|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-732 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 1078.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 16 ASIDFLACLLFACLHDGTFKFANFTSQFG-DFSFFTSTIDLFLLQFFRFALWMVPAAIHVANKAD-TLTMWKEPIFCSAL 93
Cdd:TIGR00958 1 AALAYLLPWFSLLLVDWALLRDLLQGIFGlLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAGgLLAAVKPLVAALCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 94 LICAASPTKLLLLTEKLKPDEFLTFGDTAFLVWNFISAIILNSSWTRYFSrTPSSYIILEDEDLEVAPkqtfeLIFRLLQ 173
Cdd:TIGR00958 81 ATPSLSSLRALAFWEALDPAVRVALGLWSWFVWSYGAALPAAALWAVLSS-AGASEKEAEQGQSETAD-----LLFRLLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 174 YCKREWLWHISGFSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQR 253
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 254 AIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPII 333
Cdd:TIGR00958 235 RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 334 FVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELF 413
Cdd:TIGR00958 315 FLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 414 QSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKVFEYIDREPQIQHNGEYMPEN 493
Cdd:TIGR00958 395 GMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 494 VVGKIEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIH 573
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEPVLFARSVMENVRYGVEVADTEIIRS-CEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVR 652
Cdd:TIGR00958 555 RQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAaAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 653 EPAILLLDEATSALDTESEHLVQEAiyKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDTnGTYAKLV 732
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
161-739 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 560.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 161 PKQTFELIFRLLQYCKREWLWHISGFSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFR 240
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 241 GGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSW 320
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 321 RLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKA 400
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 401 IAYIGFLWVSELFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKVFEYIDRE 480
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 481 PQIQHNGEYMP-ENVVGKIEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLV 559
Cdd:COG1132 322 PEIPDPPGAVPlPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 560 DGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVA-DTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSG 638
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDAtDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 639 GQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHE 718
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570 580
....*....|....*....|.
gi 71992290 719 TLLKdTNGTYAKLVQRQMMGD 739
Cdd:COG1132 560 ELLA-RGGLYARLYRLQFGEE 579
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
171-735 |
1.35e-153 |
|
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: 460.32 E-value: 1.35e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 171 LLQYCKReWLWHISG-FSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYA 249
Cdd:TIGR02204 9 LWPFVRP-YRGRVLAaLVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 250 RIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFIL 329
Cdd:TIGR02204 88 RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 330 VPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRtKAIAYIGFLWV 409
Cdd:TIGR02204 168 VPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAAR-QRIRTRALLTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 410 SELFQSF-IIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKVFEYIDREPQIQ--HN 486
Cdd:TIGR02204 247 IVIVLVFgAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKapAH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 487 GEYMPENVVGKIEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEE 566
Cdd:TIGR02204 327 PKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 567 FEHHYIHKKIALVGQEPVLFARSVMENVRYG-VEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIA 645
Cdd:TIGR02204 407 LDPAELRARMALVPQDPVLFAASVMENIRYGrPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 646 IARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKdTN 725
Cdd:TIGR02204 487 IARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA-KG 565
|
570
....*....|
gi 71992290 726 GTYAKLVQRQ 735
Cdd:TIGR02204 566 GLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
157-736 |
2.28e-136 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 420.01 E-value: 2.28e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 157 LEVAPKQTFE-------LIFRLLQYCKREW--LWHISGFSwlFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMT 227
Cdd:COG2274 126 LLLEPTPEFDkrgekpfGLRWFLRLLRRYRrlLLQVLLAS--LLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 228 IISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAaDCQTMSDTVALNVNVFLRNCVM 307
Cdd:COG2274 204 LALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLF 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 308 LLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYG 387
Cdd:COG2274 283 VLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWEN 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 388 KLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSV 467
Cdd:COG2274 363 LLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 468 GASRKVFEYIDREPQIQHNGEYM-PENVVGKIEFRNVHFSYPtRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLL 546
Cdd:COG2274 443 IALERLDDILDLPPEREEGRSKLsLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 547 ENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVADTE-IIRSCEMANAHGFIMQTTLKY 625
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEeIIEAARLAGLHDFIEALPMGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 626 ETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVV 705
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
570 580 590
....*....|....*....|....*....|.
gi 71992290 706 INKGRVEQIGNHETLLKdTNGTYAKLVQRQM 736
Cdd:COG2274 682 LDKGRIVEDGTHEELLA-RKGLYAELVQQQL 711
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
185-473 |
1.41e-135 |
|
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: 403.08 E-value: 1.41e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 185 GFSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLV 264
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 265 KQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYY 344
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 345 DLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWY 424
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71992290 425 GGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
498-735 |
6.98e-122 |
|
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: 365.71 E-value: 6.98e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVRYGVEVA-DTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAI 656
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDAtDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 657 LLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKdTNGTYAKLVQRQ 735
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKAQ 238
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
185-473 |
6.47e-121 |
|
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: 365.10 E-value: 6.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 185 GFSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLV 264
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 265 KQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYY 344
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 345 DLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWY 424
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71992290 425 GGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
169-731 |
7.73e-116 |
|
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: 362.11 E-value: 7.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 169 FRLLQYCKREWlwhisgfsWLFIYSITRIFVPYYTGQVIATVVA-------TKSYPALSNAVYIMTIISLVSAVAAGFRG 241
Cdd:TIGR02203 3 RRLWSYVRPYK--------AGLVLAGVAMILVAATESTLAALLKpllddgfGGRDRSVLWWVPLVVIGLAVLRGICSFVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 242 gsfEYAYARIQ----RAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMK 317
Cdd:TIGR02203 75 ---TYLLSWVSnkvvRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 318 LSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFyGKLTHTL---- 393
Cdd:TIGR02203 152 YSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRF-DAVSNRNrrla 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 394 -DVTRTKAI--AYIGFLWVSELfqSFIIVSVLWYGGHLVLTqkmKGDLlVSFLLYQMQLGDNLRQMGEVwTGLMQS-VGA 469
Cdd:TIGR02203 231 mKMTSAGSIssPITQLIASLAL--AVVLFIALFQAQAGSLT---AGDF-TAFITAMIALIRPLKSLTNV-NAPMQRgLAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 470 SRKVFEYIDREPQIQhNGEYMPENVVGKIEFRNVHFSYPTRsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENF 549
Cdd:TIGR02203 304 AESLFTLLDSPPEKD-TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 550 YVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYG--VEVADTEIIRSCEMANAHGFIMQTTLKYET 627
Cdd:TIGR02203 382 YEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrtEQADRAEIERALAAAYAQDFVDKLPLGLDT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 628 NVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVIN 707
Cdd:TIGR02203 462 PIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMD 541
|
570 580
....*....|....*....|....
gi 71992290 708 KGRVEQIGNHETLLkDTNGTYAKL 731
Cdd:TIGR02203 542 DGRIVERGTHNELL-ARNGLYAQL 564
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
487-711 |
4.62e-107 |
|
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: 326.74 E-value: 4.62e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 487 GEYMPENVVGKIEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEE 566
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 567 FEHHYIHKKIALVGQEPVLFARSVMENVRYGV-EVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIA 645
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLqSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 646 IARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRV 711
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
498-731 |
3.04e-98 |
|
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: 304.15 E-value: 3.04e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:cd03251 1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVRYGV-EVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAI 656
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 657 LLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLkDTNGTYAKL 731
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL-AQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
498-735 |
4.24e-98 |
|
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: 303.77 E-value: 4.24e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVRYG-VEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAI 656
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 657 LLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDtNGTYAKLVQRQ 735
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
255-735 |
1.17e-96 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 312.34 E-value: 1.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 255 IRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADC-QTMSDTVALNVNVfLRNCVMLLGSMIFMMKLSWRLSLVTFILVPII 333
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSeQVASSSSGALITV-VREGASIIGLFIMMFYYSWQLSLILIVIAPIV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 334 FVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTH----TLDVTRTKAIAYIgflwV 409
Cdd:PRK11176 179 SIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRmrqqGMKMVSASSISDP----I 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 410 SELFQSFIIVSVLWYGG-HLVLTQKMKGDLLVSF--LLYQMQlgdNLRQMGEVWTGLMQSVGASRKVFEYIDREPQiQHN 486
Cdd:PRK11176 255 IQLIASLALAFVLYAASfPSVMDTLTAGTITVVFssMIALMR---PLKSLTNVNAQFQRGMAACQTLFAILDLEQE-KDE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 487 GEYMPENVVGKIEFRNVHFSYPTRsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEE 566
Cdd:PRK11176 331 GKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 567 FEHHYIHKKIALVGQEPVLFARSVMENVRYGVE--VADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRI 644
Cdd:PRK11176 410 YTLASLRNQVALVSQNVHLFNDTIANNIAYARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRI 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 645 AIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKdT 724
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA-Q 568
|
490
....*....|.
gi 71992290 725 NGTYAKLVQRQ 735
Cdd:PRK11176 569 NGVYAQLHKMQ 579
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
496-722 |
8.75e-95 |
|
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: 294.90 E-value: 8.75e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYptRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKK 575
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVLFARSVMENVRYGVEVA-DTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREP 654
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 655 AILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLK 722
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
167-735 |
2.51e-93 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 304.05 E-value: 2.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 167 LIFRLLQYCKREWLWHISGFSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIIS-----LVSAVAAGFRG 241
Cdd:COG5265 20 LRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAygllrLLSVLFGELRD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 242 GSFEYAYARIQRAIRYDLF---HGLvkqDVAFYDAHKTGEVT---SRLAADCQTMSDTVALNVNVFLRNCVMLLGsmIFM 315
Cdd:COG5265 100 ALFARVTQRAVRRLALEVFrhlHAL---SLRFHLERQTGGLSrdiERGTKGIEFLLRFLLFNILPTLLEIALVAG--ILL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 316 MKLSWRLSLVTFILVpIIFVASKIFGTYYdllseRTQ--------DTiaESNDVAEEVLSTMRTVRSFSCENVEADRFYG 387
Cdd:COG5265 175 VKYDWWFALITLVTV-VLYIAFTVVVTEW-----RTKfrremneaDS--EANTRAVDSLLNYETVKYFGNEAREARRYDE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 388 KLTHtLDVTRTKAIAYIGFLWVSelfQSFII----VSVLWYGGHLVLTQKMK-GDL-LVSFLLyqMQLGDNLRQMGEVWT 461
Cdd:COG5265 247 ALAR-YERAAVKSQTSLALLNFG---QALIIalglTAMMLMAAQGVVAGTMTvGDFvLVNAYL--IQLYIPLNFLGFVYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 462 GLMQSVGASRKVFEYIDREPQIQHNGEYMPENVV-GKIEFRNVHFSYptRSDQPILKDLSFTVEPGETVALVGPSGSGKS 540
Cdd:COG5265 321 EIRQALADMERMFDLLDQPPEVADAPDAPPLVVGgGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 541 SCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYG-VEVADTEIIRSCEMANAHGFIM 619
Cdd:COG5265 399 TLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGrPDASEEEVEAAARAAQIHDFIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 620 QTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEK 699
Cdd:COG5265 479 SLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVD 558
|
570 580 590
....*....|....*....|....*....|....*..
gi 71992290 700 ADKIVVINKGR-VEQiGNHETLLKdTNGTYAKLVQRQ 735
Cdd:COG5265 559 ADEILVLEAGRiVER-GTHAELLA-QGGLYAQMWARQ 593
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
250-734 |
5.25e-92 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 299.37 E-value: 5.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 250 RIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADcqtmSDTValnVNVFLR-------NCVMLLGSMIFMMKLSWRL 322
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVAD----VDAL---DNLYLRvllpllvALLVILAAVAFLAFFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 323 SLVTFI-LVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAI 401
Cdd:COG4987 158 ALVLALgLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 402 AYIGFLWVSELFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKVFEYIDREP 481
Cdd:COG4987 238 LSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 482 QIQHNGEYMPENVVGKIEFRNVHFSYPTrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG 561
Cdd:COG4987 318 AVTEPAEPAPAPGGPSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 562 VPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGV-EVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQ 640
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 641 KQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETL 720
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|....
gi 71992290 721 LKdTNGTYAKLVQR 734
Cdd:COG4987 557 LA-QNGRYRQLYQR 569
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
170-722 |
6.85e-92 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 298.98 E-value: 6.85e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 170 RLLQYCK--REWLWHISGFSWLFiySITRIFVPYYTGQVIATVVA-TKSYPALSNAVYIMTIISLVSAVAAGFRGG-SFE 245
Cdd:COG4988 7 RLKRLARgaRRWLALAVLLGLLS--GLLIIAQAWLLASLLAGLIIgGAPLSALLPLLGLLLAVLLLRALLAWLRERaAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 246 YAyARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTsrlaadcQTMSDTVAlNVNVFLRN-----------CVMLLGSMIF 314
Cdd:COG4988 85 AA-ARVKRRLRRRLLEKLLALGPAWLRGKSTGELA-------TLLTEGVE-ALDGYFARylpqlflaalvPLLILVAVFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 315 mmkLSWRLSLVTFILVPII--FVAskIFGTYYDLLSERTQDTIAE-SNDVAEeVLSTMRTVRSFSCENVEADRFYgKLTH 391
Cdd:COG4988 156 ---LDWLSGLILLVTAPLIplFMI--LVGKGAAKASRRQWRALARlSGHFLD-RLRGLTTLKLFGRAKAEAERIA-EASE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 392 -----TLDVTRtkaiayIGFL--WVSELFQSFIIVSVLWYGGHLVLTQKMkgDLLVSFLL-------YQmqlgdNLRQMG 457
Cdd:COG4988 229 dfrkrTMKVLR------VAFLssAVLEFFASLSIALVAVYIGFRLLGGSL--TLFAALFVlllapefFL-----PLRDLG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 458 EVWTGLMQSVGASRKVFEYIDREPQIQHNGE-YMPENVVGKIEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSG 536
Cdd:COG4988 296 SFYHARANGIAAAEKIFALLDAPEPAAPAGTaPLPAAGPPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 537 SGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVA-DTEIIRSCEMANAH 615
Cdd:COG4988 374 AGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDAsDEELEAALEAAGLD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 616 GFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLS 695
Cdd:COG4988 454 EFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLA 533
|
570 580
....*....|....*....|....*..
gi 71992290 696 TVEKADKIVVINKGRVEQIGNHETLLK 722
Cdd:COG4988 534 LLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
498-710 |
1.09e-83 |
|
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: 263.47 E-value: 1.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVrygvevadteiirscemanahgfimqttlkyetnvgekgtqMSGGQKQRIAIARALVREPAIL 657
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71992290 658 LLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGR 710
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
498-735 |
9.96e-83 |
|
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: 263.58 E-value: 9.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptRSDQP-ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKI 576
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPVLFARSVMENVRYGVEVADTE-IIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPA 655
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMErVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 656 ILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLkDTNGTYAKLVQRQ 735
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-AENGLYAYLYQLQ 237
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
185-473 |
2.34e-82 |
|
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: 264.42 E-value: 2.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 185 GFSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLV 264
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 265 KQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYY 344
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 345 DLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWY 424
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71992290 425 GGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
185-735 |
5.62e-80 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 270.85 E-value: 5.62e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 185 GFSWlFIYSITR-------------------IFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFE 245
Cdd:TIGR01846 126 GFSW-FIPAIIRyrkqfrevllislalqlfaLVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 246 YAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLaadcQTMSdtvalNVNVFLRNCVM-----LLGSMIF---MMK 317
Cdd:TIGR01846 205 HLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARV----RELE-----QIRNFLTGSALtvvldLLFVVVFlavMFF 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 318 LSWRLSLVTFILVPIIFVASKIFGTyydLLSERTQD---TIAESNDVAEEVLSTMRTVRSFSCE---NVEADRFYGKLTH 391
Cdd:TIGR01846 276 YSPTLTGVVIGSLVCYALLSVFVGP---ILRKRVEDkfeRSAAATSFLVESVTGIETIKATATEpqfQNRWDRQLAAYVA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 392 T-LDVTRTKAIAYIGFlwvsELFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGAS 470
Cdd:TIGR01846 353 AsFRVTNLGNIAGQAI----ELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIAL 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 471 RKVFEYIDREPQIQHNGEYMPENVVGKIEFRNVHFSYptRSDQP-ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENF 549
Cdd:TIGR01846 429 ERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRL 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 550 YVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVADTE-IIRSCEMANAHGFIMQTTLKYETN 628
Cdd:TIGR01846 507 YTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEhVIHAAKLAGAHDFISELPQGYNTE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 629 VGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINK 708
Cdd:TIGR01846 587 VGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEK 666
|
570 580
....*....|....*....|....*..
gi 71992290 709 GRVEQIGNHETLLKdTNGTYAKLVQRQ 735
Cdd:TIGR01846 667 GQIAESGRHEELLA-LQGLYARLWQQQ 692
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
316-749 |
4.80e-78 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 262.97 E-value: 4.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 316 MKLSWRLSLVTFILVpIIFVA------SKIFG------TYYDLLSERTQDTIaeSNdVAeevlstmrTVRSFS--CENVE 381
Cdd:PRK13657 152 LFMNWRLSLVLVVLG-IVYTLittlvmRKTKDgqaaveEHYHDLFAHVSDAI--GN-VS--------VVQSYNriEAETQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 382 ADRFYGK--LTHTLDVTRTKAIAYIgflwVSELFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEV 459
Cdd:PRK13657 220 ALRDIADnlLAAQMPVLSWWALASV----LNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 460 WTGLMQSVGASRKVFEYIDREPQIQ---HNGEymPENVVGKIEFRNVHFSYPTRSdqPILKDLSFTVEPGETVALVGPSG 536
Cdd:PRK13657 296 INQVFMAAPKLEEFFEVEDAVPDVRdppGAID--LGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 537 SGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVA-DTEIIRSCEMANAH 615
Cdd:PRK13657 372 AGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDAtDEEMRAAAERAQAH 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 616 GFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLS 695
Cdd:PRK13657 452 DFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLS 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 696 TVEKADKIVVINKGRVEQIGNHETLLkDTNGTYAKLVQRQ-MMGDQKPRKRPAVA 749
Cdd:PRK13657 532 TVRNADRILVFDNGRVVESGSFDELV-ARGGRFAALLRAQgMLQEDERRKQPAAE 585
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
185-473 |
3.15e-73 |
|
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: 240.32 E-value: 3.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 185 GFSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLV 264
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 265 KQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYY 344
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 345 DLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWY 424
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71992290 425 GGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18590 241 GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
197-740 |
3.32e-73 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 250.02 E-value: 3.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 197 IFVPYYtgqvIATVVATKSYPALSNAVYIMTIISL--VSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAH 274
Cdd:PRK10790 44 LLISYF----IDNMVAKGNLPLGLVAGLAAAYVGLqlLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 275 KTGEVTSRLAADCQTMSDtvaLNVNVF---LRnCVMLLGSM-IFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSER 350
Cdd:PRK10790 120 PVGQLISRVTNDTEVIRD---LYVTVVatvLR-SAALIGAMlVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 351 TQDTIAESNDVAEEVLSTMRTVRSFScenvEADRFYGKL---THTLDVTRTKAIAYIGFLW--VSELFQSFIIVSVLWYG 425
Cdd:PRK10790 196 VRAYLADINDGFNEVINGMSVIQQFR----QQARFGERMgeaSRSHYMARMQTLRLDGFLLrpLLSLFSALILCGLLMLF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 426 GhLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKVFEYIDRePQiQHNGEYMPENVVGKIEFRNVHF 505
Cdd:PRK10790 272 G-FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDG-PR-QQYGNDDRPLQSGRIDIDNVSF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 506 SYptRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVL 585
Cdd:PRK10790 349 AY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 586 FARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSA 665
Cdd:PRK10790 427 LADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 666 LDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKdTNGTYAKLVQRQMMGDQ 740
Cdd:PRK10790 507 IDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA-AQGRYWQMYQLQLAGEE 580
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
189-473 |
1.27e-72 |
|
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: 239.07 E-value: 1.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATVVA------TKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHG 262
Cdd:cd18780 5 LLVSSGTNLALPYFFGQVIDAVTNhsgsggEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 263 LVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGT 342
Cdd:cd18780 85 IIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 343 YYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVL 422
Cdd:cd18780 165 YVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 71992290 423 WYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18780 245 WYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
204-706 |
1.33e-68 |
|
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: 235.64 E-value: 1.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 204 GQVIATVVATKSYPA-LSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSR 282
Cdd:TIGR02857 27 ARVVDGLISAGEPLAeLLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 283 LAADCQTMSDTVALNVNVfLRNCVML-LGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDV 361
Cdd:TIGR02857 107 ALEGVEALDGYFARYLPQ-LVLAVIVpLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 362 AEEVLSTMRTVRSFSCENVEADRfygkLTHTLDVTR--TKAIAYIGFL--WVSELFQSFIIVSVLWYGGHLVLTQKMkgD 437
Cdd:TIGR02857 186 FLDRLRGLPTLKLFGRAKAQAAA----IRRSSEEYRerTMRVLRIAFLssAVLELFATLSVALVAVYIGFRLLAGDL--D 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 438 LLVSFL-------LYQmqlgdNLRQMGEVWTGLMQSVGASRKVFEYIDREPQIQHNGEYMPENVVGKIEFRNVHFSYPTR 510
Cdd:TIGR02857 260 LATGLFvlllapeFYL-----PLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 511 SdqPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSV 590
Cdd:TIGR02857 335 R--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENVRYGV-EVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTE 669
Cdd:TIGR02857 413 AENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
490 500 510
....*....|....*....|....*....|....*..
gi 71992290 670 SEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVI 706
Cdd:TIGR02857 493 TEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
496-711 |
9.45e-66 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 217.84 E-value: 9.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYPTrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKK 575
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVLFARSVMENVRYGVEVADTE-IIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREP 654
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 655 AILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRV 711
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
189-473 |
1.15e-64 |
|
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: 217.77 E-value: 1.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATVVATKSYPA-----LSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGL 263
Cdd:cd18573 5 LLVSSAVTMSVPFAIGKLIDVASKESGDIEifglsLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 264 VKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTY 343
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 344 YDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLW 423
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 71992290 424 YGGHLVLTQKMK-GDlLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18573 245 YGGSLVASGELTvGD-LTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
190-732 |
2.05e-63 |
|
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: 225.77 E-value: 2.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 190 FIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVA 269
Cdd:TIGR01193 166 IIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 270 FYDAHKTGEVTSRLAaDCQTMSDTVALNV-NVFLrNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLS 348
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALASTIlSLFL-DMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLN 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 349 ERTQDTIAESNDVAEEVLSTMRTVRSFsceNVEADRfYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFI----IVSVLWY 424
Cdd:TIGR01193 324 HDAMQANAVLNSSIIEDLNGIETIKSL---TSEAER-YSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTklilNVVILWT 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 425 GGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKVFE--YIDREPQIQHNGEYMpENVVGKIEFRN 502
Cdd:TIGR01193 400 GAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEFINKKKRTEL-NNLNGDIVIND 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 503 VHFSYPTRSdqPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQE 582
Cdd:TIGR01193 479 VSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQE 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 583 PVLFARSVMENVRYGVE--VADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLD 660
Cdd:TIGR01193 557 PYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 661 EATSALDTESEHLVQEAIYkNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLkDTNGTYAKLV 732
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYASLI 706
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
189-721 |
5.30e-63 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 221.51 E-value: 5.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGqVIATVVATKSYPALSNAVYIMTIIsLVSAVAAGFR--------GGSFEYAYAriqraIRYDLF 260
Cdd:PRK10789 4 LIIIAMLQLIPPKVVG-IIVDGVTEQHMTTGQILMWIGTMV-LIAVVVYLLRyvwrvllfGASYQLAVE-----LREDFY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 261 HGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFM-MKLSWRLSLVTFILVPIIFVASKI 339
Cdd:PRK10789 77 RQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 340 FGtyyDLLSER---TQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHT----LDVTRTKAiayigflwvseL 412
Cdd:PRK10789 157 YG---DQLHERfklAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTgkknMRVARIDA-----------R 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 413 FQSFIIVSV-----LWYGG--HLVLTQKMKGDLLVSFLLYqmqlgdnLRQMgeVWTGL----MQSV-----GASRKVFEY 476
Cdd:PRK10789 223 FDPTIYIAIgmanlLAIGGgsWMVVNGSLTLGQLTSFVMY-------LGLM--IWPMLalawMFNIvergsAAYSRIRAM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 477 IDREPQIQHNGEYMPENVvGKIEFRNVHFSYPTrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQ 556
Cdd:PRK10789 294 LAEAPVVKDGSEPVPEGR-GELDVNIRQFTYPQ-TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 557 VLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVA-DTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQ 635
Cdd:PRK10789 372 IRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDAtQQEIEHVARLASVHDDILRLPQGYDTEVGERGVM 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 636 MSGGQKQRIAIARALVREPAILLLDEATSALDTESEHlvqeAIYKNL----DGKSVILIAHRLSTVEKADKIVVINKGRV 711
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH----QILHNLrqwgEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
570
....*....|
gi 71992290 712 EQIGNHETLL 721
Cdd:PRK10789 528 AQRGNHDQLA 537
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
198-736 |
2.25e-61 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 219.44 E-value: 2.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 198 FVPYYTGQVIATVVATKSYPALSNavyiMTIISLVSAVAAGfrggSFEYAYA----RIQRAIRYDLFHG----LVKQDVA 269
Cdd:TIGR03797 154 LVPIATGILIGTAIPDADRSLLVQ----IALALLAAAVGAA----AFQLAQSlavlRLETRMDASLQAAvwdrLLRLPVS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 270 FYDAHKTGEVTSRLAADCQ---TMSDTVALNV--NVFlrnCVMLLGSMIFMmklSWRLSLVTfILVPIIFVASKIFGTYY 344
Cdd:TIGR03797 226 FFRQYSTGDLASRAMGISQirrILSGSTLTTLlsGIF---ALLNLGLMFYY---SWKLALVA-VALALVAIAVTLVLGLL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 345 DLLSERTQdtIAESNDVAEEVLSTMRTVRSFSCENVEADRFY---GKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSV 421
Cdd:TIGR03797 299 QVRKERRL--LELSGKISGLTVQLINGISKLRVAGAENRAFArwaKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAAL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 422 LWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKVFEYIDREPQIQHNGeYMPENVVGKIEFR 501
Cdd:TIGR03797 377 FAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAK-TDPGKLSGAIEVD 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 502 NVHFSYptRSDQP-ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVG 580
Cdd:TIGR03797 456 RVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 581 QEPVLFARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLD 660
Cdd:TIGR03797 534 QNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFD 613
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 661 EATSALDTESEHLVQEaiykNLDGKSV--ILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKdTNGTYAKLVQRQM 736
Cdd:TIGR03797 614 EATSALDNRTQAIVSE----SLERLKVtrIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA-REGLFAQLARRQL 686
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
250-733 |
5.52e-61 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 224.14 E-value: 5.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 250 RIQRAIRYDLFHGLVKQDVAFYD--AHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMklsWRLSLVTF 327
Cdd:PTZ00265 896 KVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSF---YFCPIVAA 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 328 ILVPIIFVASKIFGTYYDLLSERTQD---------TIAESND---------VAEEVLSTMRTVRSFSCEnveaDRFYGKL 389
Cdd:PTZ00265 973 VLTGTYFIFMRVFAIRARLTANKDVEkkeinqpgtVFAYNSDdeifkdpsfLIQEAFYNMNTVIIYGLE----DYFCNLI 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 390 THTLDVT---RTKAIAYIGFLW-VSELFQSFIIVSVLWYGGHLVLTQKMKGD----LLVSFLLYQMQLGDNLRQMGEVWT 461
Cdd:PTZ00265 1049 EKAIDYSnkgQKRKTLVNSMLWgFSQSAQLFINSFAYWFGSFLIRRGTILVDdfmkSLFTFLFTGSYAGKLMSLKGDSEN 1128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 462 GLMqsvgASRKVFEYIDREPQI--QHNGEYMPEN---VVGKIEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSG 536
Cdd:PTZ00265 1129 AKL----SFEKYYPLIIRKSNIdvRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETG 1204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 537 SGKSSCISLLENFY------------------------------------------------------VPNAGQVLVDGV 562
Cdd:PTZ00265 1205 SGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvFKNSGKILLDGV 1284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 563 PLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVADTE-IIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQK 641
Cdd:PTZ00265 1285 DICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREdVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQK 1364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 642 QRIAIARALVREPAILLLDEATSALDTESEHLVQEAIY--KNLDGKSVILIAHRLSTVEKADKIVVINK-----GRVEQI 714
Cdd:PTZ00265 1365 QRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAH 1444
|
570
....*....|....*....
gi 71992290 715 GNHETLLKDTNGTYAKLVQ 733
Cdd:PTZ00265 1445 GTHEELLSVQDGVYKKYVK 1463
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
496-716 |
3.86e-60 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 202.72 E-value: 3.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYptRSD-QPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHK 574
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREP 654
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 655 AILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGN 716
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
187-473 |
9.95e-60 |
|
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: 204.24 E-value: 9.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 187 SWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQ 266
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 267 DVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDL 346
Cdd:cd18589 83 EIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 347 LSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWYGG 426
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 71992290 427 HLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18589 243 QLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
223-741 |
2.68e-59 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 219.13 E-value: 2.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 223 VYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFL 302
Cdd:PTZ00265 100 IFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIF 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 303 RNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENV-- 380
Cdd:PTZ00265 180 TYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTil 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 381 ----EADRFYGKLTHTLDVTRTKAIAYI-GFLWVSELFQsfiivsvLWYGGHLVLT----QKMKGD--------LLVSFL 443
Cdd:PTZ00265 260 kkfnLSEKLYSKYILKANFMESLHIGMInGFILASYAFG-------FWYGTRIIISdlsnQQPNNDfhggsvisILLGVL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 444 LYQMQLGDNLRQMGEvwtgLMQSVGASRKVFEYIDREPQIQHN--GEYMPEnvVGKIEFRNVHFSYPTRSDQPILKDLSF 521
Cdd:PTZ00265 333 ISMFMLTIILPNITE----YMKSLEATNSLYEIINRKPLVENNddGKKLKD--IKKIQFKNVRFHYDTRKDVEIYKDLNF 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 522 TVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLV-DGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGV-- 598
Cdd:PTZ00265 407 TLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLys 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 599 --------------------------------------------------------EVADTEIIRSCEMANAHGFIMQTT 622
Cdd:PTZ00265 487 lkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALP 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 623 LKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNLDG---KSVILIAHRLSTVEK 699
Cdd:PTZ00265 567 DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI-NNLKGnenRITIIIAHRLSTIRY 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 700 ADKIVVI-------------------------------------NKGRVEQIGN----------HETLLKDTNGTYAKLV 732
Cdd:PTZ00265 646 ANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnNNNNNNKINNagsyiieqgtHDALMKNKNGIYYTMI 725
|
....*....
