLGPGGNTSLlLLLVLGLAGAYVLSALLG-ILRGRLLARLGERItadlRRDLYEHLQRLSLSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 276 FQQNQTGAITSRVTEDTSTlseslseklslLLWYLVRGLC-----------LLGLMLWESLSLTMVTVVTLPLLFLLPEK 344
Cdd:cd18563 94 FDKRQTGSLMSRVTSDTDR-----------LQDFLSDGLPdfltnilmiigIGVVLFSLNWKLALLVLIPVPLVVWGSYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 345 LGR-----WHQV--LATQVQTSLAESsqvaievLSAMPTVRSFANEECEAQKFSQKLQKM----NTLHQKEALAYAVNLW 413
Cdd:cd18563 163 FWKkirrlFHRQwrRWSRLNSVLNDT-------LPGIRVVKAFGQEKREIKRFDEANQELldanIRAEKLWATFFPLLTF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 414 ITSISGMLlkvgILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18563 236 LTSLGTLI----VWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
503-735 |
2.67e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRyLHTQVA 582
Cdd:PRK13537 8 IDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 ------------AVRQEPQLFGRSFreniayglvqkpTMEEVIAAAMVSGAHSFiSELPQGYDTEVGEagsqLSGGQRQA 650
Cdd:PRK13537 84 vvpqfdnldpdfTVRENLLVFGRYF------------GLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 651 VALARALIRKPRVLILDDATSALDANSQL----RVKQLLykspeRRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGT 725
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHlmweRLRSLL-----ARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGA 221
|
250
....*....|.
gi 548923797 726 YRQLMERR-GC 735
Cdd:PRK13537 222 PHALIESEiGC 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
503-720 |
3.27e-20 |
|
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: 89.56 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGeVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEhRYLHTQVA 582
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQE----PQLFGRSFRENIA--YGLVQKPTMEEVIAA-AMVSgahsfiseLPQGYDTEVGeagsQLSGGQRQAVALAR 655
Cdd:cd03264 76 YLPQEfgvyPNFTVREFLDYIAwlKGIPSKEVKARVDEVlELVN--------LGDRAKKKIG----SLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 656 ALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHCLSLLEQ-ADQILFLEGGTI 720
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESlCNQVAVLNKGKL 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
520-705 |
3.39e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.26 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHrylhTQVAAVRQEPQLFGRSFR--- 596
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS----AAKAELRNQKLGFIYQFHhll 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 597 ------ENIAYGLV---QKPTMEEVIAAAMVSGAhsfiselpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILD 667
Cdd:PRK11629 100 pdftalENVAMPLLigkKKPAEINSRALEMLAAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 548923797 668 DATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSL 705
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
506-730 |
3.84e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.46 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 506 QDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVR 585
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 586 QE---PQlfGRSFRENIAYG----------LVQKPtmEEVIAAAMvsgAHSFISELPQGYDTEvgeagsqLSGGQRQAVA 652
Cdd:PRK11231 83 QHhltPE--GITVRELVAYGrspwlslwgrLSAED--NARVNQAM---EQTRINHLADRRLTD-------LSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDANSQLRVKQLLYKSpERRFRSVLLITHCLSlleQA----DQILFLEGGTICEAGTYRQ 728
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGTPEE 224
|
..
gi 548923797 729 LM 730
Cdd:PRK11231 225 VM 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
503-724 |
5.64e-20 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 88.81 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGePLPQYEHRYLhTQVA 582
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEAL-RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFG-RSFRENIayglvqkptmeeVIAAAMVSGAHSFISELPQgydtEVGEAGS------QLSGGQRQAVALAR 655
Cdd:cd03268 76 ALIEAPGFYPnLTARENL------------RLLARLLGIRKKRIDEVLD----VVGLKDSakkkvkGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 656 ALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCLSLLEQ-ADQILFLEGGTICEAG 724
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
520-730 |
5.72e-20 |
|
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: 89.42 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQY-EHRYLHTQVAAVRQEPQLFGR-SFRE 597
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpPHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 598 NiayglvqkptmeeVIAAAMVSGAHSFISELPQGYDTEVGE------------------AGSqLSGGQRQAVALARALIR 659
Cdd:cd03219 95 N-------------VMVAAQARTGSGLLLARARREEREAREraeellervgladladrpAGE-LSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 660 KPRVLILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCLSLLEQ-ADQILFLEGGT-ICEaGTYRQLM 730
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSlADRVTVLDQGRvIAE-GTPDEVR 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
500-729 |
5.78e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.53 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 500 EGLVQFQDVSFAYPNHPD---VPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRY 576
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 -LHTQVAAVRQEP--QLFGRSFRENIAYG-----LVQKPTMEEVIAAAMVSGAHSFISELPQgydtevgeagsQLSGGQR 648
Cdd:PRK13633 82 dIRNKAGMVFQNPdnQIVATIVEEDVAFGpenlgIPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 649 QAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQ 728
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
.
gi 548923797 729 L 729
Cdd:PRK13633 231 I 231
|
|
| YufO |
COG3845 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
516-718 |
1.01e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 226364 [Multi-domain] Cd Length: 501 Bit Score: 92.99 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 516 PDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPqyehryLHTQVAAVR-------QEP 588
Cdd:COG3845 15 PGVVANDDVSLSVKKGEIHALLGENGAGKSTLMKILFGLYQPDSGEIRVDGKEVR------IKSPRDAIRlgigmvhQHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 589 QLFGR-SFRENIAYGLvqkptmeEVIAAAMV--SGAHSFISELPQGY------DTEVGEagsqLSGGQRQAVALARALIR 659
Cdd:COG3845 89 MLVPTlTVAENIILGL-------EPSKGGLIdrRQARARIKELSERYglpvdpDAKVAD----LSVGEQQRVEILKALYR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 660 KPRVLILDDATSALdanSQLRVKQLLYKSpeRRFR----SVLLITHCLS-LLEQADQILFLEGG 718
Cdd:COG3845 158 GARLLILDEPTAVL---TPQEADELFEIL--RRLAaegkTIIFITHKLKeVMAIADRVTVLRRG 216
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
505-732 |
1.66e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 92.73 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 505 FQDVSFAYPNHP-DV-PVlqalTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLP---QYEHRYLht 579
Cdd:PRK10522 325 LRNVTFAYQDNGfSVgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeqPEDYRKL-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 qVAAVRQEPQLFGRsfreniayglVQKPTMEEVIAAAmvsgAHSFISELPQGYDTEVGE---AGSQLSGGQRQAVALARA 656
Cdd:PRK10522 399 -FSAVFTDFHLFDQ----------LLGPEGKPANPAL----VEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 657 LIRKPRVLILDDAtsALDANSQLR---VKQLLyksPERRF--RSVLLITHCLSLLEQADQILFLEGGTICE-AGTYRQLM 730
Cdd:PRK10522 464 LAEERDILLLDEW--AADQDPHFRrefYQVLL---PLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAA 538
|
..
gi 548923797 731 ER 732
Cdd:PRK10522 539 SR 540
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
499-732 |
2.08e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.02 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 499 LEGLVQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLH 578
Cdd:PRK13647 1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 579 TQVAAVRQEP--QLFGRSFRENIAYG-----LVQKPTMEEVIAAAMVSGAHSFISELPQgydtevgeagsQLSGGQRQAV 651
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSpERRFRSVLLITHCLSL-LEQADQILFLEGGTICEAGTYRQLM 730
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKSLLT 226
|
..
gi 548923797 731 ER 732
Cdd:PRK13647 227 DE 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
521-732 |
2.12e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.02 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQAL---TFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHrylhTQVAAVRQEPQL-FGRSF- 595
Cdd:PRK11308 28 VKALdgvSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP----EAQKLLRQKIQIvFQNPYg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 596 ----RENIAYglvqkpTMEE--VI-----AAAMVSGAHSFISEL---PQGYDtevgEAGSQLSGGQRQAVALARALIRKP 661
Cdd:PRK11308 104 slnpRKKVGQ------ILEEplLIntslsAAERREKALAMMAKVglrPEHYD----RYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 662 RVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLMER 732
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
502-734 |
2.40e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 223562 [Multi-domain] Cd Length: 530 Bit Score: 92.31 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLdGEPLPQYehrYLHTQV 581
Cdd:COG0488 321 VLEFENVSKGYDG--GRLLLKDLSFRIDRGDRIAIVGPNGAGKSTLLKLLAGELGPLSGTVKV-GETVKIG---YFDQHR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFgrsfrENIAYGLVQKPTME--EVIAAAMVSGAHsfiselpqgydteVGEAGSQLSGGQRQAVALARALIR 659
Cdd:COG0488 395 DELDPDKTVL-----EELSEGFPDGDEQEvrAYLGRFGFTGED-------------QEKPVGVLSGGEKARLLLAKLLLQ 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 660 KPRVLILDDATSALDANSQLRVKQLLykspeRRFR-SVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLMERRG 734
Cdd:COG0488 457 PPNLLLLDEPTNHLDIESLEALEEAL-----LDFEgTVLLVSHDRYFLDRvATRIWLVEDKVEEFEGGYEDYLEQKK 528
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
502-708 |
3.01e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPDVpvLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHR---YLH 578
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 579 TQVAAVRQEPQLF-GRSFRENIAYGLVQKPTMEEVIaAAMVSGAHSFISELPQGYDTEVgeagsQLSGGQRQAVALARAL 657
Cdd:PRK10908 79 RQIGMIFQDHHLLmDRTVYDNVAIPLIIAGASGDDI-RRRVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 548923797 658 IRKPRVLILDDATSALD---ANSQLRvkqlLYKSPERRFRSVLLITHCLSLLEQ 708
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDdalSEGILR----LFEEFNRVGVTVLMATHDIGLISR 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
503-729 |
3.09e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYpnHPDVP----VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDG----EPLPQYEH 574
Cdd:PRK13646 3 IRFDNVSYTY--QKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 575 RYLHTQVAAVRQ--EPQLFGRSFRENIAYGLVQ-KPTMEEVIAAAmvsgaHSFISELpqGYDTEVGEAGS-QLSGGQRQA 650
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNfKMNLDEVKNYA-----HRLLMDL--GFSRDVMSQSPfQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 651 VALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
503-717 |
3.47e-19 |
|
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: 85.28 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLlldgeplpqyeHRYLHTQVA 582
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGRSFRENIAYglvqkPTMEEviaaamvsgahsfiselpqgydtevgeagsqLSGGQRQAVALARALIRKPR 662
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 663 VLILDDATSALDANSQLRVKQLLykspERRFRSVLLITHCLSLLEQADQILFLEG 717
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
502-733 |
4.40e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.98 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPDVpvLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpQYEHR---YLH 578
Cdd:PRK13636 5 ILKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 579 TQVAAVRQEP--QLFGRSFRENIAYGLVQ----KPTMEEVIAAAMVSGAHSFISELPQGYdtevgeagsqLSGGQRQAVA 652
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGAVNlklpEDEVRKRVDNALKRTGIEHLKDKPTHC----------LSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLE-QADQILFLEGGTICEAGTYRQLME 731
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
..
gi 548923797 732 RR 733
Cdd:PRK13636 232 EK 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
508-701 |
4.63e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.45 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 508 VSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL--PQYEHrylhtqvAAVR 585
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAER-------GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 586 QEPQLFG-RSFRENIAYGL----VQKPTMEEViAAAMVSgahsfiselpqgydtEVGEAGS------QLSGGQRQAVALA 654
Cdd:PRK11248 77 QNEGLLPwRNVQDNVAFGLqlagVEKMQRLEI-AHQMLK---------------KVGLEGAekryiwQLSGGQRQRVGIA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 548923797 655 RALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITH 701
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
503-724 |
7.27e-19 |
|
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: 85.80 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpQYEHrylhtqva 582
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 avrqepqlfgrsfRENIAY-----GLVQKPT-MEEVIAAAMVSG-----AHSFISELPQGYDTEVGEAGS--QLSGGQRQ 649
Cdd:cd03269 69 -------------RNRIGYlpeerGLYPKMKvIDQLVYLAQLKGlkkeeARRRIDEWLERLELSEYANKRveELSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 650 AVALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAG 724
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI-RELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
251-449 |
8.05e-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: 87.60 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 251 SIMG-RVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEDT----STLSESlseklslllwyLVRGL--------CLL 317
Cdd:cd18574 67 SVVGeRVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQC-----------VSQGLrsvtqtvgCVV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 318 GLMLWeSLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKM 397
Cdd:cd18574 136 SLYLI-SPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKA 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 398 NTLHQKEALAYAV-----NLwitSISGMLLkvGILYIGGQLVTNGTISSGSLVTFIL 449
Cdd:cd18574 215 AKLNEKLGLGIGIfqglsNL---ALNGIVL--GVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
509-720 |
9.79e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 85.85 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 509 SFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEpLPQYEHRYLHTQVAAVR-QE 587
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 588 PQLF-----GRSFRENIA-YGLVQ---KPTMEEvIAAAMvsgahsfisELPQGYDTEVgeagSQLSGGQRQAVALARALI 658
Cdd:cd03267 104 TQLWwdlpvIDSFYLLAAiYDLPParfKKRLDE-LSELL---------DLEELLDTPV----RQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 659 RKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTI 720
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ... |
519-720 |
1.08e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 224026 [Multi-domain] Cd Length: 263 Bit Score: 86.61 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQY--EHRYLHtqVAAVRQEPQLfgrsfr 596
Cdd:COG1101 20 RALNGLSLEIAEGDFVTVIGSNGAGKSTLLNAIAGDLKPTSGQILIDGVDVTKKsvAKRANL--LARVFQDPLA------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 597 eniayGLVQKPTMEEVIAAAMVSGAH-------------SF---ISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:COG1101 92 -----GTAPELTIEENLALAESRGKKrglssalnerrrsSFrerLARLGLGLENRLSDRIGLLSGGQRQALSLLMATLHP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHClslLEQA----DQILFLEGGTI 720
Cdd:COG1101 167 PKILLLDEHTAALDPKTAEFVMELTAKIVEEHKLTTLMVTHN---MEDAldygNRLIMLHSGKI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
500-720 |
1.28e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.98 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 500 EGLVQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTvaaLLQNLYQ--------PTKGQLLLDGEPL-- 569
Cdd:PRK14239 3 EPILQVSDLSVYYN---KKKALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 570 PQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYGL-----VQKPTMEEVIAAAMVsGAHSFISELPQGYDTEVGeagsqLS 644
Cdd:PRK14239 77 PRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLrlkgiKDKQVLDEAVEKSLK-GASIWDEVKDRLHDSALG-----LS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITHClslLEQADQI-----LFLEGGT 719
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRS---MQQASRIsdrtgFFLDGDL 225
|
.
