|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
44-675 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 641.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 44 FDSVLDLWAACLYRSCLLLGATIGVAKNSAlgpRRLRASWL-VITLVCLFVGIYAMVKLLLFSEVRRPI--RDPWFWALF 120
Cdd:TIGR00958 35 EKGLYVLWLEGTLRLGVLWLGALGILLNKA---GGLLAAVKpLVAALCLATPSLSSLRALAFWEALDPAvrVALGLWSWF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 121 VWTYISLGASFLLWWLLSTvrPGTQALEPgaateaegfpgsgrpPPEQAS-GATLQKLLSYTKPDVAFLVAASFFLIVAA 199
Cdd:TIGR00958 112 VWSYGAALPAAALWAVLSS--AGASEKEA---------------EQGQSEtADLLFRLLGLSGRDWPWLISAFVFLTLSS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 200 LGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDE 279
Cdd:TIGR00958 175 LGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 280 NRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQN 359
Cdd:TIGR00958 255 NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 360 ALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQ 439
Cdd:TIGR00958 335 AVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 440 MTSGNLIAFIIYEFVLGD-------------------------------------------------------------- 457
Cdd:TIGR00958 415 VSSGNLVSFLLYQEQLGEavrvlsyvysgmmqavgasekvfeyldrkpnipltgtlaplnlegliefqdvsfsypnrpdv 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 458 -CMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDN 536
Cdd:TIGR00958 495 pVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVREN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 616
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 617 LIQQAIhgNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 675
Cdd:TIGR00958 655 LLQESR--SRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
169-681 |
2.18e-179 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 523.57 E-value: 2.18e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 169 ASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGG 248
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 249 IFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQL 328
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 329 SLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAA 408
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 409 YMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY------------------------------------- 451
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYllrlfgplrqlanvlnqlqralasaerifelldeppe 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 452 -----------------EF------------VLgdcmENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL 502
Cdd:COG1132 324 ipdppgavplppvrgeiEFenvsfsypgdrpVL----KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 503 DGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSG 582
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 583 GQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQ 662
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|....*....
gi 339895785 663 QLLAQGGLYAKLVQRQMLG 681
Cdd:COG1132 560 ELLARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
191-483 |
1.61e-172 |
|
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: 494.52 E-value: 1.61e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 339895785 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMENVSFslspgKVTALVGPSGSGKS 483
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGS-----VYTGLMQAVGAAEK 288
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
174-679 |
1.94e-134 |
|
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: 412.31 E-value: 1.94e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 174 LQKLLSYTKPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLI 253
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLAL---ATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 254 FARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 334 MGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV 413
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 414 WGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY----------------EFV--------LGDCME--------- 460
Cdd:COG2274 383 TLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILsgrflapvaqligllqRFQdakialerLDDILDlppereegr 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 ------------------------------NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAY 510
Cdd:COG2274 463 sklslprlkgdielenvsfrypgdsppvldNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 511 DHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAM 590
Cdd:COG2274 543 DPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAI 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 591 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGL 670
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGL 702
|
....*....
gi 339895785 671 YAKLVQRQM 679
Cdd:COG2274 703 YAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
174-678 |
1.22e-127 |
|
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: 390.60 E-value: 1.22e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 174 LQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLI 253
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 254 FARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:TIGR02204 86 GERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 334 MGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV 413
Cdd:TIGR02204 166 LAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 414 WGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEF-----------VLGDC------------------------ 458
Cdd:TIGR02204 246 AIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVmvagsigtlseVWGELqraagaaerliellqaepdikapa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 --------------MENVSF---------SLS-------PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS 508
Cdd:TIGR02204 326 hpktlpvplrgeieFEQVNFayparpdqpALDglnltvrPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 509 AYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRV 588
Cdd:TIGR02204 406 QLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 589 AMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQG 668
Cdd:TIGR02204 486 AIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG 565
|
570
....*....|
gi 339895785 669 GLYAKLVQRQ 678
Cdd:TIGR02204 566 GLYARLARLQ 575
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
459-655 |
1.23e-125 |
|
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: 372.19 E-value: 1.23e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNIS 538
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:cd03248 110 YGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 339895785 619 QQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 655
Cdd:cd03248 190 QQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
191-467 |
2.01e-119 |
|
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: 358.78 E-value: 2.01e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 339895785 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMENVSFSLS 467
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFS 277
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
173-674 |
2.72e-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: 360.96 E-value: 2.72e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 173 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQfstaVVIVCLLAIGSSFAAGIRGGIFTL 252
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSV----LWWVPLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 253 IFARLNIR----LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQL 328
Cdd:TIGR02203 77 LLSWVSNKvvrdIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 329 SLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAA 408
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 409 YMYYvwgSGLTLLVVQVS---ILYYGGHLVISGQMTSGNLIAFI-----------------------------IYEF--- 453
Cdd:TIGR02203 237 GSIS---SPITQLIASLAlavVLFIALFQAQAGSLTAGDFTAFItamialirplksltnvnapmqrglaaaesLFTLlds 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 454 -------------VLGD----------------CMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG 504
Cdd:TIGR02203 314 ppekdtgtraierARGDvefrnvtfrypgrdrpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 505 KPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGG 583
Cdd:TIGR02203 394 HDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 584 QKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQ 663
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNE 553
|
570
....*....|.
gi 339895785 664 LLAQGGLYAKL 674
Cdd:TIGR02203 554 LLARNGLYAQL 564
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
461-678 |
3.11e-108 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 327.96 E-value: 3.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYG 540
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQ 620
Cdd:cd03249 101 KPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 621 AIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 678
Cdd:cd03249 181 ALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
459-674 |
1.75e-96 |
|
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: 297.61 E-value: 1.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNIS 538
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:cd03251 98 YGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 619 QQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 674
Cdd:cd03251 178 QAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
173-678 |
2.74e-96 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 308.87 E-value: 2.74e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 173 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDgiviqksmDQFSTA----VVIVCLLAIGSSFAAGIRGG 248
Cdd:PRK11176 12 TFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLD--------DGFGKAdrsvLKWMPLVVIGLMILRGITSF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 249 IFTLIFA------RLNIRLRncLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMF 322
Cdd:PRK11176 84 ISSYCISwvsgkvVMTMRRR--LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 323 SLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrKLQQVYKLN 402
Cdd:PRK11176 162 YYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK----RFDKVSNRM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 403 RKEAaayMYYVWGSGLTLLVVQ-------VSILYYGGHLVISGQMTSG-------NLIA--------------------- 447
Cdd:PRK11176 238 RQQG---MKMVSASSISDPIIQliaslalAFVLYAASFPSVMDTLTAGtitvvfsSMIAlmrplksltnvnaqfqrgmaa 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 448 ----FIIY-------------EFVLGD----------------CMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP 494
Cdd:PRK11176 315 cqtlFAILdleqekdegkrviERAKGDiefrnvtftypgkevpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 495 LEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTET 573
Cdd:PRK11176 395 IDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 574 GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH-TVLIIAHRLSTVEHAHLIVVLDK 652
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALD-ELQKNrTSLVIAHRLSTIEKADEILVVED 553
|
570 580
....*....|....*....|....*.
gi 339895785 653 GRVVQQGTHQQLLAQGGLYAKLVQRQ 678
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
191-479 |
8.97e-94 |
|
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: 292.32 E-value: 8.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 339895785 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMENVSFSLSPgkVTALVGPSG 479
Cdd:cd18590 241 GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGD--MLSNVGAAA 287
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
159-678 |
8.34e-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: 300.58 E-value: 8.34e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 159 PGSGRPPPEQASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLA-- 236
Cdd:COG5265 6 AMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAyg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 237 ---IGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDL---ISRLTSDT-TMVSDLVSQNINVFLR 309
Cdd:COG5265 86 llrLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIERGTKGIeFLLRFLLFNILPTLLE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 310 nTVKVTGVVVFMFSlsWQLSLVTFmgfpiIMMVSNIYgkyYKRLSKEVQNALARASNTAEeTISAMK---------TVRS 380
Cdd:COG5265 166 -IALVAGILLVKYD--WWFALITL-----VTVVLYIA---FTVVVTEWRTKFRREMNEAD-SEANTRavdsllnyeTVKY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 381 FANEEEEAEVYLRKLQqvyklnRKEAAAYMyyVWGSGLTLLVVQ--------VSILYYGGHLVISGQMTSG--------- 443
Cdd:COG5265 234 FGNEAREARRYDEALA------RYERAAVK--SQTSLALLNFGQaliialglTAMMLMAAQGVVAGTMTVGdfvlvnayl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 444 -------NLIAFIIYE-----------FVLGD---------------------CMENVSFS----------LS----PGK 470
Cdd:COG5265 306 iqlyiplNFLGFVYREirqaladmermFDLLDqppevadapdapplvvgggevRFENVSFGydperpilkgVSfevpAGK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 471 VTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVV 550
Cdd:COG5265 386 TVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 551 EAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHT 630
Cdd:COG5265 466 AAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRT 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 339895785 631 VLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 678
Cdd:COG5265 546 TLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
461-678 |
4.15e-89 |
|
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: 278.34 E-value: 4.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYG 540
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQ 620
Cdd:cd03253 99 RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 621 AIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 678
Cdd:cd03253 179 ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
461-669 |
4.91e-88 |
|
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: 275.26 E-value: 4.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYG 540
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQ 620
Cdd:cd03254 101 RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 339895785 621 AIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGG 669
Cdd:cd03254 181 ALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
457-678 |
3.17e-87 |
|
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: 273.59 E-value: 3.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 457 DCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDN 536
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 616
Cdd:cd03252 96 IALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEH 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 617 LIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 678
Cdd:cd03252 176 AIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
191-467 |
5.19e-87 |
|
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: 274.82 E-value: 5.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 339895785 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMENVSFSLS 467
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLA 277
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
414-669 |
9.86e-82 |
|
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: 270.09 E-value: 9.86e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 414 WGSGLTLLVVQVSILYYGGHLVISGqmtsgnliafiiyefvlgdcmenVSFSLSPGKVTALVGPSGSGKSSCVNILENFY 493
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGGRPALDG-----------------------LSLTIPPGERVALVGPSGAGKSTLLNLLLGFL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 494 PLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTET 573
Cdd:COG4988 388 PPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 574 GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKG 653
Cdd:COG4988 468 GEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDG 547
|
250
....*....|....*.
gi 339895785 654 RVVQQGTHQQLLAQGG 669
Cdd:COG4988 548 RIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
193-478 |
3.38e-81 |
|
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: 259.71 E-value: 3.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 193 FFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQ 272
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 273 ETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKR 352
Cdd:cd18589 83 EIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 353 LSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGG 432
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 339895785 433 HLVISGQMTSGNLIAFIIYEFVLGDCMEnVSFSLSPgKVTALVGPS 478
Cdd:cd18589 243 QLVTAGTVSSGDLVTFVLYELQFTSAVE-VLLSYYP-SVMKAVGSS 286
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
173-687 |
5.64e-78 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 260.81 E-value: 5.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 173 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMdqfstAVVIVCLLA---IGSSFAAGIRGGI 249
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNL-----PLGLVAGLAaayVGLQLLAAGLHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 250 FTLIFARLNI----RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLS 325
Cdd:PRK10790 85 QSLLFNRAAVgvvqQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 326 WQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrKLQQVyklNRKE 405
Cdd:PRK10790 165 WRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGE----RMGEA---SRSH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 406 AAAYMYYVWGSGLTL--LVVQVSILYYGGHLVI-----SGQMTSGNLIAFIIYE-------------------------- 452
Cdd:PRK10790 238 YMARMQTLRLDGFLLrpLLSLFSALILCGLLMLfgfsaSGTIEVGVLYAFISYLgrlneplielttqqsmlqqavvager 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 453 -FVLGDC------------------MENVSFSLSPGKVT--------------ALVGPSGSGKSSCVNILENFYPLEGGR 499
Cdd:PRK10790 318 vFELMDGprqqygnddrplqsgridIDNVSFAYRDDNLVlqninlsvpsrgfvALVGHTGSGKSTLASLLMGYYPLTEGE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 500 VLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPtVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQ 579
Cdd:PRK10790 398 IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 580 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 659
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
|
570 580
....*....|....*....|....*...
gi 339895785 660 THQQLLAQGGLYAKLVQRQMLGLQPAAD 687
Cdd:PRK10790 557 THQQLLAAQGRYWQMYQLQLAGEELAAS 584
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
146-676 |
3.74e-75 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 256.02 E-value: 3.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 146 ALEPGaateaEGFPGSGRPPPEQASgatLQKLLSYTKPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQF 225
Cdd:TIGR03796 125 TFEPG-----PEFQKGGRKPSLLRA---LWRRLRGSRGALLYLLLAGLLLVLPGL---VIPAFSQIFVDEILVQGRQDWL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 226 STAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTmVSDLVSQNIN 305
Cdd:TIGR03796 194 RPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNDQ-VAEFLSGQLA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 306 VFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEE 385
Cdd:TIGR03796 273 TTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLES 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 386 EE----AEVYLRKLQQVYKLNRKEAaayMYYVWGSGLTLLVVqVSILYYGGHLVISGQMTSGNLIAF--IIYEFV----- 454
Cdd:TIGR03796 353 DFfsrwAGYQAKLLNAQQELGVLTQ---ILGVLPTLLTSLNS-ALILVVGGLRVMEGQLTIGMLVAFqsLMSSFLepvnn 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 455 -----------------LGDCM---------------------------------------------ENVSFSLSPGKVT 472
Cdd:TIGR03796 429 lvgfggtlqelegdlnrLDDVLrnpvdplleepegsaatsepprrlsgyvelrnitfgyspleppliENFSLTLQPGQRV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 473 ALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEA 552
Cdd:TIGR03796 509 ALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRA 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 553 AQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQaihgNLQKH--T 630
Cdd:TIGR03796 589 CKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDD----NLRRRgcT 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 339895785 631 VLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQ 676
Cdd:TIGR03796 665 CIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
260-677 |
8.40e-74 |
|
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: 248.91 E-value: 8.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDttmVSDLVsqniNVFLR-------NTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVAD---VDALD----NLYLRvllpllvALLVILAAVAFLAFFSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 333 FMGF-------PIIMMVSNiygkyyKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKE 405
Cdd:COG4987 162 ALGLllaglllPLLAARLG------RRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 406 AAAYMyyvWGSGLTLLVVQ---VSILYYGGHLVISGQMtSGNLIAFiiyeFVLG-------------------------- 456
Cdd:COG4987 236 ARLSA---LAQALLQLAAGlavVAVLWLAAPLVAAGAL-SGPLLAL----LVLAalalfealaplpaaaqhlgrvraaar 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 457 -----------------------------------------DCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPL 495
Cdd:COG4987 308 rlnelldappavtepaepapapggpsleledvsfrypgagrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 496 EGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGE 575
Cdd:COG4987 388 QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 576 KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 655
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
490 500
....*....|....*....|..
gi 339895785 656 VQQGTHQQLLAQGGLYAKLVQR 677
Cdd:COG4987 548 VEQGTHEELLAQNGRYRQLYQR 569
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
178-680 |
8.95e-74 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 249.49 E-value: 8.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 178 LSYTKPD---VAFLVAASFFLIVAALGEtflPYYTGRAIDgiVIQKSMDQFSTAVVIVCLlaigssfaagirgGIFTLIF 254
Cdd:PRK13657 11 LQYLGAEkrlGILLAVANVLLAAATFAE---PILFGRIID--AISGKGDIFPLLAAWAGF-------------GLFNIIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 255 A--------RLNIRLRNCL----FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVsqnINVFLRNTVKVTGVVVFM- 321
Cdd:PRK13657 73 GvlvarhadRLAHRRRLAVlteyFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLW---LEFMREHLATLVALVVLLp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 322 --FSLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQNAL--------ARASntaeETISAMKTVRSFANEEEEAEVy 391
Cdd:PRK13657 150 laLFMNWRLSLVLV----VLGIVYTLITTLVMRKTKDGQAAVeehyhdlfAHVS----DAIGNVSVVQSYNRIEAETQA- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 392 LRKLqqvykLNRKEAAAYMYYVW---GSGLTLL---VVQVSILYYGGHLVISGQMTSGNLIAFI---------------- 449
Cdd:PRK13657 221 LRDI-----ADNLLAAQMPVLSWwalASVLNRAastITMLAILVLGAALVQKGQLRVGEVVAFVgfatlligrldqvvaf 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 450 ----------IYEF---------------------VLGDC---------------MENVSFSLSPGKVTALVGPSGSGKS 483
Cdd:PRK13657 296 inqvfmaapkLEEFfevedavpdvrdppgaidlgrVKGAVefddvsfsydnsrqgVEDVSFEAKPGQTVAIVGPTGAGKS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 484 SCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIM 563
Cdd:PRK13657 376 TLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 564 ELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH 643
Cdd:PRK13657 456 RKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN 535
|
570 580 590
....*....|....*....|....*....|....*..