gi 71992290 733 QRQMMGDQK 741
Cdd:PTZ00265 726 NNQKVSSKK 734
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
189-473 |
3.81e-58 |
|
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: 199.63 E-value: 3.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDV 268
Cdd:cd18576 5 LLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 269 AFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLS 348
Cdd:cd18576 85 SFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 349 ERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWYGGHL 428
Cdd:cd18576 165 KKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 71992290 429 VLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18576 245 VLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
463-735 |
3.47e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 199.67 E-value: 3.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 463 LMQSVGASRKVFEYIDREPQIQHNGEYMPENVVGKIEFRNVHFSYPTRSdQPILKDLSFTVEPGETVALVGPSGSGKSSC 542
Cdd:PRK11160 304 LGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 543 ISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVADTEIIrsCEMANAHGF--IMQ 620
Cdd:PRK11160 383 LQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEAL--IEVLQQVGLekLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 621 TTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKA 700
Cdd:PRK11160 461 DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF 540
|
250 260 270
....*....|....*....|....*....|....*
gi 71992290 701 DKIVVINKGRVEQIGNHETLLKDtNGTYAKLVQRQ 735
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLAQ-QGRYYQLKQRL 574
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
453-735 |
6.19e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 196.60 E-value: 6.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 453 LRQMGEVWTGLMQSVGASRKVFEYIDREPQIQHNGE-YMPENVVGKIEFRN-VHFSYptrSDQPILKDLSFTVEPGETVA 530
Cdd:PRK11174 304 LRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEkELASNDPVTIEAEDlEILSP---DGKTLAGPLNFTLPAGQRIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 531 LVGPSGSGKSSCISLLENFyVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYG-VEVADTEIIRSC 609
Cdd:PRK11174 381 LVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGnPDASDEQLQQAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 610 EMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVIL 689
Cdd:PRK11174 460 ENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLM 539
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 71992290 690 IAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDTNGTYAKLVQRQ 735
Cdd:PRK11174 540 VTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
496-722 |
7.73e-53 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 193.04 E-value: 7.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYPtRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPL-----EEFEHH 570
Cdd:COG4618 329 GRLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdrEELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 571 yihkkialVG---QEPVLFARSVMENV-RYGvEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAI 646
Cdd:COG4618 408 --------IGylpQDVELFDGTIAENIaRFG-DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 647 ARALVREPAILLLDEATSALDTESEHLVQEAIyKNL--DGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLK 722
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALkaRGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
498-723 |
1.20e-50 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 177.14 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPV--LFARSVMENVRYGVE---VADTEII-RSCEMANAHGfiMQTTLKYETNvgekgtQMSGGQKQRIAIARALV 651
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPEnlgLPREEIReRVEEALELVG--LEHLADRPPH------ELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKD 723
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
498-711 |
4.97e-50 |
|
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: 173.17 E-value: 4.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSdQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:cd03246 1 LEVENVSFRYPGAE-PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVrygvevadteiirscemanahgfimqttlkyetnvgekgtqMSGGQKQRIAIARALVREPAIL 657
Cdd:cd03246 80 YLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 658 LLDEATSALDTESEHLVQEAIyKNLD--GKSVILIAHRLSTVEKADKIVVINKGRV 711
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAI-AALKaaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
498-715 |
6.45e-50 |
|
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: 173.27 E-value: 6.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyIHKKIA 577
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVrygvevadteiirscemanahgfimqttlkyetnvgekGTQMSGGQKQRIAIARALVREPAIL 657
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 658 LLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIG 715
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
250-694 |
2.22e-49 |
|
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: 182.56 E-value: 2.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 250 RIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTValnVNVFLRNCVMLLGSMIFMMKLSWRLS------ 323
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLY---VRVIVPAGVALVVGAAAVAAIAVLSVpaalil 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 324 ----LVTFILVPIIFV-ASKIFGTYYDLL-SERTQDTIAESNDVAEEVLS-----TMRTVRsfscenvEADRFYGKLtht 392
Cdd:TIGR02868 160 aaglLLAGFVAPLVSLrAARAAEQALARLrGELAAQLTDALDGAAELVASgalpaALAQVE-------EADRELTRA--- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 393 ldVTRTKAIAYIGFLwVSELFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRK 472
Cdd:TIGR02868 230 --ERRAAAATALGAA-LTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAER 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 473 VFEYIDREPQIQ----HNGEYMPENVVGkIEFRNVHFSYPTrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLEN 548
Cdd:TIGR02868 307 IVEVLDAAGPVAegsaPAAGAVGLGKPT-LELRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 549 FYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGV-EVADTEIIRSCEMANAHGFIMQTTLKYET 627
Cdd:TIGR02868 384 LLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDT 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 628 NVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRL 694
Cdd:TIGR02868 464 VLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
421-722 |
2.23e-49 |
|
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: 182.55 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 421 VLWYGGHLVLTQKMK-GDLLVSFLLYQMQLGDnLRQMGEVWTGLMQSVGASRKVFEYIDREPQiqhNGEYMP-ENVVGKI 498
Cdd:TIGR01842 242 VLGLGAYLAIDGEITpGMMIAGSILVGRALAP-IDGAIGGWKQFSGARQAYKRLNELLANYPS---RDPAMPlPEPEGHL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 499 EFRNVHFSyPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIAL 578
Cdd:TIGR01842 318 SVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGY 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 579 VGQEPVLFARSVMENV-RYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAIL 657
Cdd:TIGR01842 397 LPQDVELFPGTVAENIaRFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLV 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 658 LLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLK 722
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKAlKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
498-711 |
2.40e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.00 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:COG4619 1 LELEGLSFRV---GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVRYGVEVADTEIIRS--CEMANAHGF---IMQTTLkyetnvgekgTQMSGGQKQRIAIARALVR 652
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDREraLELLERLGLppdILDKPV----------ERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 653 EPAILLLDEATSALDTESEHLVQEAI--YKNLDGKSVILIAH------RLstvekADKIVVINKGRV 711
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLreYLAEEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
185-473 |
8.49e-48 |
|
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: 171.19 E-value: 8.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 185 GFSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLV 264
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 265 KQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYY 344
Cdd:cd07346 84 RLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 345 DLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLT----HTLDVTRTKAIAYIgflwVSELFQSFIIVS 420
Cdd:cd07346 164 RKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRdlrdANLRAARLSALFSP----LIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 71992290 421 VLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
498-714 |
4.23e-47 |
|
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: 166.88 E-value: 4.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQ-PILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfehhyIHKKI 576
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPVLFA-RSVMENVRYGVE---VADTEIirsceMANAHGFIMQttlkyetnVGEKGT------QMSGGQKQRIAI 646
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqgVPKAEA-----RERAEELLEL--------VGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71992290 647 ARALVREPAILLLDEATSALDTESEHLVQEAIYKNL--DGKSVILIAHRLS-TVEKADKIVVINK--GRVEQI 714
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
189-470 |
9.46e-47 |
|
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: 168.05 E-value: 9.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRggsfeyAYA------RIQRAIRYDLFHG 262
Cdd:cd18575 5 LLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR------FYLvswlgeRVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 263 LVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGT 342
Cdd:cd18575 79 LLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 343 YYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVT--RTKAIAYIGFLWVSELFQSfiIVS 420
Cdd:cd18575 159 RVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAAlrRIRARALLTALVIFLVFGA--IVF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 71992290 421 VLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGAS 470
Cdd:cd18575 237 VLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAA 286
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
499-710 |
1.12e-46 |
|
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: 165.33 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 499 EFRNVHFSYPTRsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIAL 578
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 579 VGQEP--VLFARSVMENVRYGVE---VADTEIIRSCEMANAHgFIMQTTLKYETNvgekgtQMSGGQKQRIAIARALVRE 653
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLEnlgLPEEEIEERVEEALEL-VGLEGLRDRSPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 654 PAILLLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTV-EKADKIVVINKGR 710
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
498-724 |
1.21e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.01 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfEHHYIHKKIA 577
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVR-----YGVEVADT-----EIIRSCEMANahgfimqttlKYETNVGekgtQMSGGQKQRIAI 646
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEAreridELLELFGLTD----------AADRKVG----TLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 647 ARALVREPAILLLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKDT 724
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
497-714 |
5.43e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 162.18 E-value: 5.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 497 KIEFRNVHFSYPTRS-DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfehhyIHKK 575
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVLFA-RSVMENVRYGVEVADTEIIRSCEMANAHgfimqttLKyetNVGEKG------TQMSGGQKQRIAIAR 648
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERAREL-------LE---LVGLAGfedaypHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 649 ALVREPAILLLDEATSALD--------TESEHLVQEaiyknlDGKSVILIAH------RLstvekADKIVVINK--GRVE 712
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDaltrerlqDELLRLWQE------TGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIV 220
|
..
gi 71992290 713 QI 714
Cdd:COG1116 221 EE 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
498-711 |
7.59e-45 |
|
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: 158.71 E-value: 7.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfEHHYIHKKIA 577
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVRYgvevadteiirscemanahgfimqttlkyetnvgekgtqmSGGQKQRIAIARALVREPAI 656
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL----------------------------------------SGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 657 LLLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
498-715 |
2.37e-44 |
|
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: 158.84 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG-----VPLEEfehhyi 572
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgVPPER------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 hKKIALVGQEPVLFA-RSVMENVRYGVE---VADTEIIRSCEMANAHgfimqttLKYETNVGEKGTQMSGGQKQRIAIAR 648
Cdd:cd03259 72 -RNIGMVFQDYALFPhLTVAENIAFGLKlrgVPKAEIRARVRELLEL-------VGLEGLLNRYPHELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 649 ALVREPAILLLDEATSALDTES-EHLVQE--AIYKNLdGKSVILIAHRLS-TVEKADKIVVINKGRVEQIG 715
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLrEELREElkELQREL-GITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
498-713 |
3.67e-44 |
|
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: 158.82 E-value: 3.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTR-SDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG---VPLEEFEHHYIH 573
Cdd:cd03257 2 LEVKNLSVSFPTGgGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEPvlfARSVmeNVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGT-------QMSGGQKQRIAI 646
Cdd:cd03257 82 KEIQMVFQDP---MSSL--NPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 647 ARALVREPAILLLDEATSALDTESEHLVQEAIY--KNLDGKSVILIAHRLSTVEK-ADKIVVINKGR-VEQ 713
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKiVEE 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
498-711 |
3.76e-44 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 158.42 E-value: 3.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQ-PILKDLSFTVEPGETVALVGPSGSGKS---SCISLLEnfyVPNAGQVLVDGVPL----EEFEH 569
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKStllNILGGLD---RPTSGEVRVDGTDIsklsEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 570 HYIHKKIALVGQEPVLFAR-SVMENVRYGVEVAdtEIIRSCEMANAHGFImqTTLKYETNVGEKGTQMSGGQKQRIAIAR 648
Cdd:cd03255 78 AFRRRHIGFVFQSFNLLPDlTALENVELPLLLA--GVPKKERRERAEELL--ERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 649 ALVREPAILLLDEATSALDTESEHLVQEAIYK--NLDGKSVILIAHRLSTVEKADKIVVINKGRV 711
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
498-710 |
3.78e-44 |
|
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: 158.02 E-value: 3.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQ--PILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVlvdgvpleefehhYIHKK 575
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVLFARSVMENVRYGVEVaDTE----IIRSCEmanahgfiMQTTLKY-----ETNVGEKGTQMSGGQKQRIAI 646
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPF-DEEryekVIKACA--------LEPDLEIlpdgdLTEIGEKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 647 ARALVREPAILLLDEATSALDTE-SEHLVQEAIYKNL-DGKSVILIAHRLSTVEKADKIVVINKGR 710
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
498-730 |
4.17e-44 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 159.58 E-value: 4.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRS-DQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDGVPLEEFEHHYIH 573
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEPvlfARSVmeNVRYGVEvadtEIIRscEMANAHGF--IMQTTLKYETNVGEKGT-------QMSGGQKQRI 644
Cdd:COG1124 79 RRVQMVFQDP---YASL--HPRHTVD----RILA--EPLRIHGLpdREERIAELLEQVGLPPSfldryphQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 645 AIARALVREPAILLLDEATSALDTesehLVQEAI------YKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNH 717
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDV----SVQAEIlnllkdLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTV 223
|
250
....*....|...
gi 71992290 718 ETLLKDTNGTYAK 730
Cdd:COG1124 224 ADLLAGPKHPYTR 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
498-730 |
4.88e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 166.62 E-value: 4.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRS--DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEH---HYI 572
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 HKKIALVGQEPV--LFAR-SVMENVRYGVEVADT-----------EIIRSC----EMANAHGFimqttlkyetnvgekgt 634
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPLRLHGLlsraerrervaELLERVglppDLADRYPH----------------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 635 QMSGGQKQRIAIARALVREPAILLLDEATSALDTesehLVQEAIYKNLD------GKSVILIAHRLSTVEK-ADKIVVIN 707
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMY 479
|
250 260
....*....|....*....|...
gi 71992290 708 KGRVEQIGNHETLLKDTNGTYAK 730
Cdd:COG1123 480 DGRIVEDGPTEEVFANPQHPYTR 502
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
498-715 |
6.59e-44 |
|
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: 159.52 E-value: 6.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGV-PLEEFEHHYIHKKI 576
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEP--VLFARSVMENVRYGVE---VADTEIIRSCEMA-NAHGfiMQTTLKYETNvgekgtQMSGGQKQRIAIARAL 650
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLEnlgVPREEMRKRVDEAlKLVG--MEDFRDREPH------LLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 651 VREPAILLLDEATSALDTESEHLVQEAIyKNL---DGKSVILIAHRLSTVEKADKIVVINKGRVEQIG 715
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETI-RKLnkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
189-449 |
8.23e-44 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 159.35 E-value: 8.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYA--RIQRAIRYDLFHGLVKQ 266
Cdd:pfam00664 8 AILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTgeRLSRRLRRKLFKKILRQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 267 DVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDL 346
Cdd:pfam00664 88 PMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 347 LSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWYGG 426
Cdd:pfam00664 168 LSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGA 247
|
250 260
....*....|....*....|...
gi 71992290 427 HLVLTQKMKGDLLVSFLLYQMQL 449
Cdd:pfam00664 248 YLVISGELSVGDLVAFLSLFAQL 270
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
496-715 |
9.37e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 157.19 E-value: 9.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYptRSDQP-ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHK 574
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEmanahgfimqttlkyetnVGEKGTQMSGGQKQRIAIARALVREP 654
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 655 AILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIG 715
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
498-711 |
1.11e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 155.40 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIhKKIA 577
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVRYGVE---VADTEIIRSCEMAnAHGFIMQTTLKyeTNVGEkgtqMSGGQKQRIAIARALVRE 653
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAElygLFDEELKKRIEEL-IELLGLEEFLD--RRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 654 PAILLLDEATSALDTESEHLVQEAIyKNL--DGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREIL-RALkkEGKTVLFSSHIMQEVEAlCDRVVILHKGKV 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
499-710 |
1.75e-42 |
|
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: 151.63 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 499 EFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIAL 578
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 579 VGQepvlfarsvmenvrygvevadteiirscemanahgfimqttlkyetnvgekgtqMSGGQKQRIAIARALVREPAILL 658
Cdd:cd00267 78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71992290 659 LDEATSALDTESEHLVQEAIYKNLD-GKSVILIAHRLSTVEKA-DKIVVINKGR 710
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
498-721 |
7.79e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 153.28 E-value: 7.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRsdqPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVL-FARSVMENVRYG----------VEVADTEIIRSC-EMANAHGFIMQTTlkyetnvgekgTQMSGGQKQRIA 645
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgrPSAEDREAVEEAlERTGLEHLADRPV-----------DELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 646 IARALVREPAILLLDEATSALDTESEHLVQEAIyKNL---DGKSVILIAH------RLstvekADKIVVINKGRVEQIGN 716
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELL-RRLareRGRTVVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGP 221
|
....*
gi 71992290 717 HETLL 721
Cdd:COG1120 222 PEEVL 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
253-722 |
1.28e-41 |
|
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: 164.73 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 253 RAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPI 332
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLL 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 333 IFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFScenvEADRFYGKLTHTLDVTRTKAIAYI-GFLWVSE 411
Cdd:TIGR00957 1118 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE----EQERFIHQSDLKVDENQKAYYPSIvANRWLAV 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 412 LFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLL-YQMQLGDNLRQMGEVWTGLMQSVGASRKVFEY--IDREPQIQHNGE 488
Cdd:TIGR00957 1194 RLECVGNCIVLFAALFAVISRHSLSAGLVGLSVsYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYseTEKEAPWQIQET 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 489 YMPEN--VVGKIEFRNVHFSYPTRSDQpILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEE 566
Cdd:TIGR00957 1274 APPSGwpPRGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK 1352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 567 FEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAI 646
Cdd:TIGR00957 1353 IGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCL 1432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 647 ARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLK 722
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
498-713 |
1.84e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 151.69 E-value: 1.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLEnfyVPNAGQVLVDGVPL--EEFEHHYI 572
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLE---EPDSGTITVDGEDLtdSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 HKKIALVGQEPVLFA-RSVMENVRYG-VEVADteiiRSCEMANAHGfimqttLKYETNVG--EKG----TQMSGGQKQRI 644
Cdd:COG1126 76 RRKVGMVFQQFNLFPhLTVLENVTLApIKVKK----MSKAEAEERA------MELLERVGlaDKAdaypAQLSGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 645 AIARALVREPAILLLDEATSALDTEsehLVQE--AIYKNL--DGKSVILIAH-----RlstvEKADKIVVINKGR-VEQ 713
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPE---LVGEvlDVMRDLakEGMTMVVVTHemgfaR----EVADRVVFMDGGRiVEE 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
516-664 |
2.23e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 148.18 E-value: 2.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFAR-SVMENV 594
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 595 RYGVEVAD-TEIIRSCEMANAHGFiMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATS 664
Cdd:pfam00005 81 RLGLLLKGlSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
498-721 |
2.62e-41 |
|
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: 151.19 E-value: 2.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYP-TRSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDGVP---LEEFEHH 570
Cdd:cd03258 2 IELKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDltlLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 571 YIHKKIALVGQEPVLF-ARSVMENVRYGVEVA---DTEIIRSCEmanahgfimqTTLKYetnVG--EKG----TQMSGGQ 640
Cdd:cd03258 79 KARRRIGMIFQHFNLLsSRTVFENVALPLEIAgvpKAEIEERVL----------ELLEL---VGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 641 KQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYK-NLD-GKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNH 717
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDiNRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....
gi 71992290 718 ETLL 721
Cdd:cd03258 226 EEVF 229
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
194-443 |
4.95e-41 |
|
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: 152.63 E-value: 4.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 194 ITRIFVPYYTGQVIATVVatksYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDA 273
Cdd:cd18577 25 LFDAFTDFGSGESSPDEF----LDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 274 HKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQD 353
Cdd:cd18577 101 NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 354 TIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIaYIGFLWVSELFQSFIIVSV-LWYGGHLVLTQ 432
Cdd:cd18577 181 AYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGL-VSGLGLGLLFFIIFAMYALaFWYGSRLVRDG 259
|
250
....*....|..
gi 71992290 433 KMK-GDLLVSFL 443
Cdd:cd18577 260 EISpGDVLTVFF 271
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
172-483 |
5.01e-41 |
|
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: 152.99 E-value: 5.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 172 LQYCKREWLWHISG-------------FSWLFiysitrifvpyytGQVIATVVATKSYPALSNAVY---IMTIISLVSAV 235
Cdd:cd18578 1 LKLNKPEWPLLLLGligaiiagavfpvFAILF-------------SKLISVFSLPDDDELRSEANFwalMFLVLAIVAGI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 236 AAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYD--AHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMI 313
Cdd:cd18578 68 AYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 314 FMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTL 393
Cdd:cd18578 148 IAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 394 DVTRTKAIaYIGFLW-VSELFQSFIIVSVLWYGGHLVLTQKMK-GDLLVSF--LLY-QMQLGDNLRQMGEVwtglMQSVG 468
Cdd:cd18578 228 KKGLRRAL-ISGLGFgLSQSLTFFAYALAFWYGGRLVANGEYTfEQFFIVFmaLIFgAQSAGQAFSFAPDI----AKAKA 302
|
330
....*....|....*
gi 71992290 469 ASRKVFEYIDREPQI 483
Cdd:cd18578 303 AAARIFRLLDRKPEI 317
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
498-715 |
5.14e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 154.10 E-value: 5.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG-----VPLEEfehhyi 572
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtgLPPEK------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 hKKIALVGQEPVLFA-RSVMENVRYGVEVADT----------EIIRSCEMAN-AHGFImqttlkyetnvgekgTQMSGGQ 640
Cdd:COG3842 77 -RNVGMVFQDYALFPhLTVAENVAFGLRMRGVpkaeirarvaELLELVGLEGlADRYP---------------HQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 641 KQRIAIARALVREPAILLLDEATSALDTES-EHLVQE--AIYKNLdGKSVILIAHRLS---TVekADKIVVINKGRVEQI 714
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLrEEMREElrRLQREL-GITFIYVTHDQEealAL--ADRIAVMNDGRIEQV 217
|
.
gi 71992290 715 G 715
Cdd:COG3842 218 G 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
498-712 |
5.90e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.81 E-value: 5.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPT-RSDQPILKDLSFTVEPGETVALVGPSGSGKS---SCISLLEnfyVPNAGQVLVDGVPLEEFEH---- 569
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllNILGGLD---RPTSGEVLIDGQDISSLSErela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 570 HYIHKKIALVGQEPVLFAR-SVMENVRY-----GVEVAD-----TEIIRSCEMAN-AHGFImqttlkyetnvgekgTQMS 637
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALplllaGVSRKErreraRELLERVGLGDrLDHRP---------------SQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 638 GGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNL---DGKSVILIAHRLSTVEKADKIVVINKGRVE 712
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELL-RELnreLGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
259-771 |
1.24e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 161.68 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 259 LFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSwRLSLVTFILVPIIFVASK 338
Cdd:PLN03232 989 MLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS-TISLWAIMPLLILFYAAY 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 339 IfgtYYDLLSE--RTQDTIAESNDVAE--EVLSTMRTVRS--------------------FSCENVEADRFYGKLTHTLD 394
Cdd:PLN03232 1068 L---YYQSTSRevRRLDSVTRSPIYAQfgEALNGLSSIRAykaydrmakingksmdnnirFTLANTSSNRWLTIRLETLG 1144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 395 VTrtkaiayigFLWVSELFqsfiivSVLWYG---GHLVLTQKMkgDLLVSFLLYQMQLGDN-LRQMGEVwtglMQSVGAS 470
Cdd:PLN03232 1145 GV---------MIWLTATF------AVLRNGnaeNQAGFASTM--GLLLSYTLNITTLLSGvLRQASKA----ENSLNSV 1203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 471 RKVFEYIDREPQ----IQHNGEYMPENVVGKIEFRNVHFSYptRSD-QPILKDLSFTVEPGETVALVGPSGSGKSSCISL 545
Cdd:PLN03232 1204 ERVGNYIDLPSEataiIENNRPVSGWPSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNA 1281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 546 LENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKY 625
Cdd:PLN03232 1282 LFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGL 1361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 626 ETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVV 705
Cdd:PLN03232 1362 DAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILV 1441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 706 INKGRVEQIGNHETLLKDTNGTYAKLVQrqmmgdqkprkrpavaRSGPQPAASI-NVAGPSQGNAMS 771
Cdd:PLN03232 1442 LSSGQVLEYDSPQELLSRDTSAFFRMVH----------------STGPANAQYLsNLVFERRENGMS 1492
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
498-720 |
1.83e-40 |
|
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: 148.48 E-value: 1.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSdqpILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENFY--VPNAGQVLVDGVPLEEFEHHYI 572
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIpgAPDEGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 H--KKIALVGQEPVLFARSVMENVRYGV--------EVADTEIIRSCEMANahgfimqttLKYETNVGEKGTQMSGGQKQ 642
Cdd:cd03260 78 ElrRRVGMVFQKPNPFPGSIYDNVAYGLrlhgiklkEELDERVEEALRKAA---------LWDEVKDRLHALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 643 RIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETL 720
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
498-753 |
3.91e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 155.45 E-value: 3.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtRSDQPILKDLSFTVEPGETVALVGPSGSGKSScISLLENFYVPN----AGQVLVDGVPLEEFEHHYIH 573
Cdd:COG1123 5 LEVRDLSVRYP-GGDVPAVDGVSLTIAPGETVALVGESGSGKST-LALALMGLLPHggriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEP--VLFARSVMENVRYGVE---VADTEII-RSCEMANAHGFimqttlkyETNVGEKGTQMSGGQKQRIAIA 647
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALEnlgLSRAEARaRVLELLEAVGL--------ERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 648 RALVREPAILLLDEATSALDteseHLVQEAIYKNLD------GKSVILIAHRLSTV-EKADKIVVINKGRVEQIGNHETL 720
Cdd:COG1123 155 MALALDPDLLIADEPTTALD----VTTQAEILDLLRelqrerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270
....*....|....*....|....*....|...
gi 71992290 721 LKDtngtYAKLVQRQMMGDQKPRKRPAVARSGP 753
Cdd:COG1123 231 LAA----PQALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
498-710 |
6.88e-40 |
|
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: 145.02 E-value: 6.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLEnfyVPNAGQVLVDGVPL--EEFEHHYI 572
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTllrCIAGLE---EPDSGSILIDGEDLtdLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 HKKIALVGQEPVLFAR-SVMENVRYGvevadteiirscemanahgfimqttlkyetnvgekgtqMSGGQKQRIAIARALV 651
Cdd:cd03229 75 RRRIGMVFQDFALFPHlTVLENIALG--------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAIyKNL---DGKSVILIAHRLSTVEK-ADKIVVINKGR 710
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALL-KSLqaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
190-473 |
7.24e-40 |
|
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: 148.72 E-value: 7.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 190 FIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVA 269
Cdd:cd18552 9 ILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 270 FYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSE 349
Cdd:cd18552 89 FFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 350 RTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGK----LTHTLDVTRTKAIAyigfLWVSELFQSFIIVSVLWYG 425
Cdd:cd18552 169 RSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKAnerlRRLSMKIARARALS----SPLMELLGAIAIALVLWYG 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 71992290 426 GHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18552 245 GYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
498-711 |
4.04e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.20 E-value: 4.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDGVPLEEFEHHYIHK 574
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTllrCLNGLVE---PTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 ---KIALVGQEPVLFAR-SVMENVRYGVeVADTEIIRSC-------EMANAHGFIMQttlkyetnVG------EKGTQMS 637
Cdd:COG3638 78 lrrRIGMIFQQFNLVPRlSVLTNVLAGR-LGRTSTWRSLlglfppeDRERALEALER--------VGladkayQRADQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 638 GGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNL---DGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLL-RRIareDGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
498-715 |
4.04e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 148.37 E-value: 4.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRsdqPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDGVPLeeFEHHYIHK 574
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDL--FTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 -KIALVGQEPVLFaR--SVMENVRYGVEVA--DTEIIRSC-----EMANAHGFImqttlkyetnvGEKGTQMSGGQKQRI 644
Cdd:COG1118 75 rRVGFVFQHYALF-PhmTVAENIAFGLRVRppSKAEIRARveellELVQLEGLA-----------DRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 645 AIARALVREPAILLLDEATSALDTeseHLVQE------AIYKNLDGKSvILIAH-RLSTVEKADKIVVINKGRVEQIG 715
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDA---KVRKElrrwlrRLHDELGGTT-VFVTHdQEEALELADRVVVMNQGRIEQVG 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
246-733 |
4.89e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 156.82 E-value: 4.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 246 YAYARIQRAirydLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLgSMIFMMKLSWRLSLV 325
Cdd:PLN03130 983 YAAKRLHDA----MLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLL-STFVLIGIVSTISLW 1057
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 326 TFILVPIIFVASKIfgtYYDLLSERTQ--DTIAESNDVAE--EVLSTMRTVRSFSCENVEADrFYGKlthTLDVTrtkai 401
Cdd:PLN03130 1058 AIMPLLVLFYGAYL---YYQSTAREVKrlDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAE-INGR---SMDNN----- 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 402 ayIGFLWVSELFQSFIIVSVLWYGGHLVLtqkmkgdLLVSFLLYQMQLGDNLR----QMGEVW------TGLMQSV---- 467
Cdd:PLN03130 1126 --IRFTLVNMSSNRWLAIRLETLGGLMIW-------LTASFAVMQNGRAENQAafasTMGLLLsyalniTSLLTAVlrla 1196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 468 -------GASRKVFEYIDREPQ----IQHNGEYMPENVVGKIEFRNVHFSYptRSD-QPILKDLSFTVEPGETVALVGPS 535
Cdd:PLN03130 1197 slaenslNAVERVGTYIDLPSEaplvIENNRPPPGWPSSGSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRT 1274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 536 GSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEMANAH 615
Cdd:PLN03130 1275 GAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLK 1354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 616 GFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLS 695
Cdd:PLN03130 1355 DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLN 1434
|
490 500 510
....*....|....*....|....*....|....*...
gi 71992290 696 TVEKADKIVVINKGRVEQIGNHETLLKDTNGTYAKLVQ 733
Cdd:PLN03130 1435 TIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
490-722 |
5.65e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.85 E-value: 5.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 490 MPENVVgkIEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfeh 569
Cdd:COG1121 1 MMMMPA--IELENLTVSY---GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 570 hyIHKKIALVGQE-------PVlfarSVMENV---RYG-------VEVADTEIIRSC-EMANAHGFImqttlkyETNVGE 631
Cdd:COG1121 73 --ARRRIGYVPQRaevdwdfPI----TVRDVVlmgRYGrrglfrrPSRADREAVDEAlERVGLEDLA-------DRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 632 kgtqMSGGQKQRIAIARALVREPAILLLDEATSALDTESehlvQEAIYKNLD-----GKSVILIAHRLSTVEK-ADKIVV 705
Cdd:COG1121 140 ----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT----EEALYELLRelrreGKTILVVTHDLGAVREyFDRVLL 211
|
250 260
....*....|....*....|..