gi 548923797 720 I 720
Cdd:PRK14239 226 I 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
503-729 |
1.60e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLqNLYQPTKGQLLLDG--EPLPQ--YEHRY-- 576
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGrvEFFNQniYERRVnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 --LHTQVAAVRQEPQLFGRSFRENIAYGLV-----QKPTMEEVIAAAMVSgahsfiSELPQGYDTEVGEAGSQLSGGQRQ 649
Cdd:PRK14258 84 nrLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 650 AVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEG-----GTICEA 723
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEF 237
|
....*.
gi 548923797 724 GTYRQL 729
Cdd:PRK14258 238 GLTKKI 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
516-724 |
4.00e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.75 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 516 PDVPVLQALTFTLRPGEVIALVGRNGSGKS-TVAALLQNL---YQPTKGQLLLDGEPLPQYEHRYLHtqVAAVRQEPQLF 591
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRGRK--IATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 592 GRSFRENIAYGL-----VQKPTMEEVIAAAM----------VSGAHSFiselpqgydtevgeagsQLSGGQRQAVALARA 656
Cdd:PRK10418 92 FNPLHTMHTHARetclaLGKPADDATLTAALeavglenaarVLKLYPF-----------------EMSGGMLQRMMIALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 657 LIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAG 724
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
521-715 |
4.17e-18 |
|
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: 84.05 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDG----EPLPQYehrylhtqvAAVRQEPQLFG-RSF 595
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitEPGPDR---------MVVFQNYSLLPwLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 596 RENIAYGL------VQKPTMEEVIAaamvsgAHSFISELPQGYDTEVGeagsQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:TIGR01184 72 RENIALAVdrvlpdLSKSERRAIVE------EHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 548923797 670 TSALDANSQLRVKQLLYKSPERRFRSVLLITHclslleQADQILFL 715
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHRVTVLMVTH------DVDEALLL 181
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
502-720 |
4.36e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.63 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPN-HPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLhtq 580
Cdd:PRK10535 4 LLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 vAAVRQEPqlFGRSFREniaYGLVQKPTMEE-VIAAAMVSG---------AHSFISELpqGYDTEVGEAGSQLSGGQRQA 650
Cdd:PRK10535 81 -AQLRREH--FGFIFQR---YHLLSHLTAAQnVEVPAVYAGlerkqrllrAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 651 VALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQADQILFLEGGTI 720
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
525-730 |
4.78e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.01 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 525 TFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLH----TQVAAVRQEPQLFGR-SFRENI 599
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 600 AYGL-VQKPTMEEVIAAAMVSGAHSFISELPQGYDTEvgeagsqLSGGQRQAVALARALIRKPRVLILDDATSALDANSQ 678
Cdd:PRK10070 128 AFGMeLAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 548923797 679 LRVKQLLYKSPERRFRSVLLITHCL-SLLEQADQILFLEGGTICEAGTYRQLM 730
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
503-718 |
5.36e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.88 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhPDVPV----LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL-PQYEHRYL 577
Cdd:PRK13641 3 IKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 578 ---HTQVAAVRQ--EPQLFGRSFRENIAYGLVQKPTMEEVIAAAmvsgAHSFISELpqGYDTEVGEAGS-QLSGGQRQAV 651
Cdd:PRK13641 81 kklRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK----ALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQlLYKSPERRFRSVLLITHCL-SLLEQADQILFLEGG 718
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHG 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion ... |
502-701 |
6.04e-18 |
|
ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 224044 [Multi-domain] Cd Length: 257 Bit Score: 84.29 E-value: 6.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGeplpqyeHRYLHTQV 581
Cdd:COG1119 31 LIELKNVSVRRNGKK---ILGDLSWQVNPGEHWAIVGPNGAGKTTLLSLLTGEHPPSSGDVTLLG-------RRFGKGET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 aavrqepqlfGRSFRENIayGLV-----QKPTMEEVIAAAMVSGAHSFISELPQGYD----------TEVGEAGS----- 641
Cdd:COG1119 101 ----------IFELRKRI--GLVsselhERFRVRETVRDVVLSGFFASIGIYQEDLTaedlaaaqwlLELLGAKHladrp 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 642 --QLSGGQRQAVALARALIRKPRVLILDDATSALD--ANSQLrVKQLLYKSPERRFRSVLLITH 701
Cdd:COG1119 169 fgSLSQGEQRRVLIARALVKDPELLILDEPAQGLDliAREQL-LNRLEELAASPGAPALLFVTH 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
516-675 |
8.83e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 8.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 516 PDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPlpqyeHRY------LHTQVAAVRQEPQ 589
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaaLAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 590 LFGR-SFRENIAYGlvQKPTMEEVI-AAAMVSGAHSFISELpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILD 667
Cdd:PRK11288 90 LVPEmTVAENLYLG--QLPHKGGIVnRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
....*...
gi 548923797 668 DATSALDA 675
Cdd:PRK11288 166 EPTSSLSA 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
502-724 |
1.08e-17 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 82.42 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAY-PNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpqyehrylHTQ 580
Cdd:cd03266 1 MITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV--------VKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFGRSF--------RENIAY-----GLvqKPTmeeviaaamvsGAHSFISELPQGYDTE--VGEAGSQLSG 645
Cdd:cd03266 73 PAEARRRLGFVSDSTglydrltaRENLEYfaglyGL--KGD-----------ELTARLEELADRLGMEelLDRRVGGFST 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 646 GQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLykspeRRFRS----VLLITHCLSLLEQ-ADQILFLEGGTI 720
Cdd:cd03266 140 GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI-----RQLRAlgkcILFSTHIMQEVERlCDRVVVLHRGRV 214
|
....
gi 548923797 721 CEAG 724
Cdd:cd03266 215 VYEG 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
526-725 |
1.25e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.12 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 526 FTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEP---LPQYehrylhtQVA---AVR--QEPQLFG----- 592
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPGH-------QIArmgVVRtfQHVRLFRemtvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 593 --------RSFRENIAYGLVQKPTMEEVIAAAMVSGAHSfiseLPQGYDTEVG--EAGSqLSGGQRQAVALARALIRKPR 662
Cdd:PRK11300 99 enllvaqhQQLKTGLFSGLLKTPAFRRAESEALDRAATW----LERVGLLEHAnrQAGN-LAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 663 VLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSL-LEQADQILFLEGGTICEAGT 725
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLvMGISDRIYVVNQGTPLANGT 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
503-725 |
1.67e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.89 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRylHTQVA 582
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGR-SFRENIAYGL----VQKPTMEEVIA-AAMVSGAHSFISELPQgydtevgeagsQLSGGQRQAVALARA 656
Cdd:PRK11650 80 MVFQNYALYPHmSVRENMAYGLkirgMPKAEIEERVAeAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 657 LIRKPRVLILDDATSALDAnsQLRV------KQLlykspERRFRSV-LLITHclsllEQ------ADQILFLEGGTICEA 723
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDA--KLRVqmrleiQRL-----HRRLKTTsLYVTH-----DQveamtlADRVVVMNGGVAEQI 216
|
..
gi 548923797 724 GT 725
Cdd:PRK11650 217 GT 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
521-728 |
1.85e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.56 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL--PQYEHRYLHTQVAAVRQEP--QLFGRSFR 596
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 597 ENIAYGLVQKPTMEEVI------AAAMVsgahsfiselpqGYDTEVGEAGS--QLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIenrvkrAMNIV------------GLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 669 ATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAGTYRQ 728
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
520-722 |
1.90e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.13 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpqyeHRYLHTQVAAVRQepQLFGRSFReni 599
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL----HQMDEEARAKLRA--KHVGFVFQ--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 600 AYGLVqkPTM---EEVIAAAMVSGAHSFISE------LPQ-GYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:PRK10584 96 SFMLI--PTLnalENVELPALLRGESSRQSRngakalLEQlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 548923797 670 TSALDANSQLRVKQLLYkSPERRFRSVL-LITHCLSLLEQADQILFLEGGTICE 722
Cdd:PRK10584 174 TGNLDRQTGDKIADLLF-SLNREHGTTLiLVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-732 |
2.18e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.27 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQ-----PTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQ-L 590
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 591 FGRSFRENIAYGLV------QKPTMEEVIAAAMVSgahsfiSELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVL 664
Cdd:PRK14247 95 PNLSIFENVALGLKlnrlvkSKKELQERVRWALEK------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 665 ILDDATSALDANSQLRVKQLLYKSpeRRFRSVLLITHclsLLEQA----DQILFLEGGTICEAGTYRQLMER 732
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTH---FPQQAarisDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
503-732 |
2.43e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.87 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAY-PNHP-DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQY----EHRY 576
Cdd:PRK13649 3 INLQNVSYTYqAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 LHTQVAAVRQ--EPQLFGRSFRENIAYGlvqkP-----TMEEVIAAAMVSGAHSFISElpqgydtEVGEAGS-QLSGGQR 648
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG----PqnfgvSQEEAEALAREKLALVGISE-------SLFEKNPfELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 649 QAVALARALIRKPRVLILDDATSALDANSQlrvKQL--LYKSPERRFRSVLLITHCL-SLLEQADQILFLEGGTICEAGT 725
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGR---KELmtLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGK 228
|
....*..
gi 548923797 726 YRQLMER 732
Cdd:PRK13649 229 PKDIFQD 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
520-724 |
3.50e-17 |
|
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: 81.16 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKST----VAALLQNLYQpTKGQLLLDGEPLpqyeHRYLHTQ-VAAVRQEPQLF-GR 593
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPR----KPDQFQKcVAYVRQDDILLpGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIAYGLV---QKPTMEEVIAAAMVsgahsfISELPQGYDTEVGEAG-SQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:cd03234 97 TVRETLTYTAIlrlPRKSSDAIRKKRVE------DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 670 TSALDANSQLRVKQLLyKSPERRFRSVLLITHC--LSLLEQADQILFLEGGTICEAG 724
Cdd:cd03234 171 TSGLDSFTALNLVSTL-SQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
493-720 |
4.49e-17 |
|
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: 79.78 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 493 VLTSLNLEGLVQFQDVSFaypnhpdvpvlqaltfTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPqy 572
Cdd:cd03215 4 VLEVRGLSVKGAVRDVSF----------------EVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 573 ehrylhtqvaavrqepqlfGRSFRENIAYGLvqkptmeeviaaAMVSG---AHSFISELPqgydteVGE---AGSQLSGG 646
Cdd:cd03215 66 -------------------RRSPRDAIRAGI------------AYVPEdrkREGLVLDLS------VAEniaLSSLLSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 647 QRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLykspeRRFR----SVLLITHCLS-LLEQADQILFLEGGTI 720
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI-----RELAdagkAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
520-742 |
4.76e-17 |
|
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: 86.12 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTV-AALLQNLyqPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGRSFREN 598
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLlSALLRLL--STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 I-AYglvQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANS 677
Cdd:TIGR01271 1312 LdPY---EQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 678 QlrvkQLLYKSPERRFR--SVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCFWTMMQA 742
Cdd:TIGR01271 1389 L----QIIRKTLKQSFSncTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSA 1451
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
519-701 |
5.01e-17 |
|
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: 80.10 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQyehrylhtqvaaVRQEPQlfgrsfrEN 598
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE------------QRDEPH-------EN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 IAY-----GLVQKPTMEEVIA--AAMVSGAHSFISELPqgydTEVGEAG------SQLSGGQRQAVALARALIRKPRVLI 665
Cdd:TIGR01189 75 ILYlghlpGLKPELSALENLHfwAAIHGGAQRTIEDAL----AAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 548923797 666 LDDATSALDANSQLRVKQLLYKSPERRfRSVLLITH 701
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARG-GIVLLTTH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
503-685 |
6.11e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 226646 [Multi-domain] Cd Length: 604 Bit Score: 84.67 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLlldgeplpqyeHRYLHTQVA 582
Cdd:COG4178 393 ITLENLSLRTPDGQ--TLLSELNFEVRPGERLLITGESGAGKTSLLRALAGLWPWGSGRI-----------SMPADSALL 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQEPQLFGRSFRENIAYGLVQKPTMEEVIAAAMVS-GAHSFISELpqgydTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:COG4178 460 FLPQRPYLPQGTLREALCYPNAAPDFSDAELVAVLHKvGLGDLAERL-----DEEDRWDRVLSGGEQQRLAFARLLLHKP 534
|
170 180
....*....|....*....|....
gi 548923797 662 RVLILDDATSALDANSQLRVKQLL 685
Cdd:COG4178 535 KWVFLDEATSALDEETEDRLYQLL 558
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-729 |
6.13e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQ------PTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQL 590
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 591 FGR-SFRENIAYGLVQKPTMEEVIAAAMVSGAHSFISELPQGYDtEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:PRK14246 102 FPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 670 TSALDANSQLRVKQLLykSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:PRK14246 181 TSMIDIVNSQAIEKLI--TELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
202-471 |
6.86e-17 |
|
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: 81.72 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLgDGVYNSIMG-RVHSQVQGEVFQAVLRQETEFFQQNQ 280
Cdd:cd18570 19 IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYI-RSYLLLKLSqKLDIRLILGYFKHLLKLPLSFFETRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 281 TGAITSRVTeDTSTlseslseklslllwylVRG----------------LCLLGLMLWESLSLTMVTVVTLPLLFLL--- 341
Cdd:cd18570 98 TGEIISRFN-DANK----------------IREaissttislfldllmvIISGIILFFYNWKLFLITLLIIPLYILIill 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 342 ---P-EKLGRWHQVLATQVQTSLaessqvaIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSI 417
Cdd:cd18570 161 fnkPfKKKNREVMESNAELNSYL-------IESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 548923797 418 SGMLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKA 471
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEA 287
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
516-675 |
7.49e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 516 PDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYqPT---KGQLLLDGEPLPQYEHRylHTQ---VAAVRQE-- 587
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIR--DTEragIAIIHQEla 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 588 --PQLfgrSFRENIAYGlvQKPTMEEVIA-AAMVSGAHSFISELpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVL 664
Cdd:PRK13549 93 lvKEL---SVLENIFLG--NEITPGGIMDyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170
....*....|.
gi 548923797 665 ILDDATSALDA 675
Cdd:PRK13549 166 ILDEPTASLTE 176
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
484-731 |
8.76e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.22 E-value: 8.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 484 RIPRCPASGVLTSLNLEGLVQFQDVSFAYPNhpdvpvlqaltftlrpGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLL 563
Cdd:PTZ00243 655 RSAKTPKMKTDDFFELEPKVLLRDVSVSVPR----------------GKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 564 LDgeplpqyehrylhTQVAAVRQEPQLFGRSFRENIaygLVQKPTMEEVIAAAM-VSGAHSFISELPQGYDTEVGEAGSQ 642
Cdd:PTZ00243 719 AE-------------RSIAYVPQQAWIMNATVRGNI---LFFDEEDAARLADAVrVSQLEADLAQLGGGLETEIGEKGVN 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 643 LSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSpERRFRSVLLITHCLSLLEQADQILFLEGGTICE 722
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLG-ALAGKTRVLATHQVHVVPRADYVVALGDGRVEF 861
|
....*....