gi 339895785 644 AHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQML 680
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGM 572
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
191-456 |
1.05e-73 |
|
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: 240.23 E-value: 1.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQ------KSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNC 264
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHsgsggeEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 265 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYvwgSGLTLLVVQ 424
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGF---NGFMGAAAQ 237
|
250 260 270
....*....|....*....|....*....|....*
gi 339895785 425 VSI---LYYGGHLVISGQMTSGNLIAFIIYEFVLG 456
Cdd:cd18780 238 LAIvlvLWYGGRLVIDGELTTGLLTSFLLYTLTVA 272
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
460-654 |
7.99e-71 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 228.04 E-value: 7.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNIsy 539
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 glptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQ 619
Cdd:cd03228 97 ----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....*
gi 339895785 620 QAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGR 654
Cdd:cd03228 137 EALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
191-463 |
1.78e-68 |
|
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: 226.24 E-value: 1.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 191 ASFFLIVAALGETFLPYYTGRAID------GIVIQKSMDQFSTAVVIVCLLAIGSsFAAGIRGGIFTLIFARLNIRLRNC 264
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDvaskesGDIEIFGLSLKTFALALLGVFVVGA-AANFGRVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 265 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQ 424
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSL 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 339895785 425 VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMENVS 463
Cdd:cd18573 240 LSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLS 278
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
193-699 |
2.26e-66 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 229.21 E-value: 2.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 193 FFLIVAALGETFLPYYTGRAIDGIviqkSMDQFSTAVVIVCL--LAIGSSFAAGIRGGIFTLIFA---RLNIRLRNCLFR 267
Cdd:PRK10789 2 ALLIIIAMLQLIPPKVVGIIVDGV----TEQHMTTGQILMWIgtMVLIAVVVYLLRYVWRVLLFGasyQLAVELREDFYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFS-LSWQLSLVTFMGFPIIMMVSNIY 346
Cdd:PRK10789 78 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 347 GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANE-------EEEAEVYLRKLQQVYKLN-RKEAAAYMyyvwGSGL 418
Cdd:PRK10789 158 GDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEdrqsalfAADAEDTGKKNMRVARIDaRFDPTIYI----AIGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 419 T-LLVVQvsilyYGGHLVISGQMTSGNLIAFIIY---------------------------------------------- 451
Cdd:PRK10789 234 AnLLAIG-----GGSWMVVNGSLTLGQLTSFVMYlglmiwpmlalawmfnivergsaaysriramlaeapvvkdgsepvp 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 452 -----------EF----VLGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLH 516
Cdd:PRK10789 309 egrgeldvnirQFtypqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 517 RVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVR 596
Cdd:PRK10789 389 SRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 597 NPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQ 676
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
570 580
....*....|....*....|...
gi 339895785 677 RQMlgLQPAADFTAGHNEPVANG 699
Cdd:PRK10789 549 YQQ--LEAALDDAPEIREEAVDA 569
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
189-675 |
4.89e-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: 223.08 E-value: 4.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 189 VAASFFLIVAALGEtflpYYTGRAIDGIVIQKSMDQFStaVVIVCLLA--IGSSFAAGIRGGIFTLIFARLNIRLRNCLF 266
Cdd:TIGR01193 163 IAAIIVTLISIAGS----YYLQKIIDTYIPHKMMGTLG--IISIGLIIayIIQQILSYIQIFLLNVLGQRLSIDIILSYI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 267 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTgVVVFMFSLSWQLSLVTFMGFPIIMMVSNIY 346
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVI-VGLFLVRQNMLLFLLSLLSIPVYAVIIILF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 347 GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE-------EAEVYLRKlqqVYKLNRKEAAAYMYYVwgsgLT 419
Cdd:TIGR01193 316 KRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAEryskidsEFGDYLNK---SFKYQKADQGQQAIKA----VT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 420 LLVVQVSILYYGGHLVISGQMTSGNLIAF--------------------------------------------------- 448
Cdd:TIGR01193 389 KLILNVVILWTGAYLVMRGKLTLGQLITFnallsyfltpleniinlqpklqaarvannrlnevylvdsefinkkkrteln 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 449 ----------IIYEFVLGD-CMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR 517
Cdd:TIGR01193 469 nlngdivindVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 518 VISLVSQEPVLFARSITDNISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVR 596
Cdd:TIGR01193 549 FINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 597 NPPVLILDEATSALDAESEYLIQQAIHgNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 675
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
191-456 |
1.11e-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: 200.02 E-value: 1.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFST-AVVIVCLLAIGSSFAAgIRGGIFTLIFARLNIRLRNCLFRSL 269
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQiALLLLGLFLLQAVFSF-FRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 270 VSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKY 349
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 350 YKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILY 429
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLW 239
|
250 260
....*....|....*....|....*..
gi 339895785 430 YGGHLVISGQMTSGNLIAFIIYEFVLG 456
Cdd:cd18576 240 YGGRLVLAGELTAGDLVAFLLYTLFIA 266
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
188-451 |
1.44e-58 |
|
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: 199.70 E-value: 1.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeAAAYMYYVWG-SGLTLLVVQVS 426
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR-AARLSALFSPlIGLLTALGTAL 239
|
250 260
....*....|....*....|....*
gi 339895785 427 ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAY 264
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
461-678 |
5.22e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 201.23 E-value: 5.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYG 540
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQ 620
Cdd:PRK11174 447 NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 621 AIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 678
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
188-455 |
9.04e-56 |
|
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: 191.70 E-value: 9.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIG--SSFAAGIRGGIFTLIFARLNIRLRNCL 265
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGlaQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 266 FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNI 345
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 346 YGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQV 425
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|
gi 339895785 426 SILYYGGHLVISGQMTSGNLIAFIIYEFVL 455
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQL 270
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
188-450 |
1.91e-55 |
|
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: 191.10 E-value: 1.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDqfstAVVIVCLLAIGSSFAAGI--RGGIFTLIFARLNI--RLRN 263
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLE----ALLLVPLAIIGLFLLRGLasYLQTYLMAYVGQRVvrDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAymyyvwgSGLTLLVV 423
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARA-------RALSSPLM 229
|
250 260 270
....*....|....*....|....*....|....
gi 339895785 424 QV-------SILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18552 230 ELlgaiaiaLVLWYGGYQVISGELTPGEFISFIT 263
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
461-667 |
2.15e-55 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 198.82 E-value: 2.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyG 540
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA-R 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQ 620
Cdd:COG4618 429 FGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 339895785 621 AIhGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG4618 509 AI-RALKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
460-659 |
3.28e-55 |
|
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: 188.18 E-value: 3.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISY 539
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 GLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQ 619
Cdd:cd03245 101 GAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 339895785 620 QAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 659
Cdd:cd03245 181 ERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
460-660 |
1.25e-54 |
|
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: 186.55 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISy 539
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 glptvPF-----EMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:cd03244 100 -----PFgeysdEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 339895785 615 EYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 660
Cdd:cd03244 175 DALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
181-650 |
2.65e-54 |
|
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: 195.20 E-value: 2.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 181 TKPDVAFLVAASFFLIVAALGETFLpyyTGRAIDGIVIQKS-MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNI 259
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWL---LARVVDGLISAGEpLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQ---LSLVTFMGF 336
Cdd:TIGR02857 78 QLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWIsglILLLTAPLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 337 PIIMMVSniyGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEA---------------------------- 388
Cdd:TIGR02857 158 PIFMILI---GWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAaairrsseeyrertmrvlriaflssavl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 389 -------------------------------------EVY--LRKLQQVY--KLNRKEAAAYMYYV-------------- 413
Cdd:TIGR02857 235 elfatlsvalvavyigfrllagdldlatglfvlllapEFYlpLRQLGAQYhaRADGVAAAEALFAVldaaprplagkapv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 414 -WGSGLTLLVVQVSILYYGGHLVISgqmtsgnliafiiyefvlgdcmeNVSFSLSPGKVTALVGPSGSGKSSCVNILENF 492
Cdd:TIGR02857 315 tAAPASSLEFSGVSVAYPGRRPALR-----------------------PVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 493 YPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTE 572
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTP 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 573 TGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVL 650
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
139-679 |
1.57e-53 |
|
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: 195.95 E-value: 1.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 139 TVRPGTQALEPGAATEAEGFPgsgRPPPEQASGAT--LQKLLSYTKPDVAFLVAASffLIVAALGeTFLPYYTGRAIDGI 216
Cdd:TIGR03797 93 TRRRVDAAMAATLAPEAYMFY---RPLPDKALGLRdlLRFALRGARRDLLAILAMG--LLGTLLG-MLVPIATGILIGTA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 217 VIQKSMDQfstaVVIVCLLAIGSSFAAGIrggiFTLIFARLNIRLRN--------CLFRSLVSQETSFFDENRTGDLISR 288
Cdd:TIGR03797 167 IPDADRSL----LVQIALALLAAAVGAAA----FQLAQSLAVLRLETrmdaslqaAVWDRLLRLPVSFFRQYSTGDLASR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 289 LTSDTTMVSDLVSQNINVFLRNTVKVTGVVVfMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTA 368
Cdd:TIGR03797 239 AMGISQIRRILSGSTLTTLLSGIFALLNLGL-MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 369 EETIS-------AMKTVRSFAneeEEAEVYLRKLQQVYKLNRkeaaaymyyvWGSGLT-----LLVVQVSILYY-GGHLV 435
Cdd:TIGR03797 318 VQLINgisklrvAGAENRAFA---RWAKLFSRQRKLELSAQR----------IENLLTvfnavLPVLTSAALFAaAISLL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 436 ISGQMTSGNLIAF-------------------------IIYE--------------------------------FVLGD- 457
Cdd:TIGR03797 385 GGAGLSLGSFLAFntafgsfsgavtqlsntlisilaviPLWErakpilealpevdeaktdpgklsgaievdrvtFRYRPd 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 458 ---CMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSIT 534
Cdd:TIGR03797 465 gplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIF 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGLPTVPfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:TIGR03797 545 ENIAGGAPLTL-DEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT 623
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 615 EYLIQQAIHGnlQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQM 679
Cdd:TIGR03797 624 QAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQL 686
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
188-467 |
6.07e-52 |
|
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: 181.86 E-value: 6.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSI 427
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 339895785 428 LYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMENVSFSLS 467
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLIN 280
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
191-463 |
1.83e-49 |
|
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: 174.98 E-value: 1.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYmyyvwgSGLTLLVVQ------ 424
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRAR------ALLTALVIFlvfgai 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 339895785 425 VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMENVS 463
Cdd:cd18575 235 VFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALS 273
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
188-451 |
2.05e-47 |
|
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: 169.51 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQK-SMDQFSTAVVIVCLLAIGSsfaAGIR-GGIFTLIFARLNI--RLRN 263
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLI---GIFRfLWRYLIFGASRRIeyDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaayMYYVWG-------- 415
Cdd:cd18541 158 YRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR-----LARVDAlffpligl 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 339895785 416 -SGLTLLVVqvsiLYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18541 233 lIGLSFLIV----LWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
460-678 |
1.34e-46 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 174.24 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISY 539
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 GLPTVPFEMVVEAAQKANAHGFImELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQ 619
Cdd:PRK11160 437 AAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 620 QAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 678
Cdd:PRK11160 516 ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
421-667 |
3.73e-45 |
|
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: 169.84 E-value: 3.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 421 LVVQVSILYYGGHLVISGQMTSGNLIA-FIIYEFVLG------------------------------------------- 456
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAgSILVGRALApidgaiggwkqfsgarqaykrlnellanypsrdpamplpepeg 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 457 ----------------DCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 520
Cdd:TIGR01842 316 hlsvenvtivppggkkPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIG 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 521 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 600
Cdd:TIGR01842 396 YLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKL 475
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 601 LILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIkALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
188-451 |
4.77e-45 |
|
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: 162.94 E-value: 4.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDqfSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARL--NI--RLRN 263
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGD--LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLgqRIiyDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18544 79 DLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEaaAYMYYVWGSGLTLL-- 421
Cdd:cd18544 159 YLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKS--IKLFALFRPLVELLss 236
|
250 260 270
....*....|....*....|....*....|
gi 339895785 422 VVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18544 237 LALALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
188-453 |
5.30e-45 |
|
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: 162.60 E-value: 5.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMdqfSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSS---GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAaymYYVWGSGLTLLVVQVS- 426
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAK---IEALIGPLMGLAVQLAl 234
|
250 260
....*....|....*....|....*....
gi 339895785 427 --ILYYGGHLVISGQMTSGNLIAFIIYEF 453
Cdd:cd18551 235 lvVLGVGGARVASGALTVGTLVAFLLYLF 263
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
188-447 |
2.73e-43 |
|
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: 158.02 E-value: 2.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIV----IQKSMDQFSTAVVIVCL----LAIGSSFAAGIRGGIFTLIFARLNI 259
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsGESSPDEFLDDVNKYALyfvyLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 339
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 340 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMyyvWGSGLT 419
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSG---LGLGLL 237
|
250 260 270
....*....|....*....|....*....|.
gi 339895785 420 LLVVQVSI---LYYGGHLVISGQMTSGNLIA 447
Cdd:cd18577 238 FFIIFAMYalaFWYGSRLVRDGEISPGDVLT 268
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
178-455 |
9.93e-43 |
|
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: 157.23 E-value: 9.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 178 LSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVV---IVCLLAIGSSFAAGIRGGIFTLIF 254
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFwalMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 255 ARLNIRLRNCLFRSLVSQETSFFD--ENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMyy 412
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISG-- 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 339895785 413 vWGSGLT---LLVVQVSILYYGGHLVISGQMTSGNLiaFIIYEFVL 455
Cdd:cd18578 239 -LGFGLSqslTFFAYALAFWYGGRLVANGEYTFEQF--FIVFMALI 281
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
256-450 |
1.16e-42 |
|
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: 156.17 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 256 RLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDttmVSDLVS---QNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSsfkQCVSQGLRSVTQTVGCVVSLYLISPKLTLLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYY 412
Cdd:cd18574 149 LVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIF 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895785 413 VWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18574 229 QGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
460-676 |
1.55e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 166.36 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE------------------------------------------- 496
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 497 -----------GGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMEL 565
Cdd:PTZ00265 1265 gsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 566 QDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK--HTVLIIAHRLSTVEH 643
Cdd:PTZ00265 1345 PNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIITIAHRIASIKR 1424
|
250 260 270
....*....|....*....|....*....|....*....
gi 339895785 644 AHLIVVLDK----GRVVQ-QGTHQQLL-AQGGLYAKLVQ 676
Cdd:PTZ00265 1425 SDKIVVFNNpdrtGSFVQaHGTHEELLsVQDGVYKKYVK 1463
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
188-451 |
7.38e-42 |
|
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: 153.78 E-value: 7.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeAAAYMYYVWGS-GLTLLVVQVS 426
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMR-AVRLNALFWPLvELISALGTAL 240
|
250 260
....*....|....*....|....*
gi 339895785 427 ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGY 265
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
460-636 |
1.18e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 150.74 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRViSLVSQEPVLFARSITDNIS 538
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQV-AYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YglptvPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:COG4619 96 F-----PFQLRERKFDRERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRR 168
|
170 180
....*....|....*....|.
gi 339895785 618 IQQAIHGNLQKH--TVLIIAH 636
Cdd:COG4619 169 VEELLREYLAEEgrAVLWVSH 189
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
460-655 |
1.71e-41 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 148.90 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNIsy 539
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 glptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQ 619
Cdd:cd03246 97 ----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 339895785 620 QAI-HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 655
Cdd:cd03246 137 QAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
189-451 |
3.89e-41 |
|
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: 151.89 E-value: 3.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 189 VAASFFLIVAAlgeTFL----PYYTGRAIDGIVIQKSMDQFSTAVVIVCL----LAIGSSFAAGIRGGIFTLIFARLNIR 260
Cdd:cd18563 1 LILGFLLMLLG---TALglvpPYLTKILIDDVLIQLGPGGNTSLLLLLVLglagAYVLSALLGILRGRLLARLGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 261 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaAAYMYYVWGSGLTL 420
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR--AEKLWATFFPLLTF 235
|
250 260 270
....*....|....*....|....*....|...