gi 71992290 706 INKGRV-----EQIGNHETLLK 722
Cdd:COG1121 212 LNRGLVahgppEEVLTPENLSR 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
498-713 |
6.92e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 147.53 E-value: 6.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQ-PILKDLSFTVEPGETVALVGPSGSGKSS---CISLLEnfyVPNAGQVLVDGVP---LEEFEHH 570
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLE---RPTSGSVLVDGVDltaLSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 571 YIHKKIALVGQEPVLF-ARSVMENVRYGVEVADT---EII-RSCEManahgfimqttLKYetnVG--EKG----TQMSGG 639
Cdd:COG1135 79 AARRKIGMIFQHFNLLsSRTVAENVALPLEIAGVpkaEIRkRVAEL-----------LEL---VGlsDKAdaypSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 640 QKQRIAIARALVREPAILLLDEATSALDTESEH----LVQEaIYKNLdGKSVILIAHRLSTVEK-ADKIVVINKGR-VEQ 713
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENGRiVEQ 222
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
189-473 |
1.16e-38 |
|
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: 145.27 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDV 268
Cdd:cd18542 8 LLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 269 AFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLS 348
Cdd:cd18542 88 SFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 349 ERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRtKAIAYIGFLW-VSELFQSFIIVSVLWYGGH 427
Cdd:cd18542 168 EEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNI-KLAKLLAKYWpLMDFLSGLQIVLVLWVGGY 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 71992290 428 LVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18542 247 LVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
498-711 |
2.55e-38 |
|
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: 141.90 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDGVPL--EEFEHHYI 572
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLKLtdDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 HKKIALVGQEPVLFA-RSVMENVRYG-VEVADteiiRSCEMANAHGfimqttLKYETNVG--EKGT----QMSGGQKQRI 644
Cdd:cd03262 75 RQKVGMVFQQFNLFPhLTVLENITLApIKVKG----MSKAEAEERA------LELLEKVGlaDKADaypaQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 645 AIARALVREPAILLLDEATSALDTEsehLVQE--AIYKNL--DGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPE---LVGEvlDVMKDLaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
490-725 |
9.73e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 141.27 E-value: 9.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 490 MPENVvgkIEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CIS-LLEnfyvPNAGQVLVDGVP-- 563
Cdd:COG1127 1 MSEPM---IEVRNLTKSF---GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVllkLIIgLLR----PDSGEILVDGQDit 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 564 -LEEFEHHYIHKKIALVGQEPVLF-ARSVMENV----RYGVEVADTEIIRSCEMAnahgfimqttLKyetNVGEKGT--- 634
Cdd:COG1127 71 gLSEKELYELRRRIGMLFQGGALFdSLTVFENVafplREHTDLSEAEIRELVLEK----------LE---LVGLPGAadk 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 635 ---QMSGGQKQRIAIARALVREPAILLLDEATSALD----TESEHLVQEaIYKNLdGKSVILIAHRLSTVEK-ADKIVVI 706
Cdd:COG1127 138 mpsELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsAVIDELIRE-LRDEL-GLTSVVVTHDLDSAFAiADRVAVL 215
|
250
....*....|....*....
gi 71992290 707 NKGRVEQIGNHETLLKDTN 725
Cdd:COG1127 216 ADGKIIAEGTPEELLASDD 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
498-716 |
9.99e-38 |
|
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: 140.84 E-value: 9.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyiHKKIA 577
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVRYGVEVA--DTEIIRScEMANAHGFImqttlKYETNVGEKGTQMSGGQKQRIAIARALVREP 654
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLRLKklPKAEIKE-RVAEALDLV-----QLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 655 AILLLDEATSALDTE-SEHLVQE--AIYKNLdGKSVILIAHRLS---TVekADKIVVINKGRVEQIGN 716
Cdd:cd03300 150 KVLLLDEPLGALDLKlRKDMQLElkRLQKEL-GITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGT 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
497-715 |
3.29e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.92 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 497 KIEFRNVHFSYPtRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKI 576
Cdd:PRK13635 5 IIRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEP--VLFARSVMENVRYGVE---VADTEIIRSCEMAnAHGFIMQTTLKYETNvgekgtQMSGGQKQRIAIARALV 651
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFGLEnigVPREEMVERVDQA-LRQVGMEDFLNREPH------RLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAI--YKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIG 715
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
498-711 |
3.33e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 139.03 E-value: 3.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHK--- 574
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQE-PVLFARSVMENVRYGVEVADT---EIIRSCEMAnahgfimqttLKYetnVG--EKGTQM----SGGQKQRI 644
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALPLRVTGKsrkEIRRRVREV----------LDL---VGlsDKAKALphelSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 645 AIARALVREPAILLLDEATSALDTE-SEHLVQ--EAIykNLDGKSVILIAHRLSTVEKADK-IVVINKGRV 711
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPEtSWEIMEllEEI--NRRGTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
498-725 |
5.31e-37 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 138.79 E-value: 5.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVP---LEEFEHHYIHK 574
Cdd:cd03261 1 IELRGLTKSF---GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEPVLF-ARSVMENV----RYGVEVADTEIIRscemanahgfimQTTLKYETnVGEKGT------QMSGGQKQR 643
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVafplREHTRLSEEEIRE------------IVLEKLEA-VGLRGAedlypaELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 644 IAIARALVREPAILLLDEATSALDTESEHLVQEAI--YKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETL 720
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIrsLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
....*
gi 71992290 721 LKDTN 725
Cdd:cd03261 225 RASDD 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
498-711 |
1.24e-36 |
|
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: 138.08 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIH---K 574
Cdd:cd03256 1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEPVLFAR-SVMENVRYGvEVADTEIIRSC-------EMANAhgfimqttLKYETNVG------EKGTQMSGGQ 640
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSG-RLGRRSTWRSLfglfpkeEKQRA--------LAALERVGlldkayQRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 641 KQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNL---DGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLL-KRInreEGITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
197-473 |
1.97e-36 |
|
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: 139.11 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 197 IFVPYYTGQVIATVVATKSypaLSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKT 276
Cdd:cd18551 16 LAQPLLVKNLIDALSAGGS---SGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 277 GEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIA 356
Cdd:cd18551 93 GDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 357 ESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRtKAIAYIGFLW-VSELFQSFIIVSVLWYGGHLVLTqkmk 435
Cdd:cd18551 173 ELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGL-KAAKIEALIGpLMGLAVQLALLVVLGVGGARVAS---- 247
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 71992290 436 GDL----LVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18551 248 GALtvgtLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
499-715 |
3.00e-36 |
|
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: 134.87 E-value: 3.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 499 EFRNVHFSYPTRsdqPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIAL 578
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 579 VGQepvlfarsVMENVrygvevadteiirscemaNAHGFIMQTTlkyetnvgekgTQMSGGQKQRIAIARALVREPAILL 658
Cdd:cd03214 78 VPQ--------ALELL------------------GLAHLADRPF-----------NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 659 LDEATSALDTESEHLVQEAI--YKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIG 715
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
496-715 |
5.03e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 139.44 E-value: 5.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDG-----VPLEEf 567
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLED---PTSGEILIGGrdvtdLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 568 ehhyihKKIALVGQEPVLF-ARSVMENVRYGVEVADT---EI---IRscEMAnahgfimqTTLKYETNVGEKGTQMSGGQ 640
Cdd:COG3839 75 ------RNIAMVFQSYALYpHMTVYENIAFPLKLRKVpkaEIdrrVR--EAA--------ELLGLEDLLDRKPKQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 641 KQRIAIARALVREPAILLLDEATSALDTES-EHLVQE--AIYKNLdGKSVILIAHRLstVEK---ADKIVVINKGRVEQI 714
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAKLrVEMRAEikRLHRRL-GTTTIYVTHDQ--VEAmtlADRIAVMNDGRIQQV 215
|
.
gi 71992290 715 G 715
Cdd:COG3839 216 G 216
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
197-444 |
6.22e-36 |
|
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: 137.68 E-value: 6.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 197 IFVPYYTGQVIATVvatKSYPALSNAVYIMTI----ISLVSAVA--AGFrggSFEYAY------ARIQRAIRYDLFHGLV 264
Cdd:cd18574 13 IQIPLLLGDLVNVI---SRSLKETNGDFIEDLkkpaLKLLGLYLlqSLL---TFAYISllsvvgERVAARLRNDLFSSLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 265 KQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYY 344
Cdd:cd18574 87 RQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 345 DLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTlDVTRTKAIAYIG-FLWVSELFQSFIIVSVLW 423
Cdd:cd18574 167 RKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKA-AKLNEKLGLGIGiFQGLSNLALNGIVLGVLY 245
|
250 260
....*....|....*....|.
gi 71992290 424 YGGHLVLTQKMKGDLLVSFLL 444
Cdd:cd18574 246 YGGSLVSRGELTAGDLMSFLV 266
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
498-723 |
1.43e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 135.89 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:PRK13632 8 IKVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEP------------VLFArsvMENVRYGVEVADTEIIRSCEMANahgfiMQTTLKYETNvgekgtQMSGGQKQRIA 645
Cdd:PRK13632 87 IIFQNPdnqfigatveddIAFG---LENKKVPPKKMKDIIDDLAKKVG-----MEDYLDKEPQ------NLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 646 IARALVREPAILLLDEATSALDTESEHLVQEAIY--KNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKD 723
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
183-471 |
6.74e-35 |
|
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: 134.82 E-value: 6.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 183 ISGFSWLFIYSITRIFVPYYTGQVI--ATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLF 260
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIddYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 261 HGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIF 340
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 341 GTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFyGKLTHTLDVTRTKAIAYIGFLW-VSELFQSFIIV 419
Cdd:cd18544 162 RKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEF-DEINQEYRKANLKSIKLFALFRpLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 71992290 420 SVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTgLMQS--VGASR 471
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFN-ILQSamASAER 293
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
183-449 |
7.48e-35 |
|
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: 134.46 E-value: 7.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 183 ISGFSWLFIYSITRIFVPYYTGQVIATVVATKSypALSNAVYIMTIISLVSAVAAGFR--------GGSFeyayaRIQRA 254
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTL--TASQLLRYALLILLLALLIGIFRflwrylifGASR-----RIEYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 255 IRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIF 334
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 335 VASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGK----LTHTLDVTRTKAIayigFLWVS 410
Cdd:cd18541 155 LLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLneeyVEKNLRLARVDAL----FFPLI 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 71992290 411 ELFQSFIIVSVLWYGGHLVLTQKMK-GDlLVSFLLYQMQL 449
Cdd:cd18541 231 GLLIGLSFLIVLWYGGRLVIRGTITlGD-LVAFNSYLGML 269
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
499-709 |
1.11e-34 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 131.50 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 499 EFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFehhyiHKKIAL 578
Cdd:cd03235 1 EVEDLTVSY---GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 579 VGQEPVL---FARSVMENV---RYG-------VEVADTEIIRSC-EMANAHGFIMQttlkyetNVGEkgtqMSGGQKQRI 644
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmgLYGhkglfrrLSKADKAKVDEAlERVGLSELADR-------QIGE----LSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 645 AIARALVREPAILLLDEATSALDTESehlvQEAIYKNLD-----GKSVILIAHRLSTVEK-ADKIVVINKG 709
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKT----QEDIYELLRelrreGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
498-705 |
2.60e-34 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 130.29 E-value: 2.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSyptRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYiHKKIA 577
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVR-----YGVEVADTEIIRSCEMANAHGFImqttlkyETNVGekgtQMSGGQKQRIAIARALV 651
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAIYKNLD-GKSVILIAHRLSTVEKADKIVV 705
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLArGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
498-721 |
5.27e-34 |
|
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: 130.50 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:cd03295 1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFA-RSVMENV-------RYGVEVADTEIIRSCEMANahgfimqttLKYETNVGEKGTQMSGGQKQRIAIARA 649
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkllKWPKEKIRERADELLALVG---------LDPAEFADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 650 LVREPAILLLDEATSALDTESEHLVQEAIYK--NLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLL 721
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
498-715 |
8.04e-34 |
|
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: 128.91 E-value: 8.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyiHKKIA 577
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVRYGVEVADT---EIIRSCEMAnAHgfimqtTLKYETNVGEKGTQMSGGQKQRIAIARALVRE 653
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKLRKVpkdEIDERVREV-AE------LLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 654 PAILLLDEATSALD------TESEhLVQeaIYKNLdGKSVILIAHrlSTVEK---ADKIVVINKGRVEQIG 715
Cdd:cd03301 149 PKVFLMDEPLSNLDaklrvqMRAE-LKR--LQQRL-GTTTIYVTH--DQVEAmtmADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
518-715 |
1.03e-33 |
|
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: 128.57 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 518 DLSFTVePGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDGVPLEEFEHHYI----HKKIALVGQEPVLFAR-S 589
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTllrCIAGLEK---PDGGTIVLNGTVLFDSRKKINlppqQRKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 590 VMENVRYGVEVADTEIIRSCEMAnahgfiMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTE 669
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVDE------LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 71992290 670 SEHLVQ---EAIYKNLDGkSVILIAHRLSTVEK-ADKIVVINKGRVEQIG 715
Cdd:cd03297 166 LRLQLLpelKQIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
516-721 |
3.13e-33 |
|
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: 129.30 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYI----HKKIALVGQEPVLFA-RSV 590
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENVRYGVEVA--DTEI-----IRSCEMANAHGFIMQttlkyetnvgeKGTQMSGGQKQRIAIARALVREPAILLLDEAT 663
Cdd:cd03294 120 LENVAFGLEVQgvPRAEreeraAEALELVGLEGWEHK-----------YPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 664 SALD----TE-SEHLVQeaIYKNLdGKSVILIAHRLS-TVEKADKIVVINKGRVEQIGNHETLL 721
Cdd:cd03294 189 SALDplirREmQDELLR--LQAEL-QKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
498-711 |
3.69e-33 |
|
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: 125.23 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvpleefehhyihkkia 577
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 lvgqEPVLFArSVMENVRYGVEVAdteiirscemanahgfimqttlkyetnvgekgTQMSGGQKQRIAIARALVREPAIL 657
Cdd:cd03216 62 ----KEVSFA-SPRDARRAGIAMV--------------------------------YQLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 658 LLDEATSAL-DTESEHLVqeAIYKNL--DGKSVILIAHRLSTV-EKADKIVVINKGRV 711
Cdd:cd03216 105 ILDEPTAALtPAEVERLF--KVIRRLraQGVAVIFISHRLDEVfEIADRVTVLRDGRV 160
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
190-471 |
5.85e-33 |
|
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: 129.06 E-value: 5.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 190 FIYSITRIFVPYYTGQVIATVVATKS------YPALSNAVYIMTIISLVSAVaagfrggsFEYAYARI-----QRA---I 255
Cdd:cd18547 9 IISTLLSVLGPYLLGKAIDLIIEGLGggggvdFSGLLRILLLLLGLYLLSAL--------FSYLQNRLmarvsQRTvydL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 256 RYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFV 335
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 336 ASKIFG----TYYDllseRTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFyGKLTHTLDVTRTKAIAYIGFLW--- 408
Cdd:cd18547 161 VTKFIAkrsqKYFR----KQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEF-DEINEELYKASFKAQFYSGLLMpim 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 409 --VSELfqSFIIVSVLwyGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSV-GASR 471
Cdd:cd18547 236 nfINNL--GYVLVAVV--GGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALaGAER 297
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
498-720 |
1.04e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 127.93 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEP--VLFARSVMENVRYGVE---VADTEII-RSCEMANAHGfiMQTTLKYETnvgekgTQMSGGQKQRIAIARALV 651
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLEnkgIPHEEMKeRVNEALELVG--MQDFKEREP------ARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 652 REPAILLLDEATSALDTESE-HLVQ--EAIyKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETL 720
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRlELIKtiKGI-RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
516-722 |
1.54e-32 |
|
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: 125.91 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHhyIHKKIALVGQEPVLFAR-SVMENV 594
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP--EKRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 595 RYGVevadteIIRSCEMANAHGFIMQTT--LKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTES-E 671
Cdd:cd03299 93 AYGL------KKRKVDKKEIERKVLEIAemLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71992290 672 HLVQE-AIYKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLK 722
Cdd:cd03299 167 KLREElKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
498-723 |
2.33e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 125.59 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNV--HFSyptrsDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENFyvpNAGQVLVDGVPLE--EFEHH 570
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLEEI---TSGDLIVDGLKVNdpKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 571 YIHKKIALVGQEPVLFAR-SVMENVRYG-VEVadteiiRSCEMANAHGFIMQTTLK--YETNVGEKGTQMSGGQKQRIAI 646
Cdd:PRK09493 74 LIRQEAGMVFQQFYLFPHlTALENVMFGpLRV------RGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 647 ARALVREPAILLLDEATSALDTESEHLVQEaIYKNL--DGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKD 723
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLK-VMQDLaeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
496-736 |
6.85e-32 |
|
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: 125.02 E-value: 6.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYPTrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKK 575
Cdd:cd03288 18 GEIKIHDLCVRYEN-NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPA 655
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 656 ILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDTNGTYAKLVQRQ 735
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTD 256
|
.
gi 71992290 736 M 736
Cdd:cd03288 257 K 257
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
498-711 |
8.12e-32 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 123.29 E-value: 8.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHH---YIHK 574
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQE-PVLFARSVMENVRYGVEVADT---EIIRSCEMAnahgfIMQTTLKYETNvgEKGTQMSGGQKQRIAIARAL 650
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVpprEIRKRVPAA-----LELVGLSHKHR--ALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71992290 651 VREPAILLLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTVEKADK-IVVINKGRV 711
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
498-711 |
1.25e-31 |
|
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: 121.89 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHF---SYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENfYVPNA---GQVLVDGVPLEEFEhhy 571
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG-RRTGLgvsGEVLINGRPLDKRS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQEPVLFAR-SVMENVRYGVEvadteiIRScemanahgfimqttlkyetnvgekgtqMSGGQKQRIAIARAL 650
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMFAAK------LRG---------------------------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 651 VREPAILLLDEATSALDTESEHLVQEAIyKNL--DGKSVILIAHRLST--VEKADKIVVINKGRV 711
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLL-RRLadTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
490-715 |
5.47e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 125.44 E-value: 5.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 490 MPENVVGK---IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG----- 561
Cdd:PRK09452 4 LNKQPSSLsplVELRGISKSF---DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdith 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 562 VPLEefehhyiHKKIALVGQEPVLFAR-SVMENVRYGV---EVADTEIIRSCEMANAhgfimqtTLKYETNVGEKGTQMS 637
Cdd:PRK09452 81 VPAE-------NRHVNTVFQSYALFPHmTVFENVAFGLrmqKTPAAEITPRVMEALR-------MVQLEEFAQRKPHQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 638 GGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNLD---GKSVILIAHrlsTVEKA----DKIVVINKGR 710
Cdd:PRK09452 147 GGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNEL-KALQrklGITFVFVTH---DQEEAltmsDRIVVMRDGR 222
|
....*
gi 71992290 711 VEQIG 715
Cdd:PRK09452 223 IEQDG 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
516-718 |
5.71e-31 |
|
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: 121.39 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEF-EHHYIHKKIALVGQEPVLFAR-SVMEN 593
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpPHEIARLGIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 594 VRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVG------EKGTQMSGGQKQRIAIARALVREPAILLLDEATSAL- 666
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREARERAEELLERVGladladRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLn 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 667 DTESEHLVqEAIYK-NLDGKSVILIAHRLSTVEK-ADKIVVINKGRV------EQIGNHE 718
Cdd:cd03219 176 PEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRViaegtpDEVRNNP 234
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
190-470 |
1.95e-30 |
|
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: 121.81 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 190 FIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVA 269
Cdd:cd18545 10 LLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 270 FYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSE 349
Cdd:cd18545 90 FFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 350 RTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRtKAIAYIGFLW-VSELFQSFIIVSVLWYGGHL 428
Cdd:cd18545 170 RVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANM-RAVRLNALFWpLVELISALGTALVYWYGGKL 248
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 71992290 429 VLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLmQSVGAS 470
Cdd:cd18545 249 VLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQL-QSAMAS 289
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
498-725 |
2.27e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.86 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRsdqpiLKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEefeHHYIHK-KI 576
Cdd:COG3840 2 LRLDDLTYRYGDF-----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT---ALPPAErPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPVLFAR-SVMENV----RYGVEVADTEIIRSCEMANahgfimqttlkyETNVGEKGT----QMSGGQKQRIAIA 647
Cdd:COG3840 74 SMLFQENNLFPHlTVAQNIglglRPGLKLTAEQRAQVEQALE------------RVGLAGLLDrlpgQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 648 RALVREPAILLLDEATSALD----TESEHLVQEaIYKNLdGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLK 722
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDpalrQEMLDLVDE-LCRER-GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
...
gi 71992290 723 DTN 725
Cdd:COG3840 220 GEP 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
498-715 |
7.61e-30 |
|
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: 117.61 E-value: 7.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSdQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfEHHYIHKKIA 577
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVRY-----GVEVADteiirscEMANAHGFIMQTTL-KYETnvgEKGTQMSGGQKQRIAIARAL 650
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSE-------IKEEVELLLRVLGLtDKAN---KRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 651 VREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIG 715
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
498-711 |
9.11e-30 |
|
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: 117.47 E-value: 9.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSY-PTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGV-----PLEefehhy 571
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvkePAE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQEPVLFAR-SVMENVRY-----GVevadteiirscEMANAHGFI--MQTTLKYETNVGEKGTQMSGGQKQR 643
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRlTARENLEYfaglyGL-----------KGDELTARLeeLADRLGMEELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 644 IAIARALVREPAILLLDEATSALDTESEHLVQEAI--YKNLdGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIrqLRAL-GKCILFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
498-715 |
1.02e-29 |
|
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: 118.21 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvplEEFEHHYIHKK-I 576
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPVLFAR-SVMENVRYGVEV------ADTEIIRscemANAHGFIMQTTLKYETNvgEKGTQMSGGQKQRIAIARA 649
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFGLRVkprserPPEAEIR----AKVHELLKLVQLDWLAD--RYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 650 LVREPAILLLDEATSALDTESEHLVQEAIYKNLD--GKSVILIAHRLS-TVEKADKIVVINKGRVEQIG 715
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
189-733 |
1.29e-29 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 126.82 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVpyYTGQVIATVVATKSYpALSNAVYIMTIISLVSAVAAG--FRGGSFEYAYARIQRAIRYDLFHGLVKQ 266
Cdd:PTZ00243 968 LATFAVTELVT--VSSGVWLSMWSTRSF-KLSAATYLYVYLGIVLLGTFSvpLRFFLSYEAMRRGSRNMHRDLLRSVSRG 1044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 267 DVAFYDAHKTGEVTSRLAADCQTMSDTVALNVnVFLRNCVMLLGSMIFMMklSWRLSLVTFILVPIIFVASKIFGTY--- 343
Cdd:PTZ00243 1045 TMSFFDTTPLGRILNRFSRDIDILDNTLPMSY-LYLLQCLFSICSSILVT--SASQPFVLVALVPCGYLYYRLMQFYnsa 1121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 344 ---------------YDLLSERTQD--TIA---ESNDVAEEVLSTMRTVrsFSCENVE--ADRFYGKLTHTLDVTRTKAI 401
Cdd:PTZ00243 1122 nreirriksvakspvFTLLEEALQGsaTITaygKAHLVMQEALRRLDVV--YSCSYLEnvANRWLGVRVEFLSNIVVTVI 1199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 402 AYIGF----LWVSElfQSFIIVSvlwygghLVLTQKMKGDLLVSFLLyqmqlgdnlRQMGEVWTGlMQSVgasRKVFEYI 477
Cdd:PTZ00243 1200 ALIGVigtmLRATS--QEIGLVS-------LSLTMAMQTTATLNWLV---------RQVATVEAD-MNSV---ERLLYYT 1257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 478 DREPQiqhngEYMPE--------------------NVV----------------GKIEFRNVHFSYptRSDQP-ILKDLS 520
Cdd:PTZ00243 1258 DEVPH-----EDMPEldeevdalerrtgmaadvtgTVViepasptsaaphpvqaGSLVFEGVQMRY--REGLPlVLRGVS 1330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 521 FTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEV 600
Cdd:PTZ00243 1331 FRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEA 1410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 601 ADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALV-REPAILLLDEATSALDTESEHLVQEAIY 679
Cdd:PTZ00243 1411 SSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVM 1490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 71992290 680 KNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDTNGTYAKLVQ 733
Cdd:PTZ00243 1491 SAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVE 1544
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
498-750 |
1.89e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.20 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYP-TRSdqpiLKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLeEFE--HHYIHK 574
Cdd:COG1129 5 LEMRGISKSFGgVKA----LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRspRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEPVLFA-RSVMENVRYGVEVADTEIIRSCEM---ANAhgfIMQtTLKYETNVGEKGTQMSGGQKQRIAIARAL 650
Cdd:COG1129 80 GIAIIHQELNLVPnLSVAENIFLGREPRRGGLIDWRAMrrrARE---LLA-RLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 651 VREPAILLLDEATSAL-DTESEHLVqeAIYKNL--DGKSVILIAHRLSTVEK-ADKIVVINKGRVeqIGNHETllKDTng 726
Cdd:COG1129 156 SRDARVLILDEPTASLtEREVERLF--RIIRRLkaQGVAIIYISHRLDEVFEiADRVTVLRDGRL--VGTGPV--AEL-- 227
|
250 260
....*....|....*....|....*...
gi 71992290 727 TYAKLVqRQMMG----DQKPRKRPAVAR 750
Cdd:COG1129 228 TEDELV-RLMVGreleDLFPKRAAAPGE 254
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
498-723 |
1.96e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 119.39 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQ-PILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNA---GQVLVDGVPL-----EEFE 568
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLlklseKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 569 HhYIHKKIALVGQEPvlFA---------RSVMENVRY--GVEVADT-----EIIRSCEMANA--------Hgfimqttlk 624
Cdd:COG0444 82 K-IRGREIQMIFQDP--MTslnpvmtvgDQIAEPLRIhgGLSKAEAreraiELLERVGLPDPerrldrypH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 625 yetnvgekgtQMSGGQKQRIAIARALVREPAILLLDEATSALD-TesehlVQEAIyknLD---------GKSVILIAHRL 694
Cdd:COG0444 150 ----------ELSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQI---LNllkdlqrelGLAILFITHDL 211
|
250 260 270
....*....|....*....|....*....|.
gi 71992290 695 STVEK-ADKIVVINKGR-VEqIGNHETLLKD 723
Cdd:COG0444 212 GVVAEiADRVAVMYAGRiVE-EGPVEELFEN 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
498-713 |
2.07e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.91 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQ-PILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDGV---PLEEFEHH 570
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQdltALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 571 YIHKKIALVGQE-PVLFARSVMENVRYGVEVADTeiirscemanAHGFIMQTTLKYETNVG--EKG----TQMSGGQKQR 643
Cdd:PRK11153 79 KARRQIGMIFQHfNLLSSRTVFDNVALPLELAGT----------PKAEIKARVTELLELVGlsDKAdrypAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 644 IAIARALVREPAILLLDEATSALDTESEH----LVQEaIYKNLdGKSVILIAHRLSTV-EKADKIVVINKGR-VEQ 713
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRsileLLKD-INREL-GLTIVLITHEMDVVkRICDRVAVIDAGRlVEQ 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
498-722 |
2.72e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.98 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNA---GQVLVDGVPLEEFEHHYIHK 574
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEP--VLFARSVMENVRYGVE---VADTEIIRscemanahgfIMQTTLkyeTNVG------EKGTQMSGGQKQR 643
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLEnraVPRPEMIK----------IVRDVL---ADVGmldyidSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 644 IAIARALVREPAILLLDEATSALDTESEHLVQEAI--YKNLDGKSVILIAHRLSTVEKADKIVVINKGRV------EQIG 715
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEANMADQVLVLDDGKLlaqgspVEIF 231
|
....*..
gi 71992290 716 NHETLLK 722
Cdd:PRK13640 232 SKVEMLK 238
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
190-445 |
3.15e-29 |
|
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: 118.32 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 190 FIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGgsfeyaY------ARIQRAIRYDLFHGL 263
Cdd:cd18549 12 VLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVT------YwghvmgARIETDMRRDLFEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 264 VKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTY 343
Cdd:cd18549 86 QKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 344 YDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFyGKLTHTLDVTRTKAIAYIGFLW-VSELFQSFIIVSVL 422
Cdd:cd18549 166 MKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKF-DEGNDRFLESKKKAYKAMAYFFsGMNFFTNLLNLVVL 244
|
250 260
....*....|....*....|...
gi 71992290 423 WYGGHLVLTQKMKGDLLVSFLLY 445
Cdd:cd18549 245 VAGGYFIIKGEITLGDLVAFLLY 267
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
516-724 |
3.35e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.84 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPL--EEFEHHYIHKKIALVGQEP--VLFARSVM 591
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 592 ENVRYG---VEVADTEI-IRSCEMANAHGfimqttLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALD 667
Cdd:PRK13637 103 KDIAFGpinLGLSEEEIeNRVKRAMNIVG------LDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 668 TESEHLVQEAIyKNLDGK---SVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKDT 724
Cdd:PRK13637 177 PKGRDEILNKI-KELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKEV 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
498-723 |
3.89e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 117.40 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSdqPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEH-HYIHKKI 576
Cdd:PRK13644 2 IRLENVSYSYPDGT--PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEP--VLFARSVMENVRYGVE---VADTEIIRSCEMANAHgfimqttLKYETNVGEKGTQMSGGQKQRIAIARALV 651
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPEnlcLPPIEIRKRVDRALAE-------IGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKD 723
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
498-700 |
4.80e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.89 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYP-TRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEE--------FE 568
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgadrgvvFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 569 HHyihkkiALVgqePVLfarSVMENVRYGVEVADTEiiRSCEMANAHGFIMQTTLKyetNVGEKGT-QMSGGQKQRIAIA 647
Cdd:COG4525 84 KD------ALL---PWL---NVLDNVAFGLRLRGVP--KAERRARAEELLALVGLA---DFARRRIwQLSGGMRQRVGIA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 648 RALVREPAILLLDEATSALDTESEHLVQEAIYK--NLDGKSVILIAHrlsTVEKA 700
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH---SVEEA 198
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
498-723 |
7.26e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 114.84 E-value: 7.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYI-HKKI 576
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPVLFAR-SVMENVRYGVEV-ADTEIIRSCEMAnahgFIMQTTLKyeTNVGEKGTQMSGGQKQRIAIARALVREP 654
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYArRRAKRKARLERV----YELFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 655 AILLLDEATSALdteSEHLVQE---AIYK-NLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKD 723
Cdd:cd03224 152 KLLLLDEPSEGL---APKIVEEifeAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
497-667 |
1.65e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.13 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 497 KIEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLeNFYVPNA---GQVLVDG-------VP 563
Cdd:COG1117 11 KIEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRM-NDLIPGArveGEILLDGediydpdVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 564 LEEfehhyIHKKIALVGQEPVLFARSVMENVRYGVEVAdtEIIRSCEMANahgfIMQTTLKyetNVG----------EKG 633
Cdd:COG1117 87 VVE-----LRRRVGMVFQKPNPFPKSIYDNVAYGLRLH--GIKSKSELDE----IVEESLR---KAAlwdevkdrlkKSA 152
|
170 180 190
....*....|....*....|....*....|....