gi 548923797 723 AGTYRQLME 731
Cdd:PTZ00243 862 SGSSADFMR 870
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
520-736 |
9.21e-17 |
|
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: 81.05 E-value: 9.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTV-AALLQNLYqpTKGQLLLDGE-----PLPQYEHRYlhtqvAAVRQEPQLFGR 593
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGVswnsvPLQKWRKAF-----GVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENI-AYGlvqKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:cd03289 92 TFRKNLdPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 673 LDANSQlrvkQLLYKSPERRFR--SVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCF 736
Cdd:cd03289 169 LDPITY----QVIRKTLKQAFAdcTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
517-685 |
2.32e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHR----YLHTQVAAvrqEPQLfg 592
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAM---KPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 593 rSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFISELPQGYdtevgeagsqLSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:PRK13539 89 -TVAENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|...
gi 548923797 673 LDANSQLRVKQLL 685
Cdd:PRK13539 158 LDAAAVALFAELI 170
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
203-478 |
4.41e-16 |
|
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: 79.50 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 203 AIPFFTGHLTDWILQDE-TASAFTRNITLMSILTTTSAVLEFLgDGVYNSIMG-RVHSQVQGEVFQAVLRQETEFFQQNQ 280
Cdd:cd18778 17 VPPWLIRELVDLVTIGSkSLGLLLGLALLLLGAYLLRALLNFL-RIYLNHVAEqKVVADLRSDLYDKLQRLSLRYFDDRQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 281 TGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSL 360
Cdd:cd18778 96 TGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 361 AESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKmntlhQKEALAYAVNLW---------ITSIsGMLLkvgILYIGG 431
Cdd:cd18778 176 GELNALLQDNLSGIREIQAFGREEEEAKRFEALSRR-----YRKAQLRAMKLWaifhplmefLTSL-GTVL---VLGFGG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 548923797 432 QLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18778 247 RLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
525-729 |
4.61e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.14 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 525 TFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRylhtQVAAVRQEPQLFgrsFRENIAyGLV 604
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDD----EWRAVRSDIQMI---FQDPLA-SLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 605 QKPTMEEVIAAAMvsgaHSFISELPQGydtEVGE--------AG----------SQLSGGQRQAVALARALIRKPRVLIL 666
Cdd:PRK15079 113 PRMTIGEIIAEPL----RTYHPKLSRQ---EVKDrvkammlkVGllpnlinrypHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 667 DDATSALDANSQLRVKQLLyKSPERRFR-SVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLL-QQLQREMGlSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
517-729 |
5.07e-16 |
|
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: 77.80 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEplpqyehrylhtqvaAVRQEPqlfgRSFR 596
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH---------------DVVREP----REVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 597 ENIAYgLVQKPTMEEVIAA-------AMVSG-----AHSFISELPQGYdtEVGEAGSQL----SGGQRQAVALARALIRK 660
Cdd:cd03265 73 RRIGI-VFQDLSVDDELTGwenlyihARLYGvpgaeRRERIDELLDFV--GLLEAADRLvktySGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
263-474 |
5.59e-16 |
|
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: 79.06 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 263 EVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLP 342
Cdd:cd18550 77 QLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 343 EKLGRWHQVLATQVQTSLAESSQVAIEVLSA--MPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAvnlWITSISGM 420
Cdd:cd18550 157 RRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGR---WFFAALGL 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 421 LLKVG---ILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGS 474
Cdd:cd18550 234 FTAIGpalVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLAL 290
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
201-450 |
7.88e-16 |
|
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: 78.65 E-value: 7.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 201 EMAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDgVYNSIMG-RVHSQVQGEVFQAVLRQETEFFQQN 279
Cdd:cd18549 18 DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVT-YWGHVMGaRIETDMRRDLFEHLQKLSFSFFDNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 280 QTGAITSRVT--------------EDtstlseslseklslllwYLVRGLCLLG---LMLWESLSLTMVTVVTLPLLFLLP 342
Cdd:cd18549 97 KTGQLMSRITndlfdiselahhgpED-----------------LFISIITIIGsfiILLTINVPLTLIVFALLPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 343 EKL-GRWHQVLaTQVQTSLAE-SSQVAiEVLSAMPTVRSFANEECEAQKFSQKlqkmNTLHQK-EALAYAVNLWITSISG 419
Cdd:cd18549 160 IYFnKKMKKAF-RRVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEG----NDRFLEsKKKAYKAMAYFFSGMN 233
|
250 260 270
....*....|....*....|....*....|....
gi 548923797 420 M---LLKVGILYIGGQLVTNGTISSGSLVTFILY 450
Cdd:cd18549 234 FftnLLNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
526-732 |
8.23e-16 |
|
ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226628 [Multi-domain] Cd Length: 352 Bit Score: 79.69 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 526 FTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHR-YLHTQ---VAAVRQEPQLFGR-SFRENIA 600
Cdd:COG4148 19 FTLPARGITALFGPSGSGKTSLINMIAGLTRPDEGRIELNGRVLVDAEKGiFLPPEkrrIGYVFQDARLFPHyTVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 601 YGL--VQKPTMEEVIAaamVSGAHSFISELPqgydtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQ 678
Cdd:COG4148 99 YGMwkSMRAQFDQLVA---LLGIEHLLDRYP-----------GTLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 679 LRVKQLLykspERRFRS----VLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLMER 732
Cdd:COG4148 165 REILPYL----ERLRDEinipILYVSHSLDEVLRlADRVVVLENGKVKASGPLEEVWGS 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
502-729 |
8.76e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.90 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPDV-PVLQALTFTLRPGEVIALVGRNGSGKSTVA-ALLQNLYQP----TKGQLLLDGEPLPQYEHR 575
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 576 YLH----TQVAAVRQEP------------QLFgrsfrENIAY--GLVQKPTMEEVIAAAMVSG---AHSFISELPQgydt 634
Cdd:PRK15134 85 TLRgvrgNKIAMIFQEPmvslnplhtlekQLY-----EVLSLhrGMRREAARGEILNCLDRVGirqAAKRLTDYPH---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 635 evgeagsQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQIL 713
Cdd:PRK15134 156 -------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVA 228
|
250
....*....|....*.
gi 548923797 714 FLEGGTICEAGTYRQL 729
Cdd:PRK15134 229 VMQNGRCVEQNRAATL 244
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
520-730 |
1.10e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.94 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKST-VAALLQNLYQP-------TKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQ-L 590
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTlLKALAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 591 FGRSFRENIAYGlvQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARAL---------IRKP 661
Cdd:PRK13547 96 FAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 662 RVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLM 730
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVL 243
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
520-701 |
1.12e-15 |
|
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: 76.38 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYlHTQVAAVRQEPQLFGR-SFREN 598
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 IAY--GLVQKPTMEEVIAAAMVSGahsfISELPQGydtevgeagsQLSGGQRQAVALARALIRKPRVLILDDATSALDAN 676
Cdd:cd03231 94 LRFwhADHSDEQVEEALARVGLNG----FEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....*
gi 548923797 677 SQLRVKQLLYKSPERRfRSVLLITH 701
Cdd:cd03231 160 GVARFAEAMAGHCARG-GMVVLTTH 183
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
493-729 |
1.13e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.00 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 493 VLTSLNLEGLVQFQD--VSFAYPNHpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQP---TKGQLLLDGE 567
Cdd:PRK09473 3 PLAQQQADALLDVKDlrVTFSTPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 568 P---LPQYE-HRYLHTQVAAVRQEPQlfgRSFReniAYGLVQKPTMEEVIAAAMVSGAHSFISELPQGYDTEVGEAGSQL 643
Cdd:PRK09473 82 EilnLPEKElNKLRAEQISMIFQDPM---TSLN---PYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 644 -------SGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFR-SVLLITHCLSLLEQ-ADQILF 714
Cdd:PRK09473 156 kmyphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLL-NELKREFNtAIIMITHDLGVVAGiCDKVLV 234
|
250
....*....|....*
gi 548923797 715 LEGGTICEAGTYRQL 729
Cdd:PRK09473 235 MYAGRTMEYGNARDV 249
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
519-736 |
1.30e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 77.97 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGeplpqyehrylhtQVAAVRQEPQLFGRSFREN 598
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 IAYGLV-QKPTMEEVIAAAMVsgaHSFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANS 677
Cdd:cd03291 118 IIFGVSyDEYRYKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 678 QLRV-KQLLYKSPERRFRsvLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCF 736
Cdd:cd03291 195 EKEIfESCVCKLMANKTR--ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
519-731 |
1.38e-15 |
|
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: 76.81 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYE-HRYLHTQVAAVRQEPQLFGR-SFR 596
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 597 ENIAYGL-VQKPTMEEVIaaamvSGAHSFISELpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDA 675
Cdd:cd03218 94 ENILAVLeIRGLSKKERE-----EKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 676 NSQLRVKQLLYKSPERRFrSVLLITHCLS-LLEQADQILFLEGGTICEAGTYRQLME 731
Cdd:cd03218 167 IAVQDIQKIIKILKDRGI-GVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
495-701 |
1.40e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.51 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 495 TSLNLEGLVQFQDVSFAYPNHPDVpvlQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQ--PT---KGQLLLDGEPL 569
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLAV---KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 570 --PQYEHRYLHTQVAAVRQEPQLFGRSFRENIAYG---LVQKPTMEEVIAAAMVSGAhsfiseLPQGYDTEVGEAGSQLS 644
Cdd:PRK14243 80 yaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELVERSLRQAA------LWDEVKDKLKQSGLSLS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERrfRSVLLITH 701
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTH 208
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
201-475 |
1.53e-15 |
|
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: 77.81 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 201 EMAIPFFTGHLTDWIL--QDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQ 278
Cdd:cd18544 15 ELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 279 NQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLlpekLGRWHQVLAT---- 354
Cdd:cd18544 95 TPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL----ATYLFRKKSRkayr 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 355 QVQTSLAE-SSQVAiEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVnLW--ITSISGMLLkVGILYIGG 431
Cdd:cd18544 171 EVREKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFAL-FRplVELLSSLAL-ALVLWYGG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 548923797 432 QLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSS 475
Cdd:cd18544 248 GQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASA 291
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
489-732 |
1.56e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 489 PASGVLTSLNLEglVQFQDvsfaypNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEP 568
Cdd:PRK10261 8 DARDVLAVENLN--IAFMQ------EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 569 LPQYEHRYLH------TQVAAVR--------QEPQL-------FGRSFRENIAygLVQKPTMEEVIAAAM-------VSG 620
Cdd:PRK10261 80 LRRRSRQVIElseqsaAQMRHVRgadmamifQEPMTslnpvftVGEQIAESIR--LHQGASREEAMVEAKrmldqvrIPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 621 AHSFISELPQgydtevgeagsQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLIT 700
Cdd:PRK10261 158 AQTILSRYPH-----------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFIT 226
|
250 260 270
....*....|....*....|....*....|...
gi 548923797 701 HCLSLL-EQADQILFLEGGTICEAGTYRQLMER 732
Cdd:PRK10261 227 HDMGVVaEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
519-736 |
2.42e-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: 80.34 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGeplpqyehrylhtQVAAVRQEPQLFGRSFREN 598
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 IAYGLvqkpTMEEVIAAAMVSGAH--SFISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDAN 676
Cdd:TIGR01271 507 IIFGL----SYDEYRYTSVIKACQleEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 677 SQLRV-KQLLYKSPERRFRsvLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMERRGCF 736
Cdd:TIGR01271 583 TEKEIfESCLCKLMSNKTR--ILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDF 641
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
502-725 |
2.64e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLH--- 578
Cdd:PRK09544 4 LVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYldt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 579 TQVAAVRQEPQLFGRSFRENIAyglvqkPTMEEVIAAAMVsgahsfisELPQgydtevgeagSQLSGGQRQAVALARALI 658
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTKKEDIL------PALKRVQAGHLI--------DAPM----------QKLSGGETQRVLLARALL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 659 RKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSL-LEQADQILFLEgGTICEAGT 725
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLvMAKTDEVLCLN-HHICCSGT 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
519-685 |
2.91e-15 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 226617 [Multi-domain] Cd Length: 209 Bit Score: 75.02 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYE---HRYLH--TQVAAVRQEpqlfgR 593
Cdd:COG4133 16 TLFSDLSFTLNAGEALQITGPNGAGKTTLLRILAGLLRPDAGEVYWQGEPIQNVResyHQALLylGHQPGIKTE-----L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIA-----YGLVQKPTMEEVIAAAmvsGAHSFIselpqgyDTEVGeagsQLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:COG4133 91 TALENLHfwqrfHGSGNAATIWEALAQV---GLAGLE-------DLPVG----QLSAGQQRRVALARLWLSPAPLWILDE 156
|
170
....*....|....*..