gi 339895785 421 LVV--QVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18563 236 LTSlgTLIVWYFGGRQVLSGTMTLGTLVAFLSY 268
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
460-667 |
4.09e-41 |
|
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: 149.79 E-value: 4.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPV--LFARSITDNI 537
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDdqLFAPTVEEDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGlPT---VPFEMVVEAAQKA-NAHGfIMELQDgYSTetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:COG1122 98 AFG-PEnlgLPREEIRERVEEAlELVG-LEHLAD-RPP------HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 614 SEYLIQQAIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG1122 169 GRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
226-638 |
4.23e-40 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 154.83 E-value: 4.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 226 STAVVIVCLLAIGSSFAAGI-RGGIFTLIFARLNiRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 304
Cdd:TIGR02868 53 SVAAVAVRAFGIGRAVFRYLeRLVGHDAALRSLG-ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 305 NVFLRNTVKVTGVVVFMFSLSWQLSLVT--------FMGFPIIMMVSNIYGKYYKRLSKEVQNALARA-SNTAEETIS-A 374
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALILaaglllagFVAPLVSLRAARAAEQALARLRGELAAQLTDAlDGAAELVASgA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 375 MKTVRSfanEEEEAEVYLRKLQQvyklNRKEAAAymyyvWGSGLTLLVVQVSI---LYYGGHLVISGQMTSGNLIAFI-- 449
Cdd:TIGR02868 212 LPAALA---QVEEADRELTRAER----RAAAATA-----LGAALTLLAAGLAVlgaLWAGGPAVADGRLAPVTLAVLVll 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 450 ---------------------------IYEfVLGD------------------------------------CMENVSFSL 466
Cdd:TIGR02868 280 plaafeafaalpaaaqqltrvraaaerIVE-VLDAagpvaegsapaagavglgkptlelrdlsagypgappVLDGVSLDL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 467 SPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPF 546
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 547 EMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNL 626
Cdd:TIGR02868 439 EELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
|
490
....*....|..
gi 339895785 627 QKHTVLIIAHRL 638
Cdd:TIGR02868 519 SGRTVVLITHHL 530
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
458-654 |
1.78e-39 |
|
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: 144.15 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 458 CMENVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgrvlldgkpisaydHKYLHRVISLVSQEPVLFARSITDN 536
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSG--------------SVSVPGSIAYVSQEPWIQNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLPTVP--FEMVVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:cd03250 86 ILFGKPFDEerYEKVIKACAlEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 339895785 614 -SEYLIQQAIHGNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGR 654
Cdd:cd03250 162 vGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
460-667 |
2.36e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 145.21 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvISLVSQEPVLFAR-SITDNIS 538
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 -----YGLPTVPFEMVVEAAQKAnahgfiMELQDgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:COG1131 96 ffarlYGLPRKEARERIDELLEL------FGLTD----AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 614 SEYLIQQAIHG-NLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG1131 166 ARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
459-660 |
3.56e-39 |
|
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: 143.71 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNIS 538
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 yglptvPFEMVVEAAqkanahgfIMElqdgySTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:cd03369 104 ------PFDEYSDEE--------IYG-----ALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 339895785 619 QQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 660
Cdd:cd03369 165 QKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
460-608 |
9.62e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 140.48 E-value: 9.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFAR-SITDNIS 538
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 539 YGLptvPFEMVVEAAQKANAHGFI--MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:pfam00005 82 LGL---LLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
460-667 |
1.61e-38 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.05 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH---KYLHRVISLVSQEPV--LFAR-SI 533
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYssLNPRmTV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:COG1123 362 GDIIAEPL------RLHGLLSRAERRERVAELLErvGLPPDLADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339895785 611 DaeseYLIQQAIHG---NLQK---HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG1123 436 D----VSVQAQILNllrDLQRelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
460-658 |
2.35e-38 |
|
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: 141.84 E-value: 2.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkyLHRVISLVSQEPVLFA-RSITDNIS 538
Cdd:cd03293 21 EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDRGYVFQQDALLPwLTVLDNVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLptvpfEM--VVEAAQKANAHGFImelqdgysTETGEKGA------QLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:cd03293 96 LGL-----ELqgVPKAEARERAEELL--------ELVGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 611 DAESEYLIQQAIHGNLQKH--TVLIIAHRLStvEHAHL---IVVLDK--GRVVQQ 658
Cdd:cd03293 163 DALTREQLQEELLDIWRETgkTVLLVTHDID--EAVFLadrVVVLSArpGRIVAE 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
460-650 |
2.59e-38 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 153.65 E-value: 2.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNIS 538
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGL---------------------------------------------------------PTVPFEMVVEAAQKANAHGF 561
Cdd:PTZ00265 482 YSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyQTIKDSEVVDVSKKVLIHDF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 562 IMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIH---GNLQKHTVlIIAHRL 638
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkGNENRITI-IIAHRL 640
|
250
....*....|..
gi 339895785 639 STVEHAHLIVVL 650
Cdd:PTZ00265 641 STIRYANTIFVL 652
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
188-451 |
2.64e-38 |
|
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: 144.08 E-value: 2.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIV------IQKSMDQFSTAVVIVCLLAIGSSfaagirggIFTLIFARLNI-- 259
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIeglgggGGVDFSGLLRILLLLLGLYLLSA--------LFSYLQNRLMArv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 260 ------RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:cd18547 73 sqrtvyDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 334 MGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaAYMYyv 413
Cdd:cd18547 153 VTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK---AQFY-- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 339895785 414 wgSGLTL-------LVVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18547 228 --SGLLMpimnfinNLGYVLVAVVGGLLVINGALTVGVIQAFLQY 270
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
460-664 |
6.70e-38 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 140.78 E-value: 6.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLE--GGRVLLDGKPISAYDHK--YLHRVISLVSQEPVLFARS 532
Cdd:cd03260 17 KDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPGApdEGEVLLDGKDIYDLDVDvlELRRRVGMVFQKPNPFPGS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYGLP-------TVPFEMVVEAAQKANAHGFIMELQDGYStetgekgaqLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:cd03260 97 IYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 606 ATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 664
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
461-654 |
6.80e-38 |
|
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: 140.29 E-value: 6.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFARSITDNIS 538
Cdd:cd03225 19 DISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEEEVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLP--TVPFEMVVEAAQKANAHGFIMELQDgYSTETgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 616
Cdd:cd03225 99 FGLEnlGLPEEEIEERVEEALELVGLEGLRD-RSPFT------LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 339895785 617 LIQQAIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGR 654
Cdd:cd03225 172 ELLELLKKlKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
460-659 |
9.60e-38 |
|
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: 139.96 E-value: 9.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVISLVSQEPVLFA-RSITDNI 537
Cdd:cd03259 17 DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpER---RNIGMVFQDYALFPhLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPtvpfEMVVEAAQKANAHGFIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:cd03259 94 AFGLK----LRGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 339895785 618 IQ---QAIHGNLQKhTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQG 659
Cdd:cd03259 169 LReelKELQRELGI-TTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
460-665 |
1.05e-36 |
|
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: 138.25 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVL-FARSITDNIS 538
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRELVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YG-LPTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:COG1120 98 LGrYPHLGLfgrpsaedrEAVEEALERTG----LEHLADRPVDE-------LSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 609 ALDAESEYLIQQAIHG--NLQKHTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLL 665
Cdd:COG1120 167 HLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
460-659 |
2.07e-36 |
|
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: 136.48 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYLHRVISLVSQEPVL---FARSI 533
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMSslnPRMTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYGLptVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:cd03257 102 GEQIAEPL--RIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 339895785 614 SEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:cd03257 180 VQAQILDLLK-KLQEElglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
460-667 |
2.36e-36 |
|
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: 136.56 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfYPLEGgRVLLDGKPISAYDHKYL---HRVISLVSQEPVLF-ARS 532
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLE--RPTSG-SVLVDGTDLTLLSGKELrkaRRRIGMIFQHFNLLsSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYglptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:cd03258 99 VFENVAL-----PLE--IAGVPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 611 DAESEYLIQQAIHgNLQKH---TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:cd03258 172 DPETTQSILALLR-DINRElglTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
463-667 |
4.46e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 135.65 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 463 SFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVISLVSQEPVLFAR-SITDNISYG 540
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAE---RPVSMLFQENNLFPHlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 L-----PTVP-FEMVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD--- 611
Cdd:COG3840 96 LrpglkLTAEqRAQVEQALERVGLAGLL-----------DRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpal 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 612 -AESEYLIQQaIHGNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG3840 165 rQEMLDLVDE-LCRERGL-TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
459-659 |
4.60e-36 |
|
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: 133.98 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDhKYLHRVISLVSQEPVLFARSITDNIs 538
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 yglptvpfemvveaaqkanahgfimelqdgystetgekGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:cd03247 96 --------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 339895785 619 QQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 659
Cdd:cd03247 138 LSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
460-669 |
2.17e-35 |
|
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: 134.21 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvISLVSQEPVLFAR-SITDNIS 538
Cdd:COG4555 18 KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVLPDERGLYDRlTVRENIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 Y-----GLPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:COG4555 97 YfaelyGLFDEELKKRIEELIEL------LGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 614 SEYLIQQAI--HGNlQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGG 669
Cdd:COG4555 167 ARRLLREILraLKK-EGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
219-676 |
2.64e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 143.96 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 219 QKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMV 296
Cdd:PLN03232 941 QSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAakRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDI 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 297 SDLVSQNINVFLRNTVKVTGVVVFMFSLSwQLSLVTFMgfPIIMMVSNIYgKYYKRLSKEVQ--NALARASNTAE--ETI 372
Cdd:PLN03232 1021 DRNVANLMNMFMNQLWQLLSTFALIGTVS-TISLWAIM--PLLILFYAAY-LYYQSTSREVRrlDSVTRSPIYAQfgEAL 1096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 373 SAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV-----WGSGLTLLVVQVSILYYG---GHLVISGQM---- 440
Cdd:PLN03232 1097 NGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTirletLGGVMIWLTATFAVLRNGnaeNQAGFASTMglll 1176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 441 -----------------------------------------------------TSGNLIAF----IIYEFVLGDCMENVS 463
Cdd:PLN03232 1177 sytlnittllsgvlrqaskaenslnsvervgnyidlpseataiiennrpvsgwPSRGSIKFedvhLRYRPGLPPVLHGLS 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 464 FSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglpt 543
Cdd:PLN03232 1257 FFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID----- 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 544 vPFEM-----VVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:PLN03232 1332 -PFSEhndadLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 619 QQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLA-QGGLYAKLVQ 676
Cdd:PLN03232 1411 QRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSrDTSAFFRMVH 1469
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
460-667 |
3.09e-35 |
|
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: 140.42 E-value: 3.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG---GRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFARSIT 534
Cdd:COG1123 23 DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRRIGMVFQDPmtQLNPVTVG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGL--PTVPFEMVVEAAQKANAHGFIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 612
Cdd:COG1123 103 DQIAEALenLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 613 ESEYLIQQAIHGNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG1123 176 TTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
461-654 |
3.51e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 130.44 E-value: 3.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQepvlfarsitdnisyg 540
Cdd:cd00267 17 NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 lptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQ 620
Cdd:cd00267 81 ---------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 339895785 621 AIHGNLQKH-TVLIIAHRLSTVEHA-HLIVVLDKGR 654
Cdd:cd00267 122 LLRELAEEGrTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
460-656 |
9.44e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 132.91 E-value: 9.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhrvISLVSQEPVLFA-RSITDNIS 538
Cdd:COG1116 28 DDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----RGVVFQEPALLPwLTVLDNVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLptvpfEMVVEAAQKANAHgfIMELQDgystETGEKGA------QLSGGQKQRVAMARALVRNPPVLILDEATSALDA 612
Cdd:COG1116 103 LGL-----ELRGVPKAERRER--ARELLE----LVGLAGFedayphQLSGGMRQRVAIARALANDPEVLLMDEPFGALDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 339895785 613 ESEYLIQQAIHGNLQKH--TVLIIAH------RLSTVehahlIVVLDK--GRVV 656
Cdd:COG1116 172 LTRERLQDELLRLWQETgkTVLFVTHdvdeavFLADR-----VVVLSArpGRIV 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
462-676 |
1.53e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 141.80 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISygl 541
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD--- 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 542 ptvPFEM-----VVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 616
Cdd:PLN03130 1335 ---PFNEhndadLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 617 LIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLA-QGGLYAKLVQ 676
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSnEGSAFSKMVQ 1472
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
189-451 |
1.75e-34 |
|
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: 132.99 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 189 VAASFFLIVA-ALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18550 1 LALVLLLILLsALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 348 KYYKRLSKEVQNALARASNTAEET--ISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQV 425
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260
....*....|....*....|....*.
gi 339895785 426 SILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTAL 266
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
460-660 |
2.49e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.46 E-value: 2.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS---AYdhkylHRVISLVSQEPVLFA-RSITD 535
Cdd:COG3842 22 DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPE-----KRNVGMVFQDYALFPhLTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGLptvpfEM--VVEAAQKANAHGFI--MELqDGYStetGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:COG3842 97 NVAFGL-----RMrgVPKAEIRARVAELLelVGL-EGLA---DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 612 AESEYLIQQAIhGNLQKH---TVLIIAHRLS---TVehAHLIVVLDKGRVVQQGT 660
Cdd:COG3842 168 AKLREEMREEL-RRLQRElgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
188-455 |
6.38e-34 |
|
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: 131.45 E-value: 6.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQnINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaAAYMYYVWGSGLTLL--VVQV 425
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLR--AARLRARFWPLLEALpeLGLA 237
|
250 260 270
....*....|....*....|....*....|
gi 339895785 426 SILYYGGHLVISGQMTSGNLIAFIIYEFVL 455
Cdd:cd18543 238 AVLALGGWLVANGSLTLGTLVAFSAYLTML 267
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
234-671 |
6.52e-34 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 139.70 E-value: 6.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 234 LLAIGSSFAAGIrGGIFTlifARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 313
Cdd:TIGR00957 1020 FAVFGYSMAVSI-GGIQA---SR---VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFN 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 314 VTGVVVFMFsLSWQLSLVTFMGFPII-MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFaNEEEEAEVyl 392
Cdd:TIGR00957 1093 VIGALIVIL-LATPIAAVIIPPLGLLyFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIH-- 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 393 rklQQVYKLNRKEAAAYMYYV---W---------------------------GSGLTLLVVQVS--ILYYGGHLV-ISGQ 439
Cdd:TIGR00957 1169 ---QSDLKVDENQKAYYPSIVanrWlavrlecvgncivlfaalfavisrhslSAGLVGLSVSYSlqVTFYLNWLVrMSSE 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 440 MTSgNLIAF--------------------------------------IIYEFVLGDCMENVSFSLSPGKVTALVGPSGSG 481
Cdd:TIGR00957 1246 MET-NIVAVerlkeysetekeapwqiqetappsgwpprgrvefrnycLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAG 1324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 482 KSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPF-----EMVVEAAQKA 556
Cdd:TIGR00957 1325 KSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD------PFsqysdEEVWWALELA 1398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 557 NAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAH 636
Cdd:TIGR00957 1399 HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH 1478
|
490 500 510
....*....|....*....|....*....|....*
gi 339895785 637 RLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLY 671
Cdd:TIGR00957 1479 RLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
195-451 |
1.94e-33 |
|
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: 130.26 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 195 LIVAALgETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQET 274
Cdd:cd18549 12 VLIAAL-DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 275 SFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLS 354
Cdd:cd18549 91 SFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 355 KEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQvYKLNRKEAAAYM-YYVWGSGLTLLVVQVSILYYGGH 433
Cdd:cd18549 171 RRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR-FLESKKKAYKAMaYFFSGMNFFTNLLNLVVLVAGGY 249
|
250
....*....|....*...