gi 71992290 634 TQMSGGQKQRIAIARALVREPAILLLDEATSALD 667
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
228-471 |
2.43e-28 |
|
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: 116.07 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 228 IISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVM 307
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 308 LLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRF-- 385
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFar 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 386 --YGKLTHTLDVTRTKAiayiGFLWVSELFQSFIIVSVLWYGGHLVLTQKMK-GDLLVsFLLYQMQLGDNLRQMGEVWTG 462
Cdd:cd18564 222 enRKSLRAGLRAARLQA----LLSPVVDVLVAVGTALVLWFGAWLVLAGRLTpGDLLV-FLAYLKNLYKPVRDLAKLTGR 296
|
250
....*....|
gi 71992290 463 LMQ-SVGASR 471
Cdd:cd18564 297 IAKaSASAER 306
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
516-718 |
2.60e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 114.37 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyihkKIALVG-----QEPVLFAR-S 589
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIARLGiartfQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 590 VMENVRYGVEVADTEIIRSC---------EMANAHGFIMQTtLKYetnVG------EKGTQMSGGQKQRIAIARALVREP 654
Cdd:COG0411 96 VLENVLVAAHARLGRGLLAAllrlprarrEEREARERAEEL-LER---VGladradEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 655 AILLLDEATSAL-DTESEHLVQ--EAIyKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRV------EQIGNHE 718
Cdd:COG0411 172 KLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRViaegtpAEVRADP 244
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
200-466 |
3.26e-28 |
|
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: 115.30 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 200 PYYTGQ----VIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHK 275
Cdd:cd18563 19 PYLTKIliddVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 276 TGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTI 355
Cdd:cd18563 99 TGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 356 AESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRtKAIAYIGFLW--VSELFQSFIIVsVLWYGGHLVLTQK 433
Cdd:cd18563 179 SRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANI-RAEKLWATFFplLTFLTSLGTLI-VWYFGGRQVLSGT 256
|
250 260 270
....*....|....*....|....*....|....*.
gi 71992290 434 MKGDLLVSFLLYQMQL-G--DNLRQMGEVWTGLMQS 466
Cdd:cd18563 257 MTLGTLVAFLSYLGMFyGplQWLSRLNNWITRALTS 292
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
512-711 |
7.25e-28 |
|
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: 111.54 E-value: 7.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 512 DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVplEEFEHHYIHKKIALVGQEPVLF-ARSV 590
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEAPGFYpNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENVRYGvevadteiirscemANAHGF---IMQTTLKYetnVGEKGT------QMSGGQKQRIAIARALVREPAILLLDE 661
Cdd:cd03268 90 RENLRLL--------------ARLLGIrkkRIDEVLDV---VGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 71992290 662 ATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:cd03268 153 PTNGLDPDGIKELRELILSlRDQGITVLISSHLLSEIQKvADRIGIINKGKL 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
490-713 |
8.39e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 112.14 E-value: 8.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 490 MPENVVGKIEFRNVHFSYPTRSDQ-PILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEF- 567
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 568 ---------EHhyihkkIALVGQ-EPVLFARSVMENVRYGVEVADteiirsceMANAHgfimQTTLKYETNVGEKG---- 633
Cdd:COG4181 81 edararlraRH------VGFVFQsFQLLPTLTALENVMLPLELAG--------RRDAR----ARARALLERVGLGHrldh 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 634 --TQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYK-NLD-GKSVILIAHRLSTVEKADKIVVINKG 709
Cdd:COG4181 143 ypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFElNRErGTTLVLVTHDPALAARCDRVLRLRAG 222
|
....
gi 71992290 710 RVEQ 713
Cdd:COG4181 223 RLVE 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
498-718 |
8.82e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.41 E-value: 8.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTrsdQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG------VPLEEFEHHY 571
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQEPVLFA-RSVMEN-VRYGVEVADTeiirSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARA 649
Cdd:COG4161 80 LRQKVGMVFQQYNLWPhLTVMENlIEAPCKVLGL----SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 650 LVREPAILLLDEATSALDTESEHLVQEaIYKNLD--GKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHE 718
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVE-IIRELSqtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
498-711 |
9.75e-28 |
|
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: 111.60 E-value: 9.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSdqpILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyihkKIA 577
Cdd:cd03269 1 LEVENVTKRFGRVT---ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFA-RSVMENVRY-------GVEVADTEIIRSCEmanahgfimqtTLKYETNVGEKGTQMSGGQKQRIAIARA 649
Cdd:cd03269 74 YLPEERGLYPkMKVIDQLVYlaqlkglKKEEARRRIDEWLE-----------RLELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 650 LVREPAILLLDEATSALDTESEHLVQEAIYKNLD-GKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
498-715 |
1.37e-27 |
|
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: 111.13 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETvALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfEHHYIHKKIA 577
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVRYGV---EVADTEIIRSCEMANAHgfimqttlkyeTNVGEKGT----QMSGGQKQRIAIARA 649
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYIAwlkGIPSKEVKARVDEVLEL-----------VNLGDRAKkkigSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 650 LVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIG 715
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
516-753 |
1.74e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.05 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEeFE--HHYIHKKIALVGQEPVLFAR-SVME 592
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRspRDAIALGIGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 593 NVRYGVEVADTEIIRsceMANAHGFIMQTTLKY------ETNVGekgtQMSGGQKQRIAIARALVREPAILLLDEATSAL 666
Cdd:COG3845 100 NIVLGLEPTKGGRLD---RKAARARIRELSERYgldvdpDAKVE----DLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 667 -DTESEHLVqeAIYKNL--DGKSVILIAHRLSTV-EKADKIVVINKGRVeqIGNHETllKDTngTYAKLVqRQMMG-DQK 741
Cdd:COG3845 173 tPQEADELF--EILRRLaaEGKSIIFITHKLREVmAIADRVTVLRRGKV--VGTVDT--AET--SEEELA-ELMVGrEVL 243
|
250
....*....|..
gi 71992290 742 PRKRPAVARSGP 753
Cdd:COG3845 244 LRVEKAPAEPGE 255
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
498-711 |
2.83e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSyptRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:PRK13548 3 LEARNLSVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVL-FARSVMENVRYG------VEVADTEIIRSCeMAnahgfimqttlkyETNVGEKG----TQMSGGQKQRIAI 646
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGraphglSRAEDDALVAAA-LA-------------QVDLAHLAgrdyPQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 647 ARALVR------EPAILLLDEATSALDTESEHLVQEaIYKNL---DGKSVILIAHRLS-TVEKADKIVVINKGRV 711
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLR-LARQLaheRGLAVIVVLHDLNlAARYADRIVLLHQGRL 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
498-729 |
5.13e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.78 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyiHKKIA 577
Cdd:PRK11607 20 LEIRNLTKSF---DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVRYGVE---VADTEI-IRSCEM-ANAHgfiMQTTLKyetnvgEKGTQMSGGQKQRIAIARALV 651
Cdd:PRK11607 95 MMFQSYALFPHmTVEQNIAFGLKqdkLPKAEIaSRVNEMlGLVH---MQEFAK------RKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAIYKNLD--GKSVILIAH-RLSTVEKADKIVVINKGRVEQIGNHETLLKDTNGTY 728
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
.
gi 71992290 729 A 729
Cdd:PRK11607 246 S 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
498-726 |
5.61e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 5.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptRSDQPI-LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKI 576
Cdd:PRK13648 8 IVFKNVSFQY--QSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPV-LFARSVME-NVRYGVE---VADTEIIRSCEMANAHgFIMQTTLKYETNvgekgtQMSGGQKQRIAIARALV 651
Cdd:PRK13648 86 GIVFQNPDnQFVGSIVKyDVAFGLEnhaVPYDEMHRRVSEALKQ-VDMLERADYEPN------ALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAIYKNLDGKSV--ILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDTNG 726
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItiISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
498-723 |
9.63e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.60 E-value: 9.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEP--VLFARSVMENVRYG---VEVADTEIIRSCEMA-NAHGfiMQttlkyetNVGEKGT-QMSGGQKQRIAIARAL 650
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnMGLDKDEVERRVEEAlKAVR--MW-------DFRDKPPyHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 651 VREPAILLLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLS-TVEKADKIVVINKGRVEQIGNHETLLKD 723
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
498-725 |
9.67e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.55 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYI--HKK 575
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEP--VLFARSVMENVRYG----------VEVADTEIIRSCEMANahgfimqttlkYETNVGEkgtQMSGGQKQR 643
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglskeeVEKRVKEALKAVGMEG-----------FENKPPH---HLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 644 IAIARALVREPAILLLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLL 721
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVF 225
|
....
gi 71992290 722 KDTN 725
Cdd:PRK13639 226 SDIE 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
498-711 |
1.06e-26 |
|
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: 108.35 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTrsdQPIlkDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyiHKKIA 577
Cdd:cd03298 1 VRLDKIRFSYGE---QPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVryGVEVADTEIIRSCEMANAHGFIMQTTLkyETNVGEKGTQMSGGQKQRIAIARALVREPAI 656
Cdd:cd03298 74 MLFQENNLFAHlTVEQNV--GLGLSPGLKLTAEDRQAIEVALARVGL--AGLEKRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 657 LLLDEATSALDTESEHLVQEAIYK--NLDGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
197-457 |
1.17e-26 |
|
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: 110.65 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 197 IFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRggsfEYAYAR----IQRAIRYDLFHGLVKQDVAFYD 272
Cdd:cd18543 16 LAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLR----RYLAGRlslgVEHDLRTDLFAHLQRLDGAFHD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 273 AHKTGEVTSRLAADCQTMSDTVALnVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQ 352
Cdd:cd18543 92 RWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 353 DTIAESNDVAEEVLSTMRTVRSFSCENVEADRFyGKLTHTLDVTRTKAIAYIGFLW-VSELFQSFIIVSVLWYGGHLVLT 431
Cdd:cd18543 171 DQAGDLATVVEESVTGIRVVKAFGRERRELDRF-EAAARRLRATRLRAARLRARFWpLLEALPELGLAAVLALGGWLVAN 249
|
250 260
....*....|....*....|....*.
gi 71992290 432 QKMKGDLLVSFLLYQMQLGDNLRQMG 457
Cdd:cd18543 250 GSLTLGTLVAFSAYLTMLVWPVRMLG 275
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
502-692 |
1.69e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 107.73 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 502 NVHFSYPTRSDqpILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyihKKIALVGQ 581
Cdd:cd03226 4 NISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 582 EP--VLFARSVMENVRYGVEVADTEIIRSCEmanahgfIMQTtLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLL 659
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAET-------VLKD-LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190
....*....|....*....|....*....|....
gi 71992290 660 DEATSALDTESEHLVQEAIYK-NLDGKSVILIAH 692
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
498-711 |
1.91e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.20 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEefehhyiHKKIA 577
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVG---QEPVLFAR-SVMENVRY-----GVEVADTEIiRSCEMANAHGfimqttlkyetnVGEKGT----QMSGGQKQRI 644
Cdd:COG4152 72 RIGylpEERGLYPKmKVGEQLVYlarlkGLSKAEAKR-RADEWLERLG------------LGDRANkkveELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 645 AIARALVREPAILLLDEATSALDTESEHLVQEAIyKNL--DGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVI-RELaaKGTTVIFSSHQMELVEElCDRIVIINKGRK 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
323-770 |
2.01e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 116.61 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 323 SLVTFILVPIifvASKIFGTYYDLLSERTQDTiAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIA 402
Cdd:PLN03232 447 SLILFLLIPL---QTLIVRKMRKLTKEGLQWT-DKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 403 YIgflwvselFQSFI------IVSVLWYGGHLVLtqkmKGDLLVSFLLYQMQLGDNLRQMGEVWTGLM-QSVGAS---RK 472
Cdd:PLN03232 523 SA--------FNSFIlnsipvVVTLVSFGVFVLL----GGDLTPARAFTSLSLFAVLRSPLNMLPNLLsQVVNANvslQR 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 473 VFEYIDREPQI-QHNGEYMPEnvVGKIEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENfYV 551
Cdd:PLN03232 591 IEELLLSEERIlAQNPPLQPG--APAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-EL 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 552 PNAGQVLVDgvpleefehhyIHKKIALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEManahgfimqTTLKYE----- 626
Cdd:PLN03232 668 SHAETSSVV-----------IRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDV---------TALQHDldllp 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 627 ----TNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKN-LDGKSVILIAHRLSTVEKAD 701
Cdd:PLN03232 728 grdlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDeLKGKTRVLVTNQLHFLPLMD 807
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 702 KIVVINKGRVEQIGNHETLLKdtNGT-YAKLVQRQ-MMGDQKPRKRPAVARSGPQPAASINVAGPSQGNAM 770
Cdd:PLN03232 808 RIILVSEGMIKEEGTFAELSK--SGSlFKKLMENAgKMDATQEVNTNDENILKLGPTVTIDVSERNLGSTK 876
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
189-473 |
2.23e-26 |
|
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: 109.93 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATV-VATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQD 267
Cdd:cd18778 8 ALLSTLLGLVPPWLIRELVDLVtIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 268 VAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTY---- 343
Cdd:cd18778 88 LRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKvrpr 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 344 YDLLSERtqdtIAESNDVAEEVLSTMRTVRSFSCENVEADRFyGKLTHTLDVTRTKAIAYIGFLW-VSELFQSFIIVSVL 422
Cdd:cd18778 168 YRKVREA----LGELNALLQDNLSGIREIQAFGREEEEAKRF-EALSRRYRKAQLRAMKLWAIFHpLMEFLTSLGTVLVL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 71992290 423 WYGGHLVLTQKMK-GDlLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18778 243 GFGGRLVLAGELTiGD-LVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
518-729 |
3.17e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 110.97 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 518 DLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYI---HK-KIALVGQEPVLFAR-SVME 592
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppEKrRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 593 NVRYGVEVADTEIIRSCEMAnahgfIMQTtLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTES-- 670
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFER-----VIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRky 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 671 ------EHLVQEAiyknldGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKDTNGTYA 729
Cdd:TIGR02142 169 eilpylERLHAEF------GIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
189-725 |
4.89e-26 |
|
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: 115.39 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATVVATKSYPAL---SNAVYIMTIISLV--SAVAAG-FRGGSFEYAYARIQRAIRYDLFHG 262
Cdd:TIGR01271 888 LWLITDNPSAPNYVDQQHANASSPDVQKPVIitpTSAYYIFYIYVGTadSVLALGfFRGLPLVHTLLTVSKRLHEQMLHS 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 263 LVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSmIFMMKLSWRLSLVTFILVPIIFVaskIFGT 342
Cdd:TIGR01271 968 VLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGA-IFVVSVLQPYIFIAAIPVAVIFI---MLRA 1043
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 343 YYDLLSERTQDTIAESND-VAEEVLSTMR---TVRSFSCENVEADRFYGKL-THTLdvtrtkaiayIGFLWVSEL--FQS 415
Cdd:TIGR01271 1044 YFLRTSQQLKQLESEARSpIFSHLITSLKglwTIRAFGRQSYFETLFHKALnLHTA----------NWFLYLSTLrwFQM 1113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 416 FI-IVSVLWYGGHL---VLTQKMKGDLLVSFLLYQMQLGDNLRqmgevWT--------GLMQSVGasrKVFEYIDREPQI 483
Cdd:TIGR01271 1114 RIdIIFVFFFIAVTfiaIGTNQDGEGEVGIILTLAMNILSTLQ-----WAvnssidvdGLMRSVS---RVFKFIDLPQEE 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 484 ----QHNGEYMPENVV--------------GKIEFRNVHFSYpTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISL 545
Cdd:TIGR01271 1186 prpsGGGGKYQLSTVLvienphaqkcwpsgGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSA 1264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 546 LENFyVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKY 625
Cdd:TIGR01271 1265 LLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKL 1343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 626 ETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVV 705
Cdd:TIGR01271 1344 DFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLV 1423
|
570 580
....*....|....*....|
gi 71992290 706 INKGRVEQIGNHETLLKDTN 725
Cdd:TIGR01271 1424 IEGSSVKQYDSIQKLLNETS 1443
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
509-721 |
6.95e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.70 E-value: 6.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 509 TRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVL-FA 587
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RSVMENVRYG-----------VEVADTEIIRSCEMANAHGFIMQTTlkyetnvgekgTQMSGGQKQRIAIARALVREPAI 656
Cdd:PRK09536 92 FDVRQVVEMGrtphrsrfdtwTETDRAAVERAMERTGVAQFADRPV-----------TSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 657 LLLDEATSALDTesEHLVQE-AIYKNL--DGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLL 721
Cdd:PRK09536 161 LLLDEPTASLDI--NHQVRTlELVRRLvdDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
498-711 |
8.18e-26 |
|
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: 106.65 E-value: 8.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRS------------------DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLV 559
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 560 DG-VPLEEFEHHYihKKIALV-GQE-------PVLFARSVMENVrYGVEVAD--TEIIRSCEMANAhGFIMQTTLKyetn 628
Cdd:cd03267 81 AGlVPWKRRKKFL--RRIGVVfGQKtqlwwdlPVIDSFYLLAAI-YDLPPARfkKRLDELSELLDL-EELLDTPVR---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 629 vgekgtQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAI--YKNLDGKSVILIAHRLSTVEK-ADKIVV 705
Cdd:cd03267 153 ------QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeYNRERGTTVLLTSHYMKDIEAlARRVLV 226
|
....*.
gi 71992290 706 INKGRV 711
Cdd:cd03267 227 IDKGRL 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
497-725 |
1.10e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.56 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 497 KIEFRNVHFSYP--TRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLeefeHH---- 570
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI----THktkd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 571 ----YIHKKIALVGQ--EPVLFARSVMENVRYGVEVADTEIirscEMANAHGFIMQTTLKYETNVGEKGT-QMSGGQKQR 643
Cdd:PRK13646 78 kyirPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNL----DEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 644 IAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNL---DGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHET 719
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLL-KSLqtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE 232
|
....*.
gi 71992290 720 LLKDTN 725
Cdd:PRK13646 233 LFKDKK 238
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
498-718 |
1.42e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrSDQpILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEeFEHHYIHKKIA 577
Cdd:PRK11124 3 IQLNGINCFYG--AHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQE-----------PVLfarSVMENVrygVEvADTEIIR-SCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIA 645
Cdd:PRK11124 79 ELRRNvgmvfqqynlwPHL---TVQQNL---IE-APCRVLGlSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 646 IARALVREPAILLLDEATSALDTE-SEHLVqeAIYKNLDGKSV--ILIAHRLSTVEK-ADKIVVINKGRVEQIGNHE 718
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEiTAQIV--SIIRELAETGItqVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
498-711 |
1.70e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.10 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQ---PILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHY-IH 573
Cdd:PRK13633 5 IKCKNVSYKYESNEEStekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEP--VLFARSVMENVRYGVE---VADTEI-IRSCEMANAHGfiMQTTLKYETNVgekgtqMSGGQKQRIAIA 647
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPEnlgIPPEEIrERVDESLKKVG--MYEYRRHAPHL------LSGGQKQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 648 RALVREPAILLLDEATSALDTESEHLVQEAIyKNLDGKS---VILIAHRLSTVEKADKIVVINKGRV 711
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTI-KELNKKYgitIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
512-723 |
1.76e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.99 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 512 DQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLEnfyVPNAGQVLVDGVPLEEFEH--------HYIHKKIALVG 580
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLE---QPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 581 QEPVLFA-RSVMENVRYGVEVADTEIiRSCEMANAHGFIMQTTLKYETNVGEKgtQMSGGQKQRIAIARALVREPAILLL 659
Cdd:PRK11264 92 QNFNLFPhRTVLENIIEGPVIVKGEP-KEEATARARELLAKVGLAGKETSYPR--RLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 660 DEATSALDTEsehLVQE--AIYKNL--DGKSVILIAHRLSTV-EKADKIVVINKGRVEQIGNHETLLKD 723
Cdd:PRK11264 169 DEPTSALDPE---LVGEvlNTIRQLaqEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
513-692 |
2.18e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.94 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 513 QPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEE--------FEHhyihkkialvgqEPV 584
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGpgaergvvFQN------------EGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 585 LFARSVMENVRYGVEVADTEiiRSCEMANAHGFIMQttlkyetnVGEKGT------QMSGGQKQRIAIARALVREPAILL 658
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVE--KMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 71992290 659 LDEATSALDTESEHLVQEAIYK--NLDGKSVILIAH 692
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
518-723 |
4.16e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 107.49 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 518 DLSFTVEPGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDGVPLEEFEHHY---IHK-KIALVGQEPVLFA-RS 589
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTllrAIAGLER---PDSGRIRLGGEVLQDSARGIflpPHRrRIGYVFQEARLFPhLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 590 VMENVRYGVEVADT--------EIIrscEManahgfimqttLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDE 661
Cdd:COG4148 94 VRGNLLYGRKRAPRaerrisfdEVV---EL-----------LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 662 ATSALDTES--------EHLVQE-AIyknldgkSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKD 723
Cdd:COG4148 160 PLAALDLARkaeilpylERLRDElDI-------PILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
498-704 |
4.42e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.41 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:PRK10247 8 LQLQNVGYLA---GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVRYGVEvadteiIR--SCEMANAHGFIMQTTLKyETNVGEKGTQMSGGQKQRIAIARALVREPA 655
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQ------IRnqQPDPAIFLDDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71992290 656 ILLLDEATSALDTESEHLVQEAI--YKNLDGKSVILIAHRLSTVEKADKIV 704
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIhrYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
500-735 |
4.50e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 500 FRNVHFSYPTRsdqPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvpleefehhyiHKKIALV 579
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 580 GQEPVLFA-RSVMENVRYGV-----------------EVADTEIIR----SCEMANAHGF--------IMQ----TTLKY 625
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDaelraleaeleeleaklAEPDEDLERlaelQEEFEALGGWeaearaeeILSglgfPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 626 ETNVGEkgtqMSGGQKQRIAIARALVREPAILLLDEATSALDTES-----EHLVQeaiYKNldgkSVILIAH-R--LSTV 697
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN---YPG----TVLVVSHdRyfLDRV 215
|
250 260 270
....*....|....*....|....*....|....*....
gi 71992290 698 ekADKIVVINKGRveqignhetlLKDTNGTYAK-LVQRQ 735
Cdd:COG0488 216 --ATRILELDRGK----------LTLYPGNYSAyLEQRA 242
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
497-716 |
5.99e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 107.24 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 497 KIEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSSC---ISLLENFyvpNAGQVLVDGVPLEEFEHHyiH 573
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERI---TSGEIWIGGRVVNELEPA--D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEPVLFAR-SVMENVRYGVEVADT---EIIRSCEMAnahgfimQTTLKYETNVGEKGTQMSGGQKQRIAIARA 649
Cdd:PRK11650 76 RDIAMVFQNYALYPHmSVRENMAYGLKIRGMpkaEIEERVAEA-------ARILELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 650 LVREPAILLLDEATSaldtesehlvqeaiykNLDGKsviLIAH----------RLST---------VEK---ADKIVVIN 707
Cdd:PRK11650 149 IVREPAVFLFDEPLS----------------NLDAK---LRVQmrleiqrlhrRLKTtslyvthdqVEAmtlADRVVVMN 209
|
....*....
gi 71992290 708 KGRVEQIGN 716
Cdd:PRK11650 210 GGVAEQIGT 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
499-723 |
6.78e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.91 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 499 EFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSS---CIS-LLEnfyvPNAGQVLVDGVPLEEFE-HHYIH 573
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkAISgLLP----PRSGSIRFDGEDITGLPpHRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEPVLFAR-SVMENVRYGVEV--ADTEIIRSCEMAnahgfimqttlkYET--NVGE----KGTQMSGGQKQRI 644
Cdd:COG0410 78 LGIGYVPEGRRIFPSlTVEENLLLGAYArrDRAEVRADLERV------------YELfpRLKErrrqRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 645 AIARALVREPAILLLDEATSALdteSEHLVQE--AIYKNL--DGKSVILI---AHRLSTVekADKIVVINKGRVEQIGNH 717
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL---APLIVEEifEIIRRLnrEGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTA 220
|
....*.
gi 71992290 718 ETLLKD 723
Cdd:COG0410 221 AELLAD 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
515-715 |
1.09e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.32 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFehHYIHKKIALVGQEPVLFAR-SVMEN 593
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 594 VRYGVEV------ADTEIIRSCEMAnahgFIMQTTLKYETNvgEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALD 667
Cdd:PRK10851 95 IAFGLTVlprrerPNAAAIKAKVTQ----LLEMVQLAHLAD--RYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71992290 668 TESEH-----LVQeaIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIG 715
Cdd:PRK10851 169 AQVRKelrrwLRQ--LHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
498-710 |
1.52e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.68 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfEHHYIHKKIA 577
Cdd:PRK13536 42 IDLAGVSKSY---GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENV----RY-GVEVADTEIIRSCEMANAhgfimqttlKYETNVGEKGTQMSGGQKQRIAIARALV 651
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENLlvfgRYfGMSTREIEAVIPSLLEFA---------RLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAIYKNL-DGKSVILIAHRLSTVEK-ADKIVVINKGR 710
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGR 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
516-734 |
1.53e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 106.66 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYI----HKKIALVGQEPVLFAR-SV 590
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENVRYGVEVADT----------EIIRSCEMAN-AHGFimqttlkyetnvgekGTQMSGGQKQRIAIARALVREPAILLL 659
Cdd:PRK10070 124 LDNTAFGMELAGInaeerrekalDALRQVGLENyAHSY---------------PDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 660 DEATSALDTESEHLVQEAIYKnLDGK---SVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKDTNGTYAKLVQR 734
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVK-LQAKhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
498-710 |
5.15e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.35 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyIHKKIA 577
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQ----EPVLfarSVMENVR-----YGVEVADteiIRScemanahgfIMQTTLKY---ETNVGEKGTQMSGGQKQRIA 645
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvfgryFGLSAAA---ARA---------LVPPLLEFaklENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 646 IARALVREPAILLLDEATSALDTESEHLVQEAIYKNL-DGKSVILIAHRLSTVEK-ADKIVVINKGR 710
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGR 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
498-732 |
7.76e-24 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 108.11 E-value: 7.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYpTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLenfyvpnagqvlvdgvpLEEFE----HHYIH 573
Cdd:TIGR00957 637 ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----------------LAEMDkvegHVHMK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEPVLFARSVMENVRYGVEVADT---EIIRSCEMANAHGFIMQTTlkyETNVGEKGTQMSGGQKQRIAIARAL 650
Cdd:TIGR00957 699 GSVAYVPQQAWIQNDSLRENILFGKALNEKyyqQVLEACALLPDLEILPSGD---RTEIGEKGVNLSGGQKQRVSLARAV 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 651 VREPAILLLDEATSALDTE-SEHLVQEAIYKN--LDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLkDTNGT 727
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEgvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL-QRDGA 854
|
....*
gi 71992290 728 YAKLV 732
Cdd:TIGR00957 855 FAEFL 859
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
499-734 |
8.81e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.91 E-value: 8.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 499 EFRNVHFSyptRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLL---ENfYVPNAGQVLVDGVPLEEFE-HHYIHK 574
Cdd:COG0396 2 EIKNLHVS---VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSpDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEPVLFArsvmenvryGVEVADteIIRSceMANAHGFIMQTTLKYETNVGEKGTQM---------------SGG 639
Cdd:COG0396 78 GIFLAFQYPVEIP---------GVSVSN--FLRT--ALNARRGEELSAREFLKLLKEKMKELgldedfldryvnegfSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 640 QKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAI--YKNlDGKSVILIAH--RLSTVEKADKIVVINKGRVEQIG 715
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVnkLRS-PDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
250 260
....*....|....*....|
gi 71992290 716 NHETLLK-DTNGtYAKLVQR 734
Cdd:COG0396 224 GKELALElEEEG-YDWLKEE 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
498-723 |
9.95e-24 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 100.31 E-value: 9.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRsdqPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvplEEFEHHYIHKK-- 575
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG---QDITKLPMHKRar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 --IALVGQEPVLFAR-SVMENVRYGVEVA-DTEIIRScEMANAhgfiMQTTLKYETNVGEKGTQMSGGQKQRIAIARALV 651
Cdd:cd03218 75 lgIGYLPQEASIFRKlTVEENILAVLEIRgLSKKERE-EKLEE----LLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAIyKNLDGKSV-ILIA-HRLS-TVEKADKIVVINKGRVEQIGNHETLLKD 723
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKII-KILKDRGIgVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
509-706 |
1.01e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.86 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 509 TRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNA---GQVLVDGVPLEEFEHHyiHKKIALVGQEPVL 585
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 586 FAR-SVMENVRYGV------EVADTEIIRSCEMANAHGFimqttlkYETNVGekgtQMSGGQKQRIAIARALVREPAILL 658
Cdd:COG4136 88 FPHlSVGENLAFALpptigrAQRRARVEQALEEAGLAGF-------ADRDPA----TLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 659 LDEATSALDTES---------EHLVQEAIyknldgkSVILIAHRLSTVEKADKIVVI 706
Cdd:COG4136 157 LDEPFSKLDAALraqfrefvfEQIRQRGI-------PALLVTHDEEDAPAAGRVLDL 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
498-723 |
1.98e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.97 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYP--TRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPL----EEFEHHY 571
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQ--EPVLFARSVMENVRYGVE---VADTEIIRSCEMANAHGFIMQTTlkYETNVGEkgtqMSGGQKQRIAI 646
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQnfgVSQEEAEALAREKLALVGISESL--FEKNPFE----LSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 647 ARALVREPAILLLDEATSALDTESEHLVQEaIYKNL--DGKSVILIAHRLSTV-EKADKIVVINKGRVEQIGNHETLLKD 723
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLhqSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
498-723 |
2.06e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.15 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTR--------SDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLenfyVPNAGQVLVDGVPLEE 566
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglALLRL----IPSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 567 FEHHYIH---KKIALVGQEPvlFA-----RSVMENVRYGVEVADTEIIRScEMANAHGFIMQTtlkyetnVGEKGTQM-- 636
Cdd:COG4172 352 LSRRALRplrRRMQVVFQDP--FGslsprMTVGQIIAEGLRVHGPGLSAA-ERRARVAEALEE-------VGLDPAARhr 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 637 -----SGGQKQRIAIARALVREPAILLLDEATSALDteseHLVQEAIyknLD---------GKSVILIAHRLSTVEK-AD 701
Cdd:COG4172 422 yphefSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQI---LDllrdlqrehGLAYLFISHDLAVVRAlAH 494
|
250 260
....*....|....*....|...
gi 71992290 702 KIVVINKGR-VEQiGNHETLLKD 723
Cdd:COG4172 495 RVMVMKDGKvVEQ-GPTEQVFDA 516
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
500-715 |
2.44e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.80 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 500 FRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENFyvpNAGQVLVDGVPLEEFEHHyiHKKI 576
Cdd:PRK11000 6 LRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTllrMIAGLEDI---TSGDLFIGEKRMNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPVLFAR-SVMENVRYGVEVADT---EIIRSCEMANAhgfIMQTTLKYEtnvgEKGTQMSGGQKQRIAIARALVR 652
Cdd:PRK11000 78 GMVFQSYALYPHlSVAENMSFGLKLAGAkkeEINQRVNQVAE---VLQLAHLLD----RKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 653 EPAILLLDEATSALDTESEhlVQEAI-----YKNLdGKSVILIAHrlSTVEK---ADKIVVINKGRVEQIG 715
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALR--VQMRIeisrlHKRL-GRTMIYVTH--DQVEAmtlADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
193-473 |
2.47e-23 |
|
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: 101.03 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 193 SITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFrggsFEYAYARIQRAIRYDL----FHGLVKQDV 268
Cdd:cd18546 12 TAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRA----QTRLTGRTGERLLYDLrlrvFAHLQRLSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 269 AFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLS 348
Cdd:cd18546 88 DFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 349 ERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFyGKLTHTLDVTRTKAIAYIGFLW-VSELFQSFIIVSVLWYGGH 427
Cdd:cd18546 168 RRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF-AELSDDYRDARLRAQRLVAIYFpGVELLGNLATAAVLLVGAW 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 71992290 428 LVLTqkmkGDL----LVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18546 247 RVAA----GTLtvgvLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
498-725 |
2.97e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 99.77 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSyptRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLL--ENFyvPNAGQVLV------DGVPLEEfeh 569
Cdd:COG1119 4 LELRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgDLP--PTYGNDVRlfgerrGGEDVWE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 570 hyIHKKIALVGQEpvLFAR-SVMENVR-------YGV-----EVADTEIIRSCEMANAHGfimqttlkyetnVGEKG--- 633
Cdd:COG1119 76 --LRKRIGLVSPA--LQLRfPRDETVLdvvlsgfFDSiglyrEPTDEQRERARELLELLG------------LAHLAdrp 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 634 -TQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYK--NLDGKSVILIAHRLSTV-EKADKIVVINKG 709
Cdd:COG1119 140 fGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIpPGITHVLLLKDG 219
|
250
....*....|....*.