gi 548923797 669 ATSALDANSQLRVKQLL 685
Cdd:COG4133 157 PFTALDKEGVALLTALM 173
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
503-722 |
3.84e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 226968 [Multi-domain] Cd Length: 546 Bit Score: 79.08 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL-PQYEHRYlHTQV 581
Cdd:COG4615 323 LELRNVRFAYQ--DNAFHVGPINLTIKRGELVFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVsAEQLEDY-RKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFGRSFreniayGLVQKPTMEEVIAaamvsgahsFISELPQGYDTEVGE---AGSQLSGGQRQAVALARALI 658
Cdd:COG4615 400 SAVFSDYHLFDQLL------GPEGKASPQLIEK---------WLQRLELAHKTSLNDgrfSNLKLSTGQKKRLALLLALL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 659 RKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICE 722
Cdd:COG4615 465 EERDILVLDEWAADQDPAFRREFYQVLLPLLKEQGKTIFAISHDDHYFIHADRLLEMRNGQLSE 528
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
238-471 |
5.06e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 76.40 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 238 SAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLL 317
Cdd:cd18564 67 RGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGML 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 318 GLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKlqkm 397
Cdd:cd18564 147 GVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARE---- 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 398 NTLHQKEAL-AYAVNLWITSISGMLLKVG---ILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKA 471
Cdd:cd18564 223 NRKSLRAGLrAARLQALLSPVVDVLVAVGtalVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKA 300
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
517-724 |
1.12e-14 |
|
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: 73.33 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNL--YQPTKGQLLLDGE---PLPQYEhrylhtqvaavRQEPQLF 591
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditDLPPEE-----------RARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 592 grsfrenIAYglvQKPtmeevIAAAMVSGAHsFISELPQGydtevgeagsqLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:cd03217 81 -------LAF---QYP-----PEIPGVKNAD-FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 672 ALDANSqLR-----VKQLLYKSperrfRSVLLITHCLSLLE--QADQILFLEGGTICEAG 724
Cdd:cd03217 134 GLDIDA-LRlvaevINKLREEG-----KSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSG 187
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
503-725 |
1.40e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.90 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHpdvpvlQAL---TFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEplpQYEHRYlHT 579
Cdd:PRK11124 3 IQLNGINCFYGAH------QALfdiTLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSK-TP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGRSFREniaYGLVQKPT-MEEVIAAAM-VSG-----AHSFISELPQGYD-TEVGEAGS-QLSGGQRQA 650
Cdd:PRK11124 73 SDKAIRELRRNVGMVFQQ---YNLWPHLTvQQNLIEAPCrVLGlskdqALARAEKLLERLRlKPYADRFPlHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 651 VALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVlLITHCLSLLEQ-ADQILFLEGGTICEAGT 725
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQV-IVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
520-730 |
1.48e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL-------------PQYEHRYLHTQVAAVRQ 586
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 587 EPQLFGR-SFRENIAYGLVQKPTMEEVIAA--AMVSGAHSFISELPQGydtevgEAGSQLSGGQRQAVALARALIRKPRV 663
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQVLGLSKQEARerAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 664 LILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLM 730
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEG-KTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
518-724 |
1.52e-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: 76.76 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 518 VPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQL-LLDGEPL-----PQYEHRYLHTQ-VAAVRQEPQL 590
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWvdmtkPGPDGRGRAKRyIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 591 FG-RSFRENI--AYGLvQKP----TMEEVIAAAMV----SGAHSFISELPqgydtevgeagSQLSGGQRQAVALARALIR 659
Cdd:TIGR03269 377 YPhRTVLDNLteAIGL-ELPdelaRMKAVITLKMVgfdeEKAEEILDKYP-----------DELSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 660 KPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAG 724
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDfVLDVCDRAALMRDGKIVKIG 510
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
522-701 |
1.72e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 522 QALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpqyehrylhtqvAAVRQEpqlfgrsFRENIAY 601
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI------------RRQRDE-------YHQDLLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 602 -----GLvqKP--TMEEVIAaamvsgahsFISELPQGYDTE--------VGEAG------SQLSGGQRQAVALARALIRK 660
Cdd:PRK13538 79 lghqpGI--KTelTALENLR---------FYQRLHGPGDDEalwealaqVGLAGfedvpvRQLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 548923797 661 PRVLILDDATSALDANSqlrVKQLlykspERRFRS-------VLLITH 701
Cdd:PRK13538 148 APLWILDEPFTAIDKQG---VARL-----EALLAQhaeqggmVILTTH 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
498-719 |
1.83e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 498 NLEGLVQFQDVSFAYPNhpdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRyL 577
Cdd:PRK09700 1 MATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 578 HTQ--VAAVRQEPQLFGR-SFRENIAYG-----------LVQKPTMEEViAAAMVsgahsFISELPQGYDTEVGEagsqL 643
Cdd:PRK09700 77 AAQlgIGIIYQELSVIDElTVLENLYIGrhltkkvcgvnIIDWREMRVR-AAMML-----LRVGLKVDLDEKVAN----L 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 644 SGGQRQAVALARALIRKPRVLILDDATSALdANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGT 719
Cdd:PRK09700 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAeIRRICDRYTVMKDGS 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
503-725 |
4.04e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 226635 [Multi-domain] Cd Length: 242 Bit Score: 72.56 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEH------RY 576
Cdd:COG4161 3 IQLNGINCFYGAHQ---ALFDITLDCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkaiRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 LHTQVAAVRQEPQLFGR-SFRENI--AYGLVQKPTMEEVIAAAMVSGAHSFISELPQGYDTevgeagsQLSGGQRQAVAL 653
Cdd:COG4161 80 LRRNVGMVFQQYNLWPHlTVQENLieAPCRVLGLSKDQALARAEKLLKRLRLKPYADRYPL-------HLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 654 ARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVlLITHCLSLLEQ-ADQILFLEGGTICEAGT 725
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIKELAETGITQV-IVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
519-724 |
4.58e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 223473 [Multi-domain] Cd Length: 251 Bit Score: 72.61 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNL--YQPTKGQLLLDGEP---LPQYE-------------------- 573
Cdd:COG0396 18 EILKGVNLTVKEGEVHAIMGPNGSGKSTLAYTIMGHpkYEVTEGEILFDGEDileLSPDEraragiflafqypveipgvt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 574 -HRYLHTQVAAVRQEPQLFgRSFRENIayglvqKPTMEEViaaamvsgahsfisELPQGY-DTEVGEAgsqLSGGQRQAV 651
Cdd:COG0396 98 nSDFLRAAMNARRGARGIL-PEFIKEL------KEKAELL--------------GLDEEFlERYVNEG---FSGGEKKRN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLL--YKSPErrfRSVLLITHCLSLLE--QADQILFLEGGTICEAG 724
Cdd:COG0396 154 EILQLLLLEPKLAILDEPDSGLDIDALKIVAEGInaLREEG---RGVLIITHYQRLLDyiKPDKVHVLYDGRIVKSG 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
519-674 |
7.36e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224060 [Multi-domain] Cd Length: 243 Bit Score: 71.85 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHRYLhtQVAAVRQEPQLFGR-S 594
Cdd:COG1137 18 KVVNDVSLEVNSGEIVGLLGPNGAGKTTTFYMIVGLVRPDSGKILLDDEditKLPMHKRARL--GIGYLPQEASIFRKlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 595 FRENIAYGLVQ-----KPTMEEVIAAAMVSGAHsfISELpqgydteVGEAGSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:COG1137 96 VEDNIMAVLEIrekdlKKAERKEELDALLEEFH--ITHL-------RDSKAYSLSGGERRRVEIARALAANPKFILLDEP 166
|
....*
gi 548923797 670 TSALD 674
Cdd:COG1137 167 FAGVD 171
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
503-724 |
7.76e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.91 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHrylht 579
Cdd:PRK11000 4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAER----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQLFGR-SFRENIAYGL----VQKPTMEEVI--AAAMVSGAHsFISELPQGydtevgeagsqLSGGQRQAVA 652
Cdd:PRK11000 76 GVGMVFQSYALYPHlSVAENMSFGLklagAKKEEINQRVnqVAEVLQLAH-LLDRKPKA-----------LSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 653 LARALIRKPRVLILDDATSALDA--NSQLRVKqlLYKSPERRFRSVLLITH----CLSLleqADQILFLEGGTICEAG 724
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDAalRVQMRIE--ISRLHKRLGRTMIYVTHdqveAMTL---ADKIVVLDAGRVAQVG 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
502-732 |
8.69e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226963 [Multi-domain] Cd Length: 252 Bit Score: 71.95 E-value: 8.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQV 581
Cdd:COG4604 1 MITIENVSKSYGTKV---VLDDVSLDIPKGGITSIIGPNGAGKSTLLSMMSRLLKKDSGEITIDGLELTSTPSKELAKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 AAVRQEPQLFGR-SFRENIAYGLVQ----KPTMEEVIaaaMVSGAHSF--ISELPQGYDTEvgeagsqLSGGQRQAVALA 654
Cdd:COG4604 78 SILKQENHINSRlTVRDLVGFGRFPysqgRLTKEDRR---IINEAIEYlhLEDLSDRYLDE-------LSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 655 RALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLMER 732
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQIMKILRRLADELGKTIVVVLHDINFASCySDHIVALKNGKVVKQGSPDEIIQP 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
517-675 |
8.94e-14 |
|
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: 74.48 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQ--PTKGQLLLDGEPLPQYEHRYLHTQ-VAAVRQEPQLFGR 593
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 -SFRENIAYGlvQKPTMEEVIA--AAMVSGAHSFISELpQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:TIGR02633 93 lSVAENIFLG--NEITLPGGRMayNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
....*
gi 548923797 671 SALDA 675
Cdd:TIGR02633 170 SSLTE 174
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
501-701 |
1.06e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 226620 [Multi-domain] Cd Length: 213 Bit Score: 70.63 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 501 GLVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPT---KGQLLLDGE---PLPQYEH 574
Cdd:COG4136 1 GMLCLKNVSLRLPGSC---LLANVNFTIAKGEIVTLMGPSGCGKSTLLSWMIGALAGQfscTGELWLNEQrldMLPAAQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 575 rylhtQVAAVRQEPQLFGR-SFRENIAYGLvqKPTME------EVIAAAMVSGAHSFISELPQgydtevgeagsQLSGGQ 647
Cdd:COG4136 78 -----QIGILFQDALLFPHlSVGQNLLFAL--PATLKgnarrnAANAALERSGLDGAFHQDPA-----------TLSGGQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 548923797 648 RQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITH 701
Cdd:COG4136 140 RARVALLRALLAQPKALLLDEPFSRLDVALRDQFRQWVFSEVRAAGIPTVQVTH 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
517-731 |
1.51e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE---PLPQYEHRYLHTQVAAVRQEP----- 588
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 589 --QLFGRSFRENI-AYGLVQKPTmeeviAAAMVSGAHSFISELPQgydtEVGEAGSQLSGGQRQAVALARALIRKPRVLI 665
Cdd:PRK10261 416 prQTVGDSIMEPLrVHGLLPGKA-----AAARVAWLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 666 LDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLME 731
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
506-701 |
1.91e-13 |
|
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: 73.43 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 506 QDVSFAYPnhPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLldgePLPQYEHRYLhtqvaavR 585
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR----PQPGIKVGYL-------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 586 QEPQL-FGRSFRENIAYGLVQKP----------------------------TMEEVIAAAmvsGAHSFISEL-------- 628
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAEIKdaldrfneisakyaepdadfdklaaeqaELQEIIDAA---DAWDLDSQLeiamdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 629 -PQGyDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPErrfrSVLLITH 701
Cdd:TIGR03719 152 cPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTH 216
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
202-478 |
2.33e-13 |
|
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: 71.34 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFlgdgVYNSIMGRVHSQV----QGEVFQAVLRQETEFFQ 277
Cdd:cd18545 17 LAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASR----LRIYLMAKVGQRIlydlRQDLFSHLQKLSFSFFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 278 QNQTGAITSRVTEDTSTLSESlseklslllwyLVRGL-----------CLLGLMLWESLSLTMVTVVTLPLLFLLPEKLG 346
Cdd:cd18545 93 SRPVGKILSRVINDVNSLSDL-----------LSNGLinlipdlltlvGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 347 RWHQVLATQVQTSLAE-SSQVAiEVLSAMPTVRSFANEECEAQKFsqklQKMNTLHQKEAL-AYAVN--LW-ITSISGML 421
Cdd:cd18545 162 RRARKAWQRVRKKISNlNAYLH-ESISGIRVIQSFAREDENEEIF----DELNRENRKANMrAVRLNalFWpLVELISAL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 422 LKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGSSKEI 478
Cdd:cd18545 237 GTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
520-730 |
2.80e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVRQEPQLFGR-SFREN 598
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 IAYGLVQKPTM--------EEVIAAAMVSGAhsfISELP-QGYDTevgeagsqLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:PRK10253 102 VARGRYPHQPLftrwrkedEEAVTKAMQATG---ITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 670 TSALDANSQLRVKQLLYKSPERRFRSVLLITHCLS-LLEQADQILFLEGGTICEAGTYRQLM 730
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
517-743 |
2.93e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQL----LLDGEPLPQYEHRYLHTQ------------ 580
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYSkkiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEP--QLFGRSFRENIAYG---LVQKPTMEEVIAAAMVSG---AHSFISELPQGydtevgeagsqLSGGQRQAVA 652
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGpvaLGVKKSEAKKLAKFYLNKmglDDSYLERSPFG-----------LSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCL-SLLEQADQILFLEGGTICEAGT-YRQLM 730
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTpYEIFT 265
|
250
....*....|...
gi 548923797 731 ERRGCFWTMMQAP 743
Cdd:PRK13631 266 DQHIINSTSIQVP 278
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
533-731 |
3.07e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 533 VIALVGRNGSGKSTVAALLQNLYQ-----PTKGQLLLDGEPL--PQYEHRYLHTQVAAVRQEPQLFGR-SFRENIAYGL- 603
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFPHlTIYDNVAIGVk 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 604 -----VQKPTMEEVIAAAMVSGAhsfiseLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQ 678
Cdd:PRK14267 112 lnglvKSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 548923797 679 LRVKQLLYKSPERrfRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLME 731
Cdd:PRK14267 186 AKIEELLFELKKE--YTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
201-461 |
3.77e-13 |
|
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: 70.59 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 201 EMAIPFFTGHLTDWILQDETASAFTRNITLMSILtttsAVLEFLGDGVYNSIMGRVHSQVQ----GEVFQAVLRQETEFF 276
Cdd:cd18543 15 GLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLAL----GVAEAVLSFLRRYLAGRLSLGVEhdlrTDLFAHLQRLDGAFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 277 QQNQTGAITSRVTEDTSTLSESLSEKLSLLLwYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQV 356
Cdd:cd18543 91 DRWQSGQLLSRATSDLSLVQRFLAFGPFLLG-NLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 357 QTSLAESSQVAIEVLSAMPTVRSFANEECEAQKF---SQKLQKMNTlhQKEALAYAVNLWITSISGMLLkVGILYIGGQL 433
Cdd:cd18543 170 QDQAGDLATVVEESVTGIRVVKAFGRERRELDRFeaaARRLRATRL--RAARLRARFWPLLEALPELGL-AAVLALGGWL 246
|
250 260
....*....|....*....|....*...