gi 339895785 434 LVISGQMTSGNLIAFIIY 451
Cdd:cd18549 250 FIIKGEITLGDLVAFLLY 267
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
188-451 |
2.37e-33 |
|
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: 130.32 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQK---------------SMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTL 252
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKplpgllglapllgpdPLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 253 IFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYY 412
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 339895785 413 VWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
461-655 |
7.83e-33 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 126.07 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK----YLHRVISLVSQEPVLFAR-SITD 535
Cdd:cd03255 22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFRRRHIGFVFQSFNLLPDlTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:cd03255 102 NVE--LP-----LLLAGVPKKERRERAEELLErvGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 339895785 614 SEYLIQQAIHG--NLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 655
Cdd:cd03255 175 TGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
460-666 |
9.70e-33 |
|
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: 126.84 E-value: 9.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFAR-SITDN 536
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPyaSLHPRhTVDRI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 IS-----YGLPTVPfEMVVEAAQKanahgfiMELQDGYSTEtgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:COG1124 102 LAeplriHGLPDRE-ERIAELLEQ-------VGLPPSFLDR---YPHQLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 612 AeseyLIQ----------QAIHGNlqkhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:COG1124 171 V----SVQaeilnllkdlREERGL----TYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
461-667 |
1.19e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 126.26 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAyDHKYLHRV---ISLVSQEPVLFA-RSI 533
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTllrCINLLE---EPDSGTITVDGEDLTD-SKKDINKLrrkVGMVFQQFNLFPhLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYGLptvpfeMVV------EAAQKAnahgfiMEL---------QDGYStetgekgAQLSGGQKQRVAMARALVRNP 598
Cdd:COG1126 95 LENVTLAP------IKVkkmskaEAEERA------MELlervgladkADAYP-------AQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 599 PVLILDEATSALDAE--SEYL--IQQAIHGNLqkhTVLIIAHRLS---TVehAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG1126 156 KVMLFDEPTSALDPElvGEVLdvMRDLAKEGM---TMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
461-667 |
1.31e-32 |
|
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: 126.99 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFA-RSITD 535
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGLPT--VP----FEMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:cd03294 122 NVAFGLEVqgVPraerEERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 610 LDA------ESEYLiqqAIHGNLQKhTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:cd03294 191 LDPlirremQDELL---RLQAELQK-TIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
460-655 |
4.24e-32 |
|
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: 122.51 E-value: 4.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvISLVSQEPVLfarsitdnisy 539
Cdd:cd03230 17 DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLPEEPSL----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 glptvpfemvveaaqkanahgfimelqdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQ 619
Cdd:cd03230 85 -----------------------------YENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895785 620 QAIHG-NLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRV 655
Cdd:cd03230 136 ELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
461-654 |
4.63e-32 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 122.68 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD--HKYLHRVISLVSQEPVLFAR-SITDNI 537
Cdd:cd03229 18 DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLptvpfemvveaaqkanahgfimelqdgystetgekgaqlSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:cd03229 98 ALGL---------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 339895785 618 IQ---QAIHGNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGR 654
Cdd:cd03229 139 VRallKSLQAQLGI-TVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
461-660 |
5.28e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 127.12 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEGgRVLLDGKPISAYDHKYLHRV---ISLVSQEPVLF-ARSI 533
Cdd:COG1135 23 DVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER--PTSG-SVLVDGVDLTALSERELRAArrkIGMIFQHFNLLsSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYglptvPFEMV----VEAAQKANahgfimELQD--GYStetgEKG----AQLSGGQKQRVAMARALVRNPPVLIL 603
Cdd:COG1135 100 AENVAL-----PLEIAgvpkAEIRKRVA------ELLElvGLS----DKAdaypSQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 604 DEATSALDAESEY----LIQQaIHGNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGT 660
Cdd:COG1135 165 DEATSALDPETTRsildLLKD-INRELGL-TIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
188-451 |
5.59e-32 |
|
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: 125.97 E-value: 5.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSsFAAGIRGGIF-TLIFARLNIRLRNCLF 266
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLG-LIAGILAGYFaAKASQGFGRDLRKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 267 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIY 346
Cdd:cd18548 80 EKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 347 GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaAYMYYVWGSGLTLLVVQVS 426
Cdd:cd18548 160 MKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLK---AGRLMALLNPLMMLIMNLA 236
|
250 260
....*....|....*....|....*...
gi 339895785 427 ---ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18548 237 ivaILWFGGHLINAGSLQVGDLVAFINY 264
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
460-659 |
2.13e-31 |
|
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: 120.62 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQepvlfarsitdnisy 539
Cdd:cd03214 16 DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 glptvpfemVVEAAQKAN-AHGFIMELqdgystetgekgaqlSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:cd03214 81 ---------ALELLGLAHlADRPFNEL---------------SGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 339895785 619 QQAIHgNLQKH---TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQG 659
Cdd:cd03214 137 LELLR-RLARErgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
188-451 |
8.86e-31 |
|
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: 122.60 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMdqfsTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIR----LRN 263
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDL----GVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERllydLRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18546 77 RVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYlRKLQQVYKLNRKEAAAYMyYVWGSGLTLL-- 421
Cdd:cd18546 157 RWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF-AELSDDYRDARLRAQRLV-AIYFPGVELLgn 234
|
250 260 270
....*....|....*....|....*....|
gi 339895785 422 VVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18546 235 LATAAVLLVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
461-667 |
1.66e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.95 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILenfYPLE---GGRVLLDGKPISAyDHKYLHRVISLVSQEPVLFaR--SITD 535
Cdd:COG1118 20 DVSLEIASGELVALLGPSGSGKTTLLRII---AGLEtpdSGRIVLNGRDLFT-NLPPRERRVGFVFQHYALF-PhmTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGLPTVPfemVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:COG1118 95 NIAFGLRVRP---PSKAEIRARVEELLELVQlEGLA---DRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 615 EYLIQQ---AIHGNLQkHTVLIIAH-RLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG1118 169 RKELRRwlrRLHDELG-GTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
455-659 |
1.70e-30 |
|
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: 119.32 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 455 LGDCMENVSFSLsPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKylhRVISLVSQEPV 527
Cdd:cd03297 10 LPDFTLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQ---RKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 LFAR-SITDNISYGLPTV-PFEMVVEAAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:cd03297 86 LFPHlNVRENLAFGLKRKrNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 606 ATSALDAESEYLIQ---QAIHGNLQKHtVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:cd03297 158 PFSALDRALRLQLLpelKQIKKNLNIP-VIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
461-658 |
2.33e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 119.38 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILenfypleG-------GRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLF 529
Cdd:COG1136 26 GVSLSIEAGEFVAIVGPSGSGKSTLLNIL-------GgldrptsGEVLIDGQDISSLSERELARLrrrhIGFVFQFFNLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 530 AR-SITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 606
Cdd:COG1136 99 PElTALENVA--LP-----LLLAGVSRKERRERARELLErvGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 339895785 607 TSALDAESEYLIQQAIHG--NLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQ 658
Cdd:COG1136 172 TGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
459-655 |
7.06e-30 |
|
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: 117.63 E-value: 7.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSS---CVNILENFyplEGGRVLLDGKPISAyDHKYLHRV---ISLVSQEPVLFA-R 531
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEEP---DSGTIIIDGLKLTD-DKKNINELrqkVGMVFQQFNLFPhL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 SITDNISYGLPTVPFEMVVEAAQKAnahgfiMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:cd03262 92 TVLENITLAPIKVKGMSKAEAEERA------LELLEkvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 339895785 610 LDAE--SEYL--IQQAIHgnlQKHTVLIIAHRLSTVEH-AHLIVVLDKGRV 655
Cdd:cd03262 166 LDPElvGEVLdvMKDLAE---EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
461-660 |
1.25e-29 |
|
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: 117.54 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITDNI- 537
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLENVm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 --------SYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:cd03219 98 vaaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 610 L-DAESEYLIQ--QAIhgNLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 660
Cdd:cd03219 174 LnPEETEELAEliREL--RERGITVLLVEHDMDVVmSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
188-451 |
1.31e-29 |
|
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: 119.18 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAID-GIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGgIFTLIFA-RLNIRLRNCL 265
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDlVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRI-YLNHVAEqKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 266 FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNI 345
Cdd:cd18778 80 YDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 346 YGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLN---RKEAAAY---MYYVWGSGlT 419
Cdd:cd18778 160 YSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQlraMKLWAIFhplMEFLTSLG-T 238
|
250 260 270
....*....|....*....|....*....|..
gi 339895785 420 LLVvqvsiLYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18778 239 VLV-----LGFGGRLVLAGELTIGDLVAFLLY 265
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
469-659 |
1.45e-29 |
|
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: 116.44 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 469 GKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVISLVSQEPVLFAR-SITDNISYGL-PTVPF 546
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLGLsPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 547 EMVVEAAQKANAHgfimelQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG-- 624
Cdd:cd03298 102 TAEDRQAIEVALA------RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDlh 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 339895785 625 NLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
452-665 |
2.03e-29 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 116.67 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 452 EFVLgdcmENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR 531
Cdd:cd03299 12 EFKL----KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 -SITDNISYGL-------PTVPfEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLIL 603
Cdd:cd03299 86 mTVYKNIAYGLkkrkvdkKEIE-RKVLEIAEMLG----IDHLLN-------RKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 604 DEATSALDAESE----YLIQQAIHGNlqKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLL 665
Cdd:cd03299 154 DEPFSALDVRTKeklrEELKKIRKEF--GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
461-664 |
2.36e-29 |
|
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: 116.57 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVISLVSQEPVLFAR-SITDNIS 538
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPpHK---RPVNTVFQNYALFPHlTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTvpfEMVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:cd03300 95 FGLRL---KKLPKAEIKERVAEALDLVQlEGYA---NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 339895785 618 IQQAIHgNLQKH---TVLIIAHRLS---TVehAHLIVVLDKGRVVQQGTHQQL 664
Cdd:cd03300 169 MQLELK-RLQKElgiTFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
187-451 |
3.42e-29 |
|
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: 117.97 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 187 FLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVI-VCLLAIgssFAAGIRGGIFT--LIFARLNIRLRN 263
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLyLGLILI---QALSVFLFIRLagKIEMGVSYDLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18540 80 KAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 344 NIygkYYKRLSKevQNALARASN---TA--EETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaAAYMyyvwgSGL 418
Cdd:cd18540 160 IY---FQKKILK--AYRKVRKINsriTGafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVR--AARL-----SAL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 339895785 419 TLLVVQV-------SILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18540 228 FLPIVLFlgsiataLVLWYGGILVLAGAITIGTLVAFISY 267
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
451-679 |
4.27e-29 |
|
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: 116.55 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 451 YEFVLGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFA 530
Cdd:cd03288 29 YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 531 RSITDNISyglP--TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:cd03288 109 GSIRFNLD---PecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 609 ALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ-GGLYAKLVQRQM 679
Cdd:cd03288 186 SIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVFASLVRTDK 257
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
428-638 |
5.63e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 116.29 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 428 LYYGGHLVIsgqmtsgnliafiiyefvlgdcmENVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP---LEgGRVL 501
Cdd:COG1117 19 VYYGDKQAL-----------------------KDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPgarVE-GEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 502 LDGKPIsaYDHKY----LHRVISLVSQEPVLFARSITDNISYGL-------PTVPFEMVVEAAQKANahgfimeLQDgys 570
Cdd:COG1117 75 LDGEDI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiksKSELDEIVEESLRKAA-------LWD--- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 571 tET----GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES----EYLIQQaihgnL-QKHTVLIIAHRL 638
Cdd:COG1117 143 -EVkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELILE-----LkKDYTIVIVTHNM 213
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
182-449 |
7.29e-29 |
|
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: 116.78 E-value: 7.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRL 261
Cdd:cd18570 1 KKLLILILLLSLLITLLGI---AGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 262 RNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQN-INVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18570 78 ILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFL-DLLMVIISGIILFFYNWKLFLITLLIIPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTL 420
Cdd:cd18570 156 LIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLIS 235
|
250 260
....*....|....*....|....*....
gi 339895785 421 LVVQVSILYYGGHLVISGQMTSGNLIAFI 449
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFN 264
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
460-666 |
7.82e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 114.84 E-value: 7.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITDNI 537
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 syglptvpfEMVVEAAQKANAHgFIME--------LQDGYSTetgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:cd03224 97 ---------LLGAYARRRAKRK-ARLErvyelfprLKERRKQ----LAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 610 LdaeSEYLIQQ---AIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:cd03224 163 L---APKIVEEifeAIRElRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
460-655 |
9.47e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.19 E-value: 9.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhrvISLVSQEpVLFARS--IT--D 535
Cdd:COG1121 23 EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IGYVPQR-AEVDWDfpITvrD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGL-PTVPF---------EMVVEAAQKANAHGF----ImelqdgystetgekgAQLSGGQKQRVAMARALVRNPPVL 601
Cdd:COG1121 97 VVLMGRyGRRGLfrrpsradrEAVDEALERVGLEDLadrpI---------------GELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 602 ILDEATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRV 655
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLR-ELRREgkTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
459-684 |
1.33e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.62 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPV-LFARSITD-N 536
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDnQFVGSIVKyD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLP--TVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAqLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:PRK13648 105 VAFGLEnhAVPYDEMHRRVSEA------LKQVDMLERADYEPNA-LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 615 -EYLIQQAIHGNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT------HQQLLAQGGLYAKLVQR--QMLGLQP 684
Cdd:PRK13648 178 rQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTpteifdHAEELTRIGLDLPFPIKinQMLGHQT 257
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
460-666 |
1.39e-28 |
|
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: 114.71 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFA-RSITDNIS 538
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPhMTVEENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 yglpTVP-FEMVVEAAQKANAHGFI-------MELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:cd03295 98 ----LVPkLLKWPKEKIRERADELLalvgldpAEFADRYP-------HELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339895785 611 DA------ESEYL-IQQAIHgnlqkHTVLIIAHRL-STVEHAHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:cd03295 167 DPitrdqlQEEFKrLQQELG-----KTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
459-666 |
1.62e-28 |
|
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: 114.14 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPVLF-ARSIT 534
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMGMLFQSGALFdSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGL---PTVPFEMVVE-AAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:cd03261 96 ENVAFPLrehTRLSEEEIREiVLEKLEAVG-LRGAEDLYP-------AELSGGMKKRVALARALALDPELLLYDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 611 DAESEYLIQQAIHgNLQKH---TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:cd03261 168 DPIASGVIDDLIR-SLKKElglTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
461-660 |
3.28e-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: 113.98 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITDNI- 537
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIARLGIARTFQNPRLFPElTVLENVl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 -------SYGLPTVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:COG0411 102 vaaharlGRGLLAALLRLPRARREEREARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 609 AL-DAESEYLIQ--QAIHGNlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 660
Cdd:COG0411 182 GLnPEETEELAEliRRLRDE-RGITILLIEHDMDLVmGLADRIVVLDFGRVIAEGT 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
460-664 |
5.44e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.94 E-value: 5.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVISLVSQEPVLF-ARSITDNIS 538
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYpHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLptvpfEM-----------VVEAAQkanahgfIMELQDgYStetGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:COG3839 98 FPL-----KLrkvpkaeidrrVREAAE-------LLGLED-LL---DRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 608 SALDAE------SEylIQQaIHGNLqKHTVLIiahrlstVEH--------AHLIVVLDKGRVVQQGTHQQL 664
Cdd:COG3839 162 SNLDAKlrvemrAE--IKR-LHRRL-GTTTIY-------VTHdqveamtlADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
461-656 |
7.96e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.83 E-value: 7.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkylhrvislvsqepvlfaRSITDNISYG 540
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF---------------------ASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 LPTVPfemvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEATSAL-DAESEYLIq 619
Cdd:cd03216 77 IAMVY---------------------------------QLSVGERQMVEIARALARNARLLILDEPTAALtPAEVERLF- 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 339895785 620 qAIHGNLQK--HTVLIIAHRLSTV-EHAHLIVVLDKGRVV 656
Cdd:cd03216 123 -KVIRRLRAqgVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
459-665 |
9.56e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.16 E-value: 9.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFARSITDN 536
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPdnQFIGATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLPTV---PFEM---VVEAAQKANAHGFImelqdgystetgEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:PRK13632 105 IAFGLENKkvpPKKMkdiIDDLAKKVGMEDYL------------DKEPQnLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 610 LDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLL 665
Cdd:PRK13632 173 LDPKGKREIKKIMV-DLRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
460-668 |
1.20e-27 |
|
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: 112.52 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-KPISAYDHKYLHRVISLVSQEP--VLFARSITDN 536
Cdd:TIGR04520 19 KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVGMVFQNPdnQFVGATVEDD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:TIGR04520 99 VAFGLENlgVPREEMRKRVDEALK---LVGMEDFRDREP----HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 615 EYLIQQAIHgNLQKH---TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQG 668
Cdd:TIGR04520 172 RKEVLETIR-KLNKEegiTVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
460-651 |
1.25e-27 |
|
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: 110.65 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVISLVSQEPVLFAR-SITDNIS 538
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 -----YGLPtVPFEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:COG4133 98 fwaalYGLR-ADREAIDEALEAVG----LAGLAD-------LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 339895785 614 SEYLIQQAIHGNLQKHTVLIIA-HRLSTVEHAHLIVVLD 651
Cdd:COG4133 166 GVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDLGD 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
460-636 |
1.44e-27 |
|
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: 110.42 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhKYLHRVISLVSQEP--VLFARSITDNI 537
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDVdyQLFTDSVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVPfemvvEAAQKANAhgfIMELQDGYSTEtgEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 616
Cdd:cd03226 94 LLGLKELD-----AGNEQAET---VLKDLDLYALK--ERHPLsLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180
....*....|....*....|.