gi 71992290 710 RVEQIGNHETLLKDTN 725
Cdd:COG1119 220 RVVAAGPKEEVLTSEN 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
498-711 |
4.23e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEP--VLFARSVMENVRYGVE---VADTEIIRSCEMAnahgFIMQTTLKYETnvgEKGTQMSGGQKQRIAIARALVR 652
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMEnqgIPREEMIKRVDEA----LLAVNMLDFKT---REPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 653 EPAILLLDEATSALDTESEHLVQEAIYKNLDGK--SVILIAHRLSTVEKADKIVVINKGRV 711
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
152-709 |
4.78e-23 |
|
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: 105.76 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 152 LEDE-DLEVAPKQTFELIFRLLQYCkreWLWHISgFSWLFIY--SITRIFVPYYTGQVIATVVAtKSYPALSNAVYIMTI 228
Cdd:TIGR01271 53 LEREwDRELASAKKNPKLLNALRRC---FFWRFV-FYGILLYfgEATKAVQPLLLGRIIASYDP-FNAPEREIAYYLALG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 229 ISLVSAVAAGFRGGSFeYAYARIQRAIRYDLFHGLVKQDVAF----YDAHKTGEVTSRLAADCQTMSDTVALNVNVFLR- 303
Cdd:TIGR01271 128 LCLLFIVRTLLLHPAI-FGLHHLGMQMRIALFSLIYKKTLKLssrvLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAp 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 304 -NCVMLLGsMIFMMKLSWRLSLVTFILVPIIFVA--SKIFGTYYDllseRTQDTIAESNDVAEEVLSTMRTVRSFSCENV 380
Cdd:TIGR01271 207 lQVILLMG-LIWELLEVNGFCGLGFLILLALFQAclGQKMMPYRD----KRAGKISERLAITSEIIENIQSVKAYCWEEA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 381 eADRFYGKLTHTlDVTRTKAIAYIGFLWVSELFQSFIIVSVLwyggHLVLTQKMKGDLL------VSF-LLYQMQLGDNL 453
Cdd:TIGR01271 282 -MEKIIKNIRQD-ELKLTRKIAYLRYFYSSAFFFSGFFVVFL----SVVPYALIKGIILrrifttISYcIVLRMTVTRQF 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 454 RQMGEVWtglMQSVGASRKVFEYIDREPQ--IQHN---GEYMPENVVG-----------KIEFRN-----------VHFS 506
Cdd:TIGR01271 356 PGAIQTW---YDSLGAITKIQDFLCKEEYktLEYNlttTEVEMVNVTAswdegigelfeKIKQNNkarkqpngddgLFFS 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 507 YPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvpleefehhyihkKIALVGQEPVLF 586
Cdd:TIGR01271 433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIM 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 587 ARSVMENVRYGV---EVADTEIIRSCEMANAhgfIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEAT 663
Cdd:TIGR01271 500 PGTIKDNIIFGLsydEYRYTSVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 71992290 664 SALDTESEHLVQEA-IYKNLDGKSVILIAHRLSTVEKADKIVVINKG 709
Cdd:TIGR01271 577 THLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
513-713 |
5.04e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 103.61 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 513 QPILKDLSFTVEPGETVALVGPSGSGKS----SCISLLENFYVPNAGQVLVDGVPLeefehhyIH-----------KKIA 577
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-------LGlserelrrirgNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPV-----LF--ARSVMENVR----YGVEVADTEII---RSCEMANAhgfimqttlkyETNVGEKGTQMSGGQKQR 643
Cdd:COG4172 96 MIFQEPMtslnpLHtiGKQIAEVLRlhrgLSGAAARARALellERVGIPDP-----------ERRLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 644 IAIARALVREPAILLLDEATSALD-TesehlVQEAIYKNLD------GKSVILIAHRLSTVEK-ADKIVVINKGR-VEQ 713
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDvT-----VQAQILDLLKdlqrelGMALLLITHDLGVVRRfADRVAVMRQGEiVEQ 238
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
190-442 |
5.67e-23 |
|
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: 99.83 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 190 FIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVA 269
Cdd:cd18570 12 LLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 270 FYDAHKTGEVTSRLAaDCQTMSDTVA-LNVNVFLrNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLS 348
Cdd:cd18570 92 FFETRKTGEIISRFN-DANKIREAISsTTISLFL-DLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 349 ERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWYGGHL 428
Cdd:cd18570 170 REVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYL 249
|
250
....*....|....
gi 71992290 429 VLTQKMKGDLLVSF 442
Cdd:cd18570 250 VIKGQLSLGQLIAF 263
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
498-714 |
6.63e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 99.11 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPT------RSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFE--- 568
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 569 HHYIHKKIALVGQE------PVLFARSVM-ENVRYGVEVADTE-IIRSCEMANAHGFIMQTTLKYETnvgekgtQMSGGQ 640
Cdd:TIGR02769 83 RRAFRRDVQLVFQDspsavnPRMTVRQIIgEPLRHLTSLDESEqKARIAELLDMVGLRSEDADKLPR-------QLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 641 KQRIAIARALVREPAILLLDEATSALDTesehLVQEAIYKNLD------GKSVILIAHRLSTVEK-ADKIVVINKGR-VE 712
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDM----VLQAVILELLRklqqafGTAYLFITHDLRLVQSfCQRVAVMDKGQiVE 231
|
..
gi 71992290 713 QI 714
Cdd:TIGR02769 232 EC 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
498-711 |
8.59e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSY-PTRSDQPI-LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG--VPLEEFEHHY-- 571
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKNLkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQ--EPVLFARSVMENVRYGVE---VADTEiirscEMANAHGFIMQTTLKyeTNVGEKGT-QMSGGQKQRIA 645
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfgFSEDE-----AKEKALKWLKKVGLS--EDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 646 IARALVREPAILLLDEATSALDTESEHLVQEaIYKNLD--GKSVILIAHRLSTV-EKADKIVVINKGRV 711
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQkaGHTVILVTHNMDDVaEYADDVLVLEHGKL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
490-720 |
8.73e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.86 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 490 MPENVVGKIEFRNVHFSYPTR--------SDQPILKDLSFTVEPGETVALVGPSGSGKSSC-ISLLEnfYVPNAGQVLVD 560
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPIRkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTgLALLR--LINSQGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 561 GVPLEEFEHHY---IHKKIALVGQEP--VLFAR-SVMENVRYGVEV------ADTEIIRSCEMANAHGFIMQTTLKYETn 628
Cdd:PRK15134 346 GQPLHNLNRRQllpVRHRIQVVFQDPnsSLNPRlNVLQIIEEGLRVhqptlsAAQREQQVIAVMEEVGLDPETRHRYPA- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 629 vgekgtQMSGGQKQRIAIARALVREPAILLLDEATSALDTEsehlVQEAI---YKNLDGK---SVILIAHRLSTVEK-AD 701
Cdd:PRK15134 425 ------EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT----VQAQIlalLKSLQQKhqlAYLFISHDLHVVRAlCH 494
|
250
....*....|....*....
gi 71992290 702 KIVVINKGRVEQIGNHETL 720
Cdd:PRK15134 495 QVIVLRQGEVVEQGDCERV 513
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
224-434 |
9.11e-23 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 99.66 E-value: 9.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 224 YIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLR 303
Cdd:cd18558 63 YYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 304 NCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEAD 383
Cdd:cd18558 143 NIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEET 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71992290 384 RFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWYGGHLVLTQKM 434
Cdd:cd18558 223 RYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEY 273
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
516-720 |
1.54e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 99.27 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIH---KKIALVGQEPvlFArSVme 592
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrQKIQIVFQNP--YG-SL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 593 NVRYGVevadteiirscemanahGFIMQTTLKYETNVG-----EKGTQM------------------SGGQKQRIAIARA 649
Cdd:PRK11308 106 NPRKKV-----------------GQILEEPLLINTSLSaaerrEKALAMmakvglrpehydryphmfSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 650 LVREPAILLLDEATSALDTEsehlVQEAIYkNL--D-----GKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETL 720
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVS----VQAQVL-NLmmDlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
498-739 |
1.80e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.79 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvplEEFEHHYIHKK-I 576
Cdd:PRK11432 7 VVLKNITKRF---GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPVLFAR-SVMENVRYGVE---VADTEIIR----SCEMANAHGFimqttlkyetnvGEKGT-QMSGGQKQRIAIA 647
Cdd:PRK11432 81 CMVFQSYALFPHmSLGENVGYGLKmlgVPKEERKQrvkeALELVDLAGF------------EDRYVdQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 648 RALVREPAILLLDEATSALDTESEHLVQEAI---YKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDT 724
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIrelQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
250
....*....|....*
gi 71992290 725 NgtyaKLVQRQMMGD 739
Cdd:PRK11432 229 A----SRFMASFMGD 239
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
498-723 |
1.99e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 97.60 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRS------DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHY 571
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQEPvlfARSVMENVRYGvEVADTEIIRSCEMANA--HGFIMQTtLKyetNVG------EKGTQM-SGGQKQ 642
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIG-QILEEPLRLNTDLTAEerEERIFAT-LR---LVGllpehaNFYPHMlSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 643 RIAIARALVREPAILLLDEATSALD----TESEHLVQEaIYKNLdGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNH 717
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDmsvrSQIINLMLE-LQEKL-GISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKT 234
|
....*.
gi 71992290 718 ETLLKD 723
Cdd:COG4167 235 AEVFAN 240
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
223-449 |
2.17e-22 |
|
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: 98.32 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 223 VYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDL----FHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNV 298
Cdd:cd18550 38 LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLrvqlYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 299 NVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLST--MRTVRSFS 376
Cdd:cd18550 118 TSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFG 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71992290 377 CENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQL 449
Cdd:cd18550 198 REDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRL 270
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
501-711 |
2.26e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.44 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 501 RNVHFSYPTRSdqpILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfehhyIHKKIALVG 580
Cdd:PRK11247 16 NAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 581 QEPVLFA-RSVMENVRYGvevadteiIRSCEMANAHGFIMQTTLkyETNVGEKGTQMSGGQKQRIAIARALVREPAILLL 659
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLG--------LKGQWRDAALQALAAVGL--ADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 660 DEATSALDTESEHLVQEAIyKNL---DGKSVILIAHRLS-TVEKADKIVVINKGRV 711
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLI-ESLwqqHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
509-711 |
3.21e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.06 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 509 TRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEF---EHHYIHKKIALVGQEPV- 584
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSIs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 585 ------LFARSVMENVRYGVEVADTE-IIRSCEMANAHGFImqttlkyETNVGEKGTQMSGGQKQRIAIARALVREPAIL 657
Cdd:PRK10419 101 avnprkTVREIIREPLRHLLSLDKAErLARASEMLRAVDLD-------DSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 658 LLDEATSALDTeseHLVQEAI--YKNLD---GKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:PRK10419 174 ILDEAVSNLDL---VLQAGVIrlLKKLQqqfGTACLFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
514-710 |
3.51e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 95.96 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 514 PILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVL-------VDGVPLEEFEHHYIHKK-IALVGQepvl 585
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwVDLAQASPREILALRRRtIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 586 FARS---------VMEN-VRYGVEVAdteiiRSCEMANAhgfiMQTTLkyetNVGEK------GTqMSGGQKQRIAIARA 649
Cdd:COG4778 101 FLRViprvsaldvVAEPlLERGVDRE-----EARARARE----LLARL----NLPERlwdlppAT-FSGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 650 LVREPAILLLDEATSALDTESEHLVQEAI--YKNlDGKSVILIAHRLSTVEK-ADKIVVINKGR 710
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIeeAKA-RGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
516-736 |
4.52e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.77 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYvPNA---GQVLVDGVPLE-----EFEHH---YIHKKIALVGQepv 584
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQasnirDTERAgiaIIHQELALVKE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 585 lfaRSVMENVRYGVEVADTEIIRSCEM-ANAHGFIMQttLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEAT 663
Cdd:PRK13549 97 ---LSVLENIFLGNEITPGGIMDYDAMyLRAQKLLAQ--LKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 664 SALdTESEHLVQEAIYKNLDGKSV--ILIAHRLSTVEK-ADKIVVINKGRveQIGNHETLLKDTNGTYAKLVQRQM 736
Cdd:PRK13549 172 ASL-TESETAVLLDIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGR--HIGTRPAAGMTEDDIITMMVGREL 244
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
518-720 |
6.54e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 97.49 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 518 DLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHY---IHKKIALVGQEPvlFArSVmeNV 594
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrpLRRRMQMVFQDP--YA-SL--NP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 595 RYGVEvadtEIIrscemanAHGFIMQTTLKyETNVGEKGTQM------------------SGGQKQRIAIARALVREPAI 656
Cdd:COG4608 111 RMTVG----DII-------AEPLRIHGLAS-KAERRERVAELlelvglrpehadryphefSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 657 LLLDEATSALDTeSehlVQEAIYkNL--D-----GKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETL 720
Cdd:COG4608 179 IVCDEPVSALDV-S---IQAQVL-NLleDlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
496-709 |
9.41e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 9.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSypTRSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENFYvpnAGQVLVDGvpleefehhyi 572
Cdd:COG4178 361 GALALEDLTLR--TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTllrAIAGLWPYG---SGRIARPA----------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 HKKIALVGQEPVLFARSVMENVRY---GVEVADTEIIRSCEMANAHGFIMQttLKYETNVGEkgtQMSGGQKQRIAIARA 649
Cdd:COG4178 425 GARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGHLAER--LDEEADWDQ---VLSLGEQQRLAFARL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 650 LVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKG 709
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
490-711 |
1.17e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 490 MPENVvgkIEFRNVHFSYPTRSDQpiLKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEH 569
Cdd:PRK13636 1 MEDYI---LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 570 HY--IHKKIALVGQEP--VLFARSVMENVRYGV---EVADTEIIRSCEMANAHGFImqttlkyeTNVGEKGTQ-MSGGQK 641
Cdd:PRK13636 76 GLmkLRESVGMVFQDPdnQLFSASVYQDVSFGAvnlKLPEDEVRKRVDNALKRTGI--------EHLKDKPTHcLSFGQK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 642 QRIAIARALVREPAILLLDEATSALD----TESEHLVQEaIYKNLdGKSVILIAHRLSTVE-KADKIVVINKGRV 711
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVE-MQKEL-GLTIIIATHDIDIVPlYCDNVFVMKEGRV 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
499-711 |
1.24e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 94.51 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 499 EFRNVHFSYpTRSdqPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFE-HHYIHKKIA 577
Cdd:TIGR03410 2 EVSNLNVYY-GQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFAR-SVMENVRYGVEV---ADTEIIrscemanAHGFIMQTTLKyeTNVGEKGTQMSGGQKQRIAIARALVRE 653
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTGLAAlprRSRKIP-------DEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 654 PAILLLDEATSALDTESEHLVQEAI--YKNLDGKSVILIAHRLS-TVEKADKIVVINKGRV 711
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIrrLRAEGGMAILLVEQYLDfARELADRYYVMERGRV 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
498-710 |
1.55e-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: 91.36 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVpleefehhyihKKIA 577
Cdd:cd03221 1 IELENLSKTY---GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVgqepvlfarsvmenvrygvevadteiirscemanahgfimqttlkyetnvgekgTQMSGGQKQRIAIARALVREPAIL 657
Cdd:cd03221 67 YF------------------------------------------------------EQLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 658 LLDEATSALDTESEHLVQEAIyKNLDGkSVILIAH-R--LSTVekADKIVVINKGR 710
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
498-711 |
1.79e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 92.98 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSyptRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENF--YVPNAGQVLVDGVPLEEFEHHYIHKK 575
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 -IALVGQEPVLFArsvmenvryGVEVADteIIRSCemanahgfimqttlkyetNVGekgtqMSGGQKQRIAIARALVREP 654
Cdd:cd03217 78 gIFLAFQYPPEIP---------GVKNAD--FLRYV------------------NEG-----FSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 655 AILLLDEATSALDTESEHLVQEAIYKNLD-GKSVILIAH--RLSTVEKADKIVVINKGRV 711
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
516-703 |
2.61e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.07 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLL--------------------ENFYVPNAgqvlvDGVPLEefehhyihKK 575
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtitgsivyngHNIYSPRT-----DTVDLR--------KE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVLFARSVMENVRYGVEVA---DTEIIRSCEMANAHGFIMQTTLK---YETNVGekgtqMSGGQKQRIAIARA 649
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENVVYGLRLKgikDKQVLDEAVEKSLKGASIWDEVKdrlHDSALG-----LSGGQQQRVCIARV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71992290 650 LVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLstvEKADKI 703
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM---QQASRI 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
498-736 |
3.18e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 99.81 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVdgvpleefehhyIHKKIA 577
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVRYGVEVADTEIIRScemanahgfIMQTTLKYE---------TNVGEKGTQMSGGQKQRIAIAR 648
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSPFDPERYERA---------IDVTALQHDldllpggdlTEIGERGVNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 649 ALVREPAILLLDEATSALDTeseHLVQEA----IYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKdt 724
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDA---HVGRQVfdkcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-- 828
|
250
....*....|..
gi 71992290 725 NGtyaKLVQRQM 736
Cdd:PLN03130 829 NG---PLFQKLM 837
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
223-459 |
3.35e-21 |
|
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: 95.33 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 223 VYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFL 302
Cdd:cd18565 57 GGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSII 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 303 RNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEA 382
Cdd:cd18565 137 RVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFER 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 383 DRF----YGKLTHTLDVTRTKaIAYIGFLWVSELFqSFIIvsVLWYGGHLVLT--QKMKGDL----LVSFLLYQMQLGDN 452
Cdd:cd18565 217 ERVadasEEYRDANWRAIRLR-AAFFPVIRLVAGA-GFVA--TFVVGGYWVLDgpPLFTGTLtvgtLVTFLFYTQRLLWP 292
|
....*..
gi 71992290 453 LRQMGEV 459
Cdd:cd18565 293 LTRLGDL 299
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
502-709 |
3.93e-21 |
|
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: 94.15 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 502 NVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvpleefehhyihkKIALVGQ 581
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 582 EPVLFARSVMENVRYGV---EVADTEIIRSCEMANAhgfIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILL 658
Cdd:cd03291 106 FSWIMPGTIKENIIFGVsydEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 71992290 659 LDEATSALDTESEHLVQEA-IYKNLDGKSVILIAHRLSTVEKADKIVVINKG 709
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
498-709 |
4.19e-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: 92.39 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKK-- 575
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 --IALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVRE 653
Cdd:cd03290 79 ysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 71992290 654 PAILLLDEATSALDTE-SEHLVQEAIYKNL--DGKSVILIAHRLSTVEKADKIVVINKG 709
Cdd:cd03290 159 TNIVFLDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
498-712 |
4.39e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVdGVPLeefehhyihkKIA 577
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLF--ARSVMENVRYGVEVADTEIIRSceMANAHGFI--MQttlkyETNVGEkgtqMSGGQKQRIAIARALVRE 653
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRG--YLGRFLFSgdDA-----FKPVGV----LSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 654 PAILLLDEATSALDTESEHLVQEAIyKNLDGkSVILIAH-R--LSTVekADKIVVINKGRVE 712
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEAL-DDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
499-738 |
4.40e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.67 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 499 EFRNVHFSYP-TRSdqpiLKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPleefeHHY------ 571
Cdd:PRK11288 6 SFDGIGKTFPgVKA----LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQE----PVLfarSVMENVRYGvevadteiirscEMANAHGFIMQTTLKYET-----NVGE------KGTQM 636
Cdd:PRK11288 77 LAAGVAIIYQElhlvPEM---TVAENLYLG------------QLPHKGGIVNRRLLNYEAreqleHLGVdidpdtPLKYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 637 SGGQKQRIAIARALVREPAILLLDEATSALDT-ESEHLVqeAIYKNL--DGKSVILIAHRLSTV-EKADKIVVINKGRve 712
Cdd:PRK11288 142 SIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLF--RVIRELraEGRVILYVSHRMEEIfALCDAITVFKDGR-- 217
|
250 260
....*....|....*....|....*.
gi 71992290 713 QIGNHETLLKDTNgtyAKLVQrQMMG 738
Cdd:PRK11288 218 YVATFDDMAQVDR---DQLVQ-AMVG 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
512-711 |
4.54e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.54 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 512 DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVL-FARSV 590
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENVRYG------------------VEVA--DTEIIrscEMANahgfimqttlkyetnvgEKGTQMSGGQKQRIAIARAL 650
Cdd:PRK11231 94 RELVAYGrspwlslwgrlsaednarVNQAmeQTRIN---HLAD-----------------RRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 651 VREPAILLLDEATSALD----TESEHLVQEAiykNLDGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNQASRyCDHLVVLANGHV 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
509-691 |
5.38e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 509 TRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEH----HYIHKKIALvgqEPV 584
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeacHYLGHRNAM---KPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 585 LfarSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETnvgekgtqMSGGQKQRIAIARALVREPAILLLDEATS 664
Cdd:PRK13539 88 L---TVAENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGY--------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*..
gi 71992290 665 ALDTESEHLVQEAIYKNLDGKSVILIA 691
Cdd:PRK13539 157 ALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
190-470 |
7.28e-21 |
|
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: 93.70 E-value: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 190 FIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGF---RGGSFEYayaRIQRAIRYDLFHGLVKQ 266
Cdd:cd18540 12 LLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLfirLAGKIEM---GVSYDLRKKAFEHLQTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 267 DVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFgtyydl 346
Cdd:cd18540 89 SFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYF------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 347 lsertQDTIAESNDVAEEVLSTM-----------RTVRSFSCENVEADRFyGKLTHTLDVTRTKAIAYIGFLWVSELFQS 415
Cdd:cd18540 163 -----QKKILKAYRKVRKINSRItgafnegitgaKTTKTLVREEKNLREF-KELTEEMRRASVRAARLSALFLPIVLFLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 416 FIIVS-VLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGlMQSVGAS 470
Cdd:cd18540 237 SIATAlVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAE-LQSAQAS 291
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
516-711 |
7.62e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.38 E-value: 7.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG-VPLEEfEHHYIhKKIALV-GQepvlfaRS---- 589
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKR-RKEFA-RRIGVVfGQ------RSqlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 590 ---VMENVR-----YGV--EVADTEIIRSCEMANAHGFIMQTTlkyetnvgekgTQMSGGQKQRIAIARALVREPAILLL 659
Cdd:COG4586 110 dlpAIDSFRllkaiYRIpdAEYKKRLDELVELLDLGELLDTPV-----------RQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 660 DEATSALDTESEHLVQEAI--YKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLkeYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
189-449 |
9.06e-21 |
|
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: 93.23 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDV 268
Cdd:cd18548 8 KLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 269 AFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLS 348
Cdd:cd18548 88 AEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 349 ERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFyGKLTHTLDVTRTKAIAYIGFLW-VSELFQSFIIVSVLWYGGH 427
Cdd:cd18548 168 KKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERF-DKANDDLTDTSLKAGRLMALLNpLMMLIMNLAIVAILWFGGH 246
|
250 260
....*....|....*....|...
gi 71992290 428 LVLTQKMK-GDlLVSFLLYQMQL 449
Cdd:cd18548 247 LINAGSLQvGD-LVAFINYLMQI 268
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
516-715 |
1.16e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 91.76 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIhkkiaLVGQEPVLFA-RSVMENV 594
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 595 RYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNvgEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLV 674
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAAD--KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71992290 675 QEAIYK--NLDGKSVILIAHRL-STVEKADKIVVINKGRVEQIG 715
Cdd:TIGR01184 154 QEELMQiwEEHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
496-725 |
1.35e-20 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 92.61 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYpTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFyVPNAGQVLVDGVPLEEFEHHYIHKK 575
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPA 655
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 656 ILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDTN 725
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
515-718 |
1.37e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 97.93 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCI-SLLENFYVpNAGQVLVDgvpleefehhyihKKIALVGQEPVLFARSVMEN 593
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFEI-SEGRVWAE-------------RSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 594 VRYGVE--VAD-TEIIRSCEManaHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTE- 669
Cdd:PTZ00243 741 ILFFDEedAARlADAVRVSQL---EADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHv 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 71992290 670 SEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHE 718
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
498-724 |
1.39e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.56 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIA 577
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEP--VLFARSVMENVRYG-VEVA-DTEIIRSCEMANAHgfimqtTLKYETNVGEKGTQMSGGQKQRIAIARALVRE 653
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpINLGlDEETVAHRVSSALH------MLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 654 PAILLLDEATSALDTESehlVQEAIYKNLD-----GKSVILIAHRLSTV-EKADKIVVINKGR------VEQIGNHETLL 721
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQG---VKELIDFLNDlpetyGMTVIFSTHQLDLVpEMADYIYVMDKGRivaygtVEEIFLQPDLL 232
|
...
gi 71992290 722 KDT 724
Cdd:PRK13652 233 ARV 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
516-720 |
1.91e-20 |
|
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: 90.51 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfEHHYIHKKIALVGQEPVL-FARSVMENV 594
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVdDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 595 R-----YGV------EVADtEIIRSCEMANAHGFIMQTtlkyetnvgekgtqMSGGQKQRIAIARALVREPAILLLDEAT 663
Cdd:cd03265 95 YiharlYGVpgaerrERID-ELLDFVGLLEAADRLVKT--------------YSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 664 SALDTESEHLVQEAIYKNLD--GKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETL 720
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
498-720 |
2.03e-20 |
|
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: 95.64 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENF--YVPNAGQVL----------------- 558
Cdd:TIGR03269 1 IEVKNLTKKF---DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 559 ------VDGVPLEEFEHHY----------IHKKIALVGQEPvlFA----RSVMENVRYGVEVADTEIIRSCEMAnahgfi 618
Cdd:TIGR03269 78 vgepcpVCGGTLEPEEVDFwnlsdklrrrIRKRIAIMLQRT--FAlygdDTVLDNVLEALEEIGYEGKEAVGRA------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 619 mqTTLKYETNVGEKGTQ----MSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNL--DGKSVILIAH 692
Cdd:TIGR03269 150 --VDLIEMVQLSHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSH 227
|
250 260
....*....|....*....|....*....
gi 71992290 693 RLSTVEK-ADKIVVINKGRVEQIGNHETL 720
Cdd:TIGR03269 228 WPEVIEDlSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
498-711 |
2.76e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.95 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQ-PILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEF--------- 567
Cdd:PRK10535 5 LELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadalaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 568 -EHH-YIHKKIALvgqepvLFARSVMENVRYGVEVADTEIIRSCEMANAhgfiMQTTLKYETNVGEKGTQMSGGQKQRIA 645
Cdd:PRK10535 85 rEHFgFIFQRYHL------LSHLTAAQNVEVPAVYAGLERKQRLLRAQE----LLQRLGLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 646 IARALVREPAILLLDEATSALDTESEHLVQeAIYKNL--DGKSVILIAHRLSTVEKADKIVVINKGRV 711
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVM-AILHQLrdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
498-720 |
3.94e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.53 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKS---SCIS-LLEnfyvPNAGQVLVDGVPLEEFEHHYIH 573
Cdd:COG4604 2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKStllSMISrLLP----PDSGEVLVDGLDVATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEPVLFAR-SVMENVRYG--------VEVADTEIIRSC-------EMANAhgFImqttlkyetnvgekgTQMS 637
Cdd:COG4604 75 KRLAILRQENHINSRlTVRELVAFGrfpyskgrLTAEDREIIDEAiayldleDLADR--YL---------------DELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 638 GGQKQRIAIARALVREPAILLLDEATSALDTesEHLVQeaIYKNLD------GKSVILIAHRLSTVEK-ADKIV------ 704
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM--KHSVQ--MMKLLRrladelGKTVVIVLHDINFASCyADHIVamkdgr 213
|
250
....*....|....*.
gi 71992290 705 VINKGRVEQIGNHETL 720
Cdd:COG4604 214 VVAQGTPEEIITPEVL 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
510-692 |
5.30e-20 |
|
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: 88.70 E-value: 5.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 510 RSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLeEFEHHYIHKKIALVGQEPVLFAR- 588
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 589 SVMENVRYGVEVADTEiirSCEMANAhgfimqttlkyetNVGEKG------TQMSGGQKQRIAIARALVREPAILLLDEA 662
Cdd:cd03231 89 SVLENLRFWHADHSDE---QVEEALA-------------RVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|.
gi 71992290 663 TSALDTESEHLVQEAIYKNLD-GKSVILIAH 692
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCArGGMVVLTTH 183
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
512-706 |
7.78e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.06 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 512 DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvpleefehhyiHKKIALVGQ---EPVLFAR 588
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 589 SVMENVRYGV----------EVADTEII-RSCEMANAHGFIMQTtlkyetnVGEkgtqMSGGQKQRIAIARALVREPAIL 657
Cdd:NF040873 73 TVRDLVAMGRwarrglwrrlTRDDRAAVdDALERVGLADLAGRQ-------LGE----LSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 71992290 658 LLDEATSALDTESEHLVQEAIYKNL-DGKSVILIAHRLSTVEKADKIVVI 706
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
498-715 |
8.31e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.10 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTrsdQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLeNFYVPNAGQVLVDGvPLEEFEH-------- 569
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEG-RVEFFNQniyerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 570 -HYIHKKIALVGQEPVLFARSVMENVRYGVEVADTEiiRSCEMANahgfIMQTTLK-------YETNVGEKGTQMSGGQK 641
Cdd:PRK14258 83 lNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWR--PKLEIDD----IVESALKdadlwdeIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 642 QRIAIARALVREPAILLLDEATSALDTES----EHLVQEAIYKNldGKSVILIAHRLSTVEKADKIVVINKGRVEQIG 715
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSLRLRS--ELTMVIVSHNLHQVSRLSDFTAFFKGNENRIG 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
498-716 |
8.85e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 8.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQP-------------------ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVL 558
Cdd:COG1134 5 IEVENVSKSYRLYHEPSrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 559 VDG--VPLeefehhyihkkIAL-VGQEPVLfarSVMENVR-----YGVEVADT-----EIIrscEMANAHGFI---MQTt 622
Cdd:COG1134 85 VNGrvSAL-----------LELgAGFHPEL---TGRENIYlngrlLGLSRKEIdekfdEIV---EFAELGDFIdqpVKT- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 623 lkYetnvgekgtqmSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNL--DGKSVILIAHRLSTVEK- 699
Cdd:COG1134 147 --Y-----------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARI-RELreSGRTVIFVSHSMGAVRRl 212
|
250
....*....|....*..