gi 548923797 434 VTNGTISSGSLVTFILYQIQFTSAVEAL 461
Cdd:cd18543 247 VANGSLTLGTLVAFSAYLTMLVWPVRML 274
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
202-474 |
5.11e-13 |
|
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: 70.53 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQ-------DETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETE 274
Cdd:cd18554 16 LLLPLILKYIVDDVIQgssltldEKVYKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 275 FFQQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLAT 354
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 355 QVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQK----EALAYAVNLWITSISGMLlkvgILYIG 430
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKhtrwNAKTFSAVNTITDLAPLL----VIGFA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 548923797 431 GQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGS 474
Cdd:cd18554 252 AYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFAS 295
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
497-725 |
5.51e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 497 LNLEGLVQFQDVSFAYPNHP--DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQ--- 571
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 572 --YEHRYLHTQVAAVRQEP--QLFGRSFRENIAYGLVQKPTMEEViAAAMVSGAHSFISeLPQGYdteVGEAGSQLSGGQ 647
Cdd:PRK13645 81 kiKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQE-AYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 648 RQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCL-SLLEQADQILFLEGGTICEAGT 725
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ... |
521-722 |
5.82e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 227019 [Multi-domain] Cd Length: 249 Bit Score: 69.29 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDG--EPLPQYEHRYLHTQVAAVRQEPQLF-GRSFRE 597
Cdd:COG4674 21 LNDLSFSVDPGELRVLIGPNGAGKTTLMDVITGKTRPQEGEVLFDGdtDLTKLPEHRIARAGIGRKFQKPTVFeNLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 598 NIAYGLVQKPTMEEVIAAAMVSGAHSFISELPQ--GYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDA 675
Cdd:COG4674 101 NLELALNRDKSVFASLFARLRAEERRRIDELLAtiGLGDERDRLAALLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 548923797 676 NSQLRVKQLLyKSPERRfRSVLLITHCLSLLEQ-ADQILFL-EGGTICE 722
Cdd:COG4674 181 AETEKTAELL-KSLAGK-HSILVVEHDMGFVREiADKVTVLhEGSVLAE 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism]; |
521-730 |
8.40e-13 |
|
ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism];
Pssm-ID: 226622 [Multi-domain] Cd Length: 248 Bit Score: 68.72 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYqPTKGQLLLDGEPLPQYEHRYLHTQVA--AVRQEPQLFGRSFRen 598
Cdd:COG4138 15 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMT-SGSGSIQFAGQPLEAWSATELARHRAylSQQQTPPFAMPVWH-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 iaYGLVQKPtmeeviaAAMVSGAHSFISELpQGYDTEVGEAGSQLSGGQRQAVALARALIR-------KPRVLILDDATS 671
Cdd:COG4138 92 --YLTLHQP-------DKTRTELLNDVAGA-LALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpdanpAGQLLLLDEPMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 672 ALDANSQLRVKQLLYKSPeRRFRSVLLITHCLS-LLEQADQILFLEGGTICEAGTYRQLM 730
Cdd:COG4138 162 SLDVAQQSALDRLLSALC-QQGLAIVMSSHDLNhTLRHAHRAWLLKRGKLLASGRREEVL 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
517-732 |
9.29e-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: 71.37 E-value: 9.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNL--YQPTKGQLL----------------LDGEPLPQYEHRYLH 578
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 579 TQVAAVRQEPQLFgRSFRENIA------YGLVQKPTMEEVIAAAM----------VSGAHSFISELPQGYdtEVGEAGSQ 642
Cdd:TIGR03269 92 EEVDFWNLSDKLR-RRIRKRIAimlqrtFALYGDDTVLDNVLEALeeigyegkeaVGRAVDLIEMVQLSH--RITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 643 LSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTIC 721
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIWLENGEIK 248
|
250
....*....|.
gi 548923797 722 EAGTYRQLMER 732
Cdd:TIGR03269 249 EEGTPDEVVAV 259
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ... |
520-718 |
1.29e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 226631 [Multi-domain] Cd Length: 300 Bit Score: 69.31 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQyehrylhtqvaavrqepqlfgrSFRENI 599
Cdd:COG4152 17 AVDNISFEVPPGEIFGLLGPNGAGKTTTFRMILGLLEPTEGEITWNGGPLSQ----------------------EIKNRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 600 AY-----GLVQKPTMEEVIAaamvsgahsFISELpQGYDT--------------EVGEAGS----QLSGGQRQAVALARA 656
Cdd:COG4152 75 GYlpeerGLYPKMTVEDQLK---------YLAEL-KGMPKaeiqkklqawlerlEIVGKKTkkikELSKGNQQKIQFISA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 657 LIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCLSLLEQ-ADQILFLEGG 718
Cdd:COG4152 145 VIHEPELLILDEPFSGLDPVNVELLKDAIFELKEEG-ATIIFSSHRMEHVEElCDRLLMLKKG 206
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
526-724 |
1.44e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.41 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 526 FTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLL---DGEP-----LPQYEHRYLH-TQVAAVRQEPQLFGR--- 593
Cdd:PRK11701 27 FDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLrdlyaLSEAERRRLLrTEWGFVHQHPRDGLRmqv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIA----------YGLVQKPT---MEEV-IAAAMvsgahsfISELPqgydtevgeagSQLSGGQRQAVALARALIR 659
Cdd:PRK11701 107 SAGGNIGerlmavgarhYGDIRATAgdwLERVeIDAAR-------IDDLP-----------TTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 660 KPRVLILDDATSALDANSQLRVKQLLyKSPERRFR-SVLLITHCLS---LLeqADQILFLEGGTICEAG 724
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVSVQARLLDLL-RGLVRELGlAVVIVTHDLAvarLL--AHRLLVMKQGRVVESG 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
502-673 |
2.99e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.83 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNhpdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYE-HRYLHTQ 580
Cdd:PRK11614 5 MLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 581 VAAVRQEPQLFGR-SFRENIAYG--LVQKPTMEEVIAAamvsgahsfISEL-PQGYDTEVGEAGSqLSGGQRQAVALARA 656
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENLAMGgfFAERDQFQERIKW---------VYELfPRLHERRIQRAGT-MSGGEQQMLAIGRA 151
|
170
....*....|....*..
gi 548923797 657 LIRKPRVLILDDATSAL 673
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGL 168
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
528-729 |
3.31e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 528 LRPGEVIALVGRNGSGKSTVAALLQNlYQPT----KGQLLLDGEPLpqyEHRYLHTQVAAVRQ-----------EPQLFG 592
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAF-RSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQddlfiptltvrEHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 593 RSFRENIAYGLVQKPTM-EEVIAA-AMVSGAHsfiselpqgydTEVGEAGSQ--LSGGQRQAVALARALIRKPRVLILDD 668
Cdd:TIGR00955 124 AHLRMPRRVTKKEKRERvDEVLQAlGLRKCAN-----------TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 669 ATSALDANSQLRVKQLLYKSPERRfRSVLLITHCLS--LLEQADQILFLEGGTICEAGTYRQL 729
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKG-KTIICTIHQPSseLFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
514-710 |
4.53e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 514 NHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYlHTQVAAVRQE----PQ 589
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGHRsginPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 590 LfgrSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFIsELPQGYdtevgeagsqLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:PRK13540 89 L---TLRENCLYDIHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 548923797 670 TSALDansQLRVKQLLYKSPERRFR--SVLLITHCLSLLEQAD 710
Cdd:PRK13540 155 LVALD---ELSLLTIITKIQEHRAKggAVLLTSHQDLPLNKAD 194
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
530-701 |
4.61e-12 |
|
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: 64.32 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 530 PGEVIALVGRNGSGKSTVA-ALLQNLYQPTKGQLLLDGEPLPQYEHRYLHtqvaavrqepqlfgrsfreniayglvqkpt 608
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLArALARELGPPGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 609 meeviaaamvsgahsfiselpqgyDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQ-----LRVKQ 683
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELR 106
|
170
....*....|....*...
gi 548923797 684 LLYKSPERRFRSVLLITH 701
Cdd:smart00382 107 LLLLLKSEKNLTVILTTN 124
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component [Inorganic ion transport and ... |
524-731 |
6.62e-12 |
|
ABC-type phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226592 [Multi-domain] Cd Length: 258 Bit Score: 66.31 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 524 LTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQL---LLDGEPLPQYE------HRYLHTQVAAVRQEPQlfgRS 594
Cdd:COG4107 25 VSFDLYPGEVLGIVGESGSGKTTLLKCISGRLTPDAGTVtyrMRDGQPRDLYTmseaerRRLLRTEWGFVHQNPR---DG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 595 FRENIAYGlvqkptmEEVIAAAMVSGAHSF--ISELPQGYDTEV-------GEAGSQLSGGQRQAVALARALIRKPRVLI 665
Cdd:COG4107 102 LRMQVSAG-------GNIGERLMAIGARHYgnIRAEAQDWLEEVeidldriDDLPRTFSGGMQQRLQIARNLVTRPRLVF 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 666 LDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCL---SLLeqADQILFLEGGTICEAGTYRQLME 731
Cdd:COG4107 175 MDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLavaRLL--ADRLMVMKQGQVVESGLTDRVLD 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
519-738 |
9.37e-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: 68.89 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGeplpqyehRYLHTQVAAVRQEpqlFGRSFREN 598
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG--------KDIETNLDAVRQS---LGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 IAYGLVQkpTMEEVIAAAMVSGAHSFISELPQ-------GYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:TIGR01257 1013 ILFHHLT--VAEHILFYAQLKGRSWEEAQLEMeamledtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 672 ALDANSQLRVKQLLYKSpeRRFRSVLLITHCLSLLE-QADQILFLEGGTICEAGTYRQLmerRGCFWT 738
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFL---KNCFGT 1153
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
520-729 |
9.61e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.65 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQ---LLLDGEPLPQYEH---------------------R 575
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEkekvleklviqktrfkkikkiK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 576 YLHTQVAAVRQ--EPQLFGRSFRENIAYGL----VQKPTMEEvIAAAMVSgahsfISELPQGYdteVGEAGSQLSGGQRQ 649
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEKDIIFGPvsmgVSKEEAKK-RAAKYIE-----LVGLDESY---LQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 650 AVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCL-SLLEQADQILFLEGGTICEAG-TYR 727
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTYD 251
|
..
gi 548923797 728 QL 729
Cdd:PRK13651 252 IL 253
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
529-726 |
1.13e-11 |
|
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: 65.47 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 529 RPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLllDGEP-------------LPQYEHRYLHTQVAAVRQePQ---LFG 592
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPdwdeildefrgseLQNYFTKLLEGDVKVIVK-PQyvdLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 593 RSFRENIAYGLVQKP---TMEEVIAAAmvsgahsfisELPQGYDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:cd03236 101 KAVKGKVGELLKKKDergKLDELVDQL----------ELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 670 TSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGgticEAGTY 726
Cdd:cd03236 167 SSYLDIKQRLNAARLI-RELAEDDNYVLVVEHDLAVLDYlSDYIHCLYG----EPGAY 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
521-730 |
1.32e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYqPTKGQLLLDGEPLPQYEHR-------YLHTQVAAVRQEP--QLF 591
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelarhraYLSQQQTPPFAMPvfQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 592 GRSFRENIAYGLVQKpTMEEVIAAAMVsgahsfiselpqgyDTEVGEAGSQLSGGQRQAVALARALIR-----KP--RVL 664
Cdd:PRK03695 91 TLHQPDKTRTEAVAS-ALNEVAEALGL--------------DDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 665 ILDDATSALDANSQLRVKQLLykspeRRF----RSVLLITHCLS-LLEQADQILFLEGGTICEAGTYRQLM 730
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLL-----SELcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
506-701 |
1.38e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 506 QDVSFAYPnhPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGqlllDGEPLPQYEHRYLhtqvaavR 585
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIKVGYL-------P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 586 QEPQL-FGRSFRENIAYGLVQKP----------------------------TMEEVIAAAmvsGAHSFISEL-------- 628
Cdd:PRK11819 77 QEPQLdPEKTVRENVEEGVAEVKaaldrfneiyaayaepdadfdalaaeqgELQEIIDAA---DAWDLDSQLeiamdalr 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 629 -PQGyDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLykspeRRFR-SVLLITH 701
Cdd:PRK11819 154 cPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL-----HDYPgTVVAVTH 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-729 |
1.41e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKG-----QLLLDGEPLPQYEHRY-LHTQVAAVRQEPQLFGR 593
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENI-----AYGLVQKPTMEEVIAAAMVSGAhsfiseLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:PRK14271 116 SIMDNVlagvrAHKLVPRKEFRGVAQARLTEVG------LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 669 ATSALDANSQLRVKQLLYKSPERrfRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQL 729
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms]; |
518-731 |
2.17e-11 |
|
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];
Pssm-ID: 226639 [Multi-domain] Cd Length: 330 Bit Score: 65.64 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 518 VPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQP----TKGQLLLDGEPL----PQYEHRYLHTQVAAVRQEPQ 589
Cdd:COG4170 20 VKAVDRVSMTLNEGEIRGLVGESGSGKSLIAKAICGVNKDnwrvTADRMRFDDIDLlrlsPRERRKLVGHNVSMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 590 L-------FGRSFRENIA-----------YGLVQKPTMEeVIAAAMVSGAHSFISELPQgydtevgeagsQLSGGQRQAV 651
Cdd:COG4170 100 ScldpserVGRQLIQNIPawtykgrwwqrFGWRKRRAIE-LLHRVGIKDHKDIMRSYPY-----------ELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLM 730
Cdd:COG4170 168 MIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLSRLNQNSNTTILLISHDLQMISQwADKINVLYCGQTVESAPSEELV 247
|
.
gi 548923797 731 E 731
Cdd:COG4170 248 T 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
493-720 |
2.65e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 224053 [Multi-domain] Cd Length: 500 Bit Score: 66.38 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 493 VLTSLNLEGLVQFQDVSFaypnhpdvpvlqaltfTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPqy 572
Cdd:COG1129 263 VLEVRNLSGGGKVRDVSF----------------TVRAGEILGIAGLVGAGRTELARALFGARPASSGEILLDGKPVR-- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 573 ehryLHTQVAAV----------RQEPQLF-GRSFRENIA---------YGLVQKPTMEEVIAAamvsgahsFISEL---P 629
Cdd:COG1129 325 ----IRSPRDAIkagiayvpedRKSEGLVlDMSIAENITlaslrrfsrRGLIDRRKERALAER--------YIRRLrikT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 630 QGYDTEVGEagsqLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLykspeRRF----RSVLLITHCLS- 704
Cdd:COG1129 393 PSPEQPIGT----LSGGNQQKVVLARWLATDPKVLILDEPTRGIDVGAKAEIYRLI-----RELaaegKAILMISSELPe 463
|
250
....*....|....*.
gi 548923797 705 LLEQADQILFLEGGTI 720
Cdd:COG1129 464 LLGLSDRILVMREGRI 479
|
|
| YufO |
COG3845 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
513-721 |
2.84e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 226364 [Multi-domain] Cd Length: 501 Bit Score: 66.41 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 513 PNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQ--VAAVRQEPQL 590
Cdd:COG3845 266 KDRRGVTAVKDVSFEVRAGEIVGIAGVAGNGQSELVEAISGLRKPASGRILLNGKDVLGRLSPRERRRlgLAYVPEDRHG 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 591 FG----RSFRENIAYGLVQKPTM-------EEVIAAAmvsgAHSFISEL---PQGYDTEVGeagsQLSGGQRQAVALARA 656
Cdd:COG3845 346 HGlvldLSLAENLVLGRHDKKPFsrggfldRRAIRKF----ARELIEEFdvrAPSPDAPAR----SLSGGNQQKLILARE 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 657 LIRKPRVLILDDATSALDANSQLRVKQLLYKSpERRFRSVLLITHCL-SLLEQADQILFLEGGTIC 721
Cdd:COG3845 418 LARRPDLLIAAQPTRGLDVGAIEFIHERLLEL-RDAGKAVLLISEDLdEILELSDRIAVIYEGRIV 482
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
225-478 |
3.22e-11 |
|
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: 64.99 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 225 TRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTEDTSTLSESLSEKLS 304
Cdd:cd18558 59 TLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 305 LLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLlpeKLGRWHQVLATQV---QTSLAESSQVAIEVLSAMPTVRSFA 381
Cdd:cd18558 139 VIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGL---SAVVWAKILSGFTdkeKKAYAKAGAVAEEVLEAFRTVIAFG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 382 NEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEAL 461
Cdd:cd18558 216 GQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQ 295
|
250
....*....|....*..