gi 339895785 617 LIQQAI-HGNLQKHTVLIIAH 636
Cdd:cd03226 164 RVGELIrELAAQGKAVIVITH 184
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
461-698 |
2.09e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 111.64 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPvLFARSIT--DNIS 538
Cdd:PRK11231 20 DLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHH-LTPEGITvrELVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGL-PTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:PRK11231 99 YGRsPWLSLwgrlsaednARVNQAMEQTR----INHLADRRLTD-------LSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 609 ALD----AESEYLIQQAihgNLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGLyaklvqRQMLGLQ 683
Cdd:PRK11231 168 YLDinhqVELMRLMREL---NTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPGLL------RTVFDVE 238
|
250
....*....|....*
gi 339895785 684 paadfTAGHNEPVAN 698
Cdd:PRK11231 239 -----AEIHPEPVSG 248
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
461-678 |
2.48e-27 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 114.04 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsaYD---------HKylhRVISLVSQEPVLFA- 530
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDsargiflppHR---RRIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 531 RSITDNISYGL-------PTVPFEMVVEAAQkanahgfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLIL 603
Cdd:COG4148 92 LSVRGNLLYGRkrapraeRRISFDEVVELLG-------IGHLLDRRP-------ATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 604 DEATSALDAES-----EYLIQqaihgnLQKHT---VLIIAHrlSTVEHAHL---IVVLDKGRVVQQGTHQQLLAQGGLYA 672
Cdd:COG4148 158 DEPLAALDLARkaeilPYLER------LRDELdipILYVSH--SLDEVARLadhVVLLEQGRVVASGPLAEVLSRPDLLP 229
|
....*.
gi 339895785 673 KLVQRQ 678
Cdd:COG4148 230 LAGGEE 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
461-664 |
2.53e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 111.30 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPVLFAR-SI 533
Cdd:COG3638 21 DVSLEIERGEFVALIGPSGAGKSTllrCLNGLV---EPTSGEILVDGQDVTALRGRALRRLrrrIGMIFQQFNLVPRlSV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYG-LPTVPF----EMVVEAAQKANAHGFI--MELQDgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 606
Cdd:COG3638 98 LTNVLAGrLGRTSTwrslLGLFPPEDRERALEALerVGLAD----KAYQRADQLSGGQQQRVAIARALVQEPKLILADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339895785 607 TSALDAES-----EYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQL 664
Cdd:COG3638 174 VASLDPKTarqvmDLLRRIAREDGI---TVVVNLHQVDLArRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
459-668 |
4.43e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 111.26 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFARSITDN 536
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdnQFVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLPT--VPFEMVVEAAQKANAHgfiMELQDGYSTETgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:PRK13635 103 VAFGLENigVPREEMVERVDQALRQ---VGMEDFLNREP----HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 615 EYLIQQAIH-----GNLqkhTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQG 668
Cdd:PRK13635 176 RREVLETVRqlkeqKGI---TVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
460-659 |
5.25e-27 |
|
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: 109.27 E-value: 5.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVISLVSQEPVLFAR-SITDNIS 538
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQNYALYPHmTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 616
Cdd:cd03301 95 FGLKLrkVPKDEIDERVREVAELLQIEHLLD-------RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 339895785 617 LIQQAI---HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 659
Cdd:cd03301 168 QMRAELkrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
460-666 |
5.35e-27 |
|
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: 110.07 E-value: 5.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPVLFArSIT-- 534
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrIGMLFQGGALFD-SLTvf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGL---PTVPFEMVVEAAqkanahgfIMELQdgystETGEKGA------QLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:COG1127 101 ENVAFPLrehTDLSEAEIRELV--------LEKLE-----LVGLPGAadkmpsELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 606 ATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:COG1127 168 PTAGLDPITSAVIDELIR-ELRDElglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
459-659 |
6.11e-27 |
|
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: 109.16 E-value: 6.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhrvISLVSQEPVL---FARSITD 535
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQRRSIdrdFPISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGL-PTVPFEMVVEAAQKANahgfIMELQDgySTETGEKG----AQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:cd03235 90 VVLMGLyGHKGLFRRLSKADKAK----VDEALE--RVGLSELAdrqiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 611 DAESeyliQQAIHGNLQK-----HTVLIIAHRLSTV-EHAHLIVVLDKgRVVQQG 659
Cdd:cd03235 164 DPKT----QEDIYELLRElrregMTILVVTHDLGLVlEYFDRVLLLNR-TVVASG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
459-664 |
9.37e-27 |
|
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: 109.35 E-value: 9.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SITDNI 537
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVP-FEMVVEAAQKANAHGFIMELQ-DGYSTETGekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE-- 613
Cdd:cd03296 96 AFGLRVKPrSERPPEAEIRAKVHELLKLVQlDWLADRYP---AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKvr 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 339895785 614 ---SEYLIQqaIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 664
Cdd:cd03296 173 kelRRWLRR--LHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
459-650 |
1.87e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.88 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNIS 538
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YglptvPFEMvveAAQKANAHGFIMELQD-GYSTETGEKG-AQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 616
Cdd:PRK10247 103 F-----PWQI---RNQQPDPAIFLDDLERfALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 339895785 617 LIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVL 650
Cdd:PRK10247 175 NVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
459-641 |
3.14e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.59 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG-----GRVLLDGKPIsaYDHKY----LHRVISLVSQEPVLF 529
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI--YERRVnlnrLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 530 ARSITDNISYGL------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL 603
Cdd:PRK14258 101 PMSVYDNVAYGVkivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 339895785 604 DEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTV 641
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQV 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
460-664 |
4.98e-26 |
|
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: 107.27 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPVLFAR-S 532
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTllrCLNGLV---EPTSGSVLIDGTDINKLKGKALRQLrrqIGMIFQQFNLIERlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYG-LPTVP-----FEMVVEAA-QKANAhgfIMElQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:cd03256 95 VLENVLSGrLGRRStwrslFGLFPKEEkQRALA---ALE-RVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 606 ATSALDAES-----EYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQL 664
Cdd:cd03256 171 PVASLDPASsrqvmDLLKRINREEGI---TVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAEL 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
461-664 |
5.44e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 109.44 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYL---HRVISLVSQEPvlFA-----RS 532
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP--YAslnprMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:COG4608 114 VGDIIAEPL------RIHGLASKAERRERVAELLElvGLRPEHADRYPhEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339895785 610 LDAeSeylIQ-QAIhgN----LQK---HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 664
Cdd:COG4608 188 LDV-S---IQaQVL--NlledLQDelgLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
460-667 |
7.31e-26 |
|
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: 108.99 E-value: 7.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP---LEGGRVLLDGKPISAYDHKYLHRV----ISLVSQE------P 526
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKIrgreIQMIFQDpmtslnP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 527 VLfarsitdnisyglpTVpFEMVVEAaqkanahgfiMELQDGYSTETGEKGA---------------------QLSGGQK 585
Cdd:COG0444 102 VM--------------TV-GDQIAEP----------LRIHGGLSKAEARERAiellervglpdperrldryphELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 586 QRVAMARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQ 658
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDV----TIQAQILNllkDLQRElglAILFITHDLGVVAEiADRVAVMYAGRIVEE 232
|
....*....
gi 339895785 659 GTHQQLLAQ 667
Cdd:COG0444 233 GPVEELFEN 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
463-667 |
1.05e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.20 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 463 SFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKpisayDHKYL---HRVISLVSQEPVLFAR-SITDNIS 538
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGL-PTVPF-----EMVVEAAQKANAHGFIMELQdgystetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALD- 611
Cdd:PRK10771 94 LGLnPGLKLnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDp 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895785 612 ---AESEYLIQQAIHGnlQKHTVLIIAHRLstvEHAHLI----VVLDKGRVVQQGTHQQLLAQ 667
Cdd:PRK10771 163 alrQEMLTLVSQVCQE--RQLTLLMVSHSL---EDAARIaprsLVVADGRIAWDGPTDELLSG 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
461-660 |
1.17e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.73 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPlEGGRVLLDGKPISAYDHKYL---HRVISLVSQE-PVLFARSI 533
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTlirCINLLER--P-TSGRVLVDGQDLTALSEKELrkaRRQIGMIFQHfNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYglptvPFEMVVEAAQKANAHgfIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PRK11153 100 FDNVAL-----PLELAGTPKAEIKAR--VTELLElvGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 612 AESeyliQQAIHGNLQK------HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGT 660
Cdd:PRK11153 173 PAT----TRSILELLKDinrelgLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
424-656 |
1.26e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.52 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 424 QVSILYYGGHLVISgqmtsgnliafiiyefvlgdcmeNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLD 503
Cdd:COG2884 6 NVSKRYPGGREALS-----------------------DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 504 GKPISAYDHK---YLHRVISLVSQE-PVLFARSITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKG 577
Cdd:COG2884 63 GQDLSRLKRReipYLRRRIGVVFQDfRLLPDRTVYENVA--LP-----LRVTGKSRKEIRRRVREVLDlvGLSDKAKALP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 578 AQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEHA-HLIVVLDKGRV 655
Cdd:COG2884 136 HELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATHDLELVDRMpKRVLELEDGRL 215
|
.
gi 339895785 656 V 656
Cdd:COG2884 216 V 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
459-665 |
1.41e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.95 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGkpISAYDHKYLHRVI----SLVSQEPVLFAR 531
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLE---EITSGDLIVDG--LKVNDPKVDERLIrqeaGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 -SITDNISYGlptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:PRK09493 92 lTALENVMFG----PLR--VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895785 609 ALDAE--SEYL--IQQ-AIHGnlqkHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLL 665
Cdd:PRK09493 166 ALDPElrHEVLkvMQDlAEEG----MTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
459-655 |
1.46e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 105.18 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLHRVISLVSQE-PVLFARSIT 534
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRRKIGVVFQDfRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNisyglptVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 612
Cdd:cd03292 97 EN-------VAFALEVTGVPPREIRKRVPAALElvGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 339895785 613 ESEYLIQQAIHG-NLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRV 655
Cdd:cd03292 170 DTTWEIMNLLKKiNKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
461-659 |
1.86e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 104.17 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--GRVLLDGKPISAYDHKYLhrvISLVSQEPVLFARSitdnis 538
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKI---IGYVPQDDILHPTL------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 yglpTVpFEMVVEAAqkanahgfimELQdgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:cd03213 98 ----TV-RETLMFAA----------KLR------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 339895785 619 QQAIHG-NLQKHTVLIIAHRLST--VEHAHLIVVLDKGRVVQQG 659
Cdd:cd03213 151 MSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
455-670 |
1.90e-25 |
|
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: 108.28 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 455 LGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKylhRVISLVSQEPV 527
Cdd:TIGR02142 9 LGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEK---RRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 LFAR-SITDNISYGL--PTVPFEMVVEAAqkanahgfIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILD 604
Cdd:TIGR02142 86 LFPHlSVRGNLRYGMkrARPSERRISFER--------VIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 605 EATSALDAESEYLIQQAIHgNLQKHT---VLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGGL 670
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLE-RLHAEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
461-656 |
1.95e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVSQEPVLFA-RSI 533
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdAQAAG-----IAIIHQELNLVPnLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYG-LPTVPF-----EMVVEAAQKANAHGFIMELqdgySTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:COG1129 97 AENIFLGrEPRRGGlidwrAMRRRARELLARLGLDIDP----DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 339895785 608 SAL-DAESEYLIqqAIHGNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVV 656
Cdd:COG1129 169 ASLtEREVERLF--RIIRRLKAQgvAIIYISHRLDEVfEIADRVTVLRDGRLV 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
460-665 |
2.21e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.97 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQ-----------EPVL 528
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQhsslafpftveEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 529 FARsitdnISYGLPTVPFEMVVEAAqkanahgfiMELqdgysTETGEKGA----QLSGGQKQRVAMARAL------VRNP 598
Cdd:COG4559 98 LGR-----APHGSSAAQDRQIVREA---------LAL-----VGLAHLAGrsyqTLSGGEQQRVQLARVLaqlwepVDGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 599 P-VLILDEATSALDaeseyLIQQaihgnlqkHTVLIIAHRLS-------TVEH--------AHLIVVLDKGRVVQQGTHQ 662
Cdd:COG4559 159 PrWLFLDEPTSALD-----LAHQ--------HAVLRLARQLArrgggvvAVLHdlnlaaqyADRILLLHQGRLVAQGTPE 225
|
...
gi 339895785 663 QLL 665
Cdd:COG4559 226 EVL 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
459-682 |
3.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFARSITDN 536
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:PRK13650 103 VAFGLENkgIPHEEMKERVNEALE---LVGMQDFKEREP----ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 615 EYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGlyaKLVQrqmLGL 682
Cdd:PRK13650 176 RLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN---DLLQ---LGL 239
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
461-664 |
7.06e-25 |
|
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: 103.35 E-value: 7.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsAYDHKYLHRVISLVSQEPVLFAR-SITDNISY 539
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCPQFDALFDElTVREHLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 -----GLPTVPFEMVVEAAQKanahgfIMELQDGYSTETGekgaQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:cd03263 99 yarlkGLPKSEIKEEVELLLR------VLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 339895785 615 EYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 664
Cdd:cd03263 169 RRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
461-659 |
1.07e-24 |
|
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: 102.66 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGkVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVISLVSQEPVLFAR-SITDNISY 539
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL-RRRIGYLPQEFGVYPNfTVREFLDY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 -----GLP--TVPfEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 612
Cdd:cd03264 96 iawlkGIPskEVK-ARVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 339895785 613 ES-----EYLIQQAihgnlQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVVQQG 659
Cdd:cd03264 164 EErirfrNLLSELG-----EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
460-659 |
1.10e-24 |
|
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: 102.30 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVSqEPVLF-ARSITDNIS 538
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE-APGFYpNLTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YglptvpfemvveaaqKANAHGF----IMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 612
Cdd:cd03268 95 L---------------LARLLGIrkkrIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 339895785 613 ESEYLIQQAIHgNLQK--HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:cd03268 160 DGIKELRELIL-SLRDqgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
460-665 |
2.26e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVL-FARSITDNIS 538
Cdd:PRK13548 19 DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGL-----PTVPFEMVVEAAqkanahgfiMELQD--GYStetGEKGAQLSGGQKQRVAMARALVR------NPPVLILDE 605
Cdd:PRK13548 99 MGRaphglSRAEDDALVAAA---------LAQVDlaHLA---GRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 606 ATSALDaeseyLIQQaihgnlqkHTVLIIAHRLST--------VEH--------AHLIVVLDKGRVVQQGTHQQLL 665
Cdd:PRK13548 167 PTSALD-----LAHQ--------HHVLRLARQLAHerglavivVLHdlnlaaryADRIVLLHQGRLVADGTPAEVL 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
461-656 |
2.88e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.03 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVSQEPVLFAR-SI 533
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdAIALG-----IGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYGLPTVPFEMV--VEAAQKanahgfIMELQDGYstetG------EKGAQLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:COG3845 98 AENIVLGLEPTKGGRLdrKAARAR------IRELSERY----GldvdpdAKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 606 ATSAL-DAESEYLIqqAIHGNL--QKHTVLIIAHRLSTV-EHAHLIVVLDKGRVV 656
Cdd:COG3845 168 PTAVLtPQEADELF--EILRRLaaEGKSIIFITHKLREVmAIADRVTVLRRGKVV 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
428-638 |
3.70e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.55 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 428 LYYGGHLVIsgqmtsgnliafiiyefvlgdcmENVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP---LEGgRVL 501
Cdd:PRK14243 18 VYYGSFLAV-----------------------KNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPgfrVEG-KVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 502 LDGKPISA--YDHKYLHRVISLVSQEPVLFARSITDNISYGlPTV-----PFEMVVEAAQKANAhgfimeLQDGYSTETG 574
Cdd:PRK14243 74 FHGKNLYApdVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYG-ARIngykgDMDELVERSLRQAA------LWDEVKDKLK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339895785 575 EKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRL 638
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
462-666 |
6.67e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.37 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEG----GRVLLDG-KPISAYDH--KYLHRVISLVSQEPVLFA- 530
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ--PEAGtirvGDITIDTaRSLSQQKGliRQLRQHVGFVFQNFNLFPh 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 531 RSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:PRK11264 100 RTVLENIIEG----PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 611 DAESEYLIQQAIHGNLQ-KHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQeKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
461-667 |
7.80e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.92 E-value: 7.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSC----VNILENfypleGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPvlFA--- 530
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDP--FGsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 531 --RSITDNISYGLpTVPF---------EMVVEAAQKAnahGFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPP 599
Cdd:COG4172 377 prMTVGQIIAEGL-RVHGpglsaaerrARVAEALEEV---GLDPAARHRYPHE-------FSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 600 VLILDEATSALDAeseyLIQQAIHG---NLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG4172 446 LLVLDEPTSALDV----SVQAQILDllrDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
459-699 |
8.05e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 107.90 E-value: 8.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGGRVLLDGKpisaydhkylhrvISLVSQEPVLFARSITDNI 537
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFNATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVP--FEMVVEAAqkANAHGFIMeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE-S 614
Cdd:PLN03130 700 LFGSPFDPerYERAIDVT--ALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvG 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 615 EYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQR--QMLGLQPAADFTAGH 692
Cdd:PLN03130 777 RQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENagKMEEYVEENGEEEDD 856
|
250
....*....|
gi 339895785 693 NE---PVANG 699
Cdd:PLN03130 857 QTsskPVANG 866
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
459-653 |
9.06e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 100.10 E-value: 9.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCV-NILENFYPLEG----GRVLLDGKPISAYDHKYLHRViSLVSQEPVLFARSI 533
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRYSV-AYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYGLP--TVPFEMVVEAAqkaNAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:cd03290 96 EENITFGSPfnKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 339895785 612 AE-SEYLIQQAIHGNLQ--KHTVLIIAHRLSTVEHAHLIVVLDKG 653
Cdd:cd03290 173 IHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
235-456 |
1.22e-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: 102.35 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 235 LAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKV 314
Cdd:cd18558 68 IGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 315 TGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRK 394
Cdd:cd18558 148 GTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQN 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 395 LQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLG 456
Cdd:cd18558 228 LEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGA 289
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
188-450 |
1.89e-23 |
|
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: 101.10 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18568 7 ILLASLLLQLLGL---ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18568 84 HLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE-----EAEvYLRKLQQVYKLNRKEAAAYMyyvwGSGLTLLV 422
Cdd:cd18568 163 PKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPirwrwENK-FAKALNTRFRGQKLSIVLQL----ISSLINHL 237
|
250 260
....*....|....*....|....*...