gi 71992290 700 ADKIVVINKGRVEQIGN 716
Cdd:COG1134 213 CDRAIWLEKGRLVMDGD 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
510-692 |
1.43e-19 |
|
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: 87.41 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 510 RSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYiHKKIALVGQEPVLFAR- 588
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 589 SVMENVRYGVEVADTEIiRSCEMANAhgfimqttlkyetNVGEKG------TQMSGGQKQRIAIARALVREPAILLLDEA 662
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQ-RTIEDALA-------------AVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 71992290 663 TSALDTESEHLVQEAIYKNLD-GKSVILIAH 692
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLArGGIVLLTTH 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
516-711 |
1.71e-19 |
|
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: 86.72 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEF-EHHYIHKKIALV----GQEPVLFARSV 590
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRsPRDAIRAGIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENVrygvevadteIIRScemanahgfimqttlkyetnvgekgtQMSGGQKQRIAIARALVREPAILLLDEATSALDTES 670
Cdd:cd03215 96 AENI----------ALSS--------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71992290 671 ehlvQEAIYKNL-----DGKSVILIahrlST-----VEKADKIVVINKGRV 711
Cdd:cd03215 140 ----KAEIYRLIreladAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
498-713 |
1.74e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNvhfsypTRSDQPILKDLSFTVEPGETVALVGPSGSGKS-SCISLLENFYVPNA----GQVLVDGVPL----EEFE 568
Cdd:PRK15134 13 VAFRQ------QQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLlhasEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 569 HHYIHKKIALVGQEPV--LFARSVMENVRYGV---------EVADTEIIRSCEMANahgfIMQTTlkyeTNVGEKGTQMS 637
Cdd:PRK15134 87 RGVRGNKIAMIFQEPMvsLNPLHTLEKQLYEVlslhrgmrrEAARGEILNCLDRVG----IRQAA----KRLTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 638 GGQKQRIAIARALVREPAILLLDEATSALDTEsehlVQEAIYKNLD------GKSVILIAHRLSTVEK-ADKIVVINKGR 710
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVS----VQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGR 234
|
....
gi 71992290 711 -VEQ 713
Cdd:PRK15134 235 cVEQ 238
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
520-721 |
1.75e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 520 SFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVpleefEHHYI---HKKIALVGQEPVLFAR-SVMENVR 595
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 596 YGV----EVADTEIIRSCEMANAHGFimqttlkyETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALD---- 667
Cdd:PRK10771 94 LGLnpglKLNAAQREKLHAIARQMGI--------EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 668 TESEHLVQE-AIYKNLdgkSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLL 721
Cdd:PRK10771 166 QEMLTLVSQvCQERQL---TLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
515-713 |
4.18e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.18 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHhyiHKKIALVGQE--------PVLF 586
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS---AAKAELRNQKlgfiyqfhHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 587 ARSVMENVRY-----GVEVADTEiIRSCEMANAHGFimqttlkyETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDE 661
Cdd:PRK11629 101 DFTALENVAMplligKKKPAEIN-SRALEMLAAVGL--------EHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 662 ATSALDTESehlvQEAIYKNL------DGKSVILIAHRLSTVEKADKIVVINKGRVEQ 713
Cdd:PRK11629 172 PTGNLDARN----ADSIFQLLgelnrlQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
520-722 |
5.49e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.35 E-value: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 520 SFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHyihkKIALVG-----QEPVLFAR-SVMEN 593
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH----QIARMGvvrtfQHVRLFREmTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 594 --------VRYGV--EVADTEIIRSCE---MANAHGFIMQTTLKYETNvGEKGTqMSGGQKQRIAIARALVREPAILLLD 660
Cdd:PRK11300 101 llvaqhqqLKTGLfsGLLKTPAFRRAEseaLDRAATWLERVGLLEHAN-RQAGN-LAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 661 EATSALDTESEHLVQEAI--YKNLDGKSVILIAHRLSTV-EKADKIVVINKGRV------EQIGNHETLLK 722
Cdd:PRK11300 179 EPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPlangtpEEIRNNPDVIK 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
498-699 |
6.07e-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: 84.51 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVhfSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVlvdgvpleefeHHYIHKKIA 577
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVRYGvevadteiirscemanahgfiMQTTLkyetnvgekgtqmSGGQKQRIAIARALVREPAIL 657
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYP---------------------WDDVL-------------SGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71992290 658 LLDEATSALDTESEhlvqEAIYKNLDGK--SVILIAHRlSTVEK 699
Cdd:cd03223 114 FLDEATSALDEESE----DRLYQLLKELgiTVISVGHR-PSLWK 152
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
515-711 |
6.17e-19 |
|
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: 86.56 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENfYVPNA----GQVLVDGVPLEEfehHYIHKKIALVGQEPVLFAR-S 589
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGgttsGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 590 VMENVRYGV--------------EVADTEIIRSCEMANAHGFIMQttlkyetnvgekgtQMSGGQKQRIAIARALVREPA 655
Cdd:cd03234 98 VRETLTYTAilrlprkssdairkKRVEDVLLRDLALTRIGGNLVK--------------GISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 656 ILLLDEATSALDTESEHLVQEaIYKNL--DGKSVILIAH--RLSTVEKADKIVVINKGRV 711
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVS-TLSQLarRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
516-736 |
7.67e-19 |
|
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: 90.65 E-value: 7.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYvPNA---GQVLVDGVPL--------EEFEHHYIHKKIALVgqePV 584
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLkasnirdtERAGIVIIHQELTLV---PE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 585 LfarSVMENVRYGVEV-------ADTEIIRSCEManahgfIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAIL 657
Cdd:TIGR02633 93 L---SVAENIFLGNEItlpggrmAYNAMYLRAKN------LLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 658 LLDEATSALdTESEHLVQEAIYKNLDGKSV--ILIAHRLSTVEK-ADKIVVINKGRveQIGNHETLLKDTNGTYAKLVQR 734
Cdd:TIGR02633 164 ILDEPSSSL-TEKETEILLDIIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQ--HVATKDMSTMSEDDIITMMVGR 240
|
..
gi 71992290 735 QM 736
Cdd:TIGR02633 241 EI 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
490-721 |
1.49e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 490 MPENvvgKIEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENfyvPNAGQVLVDGV---- 562
Cdd:PRK10619 1 MSEN---KLNVIDLHKRY---GEHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSIVVNGQtinl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 563 ------PLEEFEHHYIH---KKIALVGQEPVLFAR-SVMENVR------YGVEVADTEIiRSCEMANAHGFIMQTTLKYE 626
Cdd:PRK10619 72 vrdkdgQLKVADKNQLRllrTRLTMVFQHFNLWSHmTVLENVMeapiqvLGLSKQEARE-RAVKYLAKVGIDERAQGKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 627 TNvgekgtqMSGGQKQRIAIARALVREPAILLLDEATSALDTEsehLVQEA--IYKNL--DGKSVILIAHRLSTVEK-AD 701
Cdd:PRK10619 151 VH-------LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVlrIMQQLaeEGKTMVVVTHEMGFARHvSS 220
|
250 260
....*....|....*....|
gi 71992290 702 KIVVINKGRVEQIGNHETLL 721
Cdd:PRK10619 221 HVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
498-715 |
1.75e-18 |
|
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: 84.89 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPT-------------------RSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVL 558
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 559 VDG--VPLeefehhyihkkIAL-VGQEPVLfarSVMENVR-----YGVEVADT-----EIIRSCEMANahgFIMQTTLKY 625
Cdd:cd03220 81 VRGrvSSL-----------LGLgGGFNPEL---TGRENIYlngrlLGLSRKEIdekidEIIEFSELGD---FIDLPVKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 626 etnvgekgtqmSGGQKQRIAIARALVREPAILLLDEATSALDtesEHLVQEAIYK----NLDGKSVILIAHRLSTVEK-A 700
Cdd:cd03220 144 -----------SSGMKARLAFAIATALEPDILLIDEVLAVGD---AAFQEKCQRRlrelLKQGKTVILVSHDPSSIKRlC 209
|
250
....*....|....*
gi 71992290 701 DKIVVINKGRVEQIG 715
Cdd:cd03220 210 DRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
498-725 |
2.33e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.23 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRS--DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQV------LVDGVPLEEFEH 569
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 570 hyIHKKIALVGQ--EPVLFARSVMENV-----RYGVEVADTEIiRSCEMANAHGFimqttlkyETNVGEKGT-QMSGGQK 641
Cdd:PRK13634 83 --LRKKVGIVFQfpEHQLFEETVEKDIcfgpmNFGVSEEDAKQ-KAREMIELVGL--------PEELLARSPfELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 642 QRIAIARALVREPAILLLDEATSALDTESEHLVQEAIY-----KNLdgkSVILIAHRLSTVEK-ADKIVVINKGRVEQIG 715
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYklhkeKGL---TTVLVTHSMEDAARyADQIVVMHKGTVFLQG 228
|
250
....*....|
gi 71992290 716 NHETLLKDTN 725
Cdd:PRK13634 229 TPREIFADPD 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
498-724 |
2.45e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHK-KI 576
Cdd:PRK15439 12 LCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPVLFAR-SVMENVRYGvevadteiirsceMANAhgfiMQTTLKYETNVGEKGTQ----MSGG-----QKQRIAI 646
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFG-------------LPKR----QASMQKMKQLLAALGCQldldSSAGslevaDRQIVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 647 ARALVREPAILLLDEATSALD-TESEHLVQEaIYKNLD-GKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKD 723
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTpAETERLFSR-IRELLAqGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTD 230
|
.
gi 71992290 724 T 724
Cdd:PRK15439 231 D 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
497-737 |
3.42e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 497 KIEFRNVHFSYPTRSdqPI----LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQV---LVDGVPL---EE 566
Cdd:PRK13651 2 QIKVKNIVKIFNKKL--PTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKkktKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 567 FEHHY------------------IHKKIALVGQ--EPVLFARSVMEN-----VRYGVEVADTEiirscemanahgfimQT 621
Cdd:PRK13651 80 KEKVLeklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDiifgpVSMGVSKEEAK---------------KR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 622 TLKYETNVG------EKGT-QMSGGQKQRIAIARALVREPAILLLDEATSALDTESehlVQEA--IYKNL--DGKSVILI 690
Cdd:PRK13651 145 AAKYIELVGldesylQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEIleIFDNLnkQGKTIILV 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 71992290 691 AHRLSTV-EKADKIVVINKGRVEQIGNHETLLKDTNgtyaKLVQRQMM 737
Cdd:PRK13651 222 THDLDNVlEWTKRTIFFKDGKIIKDGDTYDILSDNK----FLIENNME 265
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
498-721 |
5.53e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.84 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVH--FSYPT----RSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHY 571
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQEPvlfARSVMENVRYGvEVADTEIIRSCEM-ANAHGFIMQTTLKyetNVGEKGTQ-------MSGGQKQR 643
Cdd:PRK15112 85 RSQRIRMIFQDP---STSLNPRQRIS-QILDFPLRLNTDLePEQREKQIIETLR---QVGLLPDHasyyphmLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 644 IAIARALVREPAILLLDEATSALD----TESEHLVQEAIYKNldGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHE 718
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDmsmrSQLINLMLELQEKQ--GISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTA 235
|
...
gi 71992290 719 TLL 721
Cdd:PRK15112 236 DVL 238
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
496-723 |
6.73e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.54 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYPTRsdqPILKDLSFTVEPGETVALVGPSGSGKSSCisllenFYV------PNAGQVLVDGvplEEFEH 569
Cdd:COG1137 2 MTLEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMivglvkPDSGRIFLDG---EDITH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 570 HYIHKKiALVG-----QEPVLFAR-SVMENVRYGVEVAD---TEIIRSCEmanahgfimqtTLKYETNVGE----KGTQM 636
Cdd:COG1137 70 LPMHKR-ARLGigylpQEASIFRKlTVEDNILAVLELRKlskKEREERLE-----------ELLEEFGITHlrksKAYSL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 637 SGGQKQRIAIARALVREPAILLLDEATSALD----TESEHLVQEAIYKNLdGksvILIA-HR----LSTVEKAdkiVVIN 707
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRHLKERGI-G---VLITdHNvretLGICDRA---YIIS 210
|
250
....*....|....*.
gi 71992290 708 KGRVEQIGNHETLLKD 723
Cdd:COG1137 211 EGKVLAEGTPEEILNN 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
516-733 |
7.18e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.53 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHK-KIALVGQE-PVLFARSVMEN 593
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 594 VR---------YGVEVADTEIIRScemaNAHGFIMQTTLKYETNvgEKGTQMSGGQKQRIAIARALVREPAILLLDEATS 664
Cdd:PRK09700 101 LYigrhltkkvCGVNIIDWREMRV----RAAMMLLRVGLKVDLD--EKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 665 AL-DTESEHLVqeAIYKNL--DGKSVILIAHRLStvekadkivvinkgRVEQIGNHETLLKDTNGTYAKLVQ 733
Cdd:PRK09700 175 SLtNKEVDYLF--LIMNQLrkEGTAIVYISHKLA--------------EIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
497-720 |
7.97e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.98 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 497 KIEFRNVHFSyptrSDQPILKDLSFTVEPGETVALVGPSGSGKS-SCISLLEnfYVP-----NAGQVLVDGVPLEEFEHH 570
Cdd:PRK10418 4 QIELRNIALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALG--ILPagvrqTAGRVLLDGKPVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 571 YIHkkIALVGQEPvlfaRSVMENVR------------YGVEVADTEIIRSCE---------MANAHGFimqttlkyetnv 629
Cdd:PRK10418 78 GRK--IATIMQNP----RSAFNPLHtmhtharetclaLGKPADDATLTAALEavglenaarVLKLYPF------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 630 gekgtQMSGGQKQRIAIARALVREPAILLLDEATSALDTES--------EHLVQEaiyknlDGKSVILIAHRLSTVEK-A 700
Cdd:PRK10418 140 -----EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqarildllESIVQK------RALGMLLVTHDMGVVARlA 208
|
250 260
....*....|....*....|
gi 71992290 701 DKIVVINKGRVEQIGNHETL 720
Cdd:PRK10418 209 DDVAVMSHGRIVEQGDVETL 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
489-711 |
8.14e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.29 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 489 YMPENVVGKIEFRNVHFS--YPTRSDQPI--LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLV----- 559
Cdd:PRK13631 11 KVPNPLSDDIILRVKNLYcvFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 560 -DGVPLEEFEHHYIHKKI----------ALVGQEP--VLFARSVMENVRYGVEVADTEIIRSCEMANAHgfIMQTTLKYe 626
Cdd:PRK13631 91 gDKKNNHELITNPYSKKIknfkelrrrvSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFY--LNKMGLDD- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 627 TNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLSTV-EKADKIV 704
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMEHVlEVADEVI 247
|
....*..
gi 71992290 705 VINKGRV 711
Cdd:PRK13631 248 VMDKGKI 254
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
516-711 |
9.37e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.00 E-value: 9.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG---VPLEEFEHHYIHKKIALVGQE-PVLFARSVM 591
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiTRLKNREVPFLRRQIGMIFQDhHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 592 ENVRYGVEVADT---EIIRSCEMANAHGFIMQTTLKYEtnvgekgTQMSGGQKQRIAIARALVREPAILLLDEATSALDT 668
Cdd:PRK10908 98 DNVAIPLIIAGAsgdDIRRRVSAALDKVGLLDKAKNFP-------IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71992290 669 E-SEHLVQEAIYKNLDGKSVILIAHRLSTVEKAD-KIVVINKGRV 711
Cdd:PRK10908 171 AlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
516-711 |
1.10e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.52 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAG-----QVLVDGVPLEEFEHHYIHKKIALVG---QEPVLFA 587
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRTVQREGRLARDIRKSRANTGyifQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 R-SVMENVRYGVeVADTEIIRSCeMANAHGFIMQTTLKYETNVG------EKGTQMSGGQKQRIAIARALVREPAILLLD 660
Cdd:PRK09984 100 RlSVLENVLIGA-LGSTPFWRTC-FSWFTREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71992290 661 EATSALDTESEHLVQEAIY--KNLDGKSVILIAHRLS-TVEKADKIVVINKGRV 711
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
502-716 |
1.22e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 502 NVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFY------VPNAGQVLVDGVPLEEFEHHYIHKK 575
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVLFAR-SVMENVRYGVEVADTEIIRSCEManahgfIMQTTLK-------YETNVGEKGTQMSGGQKQRIAIA 647
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKK------IVEECLRkvglwkeVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 648 RALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGN 716
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
498-725 |
1.86e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSD--QPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPL----EEFEHHY 571
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQEP--VLFARSVMENVRYGVE---VADTEiirsCEMANAHGFIMqttLKYETNVGEKGT-QMSGGQKQRIA 645
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQnfgIPKEK----AEKIAAEKLEM---VGLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 646 IARALVREPAILLLDEATSALDTESEHLVQ---EAIYKNldGKSVILIAHRLSTV-EKADKIVVINKGRVEQIGNHETLL 721
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQS--GQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVF 232
|
....
gi 71992290 722 KDTN 725
Cdd:PRK13643 233 QEVD 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
479-773 |
3.09e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.06 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 479 REPQIQHN----GEYMPE--NVVGKIEFRNVHFSYPTRSDQPIlKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVP 552
Cdd:PRK10261 298 QEPPIEQDtvvdGEPILQvrNLVTRFPLRSGLLNRVTREVHAV-EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVES 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 553 NAGQVLVDGV---PLEEFEHHYIHKKIALVGQEPV--LFAR-----SVMENVR-YGVEVADTEIIRSCEMANAHGFIMQT 621
Cdd:PRK10261 377 QGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYasLDPRqtvgdSIMEPLRvHGLLPGKAAAARVAWLLERVGLLPEH 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 622 TLKYETnvgekgtQMSGGQKQRIAIARALVREPAILLLDEATSALDTEsehLVQEAIYKNLD-----GKSVILIAHRLST 696
Cdd:PRK10261 457 AWRYPH-------EFSGGQRQRICIARALALNPKVIIADEAVSALDVS---IRGQIINLLLDlqrdfGIAYLFISHDMAV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 697 VEK-ADKIVVINKGRVEQIGNHETLLKDTNGTYA-KLV-------------QRQMMGDQKP---RKRPAVARSGP--QPA 756
Cdd:PRK10261 527 VERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYTrKLMaavpvadpsrqrpQRVLLSDDLPsniHLRGEEVAAVSlqCVG 606
|
330
....*....|....*..
gi 71992290 757 ASINVAGPSQGNAMSLL 773
Cdd:PRK10261 607 PGHYVAQPQSEYAFMRR 623
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
490-755 |
1.02e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 490 MPENVVGKIEFRNVHFSYpTRSDQPILKDLSFTVEPGETVALVGPSGSGKS----SCISLLENfyvpNAGQVLVDGVPLE 565
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQ----AGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 566 EFEHHYIH--------------KKIALVGQEPV-----LFA--RSVMENVRYGVEVADTEiirscEMANAHGFIMQTTL- 623
Cdd:PRK10261 82 RRSRQVIElseqsaaqmrhvrgADMAMIFQEPMtslnpVFTvgEQIAESIRLHQGASREE-----AMVEAKRMLDQVRIp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 624 KYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALD-TESEHLVQ--EAIYKNLDgKSVILIAHRLSTV-EK 699
Cdd:PRK10261 157 EAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvTIQAQILQliKVLQKEMS-MGVIFITHDMGVVaEI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 700 ADKIVVINKGRVEQIGNHETLLKDTNGTYAK----LVQR--QMMGDQKPRKRPAVARSGPQP 755
Cdd:PRK10261 236 ADRVLVMYQGEAVETGSVEQIFHAPQHPYTRallaAVPQlgAMKGLDYPRRFPLISLEHPAK 297
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
500-711 |
1.89e-16 |
|
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: 78.46 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 500 FRNVHF-SYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNA---GQVLVDGVPLEEFEHHYiHKK 575
Cdd:cd03233 6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-PGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVLFAR-SVMENVRYGVEVADTEIIRscemanahGFimqttlkyetnvgekgtqmSGGQKQRIAIARALVREP 654
Cdd:cd03233 85 IIYVSEEDVHFPTlTVRETLDFALRCKGNEFVR--------GI-------------------SGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 655 AILLLDEATSALDTESEHLVQEAIYKNLD--GKSVILIAHRLS--TVEKADKIVVINKGRV 711
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASdeIYDLFDKVLVLYEGRQ 198
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
516-694 |
3.04e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.44 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSS---CIS----LLENFYVpnAGQVLVDGVPL--EEFEHHYIHKKIALVGQEPVLF 586
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTilrCFNrlndLIPGFRV--EGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 587 ARSVMENVRYGVEV------ADTEIIRScemanahgfIMQTTLKYETN--VGEKGTQMSGGQKQRIAIARALVREPAILL 658
Cdd:PRK14243 104 PKSIYDNIAYGARIngykgdMDELVERS---------LRQAALWDEVKdkLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 71992290 659 LDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRL 694
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
512-711 |
3.46e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.67 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 512 DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYI--HKKIALVGQEP--VLFA 587
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLalRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RSVMENVRYGVE---VADTEIIRSCEMA----NAHGFIMQTTlkyetnvgekgTQMSGGQKQRIAIARALVREPAILLLD 660
Cdd:PRK13638 93 TDIDSDIAFSLRnlgVPEAEITRRVDEAltlvDAQHFRHQPI-----------QCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71992290 661 EATSALDTESEHLVQeAIYKNL--DGKSVILIAHRLSTV-EKADKIVVINKGRV 711
Cdd:PRK13638 162 EPTAGLDPAGRTQMI-AIIRRIvaQGNHVIISSHDIDLIyEISDAVYVLRQGQI 214
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
497-718 |
3.68e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 82.33 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 497 KIEFRNVHFSYPTRSDQpiLKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKI 576
Cdd:PRK10522 322 TLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 577 ALVGQEPVLFARsVMENvryGVEVADTEIIRS----CEMAN----AHGFIMQttlkyetnvgekgTQMSGGQKQRIAIAR 648
Cdd:PRK10522 400 SAVFTDFHLFDQ-LLGP---EGKPANPALVEKwlerLKMAHklelEDGRISN-------------LKLSKGQKKRLALLL 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 649 ALVREPAILLLDEATSALDTeseHLVQEaIYKNL------DGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHE 718
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDP---HFRRE-FYQVLlpllqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEE 534
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
497-715 |
4.91e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.42 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 497 KIEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCIS----LLENFYVPN-AGQVLVDGVPLEEFEHHY 571
Cdd:PRK14247 3 KIEIRDLKVSF---GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 IHKKIALVGQEPVLFAR-SVMENVRYGVEVadTEIIRS-CEMANAHGFIMQTTLKYE---TNVGEKGTQMSGGQKQRIAI 646
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNlSIFENVALGLKL--NRLVKSkKELQERVRWALEKAQLWDevkDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 647 ARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIG 715
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
498-715 |
5.24e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.73 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCIS----LLE-NFYVPNAGQVLVDGVPL--EEFEHH 570
Cdd:PRK14267 5 IETVNLRVYY---GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLElNEEARVEGEVRLFGRNIysPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 571 YIHKKIALVGQEPVLFAR-SVMENVRYGVEV-----ADTEIIRSCEMAnahgfIMQTTLKYETN--VGEKGTQMSGGQKQ 642
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHlTIYDNVAIGVKLnglvkSKKELDERVEWA-----LKKAALWDEVKdrLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 643 RIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIG 715
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
513-745 |
7.71e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 513 QPILKDLSFTVEPGETVALVGPSGSGKSSCISLLE--NFYVPN---AGQVLVDGVPLEEFEHHY-IHKKIALVGQEPVLF 586
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmNDKVSGyrySGDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 587 ARSVMENVRYGVEvADTEIIRSCEMANAHGFIMQTTL--KYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATS 664
Cdd:PRK14271 114 PMSIMDNVLAGVR-AHKLVPRKEFRGVAQARLTEVGLwdAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 665 ALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKDTNGTYAKLVQRQMMGDQKPR 743
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVKDA 272
|
..
gi 71992290 744 KR 745
Cdd:PRK14271 273 KR 274
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
515-711 |
9.22e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.25 E-value: 9.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPN---AGQVLVDGVPLEEFEhhyIHKKIALVGQE----PVLFA 587
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKE---MRAISAYVQQDdlfiPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RS---VMENVRYGVEVADTEiirscEMANAHGFIMQTTLK--YETNVGEKGTQ--MSGGQKQRIAIARALVREPAILLLD 660
Cdd:TIGR00955 117 REhlmFQAHLRMPRRVTKKE-----KRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71992290 661 EATSALDTESEHLVQEAIYK-NLDGKSVILIAHRLST--VEKADKIVVINKGRV 711
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRV 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
498-661 |
1.02e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.88 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFsypTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG--VPLEEFEHHY-IHK 574
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenIPAMSRSRLYtVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEPVLFAR-SVMENVRYGVEvadteiirscEMANAHGFIMQTT--LKYETnVGEKG------TQMSGGQKQRIA 645
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPLR----------EHTQLPAPLLHSTvmMKLEA-VGLRGaaklmpSELSGGMARRAA 153
|
170
....*....|....*.
gi 71992290 646 IARALVREPAILLLDE 661
Cdd:PRK11831 154 LARAIALEPDLIMFDE 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
511-744 |
1.13e-15 |
|
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: 81.98 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 511 SDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfEHHYIHKKIALVGQEPVLFAR-S 589
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 590 VMENVRYGVEVADteiiRSCEMAN--AHGFIMQTTLKYETNvgEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALD 667
Cdd:TIGR01257 1020 VAEHILFYAQLKG----RSWEEAQleMEAMLEDTGLHHKRN--EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 668 TESEHLVQEAIYKNLDGKSVILIAHRLSTVE-KADKIVVINKGRVEQIGNhETLLKDTNGT--YAKLVqRQMMGDQKPRK 744
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT-PLFLKNCFGTgfYLTLV-RKMKNIQSQRG 1171
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
516-711 |
1.85e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.80 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFyVPNAGQVLVDGVPLEEFEHH-------YIHKKIALVGQEPV---- 584
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPFAMPVfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 585 -LFARSVMEnvrygVEVADTEIIRSCEManahgfiMQTTLKYETNVgekgTQMSGGQKQRIAIARALVR-------EPAI 656
Cdd:COG4138 91 aLHQPAGAS-----SEAVEQLLAQLAEA-------LGLEDKLSRPL----TQLSGGEWQRVRLAAVLLQvwptinpEGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 657 LLLDEATSALDtesehLVQEAIyknLD---------GKSVILIAHRLS-TVEKADKIVVINKGRV 711
Cdd:COG4138 155 LLLDEPMNSLD-----VAQQAA---LDrllrelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKL 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
501-722 |
4.81e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 501 RNVHFSYPTRSdqpILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVG 580
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 581 QE-PVLFARSVMENV------------RYGVEvaDTEIIrscEMAnahgfIMQTTLKYETNvgEKGTQMSGGQKQRIAIA 647
Cdd:PRK10575 92 QQlPAAEGMTVRELVaigrypwhgalgRFGAA--DREKV---EEA-----ISLVGLKPLAH--RLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 648 RALVREPAILLLDEATSALDTESEHLVQEAIYK--NLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLK 722
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlsQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
498-707 |
6.44e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSdqpILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDgvplEEFEHHYIHKKIA 577
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----GKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMenVRYGVEVADteIIRSCEMANAHGFIMQTTLKyetnvgekgtqMSGGQKQRIAIARALVREPAIL 657
Cdd:PRK09544 78 LDTTLPLTVNRFLR--LRPGTKKED--ILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 658 LLDEATSALDTESehlvQEAIYKNLD------GKSVILIAHRLSTV-EKADKIVVIN 707
Cdd:PRK09544 143 VLDEPTQGVDVNG----QVALYDLIDqlrrelDCAVLMVSHDLHLVmAKTDEVLCLN 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
519-723 |
7.74e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 519 LSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQV-------LVDGVPLEEFEHHYIHKKIALVGQEPVLFA-RSV 590
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENVR--YGVEVADT-EIIRSCEMANAHGFimqtTLKYETNVGEKGT-QMSGGQKQRIAIARALVREPAILLLDEATSAL 666
Cdd:TIGR03269 383 LDNLTeaIGLELPDElARMKAVITLKMVGF----DEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 667 DTESEHLVQEAIYKNLD--GKSVILIAHRLSTV-EKADKIVVINKGRVEQIGNHETLLKD 723
Cdd:TIGR03269 459 DPITKVDVTHSILKAREemEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
498-711 |
1.08e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVH--FSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKK 575
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IALVGQEPVL--FAR-SVMEN------------VRYGVEVADTEIIRscEMANAHGFIMQTTLKyeTNVGekgtQMSGGQ 640
Cdd:COG1101 82 IGRVFQDPMMgtAPSmTIEENlalayrrgkrrgLRRGLTKKRRELFR--ELLATLGLGLENRLD--TKVG----LLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 641 KQRIAIARALVREPAILLLDEATSALD-------TE-SEHLVQEaiyKNLdgkSVILIAHRLS-TVEKADKIVVINKGRV 711
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE---NNL---TTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
516-710 |
1.28e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.14 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYvPNA---GQVLVDGVPLE-----EFEHH---YIHKKIALVgqePV 584
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCRfkdirDSEALgivIIHQELALI---PY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 585 LfarSVMENVRYGVEVADTEII-------RSCEMANAHGfimqttLKY--ETNVGEKGTqmsgGQKQRIAIARALVREPA 655
Cdd:NF040905 93 L---SIAENIFLGNERAKRGVIdwnetnrRARELLAKVG------LDEspDTLVTDIGV----GKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 656 ILLLDEATSAL-DTESEHLvqeaiyknLD--------GKSVILIAHRLSTVEK-ADKIVVINKGR 710
Cdd:NF040905 160 LLILDEPTAALnEEDSAAL--------LDlllelkaqGITSIIISHKLNEIRRvADSITVLRDGR 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
515-740 |
2.11e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.39 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG-----VPLeefeHHYIHKKIALVGQEPVLFAR- 588
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPL----HARARRGIGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 589 SVMENVRYGVEVADtEIIRSCEMANAHGFIMQTTLKYETNvgEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDT 668
Cdd:PRK10895 94 SVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 669 ESEHLVQEAIYKNLD-GKSVILIAHRL-STVEKADKIVVINKGRVEQIGNHETLLKDTNgtyaklVQRQMMGDQ 740
Cdd:PRK10895 171 ISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEH------VKRVYLGED 238
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
498-722 |
2.38e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 73.67 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLL---ENFYVpNAGQVLVDGVPLEEFE-HHYIH 573
Cdd:PRK09580 2 LSIKDLHVSV---EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagrEDYEV-TGGTVEFKGKDLLELSpEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQEPV--------LFARSVMENVR--YGVEVAD--------TEIIRSCEMAnahgfimQTTLKYETNVGekgtq 635
Cdd:PRK09580 78 EGIFMAFQYPVeipgvsnqFFLQTALNAVRsyRGQEPLDrfdfqdlmEEKIALLKMP-------EDLLTRSVNVG----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 636 MSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGK-SVILIAH--RLSTVEKADKIVVINKGRVE 712
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKrSFIIVTHyqRILDYIKPDYVHVLYQGRIV 225
|
250
....*....|
gi 71992290 713 QIGNHeTLLK 722
Cdd:PRK09580 226 KSGDF-TLVK 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
519-741 |
2.59e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 519 LSFTVEPGETVALVGPSGSGKS---SCISLLenfyVPNAGQVLVDGVPLEEFEHHYIHKKIA-LVGQEPVLFARSVMEnv 594
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKStllARMAGL----LPGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 595 rY-------GVEVADTE--IIRSCEManahgfiMQTTLKYETNVGekgtQMSGGQKQRIAIARALVR-EPAI------LL 658
Cdd:PRK03695 89 -YltlhqpdKTRTEAVAsaLNEVAEA-------LGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvWPDInpagqlLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 659 LDEATSALDTESehlvQEAIYKNLD-----GKSVILIAHRLS-TVEKADKIVVINKGRVEQIGNHETLLKDTN--GTYAK 730
Cdd:PRK03695 157 LDEPMNSLDVAQ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENlaQVFGV 232
|
250
....*....|.