gi 548923797 462 FSTYPSVQKAVGSSKEI 478
Cdd:cd18558 296 VPSIEAFANARGAAYHI 312
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
493-701 |
6.74e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 225265 [Multi-domain] Cd Length: 593 Bit Score: 65.63 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 493 VLTSLNLEGLVQ-FQDVSFAYPNHPDV---PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQ--------NLYQPTKG 560
Cdd:COG2401 367 FASELDIKGLPNeFQDILESFGVRQRVierYVLRNLNLEIKPGDVVAVVGQSGAGKTTLLRMILgaqkgrgeEKYRPDSG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 561 QLLLDGEplpqyehrylhtQVAAVRQ---EPQLFGRSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFISELpqgydtevg 637
Cdd:COG2401 447 KVEVPKN------------TVSALIPgeyEPEFGEVTILEHLRSKTGDLNAAVEILNRAGLSDAVLYRRKF--------- 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 638 eagSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITH 701
Cdd:COG2401 506 ---SELSTGQKERAKLAKLLAERPNVLLIDEFAAHLDELTAVRVARKISELAREAGITLIVVTH 566
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
527-717 |
6.93e-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: 63.20 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 527 TLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL---PQY-EHRYLHTQVAAVRQEPQLFGRS--FRENIA 600
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykPQYiKADYEGTVRDLLSSITKDFYTHpyFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 601 yglvqKPTMEEVIaaamvsgahsfiselpqgYDTEVGEagsqLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLR 680
Cdd:cd03237 101 -----KPLQIEQI------------------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 548923797 681 VKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEG 717
Cdd:cd03237 154 ASKVIRRFAENNEKTAFVVEHDIIMIDYlADRLIVFEG 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
519-691 |
1.85e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 227118 [Multi-domain] Cd Length: 235 Bit Score: 61.67 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLL--DGE--PLPQYEHRylhtQVAAVRQEPQLFGRS 594
Cdd:COG4778 25 PVLRNVSLSVNAGECVVLHGPSGSGKSTLLRSLYANYLPDEGQILVrhEGEwvDLVTAEPR----EVLEVRRTTIGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 595 FRENI----AYGLVQKPTMEEVIAAAMVSG-AHSFISELpqgydtEVGE-----AGSQLSGGQRQAVALARALIRKPRVL 664
Cdd:COG4778 101 FLRVIprvsALDVVAEPLLARGVPREVARAkAADLLTRL------NLPErlwslAPATFSGGEQQRVNIARGFIVDYPIL 174
|
170 180
....*....|....*....|....*..
gi 548923797 665 ILDDATSALDANSQLRVKQLLYKSPER 691
Cdd:COG4778 175 LLDEPTASLDATNRAVVVELIREAKAR 201
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
516-673 |
3.26e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 516 PDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLP-QYEHRYLHTQVAAVRQE-PQLFGR 593
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIAYGLVQKPTMeEVIAAAMVSGAHSFISELpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSAL 673
Cdd:PRK10982 89 SVMDNMWLGRYPTKGM-FVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
527-707 |
3.35e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224166 [Multi-domain] Cd Length: 591 Bit Score: 63.09 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 527 TLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQllLDGEP-------------LPQYEHRYLHTQVAAVrQEPQlfgr 593
Cdd:COG1245 96 TPRPGKVVGILGPNGIGKSTALKILAGELKPNLGR--YEDPPswdevikrfrgteLQNYFKKLYEGELRAV-HKPQ---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 sFRENIAYGLvqKPTMEEVIAAAMVSGAHSFISE---LPQGYDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:COG1245 169 -YVDLIPKVV--KGKVGELLKKVDERGKFDEVVErlgLENVLDRDV----SELSGGELQRVAIAAALLRDADVYFFDEPS 241
|
170 180 190
....*....|....*....|....*....|....*..
gi 548923797 671 SALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLE 707
Cdd:COG1245 242 SYLDIRQRLNAARVI-RELAEDGKYVIVVEHDLAVLD 277
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
642-725 |
3.42e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.07 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 642 QLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLL-EQADQILFLEGGTI 720
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
....*
gi 548923797 721 CEAGT 725
Cdd:PRK11022 233 VETGK 237
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
231-471 |
3.43e-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: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 231 MSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTE-------DTSTLSESLSEkl 303
Cdd:cd18588 48 LLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVRElesirqfLTGSALTLVLD-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 304 slllwyLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANE 383
Cdd:cd18588 126 ------LVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 384 eceaQKFSQKLQKMNTLHQKEALAYA-VNLWITSISGMLLK---VGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVE 459
Cdd:cd18588 200 ----PQFQRRWEELLARYVKASFKTAnLSNLASQIVQLIQKlttLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVL 275
|
250
....*....|..
gi 548923797 460 ALFSTYPSVQKA 471
Cdd:cd18588 276 RLVQLWQDFQQA 287
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
509-718 |
3.63e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.97 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 509 SFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNL---YQPTKGQLLLDGEPLPQYEHRYlHTQVAAVR 585
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 586 QE----PQLfgrsfreniayglvqkpTMEEVIAAAMVSGAHSFIselpqgydtevgeagSQLSGGQRQAVALARALIRKP 661
Cdd:cd03233 90 EEdvhfPTL-----------------TVRETLDFALRCKGNEFV---------------RGISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 662 RVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLIThCL----SLLEQADQILFLEGG 718
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCI-RTMADVLKTTTFVS-LYqasdEIYDLFDKVLVLYEG 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
527-717 |
4.12e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224166 [Multi-domain] Cd Length: 591 Bit Score: 63.09 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 527 TLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQlllDGEPLPQYEHRYLHTQvaavrqepqlfgrsfreniayglvQK 606
Cdd:COG1245 363 EIYDGEVIGILGPNGIGKTTFVKLLAGVIKPDEGS---EEDLKVSYKPQYISPD------------------------YD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 607 PTMEEVIAAAMVSGAHS--FISE------LPQGYDTEVGEagsqLSGGQRQAVALARALIRKPRVLILDDATSALDANSQ 678
Cdd:COG1245 416 GTVEDLLRSAIRSAFGSsyFKTEivkplnLEDLLERPVDE----LSGGELQRVAIAAALSREADLYLLDEPSAYLDVEQR 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 548923797 679 LRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEG 717
Cdd:COG1245 492 IIVAKVIRRFIENNEKTALVVDHDIYMIDYvSDRLIVFEG 531
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
454-717 |
4.38e-10 |
|
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: 62.84 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 454 FTSAVEALFSTYPSVQK------AVGSSKEIFEYLGRIPRCPASGVLtsLNLEGLVQFQDVSFAYPNHpDVpVLQALTFT 527
Cdd:TIGR00954 399 FTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIV--EYQDNGIKFENIPLVTPNG-DV-LIESLSFE 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 528 LRPGEVIALVGRNGSGKSTVAALLQNLYqPTKGQLLLdgEPLPQyehrylhtQVAAVRQEPQLFGRSFRENIAY-----G 602
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT--KPAKG--------KLFYVPQRPYMTLGTLRDQIIYpdsseD 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 603 LVQKPTMEEVIAAAMVSGAHSFISELPQGYDTeVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVK 682
Cdd:TIGR00954 544 MKRRGLSDKDLEQILDNVQLTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
250 260 270
....*....|....*....|....*....|....*.
gi 548923797 683 QLLykspeRRFRSVLL-ITHCLSLLEQADQILFLEG 717
Cdd:TIGR00954 623 RLC-----REFGITLFsVSHRKSLWKYHEYLLYMDG 653
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
500-673 |
4.66e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 500 EGLVQFQDVSFAYPNhpdVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRylHT 579
Cdd:PRK10762 2 QALLQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--SS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAA---VRQE----PQLfgrSFRENIAYGLVQKPTMEEVIAAAMVSGAHSFISEL--PQGYDTEVGEagsqLSGGQRQA 650
Cdd:PRK10762 77 QEAGigiIHQElnliPQL---TIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQM 149
|
170 180
....*....|....*....|...
gi 548923797 651 VALARALIRKPRVLILDDATSAL 673
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDAL 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
527-717 |
5.60e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 527 TLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDgepL-----PQY-EHRYLHTQVAAVRQEPQLFGRSF-RENI 599
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LkisykPQYiKPDYDGTVEDLLRSITDDLGSSYyKSEI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 600 AYGLvqkptmeeviaaamvsgahsfisELPQGYDTEVGEagsqLSGGQRQAVALARALIRKPRVLILDDATSALDANSQL 679
Cdd:PRK13409 438 IKPL-----------------------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 548923797 680 RVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEG 717
Cdd:PRK13409 491 AVAKAIRRIAEEREATALVVDHDIYMIDYiSDRLMVFEG 529
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
316-465 |
1.43e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 59.78 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 316 LLGLMLWESLSLTMVTVVTLPLLFLLpeklgRW------HQVLATQVQTSLAESSQVaIEVLSAMPTVRSFANEECEAQK 389
Cdd:cd18567 132 TLVMMFLYSPKLALIVLAAVALYALL-----RLalypplRRATEEQIVASAKEQSHF-LETIRGIQTIKLFGREAEREAR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 390 F----------SQKLQKMNTLHQkealayAVNLWITSISGmllkVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVE 459
Cdd:cd18567 206 WlnllvdainaDIRLQRLQILFS------AANGLLFGLEN----ILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRAS 275
|
....*.
gi 548923797 460 ALFSTY 465
Cdd:cd18567 276 SLIDKL 281
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
528-718 |
1.50e-09 |
|
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: 58.02 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 528 LRPGEVIALVGRNGSGKSTvaaLLQNLYQPT-----KGQLLLDGEPLPQY--------EHRYLHTQVAAVRqEPQLFGRS 594
Cdd:cd03232 30 VKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDKNfqrstgyvEQQDVHSPNLTVR-EALRFSAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 595 FREniayglvqkptmeeviaaamvsgahsfiselpqgydtevgeagsqLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:cd03232 106 LRG---------------------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 548923797 675 ANSQLRVKQLLYKSPERRfRSVLLITH--CLSLLEQADQILFLEGG 718
Cdd:cd03232 141 SQAAYNIVRFLKKLADSG-QAILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
319-458 |
1.78e-09 |
|
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: 59.33 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 319 LMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMN 398
Cdd:cd18548 133 MAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLT 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 399 TLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAV 458
Cdd:cd18548 213 DTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSL 272
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
529-718 |
1.93e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 529 RPGEVIALVGRNGSGKSTvaaLLQNLYQP------TKGQLLLDGEPLPQYEHR---Y-----LHTQVAAVRQEPQlFGRS 594
Cdd:TIGR00956 787 KPGTLTALMGASGAGKTT---LLNVLAERvttgviTGGDRLVNGRPLDSSFQRsigYvqqqdLHLPTSTVRESLR-FSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 595 FRENIAYGLVQKPT-MEEVIAaamvsgahsfISELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLI-LDDATSA 672
Cdd:TIGR00956 863 LRQPKSVSKSEKMEyVEEVIK----------LLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 548923797 673 LDANSQLRVKQLLYKSPERRfRSVLLITHCLS--LLEQADQILFLEGG 718
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLADHG-QAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
521-733 |
3.01e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTvaaLLQNLYQptkgqlLLDGEPLPQYEHRYLHTQVaavrQEPQLFGRSFRENIA 600
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKST---LLRHLSG------LITGDKSAGSHIELLGRTV----QREGRLARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 601 --------YGLVQKPT-MEEVIAAAMVSGAH-----SFISELPQGYD----TEVGEAG------SQLSGGQRQAVALARA 656
Cdd:PRK09984 87 ntgyifqqFNLVNRLSvLENVLIGALGSTPFwrtcfSWFTREQKQRAlqalTRVGMVHfahqrvSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 657 LIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSL-LEQADQILFLEGGTICEAGTYRQLMERR 733
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
520-685 |
3.36e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.98 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGE-----PLpqyeHRYLHTQVAAVRQEPQLFGR- 593
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPL----HARARRGIGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIAYGL-VQKPTMEEVIAAAMVSGAHSF-ISELPQGYdtevgeaGSQLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:PRK10895 94 SVYDNLMAVLqIRDDLSAEQREDRANELMEEFhIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170
....*....|....
gi 548923797 672 ALDANSQLRVKQLL 685
Cdd:PRK10895 167 GVDPISVIDIKRII 180
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
205-455 |
3.86e-09 |
|
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: 58.73 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 205 PFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAI 284
Cdd:cd18565 34 ASFLPLVPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 285 TSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAE-S 363
Cdd:cd18565 114 MSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDlN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 364 SQVAiEVLSAMPTVRSFANEECEAQ---KFSQKLqkmntlhqKEALAYAVNLWITSISGMLLKVGI-----LYIGGQLVT 435
Cdd:cd18565 194 ARLE-NNLSGIAVIKAFTAEDFERErvaDASEEY--------RDANWRAIRLRAAFFPVIRLVAGAgfvatFVVGGYWVL 264
|
250 260
....*....|....*....|....*.
gi 548923797 436 NG------TISSGSLVTFILYQIQFT 455
Cdd:cd18565 265 DGpplftgTLTVGTLVTFLFYTQRLL 290
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
525-730 |
4.19e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 525 TFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL-PQYEHRYLHTQVAAVRQEPQ----LFGRSFRENI 599
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDRKrdglVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 600 --------AYGLVQKPTMEEVIAAAmvsgahSFIS----ELPqGYDTEVGEagsqLSGGQRQAVALARALIRKPRVLILD 667
Cdd:PRK10762 352 sltalryfSRAGGSLKHADEQQAVS------DFIRlfniKTP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923797 668 DATSALDANSQLRVKQLLykspeRRFR----SVLLITHCL-SLLEQADQILFLEGGTIC-----EAGTYRQLM 730
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLI-----NQFKaeglSIILVSSEMpEVLGMSDRILVMHEGRISgeftrEQATQEKLM 488
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
501-720 |
5.12e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 501 GLVQFQDVSFAYPNH-----PDVPVLQA----------LTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLD 565
Cdd:PRK15439 244 SLSASQKLWLELPGNrrqqaAGAPVLTVedltgegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 566 GEPLPQYEHR--------YLHTQvaavRQEPQLF-GRSFRENIA------YGLVQKPTMEeviaAAMVSGAHSFISELPQ 630
Cdd:PRK15439 324 GKEINALSTAqrlarglvYLPED----RQSSGLYlDAPLAWNVCalthnrRGFWIKPARE----NAVLERYRRALNIKFN 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 631 GYDTEVGeagsQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQ-A 709
Cdd:PRK15439 396 HAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI-RSIAAQNVAVLFISSDLEEIEQmA 470
|
250
....*....|.