gi 339895785 423 VQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18568 238 GTIAVLWYGAYLVISGQLTIGQLVAFNM 265
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
459-638 |
2.01e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP--LEGGRVLLDGKPISA--YDHKYLHRVISLVSQEPVLFAR 531
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 SITDNISYGL------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:PRK14239 101 SIYENVVYGLrlkgikDKQVLDEAVEKSLKGAS------IWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190
....*....|....*....|....*....|...
gi 339895785 606 ATSALDAESEYLIQQAIHGNLQKHTVLIIAHRL 638
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
459-673 |
2.02e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.85 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVN-------------ILENFY---PLEGGRVLLDGKPISAYDHKYLHRVISLV 522
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigdKKNNHELITNPYSKKIKNFKELRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 523 SQEP--VLFARSITDNISYGlPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGekgAQLSGGQKQRVAMARALVRNPPV 600
Cdd:PRK13631 122 FQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSYLERSP---FGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 601 LILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAK 673
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHIINS 272
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
462-664 |
2.31e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.40 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGL 541
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFL 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 542 PTVPFEmVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL-DEATSALDAESEYLIQQ 620
Cdd:PTZ00243 1409 EASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQA 1487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 339895785 621 AIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 664
Cdd:PTZ00243 1488 TVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
461-681 |
2.53e-23 |
|
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: 99.15 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITDNIS 538
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlTVEENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTVPFEmvvEAAQKANAHGFIMELQdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:cd03218 98 AVLEIRGLS---KKEREEKLEELLEEFH--ITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 619 QQAIHgNLQKHT--VLIIAHR----LSTVEHAHLIVvldKGRVVQQGTHQQLLAQgglyaKLVQRQMLG 681
Cdd:cd03218 173 QKIIK-ILKDRGigVLITDHNvretLSITDRAYIIY---EGKVLAEGTPEEIAAN-----ELVRKVYLG 232
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
188-451 |
2.94e-23 |
|
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: 101.10 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKS---------------MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTL 252
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEAsflplvpaslgpadpRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 253 IFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvYLRKLQQVYKLNRKEA----AA 408
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERE-RVADASEEYRDANWRAirlrAA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 339895785 409 Y---MYYVWGSGLtllvvqVSILYYGGHLVISG------QMTSGNLIAFIIY 451
Cdd:cd18565 240 FfpvIRLVAGAGF------VATFVVGGYWVLDGpplftgTLTVGTLVTFLFY 285
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
185-448 |
2.96e-23 |
|
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: 100.66 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 185 VAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNC 264
Cdd:cd18555 4 LISILLLSLLLQLLTL---LIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 265 LFRSLVSQETSFFDENRTGDLISRLTSdTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANS-NVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQ 424
Cdd:cd18555 160 LTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAP 239
|
250 260
....*....|....*....|....
gi 339895785 425 VSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18555 240 LLILWIGAYLVINGELTLGELIAF 263
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
459-666 |
3.80e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFARSITDN 536
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:PRK13642 103 VAFGMENqgIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 339895785 615 EYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK13642 176 RQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
182-451 |
6.46e-23 |
|
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: 99.46 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRL 261
Cdd:cd18567 1 KRALLQILLLSLALELFAL---ASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 262 RNCLFRSLVSQETSFFdENR-TGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18567 78 TSNLFRHLLRLPLSYF-EKRhLGDIVSRFGSLDEIQQTLTTGFVEALL-DGLMAILTLVMMFLYSPKLALIVLAAVALYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTL 420
Cdd:cd18567 156 LLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLF 235
|
250 260 270
....*....|....*....|....*....|.
gi 339895785 421 LVVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18567 236 GLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
461-664 |
1.17e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaydhkYLH---RVISLVSQEPVLFaRSIT--D 535
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-----RLHardRKVGFVFQHYALF-RHMTvfD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGLPTVPfemvveAAQKANAHGF---IMELQDGYSTE--TGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:PRK10851 94 NIAFGLTVLP------RRERPNAAAIkakVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 611 DAE-----SEYLIQqaIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 664
Cdd:PRK10851 168 DAQvrkelRRWLRQ--LHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
459-659 |
1.20e-22 |
|
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: 96.67 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-----KPISAydhkylHRVISLVSQEPVLFAR-S 532
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEA------RRRLGFVSDSTGLYDRlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISY-----GLptvpfemvveaaQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:cd03266 95 ARENLEYfaglyGL------------KGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 606 ATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:cd03266 163 PTTGLDVMATRALREFIrQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
451-674 |
1.43e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 103.71 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 451 YEFVLGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDgkpisaydhkylhRVISLVSQEPVLFA 530
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 531 RSITDNISYGLPTVPFEM--VVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:PTZ00243 735 ATVRGNILFFDEEDAARLadAVRVSQlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 608 SALDAE-SEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQlLAQGGLYAKL 674
Cdd:PTZ00243 811 SALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATL 877
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
459-666 |
1.61e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.09 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYL---HRVISLVSQEP--VLFAR-S 532
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNPRlN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYGLPTvpFEMVVEAAQKANAHGFIMElQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PRK15134 381 VLQIIEEGLRV--HQPTLSAAQREQQVIAVME-EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 612 AESEYLIQQAIHGNLQKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK15134 458 KTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
461-682 |
2.68e-22 |
|
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: 96.20 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITDNIS 538
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlTVEENLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTVPFEMVVEAAQKanahgFIMEL---------QdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:COG0410 101 LGAYARRDRAEVRADLE-----RVYELfprlkerrrQ---------RAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 610 LDAeseyLIQQAIHGNLQK-----HTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGlyaklVQRQMLGL 682
Cdd:COG0410 167 LAP----LIVEEIFEIIRRlnregVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLADPE-----VREAYLGV 236
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
189-448 |
3.57e-22 |
|
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: 97.57 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 189 VAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMdqfSTAVVIVCLLAIGSSFAA---GIRGGIFTLIFARLNIRLRNCL 265
Cdd:cd18588 8 LLASLFLQLFALV---TPLFFQVIIDKVLVHRSL---STLDVLAIGLLVVALFEAvlsGLRTYLFSHTTNRIDAELGARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 266 FRSLVSQETSFFDENRTGDLISR----------LTSDT-TMVSDLVSqnINVFLrntvkvtgvvVFMFSLSWQLSLVTFM 334
Cdd:cd18588 82 FRHLLRLPLSYFESRQVGDTVARvrelesirqfLTGSAlTLVLDLVF--SVVFL----------AVMFYYSPTLTLIVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 335 GFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVW 414
Cdd:cd18588 150 SLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQ 229
|
250 260 270
....*....|....*....|....*....|....
gi 339895785 415 GSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18588 230 IVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
459-675 |
3.71e-22 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 102.33 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgrvlldgkpisaydHKYLHRVISLVSQEPVLFARSITDNI 537
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVP--FEMVVEAAqkanahGFIMELQ---DGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 612
Cdd:TIGR00957 720 LFGKALNEkyYQQVLEAC------ALLPDLEilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 613 E-SEYLIQQAI--HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 675
Cdd:TIGR00957 794 HvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
459-686 |
6.39e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.91 E-value: 6.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYLHRVISLVSQEP---VLFARS 532
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNIsyGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTEtgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:PRK10419 108 VREII--REPLRHLLSLDKAERLARASEMLraVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 611 DaeseyLIQQA----IHGNLQKHT---VLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLGL 682
Cdd:PRK10419 183 D-----LVLQAgvirLLKKLQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVLQNAVLPA 257
|
....
gi 339895785 683 QPAA 686
Cdd:PRK10419 258 FPVR 261
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
460-667 |
8.03e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 99.76 E-value: 8.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPV---- 527
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgnrIAMIFQEPMtsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 -LFarSITDNISYGLptvpfeMVVEAAQKANAHGFIMELQDgystETGEKGA---------QLSGGQKQRVAMARALVRN 597
Cdd:COG4172 107 pLH--TIGKQIAEVL------RLHRGLSGAAARARALELLE----RVGIPDPerrldayphQLSGGQRQRVMIAMALANE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 598 PPVLILDEATSALDAeseyLIQQAIHG---NLQKHT---VLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG4172 175 PDLLIADEPTTALDV----TVQAQILDllkDLQRELgmaLLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
459-667 |
8.93e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 8.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNI---LENfyPLEGgRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SIT 534
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLvagLEK--PTEG-QIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGLPT--VPFE----MVVEAAQKANAHGFimelQDGYSTetgekgaQLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:PRK11432 97 ENVGYGLKMlgVPKEerkqRVKEALELVDLAGF----EDRYVD-------QISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 609 ALDAESEYLIQQAIHgNLQKH---TVLIIAHRLS---TVEHAhlIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:PRK11432 166 NLDANLRRSMREKIR-ELQQQfniTSLYVTHDQSeafAVSDT--VIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
461-664 |
9.82e-22 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 94.67 E-value: 9.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSS---CVNILENfypLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPVLFAR-SI 533
Cdd:TIGR02315 20 NINLNINPGEFVAIIGPSGAGKSTllrCINRLVE---PSSGSILLEGTDITKLRGKKLRKLrrrIGMIFQHYNLIERlTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYG----LPTVP--FEMVVEAaQKANAhgfiMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:TIGR02315 97 LENVLHGrlgyKPTWRslLGRFSEE-DKERA----LSALErvGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 606 ATSALDAES-----EYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQL 664
Cdd:TIGR02315 172 PIASLDPKTskqvmDYLKRINKEDGI---TVIINLHQVDLAkKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
460-613 |
1.04e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE---GGRVLLDGKPISAYdhKYLHRVISLVSQEPVLFAR-SITD 535
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRRIGILFQDDLLFPHlSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGLP-TVPFE----MVVEAAQKANAHGFimelqdgystetGEKG-AQLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:COG4136 96 NLAFALPpTIGRAqrraRVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
....
gi 339895785 610 LDAE 613
Cdd:COG4136 164 LDAA 167
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
460-658 |
1.16e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.93 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRviSLVSQEPVLFA-RSITDNIS 538
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---R--GVVFQKDALLPwLNVLDNVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPtvpFEMVVEAAQKANAHGFI--MELQDgysteTGEKG-AQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 615
Cdd:COG4525 99 FGLR---LRGVPKAERRARAEELLalVGLAD-----FARRRiWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 339895785 616 YLIQQAIHG--NLQKHTVLIIAHrlsTVEHAHL----IVVLDK--GRVVQQ 658
Cdd:COG4525 171 EQMQELLLDvwQRTGKGVFLITH---SVEEALFlatrLVVMSPgpGRIVER 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
459-667 |
1.17e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.53 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKYLHRV---ISLVSQEP--VLFARSI 533
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVrktVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYG-----LPTVPFEMVVEAAQKANAhgfiMElqdGYstetgEKGA--QLSGGQKQRVAMARALVRNPPVLILDEA 606
Cdd:PRK13639 97 EEDVAFGplnlgLSKEEVEKRVKEALKAVG----ME---GF-----ENKPphHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895785 607 TSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
459-683 |
2.14e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFARSITDN 536
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGlptvPFEMVVEAAQKANAHGFIMELQDGYstETGEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 615
Cdd:PRK13647 101 VAFG----PVNMGLDKDEVERRVEEALKAVRMW--DFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 616 YLIQQAIHG-NLQKHTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQG-----THQQLLAQGGLYAKLVQRQMLGLQ 683
Cdd:PRK13647 175 ETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLVAQIFEDLP 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
459-682 |
3.88e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.10 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFY---PLEGGRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFARSI 533
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPdnQFVGATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDGystetgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PRK13640 103 GDDVAFGLENraVPRPEMIKIVRDVLADVGMLDYIDS-------EPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 612 AESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT------HQQLLAQGGLYAKLVQRQMLGL 682
Cdd:PRK13640 176 PAGKEQILKLIR-KLKKKnnlTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifsKVEMLKEIGLDIPFVYKLKNKL 254
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
459-659 |
5.28e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCV---NILENFYPLE--GGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFAR-S 532
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYGLP--------TVPFEMVVEAAQKAnahgfimELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILD 604
Cdd:PRK14247 99 IFENVALGLKlnrlvkskKELQERVRWALEKA-------QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 605 EATSALDAESEYLIQQAIHGNLQKHTVLIIAH------RLSTvehahLIVVLDKGRVVQQG 659
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRISD-----YVAFLYKGQIVEWG 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
460-667 |
6.27e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.98 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPvlfarsitdNISY 539
Cdd:COG4167 30 KPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---------NTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 GlPTVPFEMVVEAAQKANAH-----------------GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLI 602
Cdd:COG4167 101 N-PRLNIGQILEEPLRLNTDltaeereerifatlrlvGLLPEHANFYPHM-------LSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895785 603 LDEATSALDAEseyLIQQAIhgNL-----QKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:COG4167 173 ADEALAALDMS---VRSQII--NLmlelqEKLGIsyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
459-612 |
1.05e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.07 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRVIsLVSQEPVLFARSITDNIS 538
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGV-VFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPT--VPFEMVVEAAQKANAhgfimelqdgystETGEKGA------QLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:PRK11248 93 FGLQLagVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
..