gi 71992290 731 LVQRQMMGDQK 741
Cdd:PRK03695 233 NFRRLDVEGHP 243
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
515-692 |
2.99e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPL----EEFEHHYIHKKIALVGQE----PVLF 586
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRAKHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 587 ArsvMENVRYGVEVADTEIIRSCEMANAhgfimqttLKYETNVGEK----GTQMSGGQKQRIAIARALVREPAILLLDEA 662
Cdd:PRK10584 105 A---LENVELPALLRGESSRQSRNGAKA--------LLEQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|..
gi 71992290 663 TSALDTESEHLVQEAIYK-NLD-GKSVILIAH 692
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSlNREhGTTLILVTH 205
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
206-566 |
3.40e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 75.99 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 206 VIATVVATKSYPALSNAVYIMTIISLVsAVAAGFRGGSFEYAYARIQRAIrYDLFHGLVKQ----DVAFYDAHKTGEVTS 281
Cdd:COG4615 32 LIALINQALNATGAALARLLLLFAGLL-VLLLLSRLASQLLLTRLGQHAV-ARLRLRLSRRilaaPLERLERIGAARLLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 282 RLAADCQTMSDTVALNVNvFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFV--------ASKIFGT---YYDLLSER 350
Cdd:COG4615 110 ALTEDVRTISQAFVRLPE-LLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAgyrllvrrARRHLRRareAEDRLFKH 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 351 TQDTI----------AESNDVAEEVLStmRTVRSFSCENVEADRFYGklthtldvtrtkaiayIGFLWvSELFQSFIIVS 420
Cdd:COG4615 189 FRALLegfkelklnrRRRRAFFDEDLQ--PTAERYRDLRIRADTIFA----------------LANNW-GNLLFFALIGL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 421 VLWYGGHLVLTQkmkGDLLVSF---LLYQMQlgdNLRQMGEVWTGLMQSVGASRKV---FEYIDREPQIQHNGEYMPENV 494
Cdd:COG4615 250 ILFLLPALGWAD---PAVLSGFvlvLLFLRG---PLSQLVGALPTLSRANVALRKIeelELALAAAEPAAADAAAPPAPA 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 495 VGK-IEFRNVHFSYPTRSDQP--ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEE 566
Cdd:COG4615 324 DFQtLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA 398
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
496-716 |
4.04e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.50 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKIEFRNVHFSYPTRS--DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVD--GVP--LEEF-E 568
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPanLKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 569 HHYIHKKIALVGQEP--VLFARSVMENVRYG-VEV-ADTEiirscEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRI 644
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpVNLgENKQ-----EAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 645 AIARALVREPAILLLDEATSALDTESEH---LVQEAIYKNlDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGN 716
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKE-YKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
511-731 |
4.62e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 511 SDQPILK---------------DLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLV---DGVPLEEFehhyi 572
Cdd:PRK11701 2 MDQPLLSvrgltklygprkgcrDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLY----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 hkkiALVGQEPVLFARS----VMENVRYGV--EVADTEIIRSCEMA---NAHGFIMQTTLKYETNV-------GEKGTQM 636
Cdd:PRK11701 77 ----ALSEAERRRLLRTewgfVHQHPRDGLrmQVSAGGNIGERLMAvgaRHYGDIRATAGDWLERVeidaariDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 637 SGGQKQRIAIARALVREPAILLLDEATSALDTESE--------HLVQEAiyknldGKSVILIAHRLSTVEK-ADKIVVIN 707
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQarlldllrGLVREL------GLAVVIVTHDLAVARLlAHRLLVMK 226
|
250 260
....*....|....*....|....
gi 71992290 708 KGRVEQIGNHETLLKDTNGTYAKL 731
Cdd:PRK11701 227 QGRVVESGLTDQVLDDPQHPYTQL 250
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
200-460 |
8.99e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 72.59 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 200 PYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRggsfEYAYARIQRAIRYDLFHGLVKQDVA----FYDAHK 275
Cdd:cd18568 22 PLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVR----QYLLDYFANRIDLSLLSDFYKHLLSlplsFFASRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 276 TGEVTSRLAAD---CQTMSD---TVALNVnvflrncVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSE 349
Cdd:cd18568 98 VGDIITRFQENqkiRRFLTRsalTTILDL-------LMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 350 RTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWYGGHLV 429
Cdd:cd18568 171 EIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLV 250
|
250 260 270
....*....|....*....|....*....|.
gi 71992290 430 LTQKMKGDLLVSFLLYQMQLGDNLRQMGEVW 460
Cdd:cd18568 251 ISGQLTIGQLVAFNMLFGSVINPLLALVGLW 281
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
498-718 |
1.51e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.21 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENF--YVPNAGQVLVDGVPLEEFEHHYI-HK 574
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERaHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEPVL--------FARSVMENVR--YGVEVADT----EIIRS-CEMANahgfiMQTTLkYETNVGEKgtqMSGG 639
Cdd:CHL00131 85 GIFLAFQYPIEipgvsnadFLRLAYNSKRkfQGLPELDPleflEIINEkLKLVG-----MDPSF-LSRNVNEG---FSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 640 QKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLD-GKSVILIAH--RLSTVEKADKIVVINKGRVEQIGN 716
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
..
gi 71992290 717 HE 718
Cdd:CHL00131 236 AE 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
517-730 |
1.62e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.43 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 517 KDLSFTVEPGETVALVGPSGSGKSS----CISLLEnfyvPNAGQVLVDGVPL---EEFEHHYIHKKIALVGQEPV--LFA 587
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLasLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RS-----VMENVR-YGVEVADTEII-RSCEMANAHGFIMQTTLKYETnvgekgtQMSGGQKQRIAIARALVREPAILLLD 660
Cdd:PRK15079 114 RMtigeiIAEPLRtYHPKLSRQEVKdRVKAMMLKVGLLPNLINRYPH-------EFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992290 661 EATSALDTESE----HLVQEaIYKNLdGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKDTNGTYAK 730
Cdd:PRK15079 187 EPVSALDVSIQaqvvNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
498-709 |
1.81e-13 |
|
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: 69.58 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPT-RSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENF----YVpnAGQVLVDGVPLEEfehhYI 572
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRktagVI--TGEILINGRPLDK----NF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 573 HKKIALVGQEPVLFARS-VMENVRYGvevadteiirscemANAHGfimqttlkyetnvgekgtqMSGGQKQRIAIARALV 651
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLtVREALRFS--------------ALLRG-------------------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 652 REPAILLLDEATSALDTESEHLVQEAIyKNL--DGKSVILIAHRLSTV--EKADKIVVINKG 709
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFL-KKLadSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
511-721 |
2.23e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 511 SDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLenfyvpnAGQVLVD------------------------------ 560
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdgriiyeqdlivarlqqdpprnvegtvydf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 561 ---GVP-----LEEFeHHYIHkkiaLVGQEPVLFARSVMENVRygvevadtEIIrscEMANAHGF---IMQTTLKYETNV 629
Cdd:PRK11147 87 vaeGIEeqaeyLKRY-HDISH----LVETDPSEKNLNELAKLQ--------EQL---DHHNLWQLenrINEVLAQLGLDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 630 GEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTES-EHLvqEAIYKNLDGkSVILIAHRLSTVEK-ADKIVVIN 707
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL--EGFLKTFQG-SIIFISHDRSFIRNmATRIVDLD 227
|
250
....*....|....*
gi 71992290 708 KGR-VEQIGNHETLL 721
Cdd:PRK11147 228 RGKlVSYPGNYDQYL 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
513-711 |
2.24e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 513 QPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYV--PNAGQVLVDGVPLeefehhyihkkialvGQEpvlfaRSV 590
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF---------------GRE-----ASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENV-RYGVEVADTEIIRSCEMANAHGFIMqttlKYEtnvgekgtQMSGGQKQRIAIARALVREPAILLLDEATSALDTE 669
Cdd:COG2401 103 IDAIgRKGDFKDAVELLNAVGLSDAVLWLR----RFK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71992290 670 SEHLVQEAIYKNLD--GKSVILIAHRlSTVEKA---DKIVVINKGRV 711
Cdd:COG2401 171 TAKRVARNLQKLARraGITLVVATHH-YDVIDDlqpDLLIFVGYGGV 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
516-718 |
3.30e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVE---PGETV-ALVGPSGSGKSSCISLLENFYVPNAG------QVLVDG-----VPLEEfehhyihKKIALVG 580
Cdd:PRK11144 10 LGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAekgicLPPEK-------RRIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 581 QEPVLFAR-SVMENVRYGVevadteiirSCEMANAHGFIMQTtLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLL 659
Cdd:PRK11144 83 QDARLFPHyKVRGNLRYGM---------AKSMVAQFDKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71992290 660 DEATSALDTES--------EHLVQEA----IY--KNLDGksvILiahRLstvekADKIVVINKGRVEQIGNHE 718
Cdd:PRK11144 153 DEPLASLDLPRkrellpylERLAREInipiLYvsHSLDE---IL---RL-----ADRVVVLEQGKVKAFGPLE 214
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
502-711 |
5.10e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 502 NVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLE-NFYVPNA-------GQVLVDGVPLEEFEHHYIH 573
Cdd:PRK13547 3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 574 KKIALVGQ--EPVlFARSVMENVRYG----------VEVADTEII-RSCEMANAhgfimqttlkyETNVGEKGTQMSGGQ 640
Cdd:PRK13547 83 RLRAVLPQaaQPA-FAFSAREIVLLGrypharragaLTHRDGEIAwQALALAGA-----------TALVGRDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 641 KQRIAIARAL---------VREPAILLLDEATSALDTESEHLVQEAIYK-----NLdgkSVILIAHRLSTVEK-ADKIVV 705
Cdd:PRK13547 151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRlardwNL---GVLAIVHDPNLAARhADRIAM 227
|
....*.
gi 71992290 706 INKGRV 711
Cdd:PRK13547 228 LADGAI 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
510-692 |
7.40e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 510 RSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYiHKKIALVGQ----EPVL 585
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHqpgiKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 586 FARsvmENVRYgvevadteiirSCEMAN-AHGFIMQTTLkyeTNVGEKGT------QMSGGQKQRIAIARALVREPAILL 658
Cdd:PRK13538 90 TAL---ENLRF-----------YQRLHGpGDDEALWEAL---AQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 71992290 659 LDEATSALDTESEHLVQEAIYKNLD-GKSVILIAH 692
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEqGGMVILTTH 187
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
190-434 |
7.68e-13 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 69.93 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 190 FIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVA 269
Cdd:cd18782 12 FVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 270 FYDAHKTGEVTSRLAaDCQTMSD-------TVALNVnvflrncVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGT 342
Cdd:cd18782 92 FFDKRPVGELSTRIS-ELDTIRGfltgtalTTLLDV-------LFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 343 YYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVE----ADRFYGKLTHTLDVTRTKAIayIGFLwvSELFQSFII 418
Cdd:cd18782 164 ILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKArwrwQNRYARSLGEGFKLTVLGTT--SGSL--SQFLNKLSS 239
|
250
....*....|....*.
gi 71992290 419 VSVLWYGGHLVLTQKM 434
Cdd:cd18782 240 LLVLWVGAYLVLRGEL 255
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
205-473 |
7.92e-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: 69.76 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 205 QVIATVVATKSYpALSNAVYIMTIISLVSAVAAGF-RGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRL 283
Cdd:cd18554 31 QGSSLTLDEKVY-KLFTIIGIMFFIFLILRPPVEYyRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 284 AADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIF-GTYYDLLSERTQdTIAESNDVA 362
Cdd:cd18554 110 INDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFfGRLRKLTKERSQ-ALAEVQGFL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 363 EEVLSTMRTVRSFSCENVEADRFYGKLTHTLdvtrTKAIAYIGflWVSELFQSFIIVS------VLWYGGHLVLTQKMKG 436
Cdd:cd18554 189 HERIQGMSVIKSFALEKHEQKQFDKRNGHFL----TRALKHTR--WNAKTFSAVNTITdlapllVIGFAAYLVIEGNLTV 262
|
250 260 270
....*....|....*....|....*....|....*..
gi 71992290 437 DLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKV 473
Cdd:cd18554 263 GTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
509-690 |
8.79e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 509 TRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHhyiHKKIALVGQEPVLFAR 588
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 589 -SVMENVRYgveVADTEIIRSCEMANAHGFIMQTTLKYETNVgekgTQMSGGQKQRIAIARALVREPAILLLDEATSALD 667
Cdd:PRK13543 97 lSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|...
gi 71992290 668 TESEHLVQEAIYKNLDGKSVILI 690
Cdd:PRK13543 170 LEGITLVNRMISAHLRGGGAALV 192
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
515-667 |
8.80e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPV----LFARSV 590
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATtpgdITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENVRYGVEVADTEIIRSCEMANAHGfiMQTtlkyeTNVGEKGTQ----MSGGQKQRIAIARALVREPAILLLDEATSAL 666
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKA--MQA-----TGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
.
gi 71992290 667 D 667
Cdd:PRK10253 175 D 175
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
502-716 |
1.16e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.75 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 502 NVHFSYPTrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPN---AGQVLVDGVPLEEFEHHYIHK---- 574
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKlrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQEPVLFARSVMenvRYGVEVADTEIIRScEMANAHGFIMQTTLKYETNVGEKGTQM-------SGGQKQRIAIA 647
Cdd:PRK09473 98 QISMIFQDPMTSLNPYM---RVGEQLMEVLMLHK-GMSKAEAFEESVRMLDAVKMPEARKRMkmyphefSGGMRQRVMIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 648 RALVREPAILLLDEATSALDTEsehlVQEAIYKNLD------GKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGN 716
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVT----VQAQIMTLLNelkrefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
510-725 |
1.68e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 510 RSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIhkkIALVGQE------- 582
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 583 PVLFARSVMENvRYG-------VEVADTEIIRScemanAHGFIMQTTLKYEtNVGEkgtqMSGGQKQRIAIARALVREPA 655
Cdd:PRK15056 94 PVLVEDVVMMG-RYGhmgwlrrAKKRDRQIVTA-----ALARVDMVEFRHR-QIGE----LSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 656 ILLLDEATSALDTESEHLVQEAIYKNLD-GKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDTN 725
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAEN 233
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
525-710 |
1.78e-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: 65.47 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 525 PGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVdgvpleefehhyihkkialvgqepvlfarsvmenvrygvevADTE 604
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 605 IIRSCEMANAHGFImqttlkyetnVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLD- 683
Cdd:smart00382 40 DILEEVLDQLLLII----------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLl 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 71992290 684 ------GKSVILIAHRLSTVEKA------DKIVVINKGR 710
Cdd:smart00382 110 llksekNLTVILTTNDEKDLGPAllrrrfDRRIVLLLIL 148
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
511-711 |
6.25e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 511 SDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLenF--YVPNAGQVLVDGVPLEEfeHHY---IHKKIALV----GQ 581
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDGKPVRI--RSPrdaIRAGIAYVpedrKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 582 EPVLFARSVMENV---------RYGVevadteIIRSCEMANAHGFIMQTTLKY---ETNVGekgtQMSGGQKQRIAIARA 649
Cdd:COG1129 339 EGLVLDLSIRENItlasldrlsRGGL------LDRRRERALAEEYIKRLRIKTpspEQPVG----NLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 650 LVREPAILLLDEATSALD--TESEhlvqeaIYKNL-----DGKSVILIahrlST-----VEKADKIVVINKGRV 711
Cdd:COG1129 409 LATDPKVLILDEPTRGIDvgAKAE------IYRLIrelaaEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
502-701 |
8.28e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 502 NVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYiHKKIALVGQ 581
Cdd:PRK13540 6 ELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 582 E----PVLFARsvmENVRYGVEVADT--EIIRSCEManahgFIMQTTLKYETNVgekgtqMSGGQKQRIAIARALVREPA 655
Cdd:PRK13540 82 RsginPYLTLR---ENCLYDIHFSPGavGITELCRL-----FSLEHLIDYPCGL------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71992290 656 ILLLDEATSALDTESEHLVQEAIYKN-LDGKSVILIAHRLSTVEKAD 701
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHrAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
496-692 |
1.21e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 496 GKI--EFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVdGVPLE--EFEHHy 571
Cdd:PRK11147 316 GKIvfEMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvaYFDQH- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 ihkKIALvgqEPvlfARSVMENVRYGVEvadtEIirsceMANA---H--GFiMQTTL----KYETNVgekgTQMSGGQKQ 642
Cdd:PRK11147 391 ---RAEL---DP---EKTVMDNLAEGKQ----EV-----MVNGrprHvlGY-LQDFLfhpkRAMTPV----KALSGGERN 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 71992290 643 RIAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNLDGkSVILIAH 692
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSH 495
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
519-734 |
1.23e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.69 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 519 LSFTVEPGETVALVGPSGSGKS-SCISLLENFYVPnaGQVLVDGVpleEFEHHYIHK-----KIALVGQEPVLFARSVME 592
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKL---EFNGQDLQRisekeRRNLVGAEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 593 --NVRYGVEVADTEIIRSCEMANaHGFIMQTTLKYETNVGEKGT---------QMSGGQKQRIAIARALVREPAILLLDE 661
Cdd:PRK11022 101 slNPCYTVGFQIMEAIKVHQGGN-KKTRRQRAIDLLNQVGIPDPasrldvyphQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 662 ATSALDTEsehlVQEAIYKNL------DGKSVILIAHRLSTV-EKADKIVVINKGRVEQIGNHETLLKDTNGTYAKLVQR 734
Cdd:PRK11022 180 PTTALDVT----IQAQIIELLlelqqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
516-666 |
1.76e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKK-IALVGQEPVLFAR-SVMEN 593
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71992290 594 VRYGVEVADTEIIRScEMANAHGFIMQTtlkYETNVGEKGTqMSGGQKQRIAIARALVREPAILLLDEATSAL 666
Cdd:PRK11614 101 LAMGGFFAERDQFQE-RIKWVYELFPRL---HERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
516-710 |
5.52e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPL------EEFEH--HYIHKKIALVGQepvlfa 587
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskEALENgiSMVHQELNLVLQ------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RSVMENV---RY---GVEVADTEIIRSCEMANAHgfimqttLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDE 661
Cdd:PRK10982 88 RSVMDNMwlgRYptkGMFVDQDKMYRDTKAIFDE-------LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71992290 662 ATSAL-DTESEHLVQeaIYKNLD--GKSVILIAHRLSTVEK-ADKIVVINKGR 710
Cdd:PRK10982 161 PTSSLtEKEVNHLFT--IIRKLKerGCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
512-692 |
1.22e-10 |
|
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: 64.57 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 512 DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLenfyvpnAGqvlVDgvplEEFEHHYIHKKIALVG---QEPVL-FA 587
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD----KDFNGEARPQPGIKVGylpQEPQLdPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RSVMENV-------------------RYGVEVAD--------TEIIRSCEMANAHGfiMQTTLK----------YETNVg 630
Cdd:TIGR03719 83 KTVRENVeegvaeikdaldrfneisaKYAEPDADfdklaaeqAELQEIIDAADAWD--LDSQLEiamdalrcppWDADV- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 631 ekgTQMSGGQKQRIAIARALVREPAILLLDEATSALDTES----EHLVQEaiYKNldgkSVILIAH 692
Cdd:TIGR03719 160 ---TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE--YPG----TVVAVTH 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
515-668 |
1.55e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCI----SLLENFYVPNAGQVLVDGVPLEEFEHHY-----------IHKKIALV 579
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLktiaSNTDGFHIGVEGVITYDGITPEEIKKHYrgdvvynaetdVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 580 GQEPVLFARSVMENVRY-GVevadTEIIRSCEMANAHGFIMQTTLKYETNVGE---KGtqMSGGQKQRIAIARALVREPA 655
Cdd:TIGR00956 156 GETLDFAARCKTPQNRPdGV----SREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAK 229
|
170
....*....|...
gi 71992290 656 ILLLDEATSALDT 668
Cdd:TIGR00956 230 IQCWDNATRGLDS 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
486-709 |
1.69e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 486 NGEYMPENVVGKIEF--RNVHFSYPTRS-DQPILKDLSFTVEPGETVALVGPSGSGKSS---CISLLENFYVPNAGQVLV 559
Cdd:TIGR00956 746 NDEKDMEKESGEDIFhwRNLTYEVKIKKeKRVILNNVDGWVKPGTLTALMGASGAGKTTllnVLAERVTTGVITGGDRLV 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 560 DGVPLEE-FEhhyihKKIALVGQEPVLFARS-VMENVRYGV------EVADTE-------IIRSCEManahgfimqTTLK 624
Cdd:TIGR00956 826 NGRPLDSsFQ-----RSIGYVQQQDLHLPTStVRESLRFSAylrqpkSVSKSEkmeyveeVIKLLEM---------ESYA 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 625 yETNVGEKGTQMSGGQKQRIAIARALVREPAILL-LDEATSALDTESEHLVQEAIYKNLD-GKSVILIAHRLSTV--EKA 700
Cdd:TIGR00956 892 -DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAIlfEEF 970
|
....*....
gi 71992290 701 DKIVVINKG 709
Cdd:TIGR00956 971 DRLLLLQKG 979
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
505-678 |
2.06e-10 |
|
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: 61.66 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 505 FSYPTRSDQpiLKDLSFTVEPG-----ETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEeFEHHYIHKKIALV 579
Cdd:cd03237 1 YTYPTMKKT--LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 580 GQEpvlFARSVMENVrYGVEVADTEIIRScemanahgfiMQTTLKYETNVgekgTQMSGGQKQRIAIARALVREPAILLL 659
Cdd:cd03237 78 VRD---LLSSITKDF-YTHPYFKTEIAKP----------LQIEQILDREV----PELSGGELQRVAIAACLSKDADIYLL 139
|
170
....*....|....*....
gi 71992290 660 DEATSALDTESEHLVQEAI 678
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVI 158
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
498-695 |
3.54e-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: 63.61 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYvPNAGQVLVdgVPLEEfehhyihkKIA 577
Cdd:TIGR00954 452 IKFENIPLVTP--NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT--KPAKG--------KLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 578 LVGQEPVLFARSVMENVRY--GVE------VADTEIIRSCEMANAHGFImqttlkyETNVGEKGTQ-----MSGGQKQRI 644
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIIYpdSSEdmkrrgLSDKDLEQILDNVQLTHIL-------EREGGWSAVQdwmdvLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71992290 645 AIARALVREPAILLLDEATSALDTEsehlVQEAIYKNLD--GKSVILIAHRLS 695
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVD----VEGYMYRLCRefGITLFSVSHRKS 640
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
486-696 |
3.85e-10 |
|
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: 63.03 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 486 NGEYMPENVvgkIEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLV-DGVpl 564
Cdd:TIGR03719 314 PGPRLGDKV---IEAENLTKAF---GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 565 eefehhyihkKIALVGQ--EPVLFARSVMENVRYG---VEVADTEIirscemaNAHGFIMQTTLK---YETNVGekgtQM 636
Cdd:TIGR03719 386 ----------KLAYVDQsrDALDPNKTVWEEISGGldiIKLGKREI-------PSRAYVGRFNFKgsdQQKKVG----QL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 637 SGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNLDGkSVILIAH------RLST 696
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAG-CAVVISHdrwfldRIAT 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
513-711 |
4.25e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 513 QPIlkdlSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLE-EFEHHYIHKKIALV----GQEPVLFA 587
Cdd:PRK11288 270 EPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCpedrKAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RSVMENV---------RYGVevadteII-RSCEMANAHGFIMQttLKYET-NVGEKGTQMSGGQKQRIAIARALVREPAI 656
Cdd:PRK11288 346 HSVADNInisarrhhlRAGC------LInNRWEAENADRFIRS--LNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 657 LLLDEATSALDTESEHLVQEAIYkNL--DGKSVILIAHRLSTVEK-ADKIVVINKGRV 711
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIY-ELaaQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
179-442 |
4.84e-10 |
|
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: 61.37 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 179 WLWHISGFSwLFIYSITrIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGgsfeYAYARIQRAIRYD 258
Cdd:cd18555 3 LLISILLLS-LLLQLLT-LLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRG----YIIIKLQTKLDKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 259 L----FHGLVKQDVAFYDAHKTGEVTSR---LAADCQTMSDTValnVNVFLrNCVMLLGSMIFMMKLSWRLSLVTFILVP 331
Cdd:cd18555 77 LmsdfFEHLLKLPYSFFENRSSGDLLFRansNVYIRQILSNQV---ISLII-DLLLLVIYLIYMLYYSPLLTLIVLLLGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 332 IIFVASkIFGTYYdlLSERTQDTI---AESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLW 408
Cdd:cd18555 153 LIVLLL-LLTRKK--IKKLNQEEIvaqTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNS 229
|
250 260 270
....*....|....*....|....*....|....
gi 71992290 409 VSELFQSFIIVSVLWYGGHLVLTQKMKGDLLVSF 442
Cdd:cd18555 230 ISSSIQFIAPLLILWIGAYLVINGELTLGELIAF 263
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
512-692 |
5.63e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 512 DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLenfyvpnAGqvlVDgvplEEFEHHYIHKKIALVG---QEPVL-FA 587
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD----KEFEGEARPAPGIKVGylpQEPQLdPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RSVMENVRYGV-EVADT-----EIirSCEMANAHGFiMQTTLKYETNVGEK----------------------------G 633
Cdd:PRK11819 85 KTVRENVEEGVaEVKAAldrfnEI--YAAYAEPDAD-FDALAAEQGELQEIidaadawdldsqleiamdalrcppwdakV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 634 TQMSGGQKQRIAIARALVREPAILLLDEATSALDTES-----EHLVQeaiYKNldgkSVILIAH 692
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawleQFLHD---YPG----TVVAVTH 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
480-678 |
7.29e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 480 EPQIQHNgeyMPENVvGKIEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYvPNA----- 554
Cdd:PRK10938 247 EPSARHA---LPANE-PRIVLNNGVVSY---NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGysndl 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 555 ---------GQVLVDgvpleefehhyIHKKIALVGQEPVLFARsVMENVRygvevadtEIIRScemanahGF-----IMQ 620
Cdd:PRK10938 319 tlfgrrrgsGETIWD-----------IKKHIGYVSSSLHLDYR-VSTSVR--------NVILS-------GFfdsigIYQ 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 621 TT--------------LKYETNVGEKGTQ-MSGGQkQRIA-IARALVREPAILLLDEATSALDTESEHLVQEAI 678
Cdd:PRK10938 372 AVsdrqqklaqqwldiLGIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV 444
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
512-710 |
1.38e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 512 DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPN--AGQVLVDGVPLEEfehhYIHKKIALVGQEPVLFAR- 588
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK----QILKRTGFVTQDDILYPHl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 589 SVMENVRY-GVEVADTEIIRSCEMANAHGFIMQTTL-KYE-TNVGEKGTQ-MSGGQKQRIAIARALVREPAILLLDEATS 664
Cdd:PLN03211 156 TVRETLVFcSLLRLPKSLTKQEKILVAESVISELGLtKCEnTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 71992290 665 ALD-TESEHLVQEAIYKNLDGKSVILIAHRLST--VEKADKIVVINKGR 710
Cdd:PLN03211 236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
516-709 |
2.55e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPL--------EEFEHHYIHKKIALVGQepvlfa 587
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssQEAGIGIIHQELNLIPQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RSVMENVRYGVEVADT-EIIRSCEM-ANAHGFIMQTTLKY--ETNVGEkgtqMSGGQKQRIAIARALVREPAILLLDEAT 663
Cdd:PRK10762 94 LTIAENIFLGREFVNRfGRIDWKKMyAEADKLLARLNLRFssDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 71992290 664 SAL-DTESEHLVQeaIYKNL--DGKSVILIAHRLSTV-EKADKIVVINKG 709
Cdd:PRK10762 170 DALtDTETESLFR--VIRELksQGRGIVYISHRLKEIfEICDDVTVFRDG 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
516-723 |
3.17e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.67 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvpleefEHHYIHKKIALVGQ----EPVLFARSVM 591
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQltgiENIEFKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 592 ENVRYGVEVADTEIIRSCEMANahgFIMQTTLKYetnvgekgtqmSGGQKQRIAIARALVREPAILLLDEATSALDTESE 671
Cdd:PRK13546 114 GFKRKEIKAMTPKIIEFSELGE---FIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71992290 672 HLVQEAIYK-NLDGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETLLKD 723
Cdd:PRK13546 180 QKCLDKIYEfKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
463-715 |
3.82e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 463 LMqsVGasRKVFEYIDREPQiqHNGEympenVVgkIEFRNVhfSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSC 542
Cdd:COG3845 236 LM--VG--REVLLRVEKAPA--EPGE-----VV--LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 543 ISLLENFYVPNAGQVLVDGVPLEEFE-HHYIHKKIALVGQEP-----VLfARSVMENV---RYgvevadteiiRSCEMAN 613
Cdd:COG3845 301 AEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRlgrglVP-DMSVAENLilgRY----------RRPPFSR 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 614 aHGFIMQTTLKYET------------NVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESehlvQEAIYKN 681
Cdd:COG3845 370 -GGFLDRKAIRAFAeelieefdvrtpGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGA----IEFIHQR 444
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 71992290 682 L-----DGKSVILIAHRLSTV-EKADKIVVINKGRV-----------EQIG 715
Cdd:COG3845 445 LlelrdAGAAVLLISEDLDEIlALSDRIAVMYEGRIvgevpaaeatrEEIG 495
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
180-448 |
5.32e-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: 58.24 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 180 LWHISGFSwLFIYSITrIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDL 259
Cdd:cd18567 4 LLQILLLS-LALELFA-LASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 260 FHGLVKQDVAFYDAHKTGEVTSRLAAdCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVpIIFVASKI 339
Cdd:cd18567 82 FRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAV-ALYALLRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 340 FgtYYDLLSERTQDTI---AESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSF 416
Cdd:cd18567 160 A--LYPPLRRATEEQIvasAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGL 237
|
250 260 270
....*....|....*....|....*....|..