gi 548923797 710 DQILFLEGGTI 720
Cdd:PRK15439 471 DRVLVMHQGEI 481
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
521-725 |
5.83e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLhtqVAAVRQEPQLfGRSFR---E 597
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEV-DWSFPvlvE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 598 NIA-------YGLVQKPTMEEviaAAMVSGAHSFISELPQGYdTEVGEagsqLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:PRK15056 99 DVVmmgryghMGWLRRAKKRD---RQIVTAALARVDMVEFRH-RQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 671 SALDANSQLRVKQLLyKSPERRFRSVLLITHCL-SLLEQADQILFLEGGTICEAGT 725
Cdd:PRK15056 171 TGVDVKTEARIISLL-RELRDEGKTMLVSTHNLgSVTEFCDYTVMVKGTVLASGPT 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
517-674 |
6.10e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLqnlyqpTKGQLLLDGEPlpQYEHRYLhtqVAAVRQEP--QLFGRS 594
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL------NGEVLLDDGRI--IYEQDLI---VARLQQDPprNVEGTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 595 FrENIAYGL-----------------VQKPT------MEEVIAAAMVSGAHSFISELPQ-----GYDTEvgEAGSQLSGG 646
Cdd:PRK11147 84 Y-DFVAEGIeeqaeylkryhdishlvETDPSeknlneLAKLQEQLDHHNLWQLENRINEvlaqlGLDPD--AALSSLSGG 160
|
170 180
....*....|....*....|....*...
gi 548923797 647 QRQAVALARALIRKPRVLILDDATSALD 674
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
533-720 |
7.31e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.35 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 533 VIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHR-YLHTQ---VAAVRQEPQLFGR-SFRENIAYGLvqKP 607
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLPPEkrrIGYVFQDARLFPHyKVRGNLRYGM--AK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 608 TMEEVIAAaMVS--GAHSFISELPqgydtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDansqLRVKQLL 685
Cdd:PRK11144 104 SMVAQFDK-IVAllGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD----LPRKREL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 548923797 686 YKSPERRFRSV----LLITHCL-SLLEQADQILFLEGGTI 720
Cdd:PRK11144 168 LPYLERLAREInipiLYVSHSLdEILRLADRVVVLEQGKV 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
520-685 |
1.16e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 520 VLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQP---TKGQLLLDGEPLPQYEHRylhtqVAAVRQEPQLFGR-SF 595
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnfTGTILANNRKPTKQILKR-----TGFVTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 596 RENIAY-GLVQKPtmEEVIAAAMVSGAHSFISEL--PQGYDTEVGEAGSQ-LSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:PLN03211 158 RETLVFcSLLRLP--KSLTKQEKILVAESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170
....*....|....
gi 548923797 672 ALDANSQLRVKQLL 685
Cdd:PLN03211 236 GLDATAAYRLVLTL 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
517-737 |
1.35e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQN--LYQPTKGQLLLDGEPLPQYE-----HR--YLHTQ----VAA 583
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEpeeraHLgiFLAFQypieIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 584 VRQEPQLfgrsfreNIAYGLVQK----PTME-----EVIAAA--MVSGAHSFISElpqgydtEVGEAgsqLSGGQRQAVA 652
Cdd:CHL00131 99 VSNADFL-------RLAYNSKRKfqglPELDpleflEIINEKlkLVGMDPSFLSR-------NVNEG---FSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 653 LARALIRKPRVLILDDATSALDANSqLR-----VKQLLYKSperrfRSVLLITHCLSLLE--QADQILFLEGGTICEAG- 724
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDA-LKiiaegINKLMTSE-----NSIILITHYQRLLDyiKPDYVHVMQNGKIIKTGd 235
|
250
....*....|....
gi 548923797 725 -TYRQLMERRGCFW 737
Cdd:CHL00131 236 aELAKELEKKGYDW 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
525-720 |
1.90e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 525 TFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPqyehryLHTQVAAVR-----------QEPQLFGR 593
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIRagimlcpedrkAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIA---------YGLVQKPTMEEviaaamvSGAHSFISEL----PQGyDTEVGeagsQLSGGQRQAVALARALIRK 660
Cdd:PRK11288 347 SVADNINisarrhhlrAGCLINNRWEA-------ENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCL-SLLEQADQILFLEGGTI 720
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQG-VAVLFVSSDLpEVLGVADRIVVMREGRI 474
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
203-485 |
2.28e-08 |
|
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: 55.98 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 203 AIPFFTGHLTDWILQDEtasaftrNITLMSILTTTSAVLeFLGDGVYNSIMGRV--------HSQVQGEVFQAVLRQETE 274
Cdd:cd18555 20 LIPILTQYVIDNVIVPG-------NLNLLNVLGIGILIL-FLLYGLFSFLRGYIiiklqtklDKSLMSDFFEHLLKLPYS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 275 FFQQNQTGAITSRVTEDT------STLseslseklslllwyLVRGL--CLL-----GLMLWESLSLTMVTVVTLPLLFLL 341
Cdd:cd18555 92 FFENRSSGDLLFRANSNVyirqilSNQ--------------VISLIidLLLlviylIYMLYYSPLLTLIVLLLGLLIVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 342 peklgrwhqVLATQ------VQTSLAESSQVA---IEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALayaVNL 412
Cdd:cd18555 158 ---------LLLTRkkikklNQEEIVAQTKVQsylTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKER---LSN 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 413 WITSISG---MLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKaVGSskeifeYLGRI 485
Cdd:cd18555 226 ILNSISSsiqFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFIL-LKS------YLERL 294
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
508-730 |
2.60e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.35 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 508 VSFAYPNHPdVPVLQALTFTLRPGEVIALVGRNGSGKSTVA----ALLQNLYQPTKGQLLLDGEPL----PQYEHRYLHT 579
Cdd:PRK15093 11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLlrlsPRERRKLVGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 580 QVAAVRQEPQ-LFGRSfrENIAYGLVQ------------------KPTMEEVIAAAMVSGAHSFISELPQgydtevgeag 640
Cdd:PRK15093 90 NVSMIFQEPQsCLDPS--ERVGRQLMQnipgwtykgrwwqrfgwrKRRAIELLHRVGIKDHKDAMRSFPY---------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 641 sQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQ-ADQILFLEGGT 719
Cdd:PRK15093 158 -ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQ 236
|
250
....*....|.
gi 548923797 720 ICEAGTYRQLM 730
Cdd:PRK15093 237 TVETAPSKELV 247
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
496-668 |
2.80e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.54 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 496 SLNLEGLVQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHR 575
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 576 YLHT---QVAAVRQEPQLF-GRSFRENIAYGLVQKPTMEEVIAAAMVsgahsfISELpqgydTEVGEAG------SQLSG 645
Cdd:PRK11831 78 RLYTvrkRMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAPLLHSTV------MMKL-----EAVGLRGaaklmpSELSG 146
|
170 180
....*....|....*....|...
gi 548923797 646 GQRQAVALARALIRKPRVLILDD 668
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDE 169
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
517-741 |
4.13e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALL--QNLYQPTKGQLLLDGEPL----P------------QY------ 572
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLlelsPedragegifmafQYpveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 573 --EHRYLHTQVAAV---RQEPQLFGRSFREniayglvqkpTMEEVIAaamvsgahsfISELPQGYDTEVGEAGsqLSGGQ 647
Cdd:PRK09580 93 vsNQFFLQTALNAVrsyRGQEPLDRFDFQD----------LMEEKIA----------LLKMPEDLLTRSVNVG--FSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 648 RQAVALARALIRKPRVLILDDATSALDANSqLRVKQLLYKSPERRFRSVLLITHCLSLLE--QADQILFLEGGTICEAG- 724
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDA-LKIVADGVNSLRDGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSGd 229
|
250
....*....|....*...
gi 548923797 725 -TYRQLMERRGCFWTMMQ 741
Cdd:PRK09580 230 fTLVKQLEEQGYGWLTEQ 247
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
317-461 |
4.27e-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: 55.26 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 317 LGLMLWESLSLTMVTVVTLPLLFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQK 396
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAK 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 397 -MNTLHQKEALAYAVNLwITSISGMLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEAL 461
Cdd:cd18568 213 aLNTRFRGQKLSIVLQL-ISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLAL 277
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
502-731 |
5.70e-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: 55.99 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPDVPVLQALTFTLRPGEVIALVGRNGSGKS-TVAALLQNLYQPTKGQLLLDGEPL----PQYEHRY 576
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVdirnPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 577 LHTQVAAVRQE----PQLfgrSFRENIAYGLVQKPTMEEVIAAAMVSGA----------HSFISELPQGydtevgeagsQ 642
Cdd:TIGR02633 337 GIAMVPEDRKRhgivPIL---GVGKNITLSVLKSFCFKMRIDAAAELQIigsaiqrlkvKTASPFLPIG----------R 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 643 LSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTIC- 721
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKg 483
|
250
....*....|....
gi 548923797 722 ----EAGTYRQLME 731
Cdd:TIGR02633 484 dfvnHALTQEQVLA 497
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
503-680 |
2.48e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 503 VQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLdGEPLpqyehrylhtQVA 582
Cdd:TIGR03719 323 IEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 583 AVRQ-----EPqlfGRSFRENIAYGLvqkPTME----EVIAAAMVsGAHSFiselpQGYDTE--VGeagsQLSGGQRQAV 651
Cdd:TIGR03719 389 YVDQsrdalDP---NKTVWEEISGGL---DIIKlgkrEIPSRAYV-GRFNF-----KGSDQQkkVG----QLSGGERNRV 452
|
170 180
....*....|....*....|....*....
gi 548923797 652 ALARALIRKPRVLILDDATSALDANSqLR 680
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVET-LR 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
502-674 |
4.10e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPNHPdvPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGqllldgeplpqyehrylhtqv 581
Cdd:PLN03073 508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG--------------------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 582 aAVRQEPQLFGRSFRENIAYGLvqkptmeEVIAAAMVSGAHSFISELPQGYDTEVGEAG----------SQLSGGQRQAV 651
Cdd:PLN03073 565 -TVFRSAKVRMAVFSQHHVDGL-------DLSSNPLLYMMRCFPGVPEQKLRAHLGSFGvtgnlalqpmYTLSGGQKSRV 636
|
170 180
....*....|....*....|...
gi 548923797 652 ALARALIRKPRVLILDDATSALD 674
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
525-742 |
6.34e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 525 TFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGeplpqyehrylHTQVAAVRQEPQLFGRSFRENIAYGLV 604
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------NWQLAWVNQETPALPQPALEYVIDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 605 QKPTMEEVIAAA-----------------------MVSGAHSFISELpqGYDTE-VGEAGSQLSGGQRQAVALARALIRK 660
Cdd:PRK10636 90 EYRQLEAQLHDAnerndghaiatihgkldaidawtIRSRAASLLHGL--GFSNEqLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 661 PRVLILDDATSALDANSQLRVKQLLYKSPErrfrSVLLITHCLSLLEQ-ADQILFLEGGTICE-AGTYRQLMERRGCFWT 738
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPiVDKIIHIEQQSLFEyTGNYSSFEVQRATRLA 243
|
....
gi 548923797 739 MMQA 742
Cdd:PRK10636 244 QQQA 247
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
202-474 |
6.45e-07 |
|
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: 51.82 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQT 281
Cdd:cd18782 19 LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 282 GAITSRVTE---------DTSTLSESLseklslllwyLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLPEKLGRwhqVL 352
Cdd:cd18782 99 GELSTRISEldtirgfltGTALTTLLD----------VLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGP---IL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 353 ATQVQTSLAESSQVA---IEVLSAMPTVRSfANEECEA-----QKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLlkv 424
Cdd:cd18782 166 RRQIRRRAEASAKTQsylVESLTGIQTVKA-QNAELKArwrwqNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLL--- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 548923797 425 gILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGS 474
Cdd:cd18782 242 -VLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVS 290
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
517-732 |
9.73e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVA-ALLQNLyqptkgqLLLDGEplpqYEHRYLHTQVAAVRQEPQL----- 590
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALArALAGEL-------PLLSGE----RQSQFSHITRLSFEQLQKLvsdew 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 591 --------------FGRSFRENIAYGlVQKPTMEEVIAAamvsgahSF-ISELpqgydteVGEAGSQLSGGQRQAVALAR 655
Cdd:PRK10938 84 qrnntdmlspgeddTGRTTAEIIQDE-VKDPARCEQLAQ-------QFgITAL-------LDRRFKYLSTGETRKTLLCQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923797 656 ALIRKPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGGTICEAGTYRQLMER 732
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
202-471 |
1.10e-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: 50.95 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFFTGHLTDWILQDETASAftrnITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQ----GEVFQAVLRQETEFFQ 277
Cdd:cd18546 16 LAGPLLVRYGIDSGVRAGDLGV----LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLydlrLRVFAHLQRLSLDFHE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 278 QNQTGAITSRVTEDTSTLSESLSEKLSLLlwyLVRGLCLLG---LMLWESLSLTMVTVVTLPLLFLLpeklGRWHQVLAT 354
Cdd:cd18546 92 RETSGRIMTRMTSDIDALSELLQTGLVQL---VVSLLTLVGiavVLLVLDPRLALVALAALPPLALA----TRWFRRRSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 355 ----QVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIG 430
Cdd:cd18546 165 rayrRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVG 244
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 548923797 431 GQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKA 471
Cdd:cd18546 245 AWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQA 285
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
513-674 |
1.67e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 513 PNHPDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTK-GQLLLDGEPL----PQYEHRYlhtQVAAVRQE 587
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVkirnPQQAIAQ---GIAMVPED 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 588 PQLFG----RSFRENIAYGLVQKPTMEEVI-AAAMVSGAHSFISELpqgydtEVGEAG-----SQLSGGQRQAVALARAL 657
Cdd:PRK13549 347 RKRDGivpvMGVGKNITLAALDRFTGGSRIdDAAELKTILESIQRL------KVKTASpelaiARLSGGNQQKAVLAKCL 420
|
170
....*....|....*..
gi 548923797 658 IRKPRVLILDDATSALD 674
Cdd:PRK13549 421 LLNPKILILDEPTRGID 437
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
502-674 |
2.11e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 502 LVQFQDVSFAYPnhpDVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQL-LLDGEPL---PQYEHRYL 577
Cdd:PRK10636 312 LLKMEKVSAGYG---DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 578 HTQVAA----VRQEPQLFGRSFRENIayglvqkptmeeviaaamvsGAHSFiselpQGydTEVGEAGSQLSGGQRQAVAL 653
Cdd:PRK10636 389 RADESPlqhlARLAPQELEQKLRDYL--------------------GGFGF-----QG--DKVTEETRRFSGGEKARLVL 441
|
170 180
....*....|....*....|.
gi 548923797 654 ARALIRKPRVLILDDATSALD 674
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
517-674 |
2.47e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 517 DVPVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEH-RYlhtqVAAVRQEPQLfgrsf 595
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsRF----MAYLGHLPGL----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 596 reniayglvqKPTMEEVIAAAMVSGAHSF-ISELPQGYDTEVGEAG------SQLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:PRK13543 94 ----------KADLSTLENLHFLCGLHGRrAKQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*.