gi 339895785 611 DA 612
Cdd:PRK11248 160 DA 161
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
459-667 |
1.16e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHK---YLHRVISLVSQEP--VLFARSI 533
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmKLRESVGMVFQDPdnQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PRK13636 101 YQDVSFGAVNlkLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 612 AESEYLIQQAIHgNLQKH---TVLIIAHRLSTVE-HAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:PRK13636 174 PMGVSEIMKLLV-EMQKElglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
462-667 |
1.64e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 93.11 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH---KYLHRVISLVSQ-------------- 524
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQnpygslnprkkvgq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 525 ---EPVLfarsITDNISyglptvpfemVVEAAQKANAhgfiMELQDGYSTE-TGEKGAQLSGGQKQRVAMARALVRNPPV 600
Cdd:PRK11308 114 ileEPLL----INTSLS----------AAERREKALA----MMAKVGLRPEhYDRYPHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339895785 601 LILDEATSALDAEseylIQQAIHG---NLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:PRK11308 176 VVADEPVSALDVS----VQAQVLNlmmDLQQElglSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
459-666 |
2.37e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.70 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEG----GRVLLDGKPISAY-DHKYLHRVISLVSQEPVLFARS 532
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 612
Cdd:PRK14271 117 IMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 613 ESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK14271 197 TTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
460-635 |
2.41e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK----YL-HRVislvSQEPVLfarSIT 534
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHRN----AMKPAL---TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNIS-----YGlptvPFEMVVEAAQKANAHGFIMELQDGYstetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:PRK13539 92 ENLEfwaafLG----GEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*.
gi 339895785 610 LDAESEYLIQQAIHGNLQKHTVLIIA 635
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
461-660 |
3.72e-20 |
|
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: 89.89 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITDNIS 538
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVPQGREIFPRlTVEENLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTVPfemvveaAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:TIGR03410 98 TGLAALP-------RRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 339895785 619 QQAIhGNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGT 660
Cdd:TIGR03410 171 GRVI-RRLRAEggmAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
459-666 |
4.34e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSScvnILENFYPL---EGGRVLLDGKPISAYDH----KYLHRVISLVSQ--EPVLF 529
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKST---LMQHFNALlkpSSGTITIAGYHITPETGnknlKKLRKKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 530 ARSITDNISYGLPTVPFEmvvEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:PRK13641 100 ENTVLKDVEFGPKNFGFS---EDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 609 ALDAESEYLIQQaIHGNLQK--HTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK13641 175 GLDPEGRKEMMQ-LFKDYQKagHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
459-660 |
4.84e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 92.70 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVISLVSQEPVLFAR-SITDNI 537
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPHmTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGL--PTVPFE----MVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PRK09452 108 AFGLrmQKTPAAeitpRVMEALRMVQLEEFA-----------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 612 AESEYLIQQAIHGnLQKH---TVLIIAH----RLSTVEHahlIVVLDKGRVVQQGT 660
Cdd:PRK09452 177 YKLRKQMQNELKA-LQRKlgiTFVFVTHdqeeALTMSDR---IVVMRDGRIEQDGT 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
459-684 |
6.82e-20 |
|
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: 89.86 E-value: 6.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYLHRVISLVSQE-PVLFARSIT 534
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDsPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGLPTVPFEMVVEAAQKANAHGfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDaes 614
Cdd:TIGR02769 107 VRQIIGEPLRHLTSLDESEQKARIAE-LLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD--- 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 615 eYLIQQAIHGNLQK------HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLGLQP 684
Cdd:TIGR02769 183 -MVLQAVILELLRKlqqafgTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQSAVLPEHP 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
460-636 |
8.24e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpisaydhkylHRVISLVSQEPVLFA-RSITDNIS 538
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDdLTVLDTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTV-------------PFEMVVEAAQKANAHGfIMELQDGYSTET----------------GEKGAQLSGGQKQRVA 589
Cdd:COG0488 84 DGDAELraleaeleeleakLAEPDEDLERLAELQE-EFEALGGWEAEAraeeilsglgfpeedlDRPVSELSGGWRRRVA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 339895785 590 MARALVRNPPVLILDEATSALDAES-----EYLIQqaihgnlQKHTVLIIAH 636
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESiewleEFLKN-------YPGTVLVVSH 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
460-653 |
1.30e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL-DGKPISaydhkylhrvisLVSQEPVLFARSITDNIS 538
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL------------FLPQRPYLPLGTLREALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTVPF--EMVVEAAQKANAHGFIMELQdgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 616
Cdd:COG4178 448 YPATAEAFsdAELREALEAVGLGHLAERLD-----EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
170 180 190
....*....|....*....|....*....|....*..
gi 339895785 617 LIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKG 653
Cdd:COG4178 523 ALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
451-668 |
1.62e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.45 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 451 YEFVlgdCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA-YDHKYLHRV---ISLVSQ-- 524
Cdd:PRK13646 18 YEHQ---AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRPVrkrIGMVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 525 EPVLFARSITDNISYGLPTvpFEMVVEAAqKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPVLIL 603
Cdd:PRK13646 95 ESQLFEDTVEREIIFGPKN--FKMNLDEV-KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 604 DEATSALDAESEYLIQQAIHgNLQ---KHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQG 668
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLK-SLQtdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
459-664 |
1.78e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.05 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SITDNI 537
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVPFEMVvEAAQKANAHGFIMELQDGysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:PRK11607 113 AFGLKQDKLPKA-EIASRVNEMLGLVHMQEF----AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 339895785 618 IQQAIHGNLQK--HTVLIIAH-RLSTVEHAHLIVVLDKGRVVQQGTHQQL 664
Cdd:PRK11607 188 MQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
461-666 |
1.80e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.16 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITDNIs 538
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHKRARLGIGYLPQEASIFRKlTVEDNI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 yglptvpfEMVVE------AAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD- 611
Cdd:COG1137 100 --------LAVLElrklskKEREERLEELLEEFGITHLRKS--KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDp 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 612 -AESEylIQQAIHgNLQKH--TVLIIAHR----LSTVEHAHLIvvlDKGRVVQQGTHQQLLA 666
Cdd:COG1137 170 iAVAD--IQKIIR-HLKERgiGVLITDHNvretLGICDRAYII---SEGKVLAEGTPEEILN 225
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
188-450 |
2.77e-19 |
|
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: 88.79 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18566 7 VLLASLFINILALA---TPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrntvKVTGVVVF---MFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18566 84 HLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALL----DLPFVLIFlglIWYLGGKLVLVPLVLLGLFVLVAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQ----VYKLNRKEAAAYMyyvwGSGLTL 420
Cdd:cd18566 160 LLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANaayaGFKVAKINAVAQT----LGQLFS 235
|
250 260 270
....*....|....*....|....*....|
gi 339895785 421 LVVQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18566 236 QVSMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
460-635 |
2.91e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.39 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsAYDHKYLHRVISLVSQEPVLFAR-SITDNIS 538
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTVPFEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:cd03231 96 FWHADHSDEQVEEALARVGLNGF-----------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170
....*....|....*..
gi 339895785 619 QQAIHGNLQKHTVLIIA 635
Cdd:cd03231 165 AEAMAGHCARGGMVVLT 181
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
462-659 |
3.22e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.65 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SITDNISY 539
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNlSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 GLPTVPfemvvEAAQKANAhgFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD-AESEYLI 618
Cdd:PRK15439 110 GLPKRQ-----ASMQKMKQ--LLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLF 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 339895785 619 QQaIHGNLQK-HTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQG 659
Cdd:PRK15439 181 SR-IRELLAQgVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
459-621 |
4.16e-19 |
|
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: 86.72 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSS---CvnILENFYPlEGGRVLL--DGKPI---SAYDHKYLH---RVISLVSQepv 527
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTllkC--IYGNYLP-DSGSILVrhDGGWVdlaQASPREILAlrrRTIGYVSQ--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 lFARSItdnisyglPTVP-FEMVVEAAqkanahgfimeLQDGYSTETG-EKGAQL------------------SGGQKQR 587
Cdd:COG4778 101 -FLRVI--------PRVSaLDVVAEPL-----------LERGVDREEArARARELlarlnlperlwdlppatfSGGEQQR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895785 588 VAMARALVRNPPVLILDEATSALDAESE----YLIQQA 621
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEA 198
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
459-665 |
4.41e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.41 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG------GRVLLDGKPISAYDHKYLHRVISLVSQEPVLFAR- 531
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 SITDNISYGLPTVPFE-------MVVEAAQKAnahGFIMELQDGYSTetgeKGAQLSGGQKQRVAMARALVRNPPVLILD 604
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKekreikkIVEECLRKV---GLWKEVYDRLNS----PASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 605 EATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLL 665
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
460-635 |
4.46e-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: 85.87 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVISLVSQEPVLFAR-SITDNIS 538
Cdd:TIGR01189 17 EGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YGLPTVPFE--MVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 616
Cdd:TIGR01189 96 FWAAIHGGAqrTIEDALAAVGLTGF-----------EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170
....*....|....*....
gi 339895785 617 LIQQAIHGNLQKHTVLIIA 635
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLT 183
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
182-450 |
4.79e-19 |
|
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: 88.03 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRL 261
Cdd:cd18782 1 RRALIEVLALSFVVQLLGL---ANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 262 RNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 341
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 342 VSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEE----EEAEVYLRKLQQVYKLNRKEAAAYMYyvwgSG 417
Cdd:cd18782 157 LTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELkarwRWQNRYARSLGEGFKLTVLGTTSGSL----SQ 232
|
250 260 270
....*....|....*....|....*....|...
gi 339895785 418 LTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18782 233 FLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRI 265
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
459-684 |
6.08e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpISAYDHKYLH---RVISLVSQEP--VLFARSI 533
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQgirKLVGIVFQNPetQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYG-----LPTVPFEMVVEAAqkanahgfIMELQDGYSTETGEKgaQLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:PRK13644 96 EEDLAFGpenlcLPPIEIRKRVDRA--------LAEIGLEKYRHRSPK--TLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 609 ALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLyaklvqrQMLGLQP 684
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL-------QTLGLTP 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
469-655 |
7.08e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 469 GKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkyLHRVISLVSQEPVLFA-RSITDNISYGLptvpfe 547
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMFQDARLLPwKKVIDNVGLGL------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 548 mvvEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQ 627
Cdd:PRK11247 107 ---KGQWRDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQ 181
|
170 180 190
....*....|....*....|....*....|.
gi 339895785 628 KH--TVLIIAHRLS-TVEHAHLIVVLDKGRV 655
Cdd:PRK11247 182 QHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
459-665 |
7.37e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.32 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFAR-SI 533
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYG--LPTVPFEMVVEAAQKANAHGFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PRK10070 124 LDNTAFGmeLAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 612 A------ESEYLIQQAIHgnlqKHTVLIIAHRL-STVEHAHLIVVLDKGRVVQQGTHQQLL 665
Cdd:PRK10070 197 PlirtemQDELVKLQAKH----QRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
459-676 |
7.97e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.58 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGGRVLLDGKpisaydhkylhrvISLVSQEPVLFARSITDNI 537
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------------VAYVPQVSWIFNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVPFEMVVEAAQKANAHGfiMELQDGYS-TETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE-SE 615
Cdd:PLN03232 700 LFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAH 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 616 YLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQ 676
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
457-673 |
1.56e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 457 DCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEP--VLFARSIT 534
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYG-----LPTVPFEMVVEAAQKANAhgfIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:PRK13652 98 QDIAFGpinlgLDEETVAHRVSSALHMLG---LEELRD-------RVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 610 LDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAK 673
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
461-669 |
1.71e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.70 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKylhRVISLVSQEPVLFAR-SITDNISY 539
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDR---RRIGYLPEERGLYPKmKVGEQLVY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 -----GLPtvpfemvvEAAQKANAHGFI--MELQDgYSTETGEKgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDA 612
Cdd:COG4152 95 larlkGLS--------KAEAKRRADEWLerLGLGD-RANKKVEE---LSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 613 ESEYLIQQAIhgnLQKH----TVLIIAHRLSTVE----HahlIVVLDKGRVVQQGTHQQLLAQGG 669
Cdd:COG4152 163 VNVELLKDVI---RELAakgtTVIFSSHQMELVEelcdR---IVIINKGRKVLSGSVDEIRRQFG 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
461-664 |
1.89e-18 |
|
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: 84.73 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVSQEPVLfARSIT--DNIS 538
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV-DDELTgwENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 -----YGLPTvpfemvVEAAQKanahgfIMELQDGYstETGEKGAQL----SGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:cd03265 96 iharlYGVPG------AERRER------IDELLDFV--GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 610 LDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 664
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
459-660 |
3.09e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.48 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY--LHRVISLVSQEP--VLFARSIT 534
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGlptvPFEMVVEAAQKANAHGFIMELQdGYSTET-GEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALD- 611
Cdd:PRK13637 103 KDIAFG----PINLGLSEEEIENRVKRAMNIV-GLDYEDyKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDp 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 339895785 612 -AESEYLIQ-QAIHGNlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 660
Cdd:PRK13637 178 kGRDEILNKiKELHKE-YNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
460-645 |
3.11e-18 |
|
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: 82.59 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVlldgkpisaydHKYLHRVISLVSQEPVLFARSITDNISY 539
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFLPQRPYLPLGTLREQLIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 glptvPFEMVveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEyliq 619
Cdd:cd03223 87 -----PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE---- 127
|
170 180
....*....|....*....|....*...
gi 339895785 620 QAIHGNLQKH--TVLIIAHRlSTVEHAH 645
Cdd:cd03223 128 DRLYQLLKELgiTVISVGHR-PSLWKFH 154
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
416-660 |
3.54e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.82 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 416 SGLTLLVVQVSilYYGGHLVISGqmtsgnliafiiyefvlgdcmenVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPL 495
Cdd:PRK11650 2 AGLKLQAVRKS--YDGKTQVIKG-----------------------IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 496 EGGRVLLDGKPISAYDHKylHRVISLVSQEPVLFAR-SITDNISYGLPT--VP----FEMVVEAAQkanahgfIMELQ-- 566
Cdd:PRK11650 57 TSGEIWIGGRVVNELEPA--DRDIAMVFQNYALYPHmSVRENMAYGLKIrgMPkaeiEERVAEAAR-------ILELEpl 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 567 -DgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA--------EseylIQQaihgnLQKhtvliiahR 637
Cdd:PRK11650 128 lD-------RKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvqmrlE----IQR-----LHR--------R 183
|
250 260 270
....*....|....*....|....*....|....*
gi 339895785 638 LST----VEH--------AHLIVVLDKGRVVQQGT 660
Cdd:PRK11650 184 LKTtslyVTHdqveamtlADRVVVMNGGVAEQIGT 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
459-681 |
5.91e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.79 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITDN 536
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 IsygLPTVPFEMVVEAAQKANAHGFIME------LQDGYstetgekGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:PRK10895 99 L---MAVLQIRDDLSAEQREDRANELMEefhiehLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 611 DAESEYLIQQAI-HGNLQKHTVLIIAHR----LSTVEHAHLIvvlDKGRVVQQGTHQQLLAQgglyaKLVQRQMLG 681
Cdd:PRK10895 169 DPISVIDIKRIIeHLRDSGLGVLITDHNvretLAVCERAYIV---SQGHLIAHGTPTEILQD-----EHVKRVYLG 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
454-660 |
6.97e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.98 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 454 VLGDcmenVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFAR-S 532
Cdd:COG4604 16 VLDD----VSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYG-------LPTVPFEMVVEAAqkanahgfI-----MELQDGYSTEtgekgaqLSGGQKQR--VAMarALVRNP 598
Cdd:COG4604 92 VRELVAFGrfpyskgRLTAEDREIIDEA--------IayldlEDLADRYLDE-------LSGGQRQRafIAM--VLAQDT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 599 PVLILDEATSALD----AESEYLIQQAIHgNLQKhTVLIIAHRL---STveHAHLIVVLDKGRVVQQGT 660
Cdd:COG4604 155 DYVLLDEPLNNLDmkhsVQMMKLLRRLAD-ELGK-TVVIVLHDInfaSC--YADHIVAMKDGRVVAQGT 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
462-665 |
7.43e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.74 E-value: 7.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRVIS-LVSQEPVLFARSITDNISYG 540
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQG-EILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 LPTVPFEMVVEA--AQKANAhgfiMELQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NPP--VLILDEATSALD 611
Cdd:COG4138 94 QPAGASSEAVEQllAQLAEA----LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 612 aeseyLIQQAIHGNL------QKHTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLL 665
Cdd:COG4138 166 -----VAQQAALDRLlrelcqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
459-636 |
7.50e-18 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 83.28 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLhrvisLVSQEPVLFA-RSITDNI 537
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVPFEMVVEAAQKANAHGFIMElqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALV---GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|.