gi 71992290 417 IIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQ 448
Cdd:cd18567 238 ENILVIYLGALLVLDGEFTVGMLFAFLAYKDQ 269
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
498-737 |
7.56e-09 |
|
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: 59.07 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYvPN--AGQVLVDGVPLE-EFEHHYIHK 574
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGkfEGNVFINGKPVDiRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 KIALVGQE-------PVLfarSVMENVRYGV-----------EVADTEIIRS----CEMANAHGFIMQTTLkyetnvgek 632
Cdd:TIGR02633 337 GIAMVPEDrkrhgivPIL---GVGKNITLSVlksfcfkmridAAAELQIIGSaiqrLKVKTASPFLPIGRL--------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 633 gtqmSGGQKQRIAIARALVREPAILLLDEATSALDTESEHlvqeAIYKNL-----DGKSVILIAHRLSTVEK-ADKIVVI 706
Cdd:TIGR02633 405 ----SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY----EIYKLInqlaqEGVAIIVVSSELAEVLGlSDRVLVI 476
|
250 260 270
....*....|....*....|....*....|..
gi 71992290 707 NKGRVE-QIGNHEtllkdtngtyakLVQRQMM 737
Cdd:TIGR02633 477 GEGKLKgDFVNHA------------LTQEQVL 496
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
459-714 |
7.64e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 459 VWTGLMQSVGASRKVFEYIDREPQIQHNG-EYMPENVVGKI--EFRNVhfsypTRSDQPILKDLSFTVEPGETVALVGPS 535
Cdd:PRK09700 224 VCSGMVSDVSNDDIVRLMVGRELQNRFNAmKENVSNLAHETvfEVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLV 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 536 GSGKSSCISLLENFYVPNAGQVLVDGVPLE-EFEHHYIHKKIALVGQ---EPVLFAR-SVMENVrygvevadtEIIRSCE 610
Cdd:PRK09700 299 GSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSIAQNM---------AISRSLK 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 611 MANAHGFIMQTTLKYETNVGEKG---------------TQMSGGQKQRIAIARALVREPAILLLDEATSALD--TESEhl 673
Cdd:PRK09700 370 DGGYKGAMGLFHEVDEQRTAENQrellalkchsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAE-- 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 71992290 674 vqeaIYKNL-----DGKSVILIAHRLSTV-EKADKIVVINKGRVEQI 714
Cdd:PRK09700 448 ----IYKVMrqladDGKVILMVSSELPEIiTVCDRIAVFCEGRLTQI 490
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
516-709 |
1.15e-08 |
|
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: 55.41 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCisLLENFYvPNAGQVLVDGVPLeeFEHHyihkkialvgqePVLFARSVmenvr 595
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY-ASGKARLISFLPK--FSRN------------KLIFIDQL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 596 ygvevadteiirscemanahGFIMQTTLKYETnVGEKGTQMSGGQKQRIAIARALVREP--AILLLDEATSALDTESEHL 673
Cdd:cd03238 69 --------------------QFLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|....*..
gi 71992290 674 VQEAIYKNLD-GKSVILIAHRLSTVEKADKIVVINKG 709
Cdd:cd03238 128 LLEVIKGLIDlGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
512-755 |
1.34e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 512 DQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQV-LVDGVPLEEFEHHYIHkkialvgqepvlFARSV 590
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLE------------FLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 591 MENVRYGVEVADTEIIRSC-EMANAHGFimqttlkYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTE 669
Cdd:PRK10636 392 ESPLQHLARLAPQELEQKLrDYLGGFGF-------QGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 670 SEHLVQEAIYkNLDGKSVILIAHRLSTVEKADKIVVINKGRVE------------------QIGNHETLLKDTNGTYAkl 731
Cdd:PRK10636 465 MRQALTEALI-DFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEpfdgdledyqqwlsdvqkQENQTDEAPKENNANSA-- 541
|
250 260
....*....|....*....|....
gi 71992290 732 vqrQMMGDQKprKRPAVARSGPQP 755
Cdd:PRK10636 542 ---QARKDQK--RREAELRTQTQP 560
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
498-711 |
2.11e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPIL-KDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDG-VPLEEFEHHYIHkk 575
Cdd:PLN03073 509 ISFSDASFGYP---GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkVRMAVFSQHHVD-- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 ialvgqepvlfarsvmenvryGVEVADTEIIRsceMANAHGFIMQTTLKyeTNVGEKGTQ----------MSGGQKQRIA 645
Cdd:PLN03073 584 ---------------------GLDLSSNPLLY---MMRCFPGVPEQKLR--AHLGSFGVTgnlalqpmytLSGGQKSRVA 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 646 IARALVREPAILLLDEATSALDTES-EHLVQEAIyknLDGKSVILIAHRLSTVE-KADKIVVINKGRV 711
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV---LFQGGVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
522-706 |
3.10e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 522 TVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLV----DGVpLEEFE----HHYIHK------KIALVGQEPVLFA 587
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEepswDEV-LKRFRgtelQNYFKKlyngeiKVVHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RSVMENVRYGVEVADT-----EIIRSCEMANAhgfimqttlkyetnVGEKGTQMSGGQKQRIAIARALVREPAILLLDEA 662
Cdd:PRK13409 174 KVFKGKVRELLKKVDErgkldEVVERLGLENI--------------LDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71992290 663 TSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEK-ADKIVVI 706
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
518-704 |
3.35e-08 |
|
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: 53.52 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 518 DLSFTvePGETVALVGPSGSGKSSCIsllenfyvpnagqvlvdgvpleefehhyihKKIALVgqepvLFARSVMENVRYG 597
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTIL------------------------------DAIGLA-----LGGAQSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 598 VEVAdteIIRSCEMANAHGFIMQttlkyetnvgekgtqMSGGQKQRIAIARAL----VREPAILLLDEATSALDTESEHL 673
Cdd:cd03227 58 VKAG---CIVAAVSAELIFTRLQ---------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|..
gi 71992290 674 VQEAIYKNLDGKS-VILIAHRLSTVEKADKIV 704
Cdd:cd03227 120 LAEAILEHLVKGAqVIVITHLPELAELADKLI 151
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
522-706 |
3.89e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 522 TVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVlvDGVP-----LEEFE----HHYIHK----------KIALVGQE 582
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevLKRFRgtelQDYFKKlangeikvahKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 583 PVLF---ARSVMENV--RygvEVADtEIIRSCEMANAhgfimqttlkYETNVGEkgtqMSGGQKQRIAIARALVREPAIL 657
Cdd:COG1245 173 PKVFkgtVRELLEKVdeR---GKLD-ELAEKLGLENI----------LDRDISE----LSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 71992290 658 LLDEATSALDTESEHLVQEAIyKNL--DGKSVILIAHRLSTVEK-ADKIVVI 706
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLI-RELaeEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
516-716 |
4.26e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.44 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPleefehhyihKKIA--------LVGQEPVLFA 587
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA----------ALIAissglngqLTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 588 RSVMENVRYGVEVADTEIIrscEMANAHGFIMQTTLKYetnvgekgtqmSGGQKQRIAIARALVREPAILLLDEATSALD 667
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEII---EFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 668 tesehlvQEAIYKNLD--------GKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGN 716
Cdd:PRK13545 176 -------QTFTKKCLDkmnefkeqGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGD 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
522-695 |
5.38e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 522 TVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVlvDGVP-----LEEFE----HHYIHK------KIALVGQEPVLF 586
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPdwdeiLDEFRgselQNYFTKllegdvKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 587 ARSVMENVRygvevadtEIIRSCEMANAHGFIMQTtLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSAL 666
Cdd:cd03236 100 PKAVKGKVG--------ELLKKKDERGKLDELVDQ-LELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|
gi 71992290 667 DTESEHLVQEAIYK-NLDGKSVILIAHRLS 695
Cdd:cd03236 171 DIKQRLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
481-711 |
7.34e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 481 PQIQHNgeympenvVGKIEFRNVHFS--YPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYvPNA--GQ 556
Cdd:PRK13549 249 PREPHT--------IGEVILEVRNLTawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 557 VLVDGVPLE-EFEHHYIHKKIALV-------GQEPVLfarSVMENVRYGV--EVADTEIIR-SCEMANAHGFIMQTTLKY 625
Cdd:PRK13549 320 IFIDGKPVKiRNPQQAIAQGIAMVpedrkrdGIVPVM---GVGKNITLAAldRFTGGSRIDdAAELKTILESIQRLKVKT 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 626 ---ETNVGekgtQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHlvqeAIYKNLD-----GKSVILIAHRLSTV 697
Cdd:PRK13549 397 aspELAIA----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY----EIYKLINqlvqqGVAIIVISSELPEV 468
|
250
....*....|....*
gi 71992290 698 -EKADKIVVINKGRV 711
Cdd:PRK13549 469 lGLSDRVLVMHEGKL 483
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
511-704 |
1.03e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 511 SDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIhkkiALVGQEPVL-FARS 589
Cdd:PRK13541 11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYIGHNLGLkLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 590 VMENVRYGvevadTEIIRSCEMANA--HGFIMQTTLKyetnvgEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALD 667
Cdd:PRK13541 87 VFENLKFW-----SEIYNSAETLYAaiHYFKLHDLLD------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 71992290 668 TESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIV 704
Cdd:PRK13541 156 KENRDLLNNLIVMKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
630-752 |
1.35e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 630 GEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNL-DGKSVILIAHRLSTVEK-ADKIVVIN 707
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVID 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 71992290 708 KGRVEQIGNHETLLKDTNGTYAKLvqRQMMGDQKPRKRPAVARSG 752
Cdd:NF000106 219 RGRVIADGKVDELKTKVGGRTLQI--RPAHAAELDRMVGAIAQAG 261
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
516-705 |
1.86e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPG-----ETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDgvpleefehhyihKKIALVGQ-------EP 583
Cdd:PRK13409 350 LGDFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQyikpdydGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 584 V-LFARSVmeNVRYGVEVADTEIIRScemanahgfiMQTTLKYETNVGEkgtqMSGGQKQRIAIARALVREPAILLLDEA 662
Cdd:PRK13409 417 VeDLLRSI--TDDLGSSYYKSEIIKP----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71992290 663 TSALDTESEHLVQEAI--YKNLDGKSVILIAHRLSTVEK-ADKIVV 705
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIrrIAEEREATALVVDHDIYMIDYiSDRLMV 526
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
187-467 |
2.76e-07 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 53.00 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 187 SWLFIYS--ITRIFVPYYTGQVIaTVVATKSYPALSNAVYIMTIISLVSAVAAGF---RGGSFEYAYARIQRAIRYDLFH 261
Cdd:cd18560 1 SLLLLILgkACNVLAPLFLGRAV-NALTLAKVKDLESAVTLILLYALLRFSSKLLkelRSLLYRRVQQNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 262 GLVKQDVAFYDAHKTGEVTS---RLAADCQTMSDTVALNVNVFLRNCVMllGSMIFMMKLSWRLSLVTFILVpIIFVASK 338
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRimdRGTESANTLLSYLVFYLVPTLLELIV--VSVVFAFHFGAWLALIVFLSV-LLYGVFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 339 IFGTYYDL-LSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRfYGKLTHTLDVTRTKAIAYIGFL-WVSELFQSF 416
Cdd:cd18560 157 IKVTEWRTkFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDR-YGEAVKEYQKSSVKVQASLSLLnVGQQLIIQL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 71992290 417 IIVSVLWYGGHLVLTQKMK-GDlLVSFLLYQMQLGDNLRQMGEVWTGLMQSV 467
Cdd:cd18560 236 GLTLGLLLAGYRVVDGGLSvGD-FVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
509-716 |
3.71e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 509 TRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvplEEFEHHYIHKKI----ALVGQE-- 582
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNANEAInhgfALVTEErr 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 583 --------PVLFaRSVMENVR-YGVEVAdteIIRSCEMANAHGFIMQT----TLKYETNVGekgtQMSGGQKQRIAIARA 649
Cdd:PRK10982 334 stgiyaylDIGF-NSLISNIRnYKNKVG---LLDNSRMKSDTQWVIDSmrvkTPGHRTQIG----SLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 650 LVREPAILLLDEATSALDT----ESEHLVQEAIYKnldGKSVILIAHRL-STVEKADKIVVINKGRVEQIGN 716
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVgakfEIYQLIAELAKK---DKGIIIISSEMpELLGITDRILVMSNGLVAGIVD 474
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
510-737 |
3.74e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 510 RSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGvpleefehhyiHKKIALVGQEPVLFARS 589
Cdd:PRK10636 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------NWQLAWVNQETPALPQP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 590 VMENVRYGvevaDTEIiRSCE--------------MANAHG---FIMQTTLKYET-----NVGEKGTQM-------SGGQ 640
Cdd:PRK10636 80 ALEYVIDG----DREY-RQLEaqlhdanerndghaIATIHGkldAIDAWTIRSRAasllhGLGFSNEQLerpvsdfSGGW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 641 KQRIAIARALVREPAILLLDEATSALDTESEhLVQEAIYKNLDGkSVILIAHRLSTVEK-ADKIVVINKGRV-EQIGNHE 718
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLDLDAV-IWLEKWLKSYQG-TLILISHDRDFLDPiVDKIIHIEQQSLfEYTGNYS 232
|
250
....*....|....*....
gi 71992290 719 TLLKDTNgtyAKLVQRQMM 737
Cdd:PRK10636 233 SFEVQRA---TRLAQQQAM 248
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
206-447 |
4.66e-07 |
|
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: 52.12 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 206 VIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRggsfEYAYARIqrAIRYD------LFHGLVKQDVAFYDAHKTGEV 279
Cdd:cd18588 28 IIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLR----TYLFSHT--TNRIDaelgarLFRHLLRLPLSYFESRQVGDT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 280 TSR---LAADCQTMSD---TVALNVnVFLrncVMLLGSMIFmmkLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQD 353
Cdd:cd18588 102 VARvreLESIRQFLTGsalTLVLDL-VFS---VVFLAVMFY---YSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 354 TIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVT-RTKAIAYIGFLWVSeLFQSFIIVSVLWYGGHLVltq 432
Cdd:cd18588 175 RGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASfKTANLSNLASQIVQ-LIQKLTTLAILWFGAYLV--- 250
|
250
....*....|....*....
gi 71992290 433 kMKGDL----LVSFllyQM 447
Cdd:cd18588 251 -MDGELtigqLIAF---NM 265
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
509-711 |
5.39e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 509 TRSDQPIL----------KDLSFTVEPGETVALVGPSGSGKSScisLLENFY---VPNAGQVLVDGvplEEFEHHYIHKK 575
Cdd:PRK15439 262 QAAGAPVLtvedltgegfRNISLEVRAGEILGLAGVVGAGRTE---LAETLYglrPARGGRIMLNG---KEINALSTAQR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 576 IA--LV-----GQEPVLFARSVME-NVrygvevadteiirSCEMANAHGFIMQTtlKYETNVGEK-----------GTQ- 635
Cdd:PRK15439 336 LArgLVylpedRQSSGLYLDAPLAwNV-------------CALTHNRRGFWIKP--ARENAVLERyrralnikfnhAEQa 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 636 ---MSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIyKNL--DGKSVILIAHRLSTVEK-ADKIVVINKG 709
Cdd:PRK15439 401 artLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI-RSIaaQNVAVLFISSDLEEIEQmADRVLVMHQG 479
|
..
gi 71992290 710 RV 711
Cdd:PRK15439 480 EI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
493-669 |
5.63e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 493 NVVgkIEFRNVHFSYptrSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLV-DGVpleefehhy 571
Cdd:PRK11819 322 DKV--IEAENLSKSF---GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETV--------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 572 ihkKIALVGQ-----EPvlfARSVMEnvrygvEVAD-TEIIRScemanahGfimqttlKYETN----VGE---KGT---- 634
Cdd:PRK11819 388 ---KLAYVDQsrdalDP---NKTVWE------EISGgLDIIKV-------G-------NREIPsrayVGRfnfKGGdqqk 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 71992290 635 ---QMSGGQKQRIAIARALVREPAILLLDEATSALDTE 669
Cdd:PRK11819 442 kvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
516-705 |
6.93e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPG-----ETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDgvpleefehhyihKKIALVGQEPV-LFARS 589
Cdd:COG1245 351 YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQYISpDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 590 VMENVR------YGVEVADTEIIRScemanahgfiMQTTLKYETNVGEkgtqMSGGQKQRIAIARALVREPAILLLDEAT 663
Cdd:COG1245 418 VEEFLRsantddFGSSYYKTEIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71992290 664 SALDTESEHLVQEAIyKNL---DGKSVILIAHRLSTVEK-ADKIVV 705
Cdd:COG1245 484 AHLDVEQRLAVAKAI-RRFaenRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
186-477 |
1.08e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 50.97 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 186 FSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVK 265
Cdd:cd18580 5 LLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 266 QDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWrlslVTFILVPIIFVASKIFGTYY- 344
Cdd:cd18580 85 APMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYYLLQRYYl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 345 ----DLlseRTQDTIAES--NDVAEEVLSTMRTVRSFSCEnveaDRFYGKLTHTLDV-TRTKAIAYIGFLWVS---ELFQ 414
Cdd:cd18580 161 rtsrQL---RRLESESRSplYSHFSETLSGLSTIRAFGWQ----ERFIEENLRLLDAsQRAFYLLLAVQRWLGlrlDLLG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 415 SFIIVSVLWYgghLVLTQKMKGDLLVSF-LLYQMQLGDNLRQMGEVWTGLMQSVGASRKVFEYI 477
Cdd:cd18580 234 ALLALVVALL---AVLLRSSISAGLVGLaLTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
515-709 |
1.12e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 515 ILKDLSFTVEPGETVALVGPSGSGKSSCISLLENF----YVpnAGQVLVDGVP--LEEF-------EHHYIHKKIALVgQ 581
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRktggYI--EGDIRISGFPkkQETFarisgycEQNDIHSPQVTV-R 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 582 EPVLFARSVmenvRYGVEVADTEIIRscemanahgFIMQTTLKYETN------VGEKG-TQMSGGQKQRIAIARALVREP 654
Cdd:PLN03140 972 ESLIYSAFL----RLPKEVSKEEKMM---------FVDEVMELVELDnlkdaiVGLPGvTGLSTEQRKRLTIAVELVANP 1038
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71992290 655 AILLLDEATSALDTESEHLVQEAIYKNLD-GKSVILIAHRLS--TVEKADKIVVINKG 709
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
511-720 |
1.39e-06 |
|
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: 52.32 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 511 SDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEfEHHYIHKKIA-----------LV 579
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGycpqfdaiddlLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 580 GQEPV-LFARsvmenVRyGVEVADTEiirscEMANAHGFIMQTTLKYETNVGekgtQMSGGQKQRIAIARALVREPAILL 658
Cdd:TIGR01257 2029 GREHLyLYAR-----LR-GVPAEEIE-----KVANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 659 LDEATSALDTESEHLVQEAIYKNL-DGKSVILIAHRLSTVEK-ADKIVVINKGRVEQIGNHETL 720
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
514-711 |
2.54e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 514 PILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHH--------YI---HKKIALVgqe 582
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivYIsedRKRDGLV--- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 583 pvlFARSVMEN-----VRYGVEVAdTEIIRSCEMANAHGFIMQTTLK---YETNVGEkgtqMSGGQKQRIAIARALVREP 654
Cdd:PRK10762 343 ---LGMSVKENmsltaLRYFSRAG-GSLKHADEQQAVSDFIRLFNIKtpsMEQAIGL----LSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 655 AILLLDEATSALDTESEHLVQEAI--YKNlDGKSVILIAHRLSTV-EKADKIVVINKGRV 711
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLInqFKA-EGLSIILVSSEMPEVlGMSDRILVMHEGRI 473
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
516-704 |
2.70e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.54 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 516 LKDLSFTVEPGETVALVGPSGSGKSScisLLENFYVPNAGQVL----VDGVPLEEFE-HHYIHKKIAlVGQEPV------ 584
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSS---LINDTLYPALARRLhlkkEQPGNHDRIEgLEHIDKVIV-IDQSPIgrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 585 --------------LFA---------RSVMEnVRY-GVEVADTeiirsCEM--ANAHGF---------IMQTT----LKY 625
Cdd:cd03271 87 npatytgvfdeireLFCevckgkrynRETLE-VRYkGKSIADV-----LDMtvEEALEFfenipkiarKLQTLcdvgLGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 626 ETnVGEKGTQMSGGQKQRIAIARALVRE---PAILLLDEATSALDTESEHLVQEAIYKNLD-GKSVILIAHRLSTVEKAD 701
Cdd:cd03271 161 IK-LGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCAD 239
|
...
gi 71992290 702 KIV 704
Cdd:cd03271 240 WII 242
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
225-391 |
3.33e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 49.84 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 225 IMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRN 304
Cdd:cd18605 47 VYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 305 CVMLLGSMIFMM-KLSWrlslVTFILVPIIFVASKIFgTYYDLLSE--RTQDTIAESN--DVAEEVLSTMRTVRSFSCEN 379
Cdd:cd18605 127 LFGLLGYLVVICyQLPW----LLLLLLPLAFIYYRIQ-RYYRATSRelKRLNSVNLSPlyTHFSETLKGLVTIRAFRKQE 201
|
170
....*....|..
gi 71992290 380 VEADRFYGKLTH 391
Cdd:cd18605 202 RFLKEYLEKLEN 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
476-711 |
4.26e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 476 YIDREPQIqhnGEympenVVGKIEFRNVHfsYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSS-CISLLENFYVPN- 553
Cdd:NF040905 246 YPERTPKI---GE-----VVFEVKNWTVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTElAMSVFGRSYGRNi 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 554 AGQVLVDGVPLE-EFEHHYIHKKIALVGQEpvlfaRSvmenvRYGVEVADTeIIRSCEMAN-----AHGFI--------- 618
Cdd:NF040905 316 SGTVFKDGKEVDvSTVSDAIDAGLAYVTED-----RK-----GYGLNLIDD-IKRNITLANlgkvsRRGVIdeneeikva 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 619 --MQTTLKYET-NVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHlvqeAIYKNLD-----GKSVILI 690
Cdd:NF040905 385 eeYRKKMNIKTpSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKY----EIYTIINelaaeGKGVIVI 460
|
250 260
....*....|....*....|..
gi 71992290 691 AHRLSTV-EKADKIVVINKGRV 711
Cdd:NF040905 461 SSELPELlGMCDRIYVMNEGRI 482
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
202-395 |
9.99e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 48.37 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 202 YTGQVIATVVATKSYPALSNAVYIM--TIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEV 279
Cdd:cd18602 30 HDVASVVFNITSSSLEDDEVSYYISvyAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 280 TSRLAADCQTMSDTVALNVNVFLRnCVMLLGSMIFMMklswrlSLVT----FILVPIIFVASKIFgTYYDLLSERTQ--D 353
Cdd:cd18602 110 LNRFSSDTNVIDQKLPTTLERLLR-FLLLCLSAIIVN------AIVTpyflIALIPIIIVYYFLQ-KFYRASSRELQrlD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71992290 354 TIAESNDVAE--EVLSTMRTVRSFSCENveadRFYGKLTHTLDV 395
Cdd:cd18602 182 NITKSPVFSHfsETLGGLTTIRAFRQQA----RFTQQMLELIDR 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
498-744 |
1.47e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPTrSDQPI--LKDLSFTVEPGETVALVGPSGSGKS-----SCISLLENFYVpNAGQVLVDGVPLEEF--- 567
Cdd:PRK15093 4 LDIRNLTIEFKT-SDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSliakaICGVTKDNWRV-TADRMRFDDIDLLRLspr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 568 -EHHYIHKKIALVGQEP-------VLFARSVMENV-----------------RYGVEVADTEIIRScemanaHGFIMQTt 622
Cdd:PRK15093 82 eRRKLVGHNVSMIFQEPqscldpsERVGRQLMQNIpgwtykgrwwqrfgwrkRRAIELLHRVGIKD------HKDAMRS- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 623 LKYEtnvgekgtqMSGGQKQRIAIARALVREPAILLLDEATSALdtesEHLVQEAIYKNL------DGKSVILIAHRLST 696
Cdd:PRK15093 155 FPYE---------LTEGECQKVMIAIALANQPRLLIADEPTNAM----EPTTQAQIFRLLtrlnqnNNTTILLISHDLQM 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 71992290 697 VEK-ADKIVVINKGRVEQIGNHETLLKDTNGTYAKLVQRQM--MGDQKPRK 744
Cdd:PRK15093 222 LSQwADKINVLYCGQTVETAPSKELVTTPHHPYTQALIRAIpdFGSAMPHK 272
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
565-704 |
2.12e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 565 EEFEHHYIHKKIALVGQEPVLFARSVMENVrygvevadTEIIRSCEmanahgFIMQTTLKYETnVGEKGTQMSGGQKQRI 644
Cdd:TIGR00630 774 ETLEVKYKGKNIADVLDMTVEEAYEFFEAV--------PSISRKLQ------TLCDVGLGYIR-LGQPATTLSGGEAQRI 838
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71992290 645 AIARALVRE---PAILLLDEATSALDTESEHLVQEAIYKNLD-GKSVILIAHRLSTVEKADKIV 704
Cdd:TIGR00630 839 KLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYII 902
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
498-670 |
2.60e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 498 IEFRNVHFSYPtrsDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVlvdgvpleefehhyihK--- 574
Cdd:PRK15064 320 LEVENLTKGFD---NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------------Kwse 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 575 --KIALVGQEPVL-FA--RSVMENVR-YGVEVADTEIIRScemanahgfIMQTTLKYETNVGEKGTQMSGGQKQRIAIAR 648
Cdd:PRK15064 381 naNIGYYAQDHAYdFEndLTLFDWMSqWRQEGDDEQAVRG---------TLGRLLFSQDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180
....*....|....*....|..
gi 71992290 649 ALVREPAILLLDEATSALDTES 670
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMES 473
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
189-467 |
3.09e-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: 46.72 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 189 LFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIM--TIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQ 266
Cdd:cd18582 5 LVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLayGLARILSSLFNELRDALFARVSQRAVRRLALRVFRHLHSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 267 DVAFYDAHKTGEVTS---RLAADCQTMSDTVALNV-NVFLRncvMLLGSMIFMMKLSWRLSLVTFILVpIIFVASKIFGT 342
Cdd:cd18582 85 SLRFHLSRKTGALSRaieRGTRGIEFLLRFLLFNIlPTILE---LLLVCGILWYLYGWSYALITLVTV-ALYVAFTIKVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 343 yydllsERTQDTIAESNDVAEEV-------LSTMRTVRSFSCENVEADRFYGKL----THTLDVTRTKAIAYIGflwvse 411
Cdd:cd18582 161 ------EWRTKFRREMNEADNEAnakavdsLLNYETVKYFNNEEYEAERYDKALakyeKAAVKSQTSLALLNIG------ 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71992290 412 lfQSFII----VSVLWYGGHLVLTQKMK-GDL-LVSFLLyqMQLGDNLRQMGEVWTGLMQSV 467
Cdd:cd18582 229 --QALIIslglTAIMLLAAQGVVAGTLTvGDFvLVNTYL--LQLYQPLNFLGFVYREIRQSL 286
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
523-706 |
4.53e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 523 VEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEefehhYIHKKIALvgqepvlfarsvmenvrygvevad 602
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-----YKPQYIDL------------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 603 teiirscemanahgfimqttlkyetnvgekgtqmSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNL 682
Cdd:cd03222 73 ----------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*..
gi 71992290 683 D--GKSVILIAHRLSTVEK-ADKIVVI 706
Cdd:cd03222 119 EegKKTALVVEHDLAVLDYlSDRIHVF 145
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
635-667 |
8.20e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 8.20e-05
10 20 30
....*....|....*....|....*....|...
gi 71992290 635 QMSGGQKQRIAIARALVREPAILLLDEATSALD 667
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
180-472 |
9.97e-05 |
|
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: 44.88 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 180 LWHISGFSwLFIySITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDL 259
Cdd:cd18566 4 LPQVLLAS-LFI-NILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 260 FHGLVKQDVAFYDAHKTGEVTSRLaADCQTMSDTV---ALNVNVFLRNCVMLLGSMIFmmkLSWRLSLVTFILVPIIFVA 336
Cdd:cd18566 82 FEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLtgqALLALLDLPFVLIFLGLIWY---LGGKLVLVPLVLLGLFVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 337 SKIFGTYY-DLLSERTQDTiAESNDVAEEVLSTMRTVRSFSCENVEADRF----YGKLTHTLDVTRTKAIAYIGflwvSE 411
Cdd:cd18566 158 AILLGPILrRALKERSRAD-ERRQNFLIETLTGIHTIKAMAMEPQMLRRYerlqANAAYAGFKVAKINAVAQTL----GQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992290 412 LFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLmQSVGASRK 472
Cdd:cd18566 233 LFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRF-QQVRVAVR 292
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
190-456 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 190 FIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVA 269
Cdd:cd18783 12 LILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPID 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 270 FYDAHKTGEVTSRLAadcQTMSDTVALNVNVF--LRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLL 347
Cdd:cd18783 92 FFERTPAGVLTKHMQ---QIERIRQFLTGQLFgtLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 348 SERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTldVTRTKAIAYIGfLWVSEL---FQSFIIVSVLWY 424
Cdd:cd18783 169 LQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARA--IRARFAVGRLS-NWPQTLtgpLEKLMTVGVIWV 245
|
250 260 270
....*....|....*....|....*....|..
gi 71992290 425 GGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQM 456
Cdd:cd18783 246 GAYLVFAGSLTVGALIAFNMLAGRVAGPLVQL 277
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
634-704 |
1.00e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 1.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992290 634 TQMSGGQKQRIAIAraLV-----REPA-ILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIV 704
Cdd:pfam02463 1076 DLLSGGEKTLVALA--LIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
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| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
636-704 |
1.34e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71992290 636 MSGGQKQRIAIARAL---VREPAILLLDEATSALDTESE----HLVQEAIYKnldGKSVILIAHRLSTVEKADKIV 704
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIkaliYVLQSLTHQ---GHTVVIIEHNMHVVKVADYVL 882
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| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
629-709 |
3.93e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992290 629 VGEKGTQMSGGQKQRIAIARALV---REPAILLLDEATSALDTESEHLVQEaIYKNL--DGKSVILIAHRLSTVEKADKI 703
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLV-QLRTLvsLGHSVIYIDHDPALLKQADYL 1771
|
....*.
gi 71992290 704 VVINKG 709
Cdd:PRK00635 1772 IEMGPG 1777
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