gi 548923797 669 ATSALD 674
Cdd:PRK13543 164 PYANLD 169
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
521-724 |
7.73e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEplpqyehrylhTQVAAVRQ--EPQLFGrsfREN 598
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAglSGQLTG---IEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 599 IAYGLVQ--------KPTMEEVIAaamVSGAHSFISELPQGYdtevgeagsqlSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:PRK13546 106 IEFKMLCmgfkrkeiKAMTPKIIE---FSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 671 SALDANSQLRVKQLLYKSPERRfRSVLLITHCLSLLEQ-ADQILFLEGGTICEAG 724
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEFKEQN-KTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYG 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
525-717 |
1.48e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 525 TFTLRPGEVIALVGRNGSGKST------------------------------VAALLQNLYQPTKGQLLLDGEPLPQYEH 574
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTflrymamhaidgipkncqilhveqevvgddTTALQCVLNTDIERTQLLEEEAQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 575 RYLHTQVAAVRQEPQLFGRSFRENIAYGLVQKPTMEEVI--------AAAMVSGAhSFISELPQgydtevgEAGSQLSGG 646
Cdd:PLN03073 277 RELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIdaytaearAASILAGL-SFTPEMQV-------KATKTFSGG 348
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923797 647 QRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLYKSPerrfRSVLLITHCLSLLEQ-ADQILFLEG 717
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP----KTFIVVSHAREFLNTvVTDILHLHG 416
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
526-674 |
1.81e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 411426 [Multi-domain] Cd Length: 907 Bit Score: 48.19 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 526 FTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLpqyEHRYLHT--QVAAVRQEPQLFGR-SFRENIA-- 600
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIATrrRVGYMSQAFSLYGElTVRQNLElh 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 601 ---YGLvqkPtmEEVIAAAmvsgahsfISELPQGYD-TEVGEA-GSQLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:NF033858 364 arlFHL---P--AAEIAAR--------VAEMLERFDlADVADAlPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
203-454 |
3.11e-05 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 46.34 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 203 AIPFFTGHLTDwILQDETASAFTRNITLM---SILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQN 279
Cdd:cd18582 14 AVPFLLKYAVD-ALSAPASALLAVPLLLLlayGLARILSSLFNELRDALFARVSQRAVRRLALRVFRHLHSLSLRFHLSR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 280 QTGAITS---RVTEDTSTlseslseklslllwyLVRGLCL------------LGLMLWE-SLSLTMVTVVTLPLLFLLPE 343
Cdd:cd18582 93 KTGALSRaieRGTRGIEF---------------LLRFLLFnilptilelllvCGILWYLyGWSYALITLVTVALYVAFTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 344 KLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAV-NLWITSISGMLL 422
Cdd:cd18582 158 KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALlNIGQALIISLGL 237
|
250 260 270
....*....|....*....|....*....|..
gi 548923797 423 kVGILYIGGQLVTNGTISSGSLVTFILYQIQF 454
Cdd:cd18582 238 -TAIMLLAAQGVVAGTLTVGDFVLVNTYLLQL 268
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
623-724 |
6.26e-05 |
|
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: 44.24 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 623 SFISELPQGYDTeVGEAGSQLSGGQRQAVALARALIR--KPRVLILDDATSALDANSQLR----VKQLLYKSperrfRSV 696
Cdd:cd03238 69 QFLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQllevIKGLIDLG-----NTV 142
|
90 100 110
....*....|....*....|....*....|....
gi 548923797 697 LLITHCLSLLEQADQILFL------EGGTICEAG 724
Cdd:cd03238 143 ILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
519-718 |
7.91e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 519 PVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYE-HRYLHTQVAAVRQEPQLFG----- 592
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEERRSTGiyayl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 593 ----RSFRENI-----AYGLVQKPTMEE----VIAAAMVsgahsfisELPqGYDTEVGeagsQLSGGQRQAVALARALIR 659
Cdd:PRK10982 342 digfNSLISNIrnyknKVGLLDNSRMKSdtqwVIDSMRV--------KTP-GHRTQIG----SLSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 548923797 660 KPRVLILDDATSALDANSQLRVKQLLYKSPERRFRSVLLITHCLSLLEQADQILFLEGG 718
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
536-677 |
1.10e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 536 LVGRNGSGKSTVAALLQNLYQPTKGQLLLD-GEPL-----PQY---EHRYL------HTQVAAVRQEpqlfgrsfRENIa 600
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLgklrqDQFafeEFTVLdtvimgHTELWEVKQE--------RDRI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 601 YGLvqkPTM--EEVIAAAMVSGAhsfISELpQGYDTEvGEAGSQLSG---------GQRQAVA--------LARALIRKP 661
Cdd:PRK15064 103 YAL---PEMseEDGMKVADLEVK---FAEM-DGYTAE-ARAGELLLGvgipeeqhyGLMSEVApgwklrvlLAQALFSNP 174
|
170
....*....|....*.
gi 548923797 662 RVLILDDATSALDANS 677
Cdd:PRK15064 175 DILLLDEPTNNLDINT 190
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
637-734 |
1.10e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 637 GEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQ-ADQILFL 715
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQlAHELTVI 217
|
90
....*....|....*....
gi 548923797 716 EGGTICEAGTYRQLMERRG 734
Cdd:NF000106 218 DRGRVIADGKVDELKTKVG 236
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
521-736 |
1.13e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 521 LQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPLPQYEHRYLHTQVAAVrqepqlfgrsfrENIA 600
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 601 Y-GLVQKPTMEEV--IAAAMVSGAH--SFISELPQGYdtevgeagsqlSGGQRQAVALARALIRKPRVLILDDATSALDa 675
Cdd:PRK13545 108 LkGLMMGLTKEKIkeIIPEIIEFADigKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 676 nsQLRVKQLLYKSPE--RRFRSVLLITHCLSLLEQ-ADQILFLEGGTICEAGTYRQLMERRGCF 736
Cdd:PRK13545 176 --QTFTKKCLDKMNEfkEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
231-447 |
1.14e-04 |
|
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: 44.81 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 231 MSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQETEFFQQNQTGAITSRVTE-----------------DTS 293
Cdd:cd18783 48 VVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQierirqfltgqlfgtllDAT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 294 TLseslseklslllwylvrgLCLLGLMLWESLSLTMVT-----VVTLPLLFLLPEKLGRWHQVLAtqvqtslAESSQVA- 367
Cdd:cd18783 128 SL------------------LVFLPVLFFYSPTLALVVlafsaLIALIILAFLPPFRRRLQALYR-------AEGERQAf 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 368 -IEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALayaVNLWITSISG---MLLKVGILYIGGQLVTNGTISSGS 443
Cdd:cd18783 183 lVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGR---LSNWPQTLTGpleKLMTVGVIWVGAYLVFAGSLTVGA 259
|
....
gi 548923797 444 LVTF 447
Cdd:cd18783 260 LIAF 263
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
203-474 |
1.22e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 44.78 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 203 AIPFFTGHLTDWILQDETASAFTRNITLMSILTTTSAVleflgdGVYNSIM--GRVHSQVQGEVFQAVLR--QETEF--F 276
Cdd:cd18540 20 VFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQAL------SVFLFIRlaGKIEMGVSYDLRKKAFEhlQTLSFsyF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 277 QQNQTGAITSRVTEDTSTLSESLSEKLSLLLWYLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLlpekLGRWHQVLATQV 356
Cdd:cd18540 94 DKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV----VSIYFQKKILKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 357 QTSL-AESSQV--AI-EVLSAMPTVRSFANEECEAQKFSQKLQKM------NTLHQkeALAYAVNLWITSISGMLlkvgI 426
Cdd:cd18540 170 YRKVrKINSRItgAFnEGITGAKTTKTLVREEKNLREFKELTEEMrrasvrAARLS--ALFLPIVLFLGSIATAL----V 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 548923797 427 LYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGS 474
Cdd:cd18540 244 LWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQAS 291
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
522-717 |
1.56e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 522 QALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKGQLLLDGEPL-PQYEHRYLHTQVAAV---RQEPQLFGR-SFR 596
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsPRSPLDAVKKGMAYItesRRDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 597 ENIA-------------YGLVQkPTMEEVIAAAMvsgahsfiSELPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPRV 663
Cdd:PRK09700 360 QNMAisrslkdggykgaMGLFH-EVDEQRTAENQ--------RELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 664 LILDDATSALDANSQLRVKQLLYKSPERRfRSVLLITHCL-SLLEQADQI-LFLEG 717
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELpEIITVCDRIaVFCEG 485
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
641-716 |
3.19e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 44.37 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 641 SQLSGGQRQ------AVALARALIRKPRV--LILDDATSALDANSQLRVKQLLyKSPERRFRSVLLITHCLSLLEQADQI 712
Cdd:COG0419 814 KTLSGGERFlaslalRLALSDLLQGRARLelLFLDEPFGTLDEERLEKLAEIL-EELLSDGRQIIIISHVEELKERADVR 892
|
....
gi 548923797 713 LFLE 716
Cdd:COG0419 893 IRVK 896
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
637-725 |
3.26e-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: 44.23 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 637 GEAGSQLSGGQRQAVALARALIRK---PRVLILDDATSAL---DANSQLRVKQLLYKSPErrfrSVLLITHCLSLLEQAD 710
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVDKGN----TVVVIEHNLDVIKTAD 899
|
90 100
....*....|....*....|.
gi 548923797 711 QILFL------EGGTICEAGT 725
Cdd:TIGR00630 900 YIIDLgpeggdGGGTVVASGT 920
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
514-713 |
5.13e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 514 NHPDVPVLQALTFTlrPGEVIALVGRNGSGKSTVAallqnlyqptkgqllldgeplpqyehrylhTQVAAVrqepqLFGR 593
Cdd:cd03227 6 RFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTIL------------------------------DAIGLA-----LGGA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 594 SFRENIAYGLVQKPTMEEVIAaamvsgahSFISELPQgydtevgeagsqLSGGQRQAVALARALI---RKPRVL-ILDDA 669
Cdd:cd03227 49 QSATRRRSGVKAGCIVAAVSA--------ELIFTRLQ------------LSGGEKELSALALILAlasLKPRPLyILDEI 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 548923797 670 TSALDANSQLRVKQLLYKSPERRFRsVLLITHCLSLLEQADQIL 713
Cdd:cd03227 109 DRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLPELAELADKLI 151
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
362-456 |
1.98e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 40.97 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 362 ESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALAYAvnlWITSISGMLLKVGIL---YIGGQLVTNGT 438
Cdd:cd18583 174 EERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLN---LLNAVQSLILTLGLLagcFLAAYQVSQGQ 250
|
90
....*....|....*...
gi 548923797 439 ISSGSLVTFILYQIQFTS 456
Cdd:cd18583 251 ATVGDFVTLLTYWAQLSG 268
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
202-474 |
2.79e-03 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 40.54 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 202 MAIPFF---------TGHLTDWILQdetasaftrNITLMSILTTTSAVLEFLGDGVYNSIMGRVHSQVQGEVFQAVLRQE 272
Cdd:cd18569 19 LVIPVFsrifiddilVGGLPDWLRP---------LLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 273 TEFFQQNQTGAITSRV----------TEDTSTLSESlseklslllwyLVRGLCLLGLMLWESLSLTMVTVVTLPLLFLLP 342
Cdd:cd18569 90 VEFFSQRYAGDIASRVqsndrvanllSGQLATTVLN-----------LVMAVFYALLMLQYDVPLTLIGIAIALLNLLVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 343 EKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKFSQKLQKMNTLHQKEALayaVNLWITSISGMLL 422
Cdd:cd18569 159 RLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESDFFSRWAGYQAKVLNAQQELGR---TNQLLGALPTLLS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 548923797 423 KVG---ILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVGS 474
Cdd:cd18569 236 ALTnaaILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGD 290
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
631-725 |
3.86e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223256 [Multi-domain] Cd Length: 935 Bit Score: 40.64 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 631 GYDTeVGEAGSQLSGGQRQAVALARALIRK---PRVLILDDATSAL---DANSQLRVKQ-LLYKSperrfRSVLLITHCL 703
Cdd:COG0178 812 GYIK-LGQPATTLSGGEAQRVKLAKELSKRstgKTLYILDEPTTGLhfdDIKKLLEVLHrLVDKG-----NTVIVIEHNL 885
|
90 100
....*....|....*....|....*...
gi 548923797 704 SLLEQADQILFL------EGGTICEAGT 725
Cdd:COG0178 886 DVIKTADWIIDLgpeggdGGGEIVASGT 913
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
503-560 |
3.97e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 3.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 548923797 503 VQFQDVSFAYPNHPdvpVLQALTFTLRPGEVIALVGRNGSGKSTVAALLQNLYQPTKG 560
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
314-449 |
5.00e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 39.39 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 314 LCLLGLMLWESLSLTMVTVVTLPL-LFLLPEKLGRWHQVLATQVQTSLAESSQVAIEVLSAMPTVRSFANEECEAQKF-- 390
Cdd:cd18585 124 LATILFLAFFSPALALILLAGLLLaGVVIPLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLeq 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923797 391 -SQKL----QKMNTLHqkeALAYAVNLWITsisgMLLKVGILYIGGQLVTNGTISSGSLVTFIL 449
Cdd:cd18585 204 lSDALikeqRRLARLS---GLSQALMILLS----GLTVWLVLWLGAPLVQNGALDGALLAMLVF 260
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
525-716 |
5.39e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.74 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 525 TFTLRPGeVIALVGRNGSGKSTV-AALLQNLY---QPTKGQLLLDGEPLPQYEHR---YLHTQVAA-----VRQEPQLFg 592
Cdd:cd03240 17 EIEFFSP-LTLIVGQNGAGKTTIiEALKYALTgelPPNSKGGAHDPKLIREGEVRaqvKLAFENANgkkytITRSLAIL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 593 rsfrENIAY---GLVQKPTMEEViaaamvsgahsfiselpqgydtevgeagSQLSGGQRQAV------ALARALIRKPRV 663
Cdd:cd03240 95 ----ENVIFchqGESNWPLLDMR----------------------------GRCSGGEKVLAsliirlALAETFGSNCGI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 548923797 664 LILDDATSALDANSqlRVKQLLYKSPERR---FRSVLLITHCLSLLEQADQILFLE 716
Cdd:cd03240 143 LALDEPTTNLDEEN--IEESLAEIIEERKsqkNFQLIVITHDEELVDAADHIYRVE 196
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
317-478 |
6.31e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 39.10 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 317 LGLMLWESLSLTMVTVVTLPLLFLLPEKLGRwhqVLATQV-QTSLAESSQVA--IEVLSAMPTVRSFANEECEAQKFSQK 393
Cdd:cd18566 133 LGLIWYLGGKLVLVPLVLLGLFVLVAILLGP---ILRRALkERSRADERRQNflIETLTGIHTIKAMAMEPQMLRRYERL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923797 394 LQKMNTLHQKEALAYAVNLWITSISGMLLKVGILYIGGQLVTNGTISSGSLVTFILYQIQFTSAVEALFSTYPSVQKAVG 473
Cdd:cd18566 210 QANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRV 289
|
....*
gi 548923797 474 SSKEI 478
Cdd:cd18566 290 AVRRL 294
|
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