gi 339895785 618 IQQAIHGNLQKH--TVLIIAH 636
Cdd:TIGR01184 153 LQEELMQIWEEHrvTVLMVTH 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
462-657 |
7.84e-18 |
|
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: 83.25 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENfypLE---GGRVLLDGKPISAYDHKYLHRV----ISLVSQE----PVLFA 530
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAG---LDrptSGTVRLAGQDLFALDEDARARLrarhVGFVFQSfqllPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 531 RsitDNIsyglpTVPFEM--VVEAAQKANAhgfimELQD-GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:COG4181 108 L---ENV-----MLPLELagRRDARARARA-----LLERvGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 339895785 608 SALDAESEYLIQQAIHG-NLQKHTVLIIA-HRLSTVEHAHLIVVLDKGRVVQ 657
Cdd:COG4181 175 GNLDAATGEQIIDLLFElNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
459-659 |
1.03e-17 |
|
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: 82.33 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHkylHRvISLVSQEPVLF-ARSITDNI 537
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR---NR-IGYLPEERGLYpKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SY-----GLPTvpfemvvEAAQKANAHGF----IMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:cd03269 92 VYlaqlkGLKK-------EEARRRIDEWLerleLSEYAN-------KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 339895785 609 ALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
461-665 |
1.22e-17 |
|
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: 83.21 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNIL--ENfYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEpvlFARSITDNIs 538
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLItgDL-PPTYGNDVRLFGERRGGEDVWELRKRIGLVSPA---LQLRFPRDE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 yglpTVpFEMV-------------VEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:COG1119 96 ----TV-LDVVlsgffdsiglyrePTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 606 ATSALDAES-EYLIQ--QAIHGNLQKHTVLiIAHRL----STVEHAhliVVLDKGRVVQQGTHQQLL 665
Cdd:COG1119 169 PTAGLDLGArELLLAllDKLAAEGAPTLVL-VTHHVeeipPGITHV---LLLKDGRVVAAGPKEEVL 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
460-659 |
1.31e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.21 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKS-SCVNILENFYP---LEGGRVLLDGKPISAYDHKylHRVISLVSQEPvlfaRSITD 535
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVAPCALR--GRKIATIMQNP----RSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NI----SYGLPTvpfemvVEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQRVAMARALVRNPPVLILDEA 606
Cdd:PRK10418 94 PLhtmhTHARET------CLALGKPADDATLTAALEAVGLENAARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 607 TSALDAESEYLIQQAIHGNLQKHT--VLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
461-671 |
1.35e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP---LEGGRVLLDGKPIsayDHKYLHRVISLVSQepvlfarsitDNI 537
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI---DAKEMRAISAYVQQ----------DDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVPFEMVVEAAQKANAHGFI-------------MELQDGYSTETGEKGAQ--LSGGQKQRVAMARALVRNPPVLI 602
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRRVTKkekrervdevlqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 603 LDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLST--VEHAHLIVVLDKGRVVQQGTHQQL---LAQGGLY 671
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAvpfFSDLGHP 264
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
459-684 |
1.53e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.14 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE--GGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SIT 534
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALdAES 614
Cdd:PRK13549 101 ENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPAT--PVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TES 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339895785 615 EYLIQQAIHGNLQKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVqqGTH-QQLLAQGGLYAKLVQRQMLGLQP 684
Cdd:PRK13549 178 ETAVLLDIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGRHI--GTRpAAGMTEDDIITMMVGRELTALYP 249
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
261-451 |
1.71e-17 |
|
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: 83.62 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 261 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAaymyyvWgSGLTL 420
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTR------W-NAKTF 233
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895785 421 LVVQVS-------ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18554 234 SAVNTItdlapllVIGFAAYLVIEGNLTVGTLVAFVGY 271
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
459-666 |
4.46e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISL-----------VSQEPV 527
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVpqfdnldpdftVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 LFARSitdnisYGLPT------VPfeMVVEAA---QKANAhgfimelqdgystetgeKGAQLSGGQKQRVAMARALVRNP 598
Cdd:PRK13537 103 VFGRY------FGLSAaaaralVP--PLLEFAkleNKADA-----------------KVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 599 PVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
454-660 |
4.48e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.02 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 454 VLGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI----SAYDHKYLHRVISLVSQepvlF 529
Cdd:PRK11629 20 VQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRNQKLGFIYQ----F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 530 ARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:PRK11629 96 HHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 339895785 610 LDAESEYLIQQAIhGNL---QKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 660
Cdd:PRK11629 176 LDARNADSIFQLL-GELnrlQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
461-659 |
4.56e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 80.78 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILEN---FYPLEGGRVLLDGKPISAYDHKYlhrVISLVSQEPVlFARSIT--D 535
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQK---CVAYVRQDDI-LLPGLTvrE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYglpTVPFEMVVEA--AQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:cd03234 101 TLTY---TAILRLPRKSsdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 339895785 614 SEYLI----QQAIHGNlqkHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQG 659
Cdd:cd03234 178 TALNLvstlSQLARRN---RIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
459-660 |
5.07e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 5.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQE-PVLFARSITDN 536
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYG-LPT-----VPF----EMVVEAAqkanahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 606
Cdd:PRK09700 101 LYIGrHLTkkvcgVNIidwrEMRVRAA--------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 607 TSAL-DAESEYLIqqAIHGNLQKH--TVLIIAHRLstvehAHLIVVLDKGRVVQQGT 660
Cdd:PRK09700 173 TSSLtNKEVDYLF--LIMNQLRKEgtAIVYISHKL-----AEIRRICDRYTVMKDGS 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
459-659 |
5.78e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.91 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI---SAYDHKYLHRVISLVSQEPV--LFAR-S 532
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYasLDPRqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYGLpTVPFEMVVEAAQKANAH-----GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:PRK10261 420 VGDSIMEPL-RVHGLLPGKAAAARVAWllervGLLPEHAWRYPHE-------FSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 608 SALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:PRK10261 492 SALDVSIRGQIINLLL-DLQRDfgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
459-684 |
1.26e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.34 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP--LEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SIT 534
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGaQLSGGQKQRVAMARALVRNPPVLILDEATSAL-DA 612
Cdd:TIGR02633 97 ENIFLGNEiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEK 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 613 ESEYLIQqaIHGNLQKHTV--LIIAHRLSTVEhahliVVLDKGRVVQQGTH-----QQLLAQGGLYAKLVQRQMLGLQP 684
Cdd:TIGR02633 176 ETEILLD--IIRDLKAHGVacVYISHKLNEVK-----AVCDTICVIRDGQHvatkdMSTMSEDDIITMMVGREITSLYP 247
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
461-660 |
1.45e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.56 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAY----DHKYLHRVISLVSQ--EPVLFARSIT 534
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQIRKKVGLVFQfpESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALDA- 612
Cdd:PRK13649 105 KDVAFGPQN--FGVSQEEAEALAREKLALV---GISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPk 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 339895785 613 ---ESEYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 660
Cdd:PRK13649 180 grkELMTLFKKLHQSGM---TIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
457-666 |
1.53e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.22 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 457 DCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPvlfARSITDN 536
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYG-LPTVPFEMVVEAAQKANAHGFIMEL-QDGYSTE-TGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:PRK15112 104 QRISqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 614 seyLIQQAIHGNL---QKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK15112 184 ---MRSQLINLMLelqEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
461-661 |
1.76e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCV---NILEnfYPLEGGRVLLDGK-----PISAYDHKYLHRVISLVSQEPVLFA-R 531
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLrvlNLLE--TPDSGQLNIAGHQfdfsqKPSEKAIRLLRQKVGMVFQQYNLWPhL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 SITDNISYGlPTVPFEMVVEAAQ-KANAHGFIMELQDgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:COG4161 98 TVMENLIEA-PCKVLGLSKEQAReKAMKLLARLRLTD----KADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 611 DAESEYLIQQAIHgNLQKH--TVLIIAHRlstVEHAHLI----VVLDKGRVVQQGTH 661
Cdd:COG4161 173 DPEITAQVVEIIR-ELSQTgiTQVIVTHE---VEFARKVasqvVYMEKGRIIEQGDA 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
461-662 |
2.17e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCV---NILEnfYPLEG-----GRVLLDGKPISAYDHKYLHRVISLVSQEPVLFAR- 531
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLrvlNLLE--MPRSGtlniaGNHFDFSKTPSDKAIRELRRNVGMVFQQYNLWPHl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 SITDNisygLPTVPfeMVVEAAQKANAHGFIMELQDGYS-TETGEK-GAQLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:PRK11124 98 TVQQN----LIEAP--CRVLGLSKDQALARAEKLLERLRlKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 610 LDAESEYLIQQAIHGNLQKH-TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQ 662
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
462-665 |
4.37e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR-VISLVSQEPVLFARSITDNISYG 540
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLPQQLPAAEGMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 lpTVPF------------EMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:PRK10575 110 --RYPWhgalgrfgaadrEKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 609 ALDAESEYLIQQAIHGNLQKH--TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLL 665
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
461-688 |
4.58e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEP--VLFARSIT 534
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVVSSTSKQKEIKPVrkkVGVVFQFPesQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:PRK13643 104 KDVAFGPQN--FGIPKEKAEKIAAEKLEMV---GLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 614 SEYLIQ---QAIHGNLQkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQgglyAKLVQRQMLGLQPAADF 688
Cdd:PRK13643 179 ARIEMMqlfESIHQSGQ--TVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE----VDFLKAHELGVPKATHF 251
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
457-667 |
6.58e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.09 E-value: 6.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 457 DCMENVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEGGrVLLDGKPIS----------AYDHKYLHRV---IS 520
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK--PSEGS-IVVNGQTINlvrdkdgqlkVADKNQLRLLrtrLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 521 LVSQEPVLFAR-SITDNISYGLPTVPFEMVVEAAQKA----NAHGFIMELQDGYStetgekgAQLSGGQKQRVAMARALV 595
Cdd:PRK10619 96 MVFQHFNLWSHmTVLENVMEAPIQVLGLSKQEARERAvkylAKVGIDERAQGKYP-------VHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 596 RNPPVLILDEATSALDAE--SEYL-IQQAIHGnlQKHTVLIIAHRLSTVEH--AHLIvVLDKGRVVQQGTHQQLLAQ 667
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPElvGEVLrIMQQLAE--EGKTMVVVTHEMGFARHvsSHVI-FLHQGKIEEEGAPEQLFGN 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
451-674 |
1.06e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 451 YEFvlgDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA-----YDHKYLHRVISLVSQE 525
Cdd:PRK13645 22 FEF---KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRKEIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 526 P--VLFARSITDNISYGlptvPFEMvveAAQKANAHGFIMELQDGYS--TETGEKGA-QLSGGQKQRVAMARALVRNPPV 600
Cdd:PRK13645 99 PeyQLFQETIEKDIAFG----PVNL---GENKQEAYKKVPELLKLVQlpEDYVKRSPfELSGGQKRRVALAGIIAMDGNT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 601 LILDEATSALD--AESEYL-IQQAIHGNlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 674
Cdd:PRK13645 172 LVLDEPTGGLDpkGEEDFInLFERLNKE-YKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFSNQELLTKI 248
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
461-659 |
1.26e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.30 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SITDNISY 539
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMVFQSYALYPHlSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 GLPTVPFEMVvEAAQKANAHGFImeLQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEylIQ 619
Cdd:PRK11000 99 GLKLAGAKKE-EINQRVNQVAEV--LQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 339895785 620 QAI-----HGNLQKhTVLIIAHrlSTVEH---AHLIVVLDKGRVVQQG 659
Cdd:PRK11000 172 MRIeisrlHKRLGR-TMIYVTH--DQVEAmtlADKIVVLDAGRVAQVG 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
459-687 |
1.49e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPvlfarsitdnis 538
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 yglpTVPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ------------------LSGGQKQRVAMARALVRNPPV 600
Cdd:PRK09536 87 ----SLSFEFDVRQVVEMGRTPHRSRF--DTWTETDRAAVEramertgvaqfadrpvtsLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 601 LILDEATSALD--------------AESEYLIQQAIHGnlqkhtvLIIAHRlstveHAHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK09536 161 LLLDEPTASLDinhqvrtlelvrrlVDDGKTAVAAIHD-------LDLAAR-----YCDELVLLADGRVRAAGPPADVLT 228
|
250 260
....*....|....*....|.
gi 339895785 667 QGGLYAKLVQRQMLGLQPAAD 687
Cdd:PRK09536 229 ADTLRAAFDARTAVGTDPATG 249
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
459-665 |
2.90e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydHKYLHRV-ISLVSQ----EPVLFARsi 533
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARArIGVVPQfdnlDLEFTVR-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 tDNI-----SYGLPTVPFEMVV----EAAQ---KANAhgfimelqdgystetgeKGAQLSGGQKQRVAMARALVRNPPVL 601
Cdd:PRK13536 133 -ENLlvfgrYFGMSTREIEAVIpsllEFARlesKADA-----------------RVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 602 ILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLL 665
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
461-668 |
2.97e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.98 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA----YDHKYLHRVISLVSQ--EPVLFARSIT 534
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKPLRKKVGIVFQfpEHQLFEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGlPT---VPFEmvvEAAQKANAhgfIMELQdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:PRK13634 105 KDICFG-PMnfgVSEE---DAKQKARE---MIELV-GLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 611 DAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQG 668
Cdd:PRK13634 177 DPKGRKEMMEMFY-KLHKEkglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
459-656 |
3.34e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLHRVISLVSQEP-VLFARSIT 534
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD- 611
Cdd:PRK10908 98 DNVA--IP-----LIIAGASGDDIRRRVSAALDkvGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDd 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 339895785 612 AESEYLIQQAIHGNLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVV 656
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATHDIGLISrRSYRMLTLSDGHLH 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
460-674 |
3.37e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI----------SLVSQEPVLF 529
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpgiktELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 530 ARSITDNISYglptvpfEMVVEAAQKANAHGFiMELqdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:PRK13538 98 YQRLHGPGDD-------EALWEALAQVGLAGF-EDV----------PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 610 LDaeseyliqqaihgnlqKHTVLIIAHRLStvEHAhlivvlDKGRVVQQGTHQQLLAQGGLYAKL 674
Cdd:PRK13538 160 ID----------------KQGVARLEALLA--QHA------EQGGMVILTTHQDLPVASDKVRKL 200
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
188-395 |
5.07e-15 |
|
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: 76.39 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVtfmgFPIIMMVSNIYG 347
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV----LPPLLVVYYLLQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 339895785 348 KYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEEEEAEVYLRKL 395
Cdd:cd18580 157 RYYLRTSRQLRrlESESRSPlySHFSETLSGLSTIRAFGWQERFIEENLRLL 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
434-664 |
5.17e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.41 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 434 LVISG-QMTSGNLIAfiiyefvlgdcMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA--- 509
Cdd:PRK11300 6 LSVSGlMMRFGGLLA-----------VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 510 -----------YDHKYLHRVISLVsqEPVLFA--RSITDNISYGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTETG 574
Cdd:PRK11300 75 hqiarmgvvrtFQHVRLFREMTVI--ENLLVAqhQQLKTGLFSGLLKTPAFRRAESEALDRAATWLerVGLLEHANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 575 ekgaQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKH---TVLIIAHRLSTV----EHahlI 647
Cdd:PRK11300 153 ----NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELI-AELRNEhnvTVLLIEHDMKLVmgisDR---I 224
|
250
....*....|....*..
gi 339895785 648 VVLDKGRVVQQGTHQQL 664
Cdd:PRK11300 225 YVVNQGTPLANGTPEEI 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
460-655 |
5.21e-15 |
|
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: 73.62 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEP----VLFARSIT 534
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYGlptvpfemvveaaqkanahgfimelqdgystetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:cd03215 97 ENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 339895785 615 eyliQQAIHGNLQK-----HTVLIIAHRLSTVEH-AHLIVVLDKGRV 655
Cdd:cd03215 140 ----KAEIYRLIREladagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
461-677 |
7.60e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.72 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPV--------LF 529
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSpDERARAGIFLAFQYPVeipgvsvsNF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 530 ARSITDNISYGLPTVPfEMVVEAAQKANAHGFIMELQDGYSTETgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:COG0396 98 LRTALNARRGEELSAR-EFLKLLKEKMKELGLDEDFLDRYVNEG------FSGGEKKRNEILQMLLLEPKLAILDETDSG 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 610 LDAE-----SEYLiqQAIHGnlQKHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQGTH---QQLLAQGglYAKLVQR 677
Cdd:COG0396 171 LDIDalrivAEGV--NKLRS--PDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKelaLELEEEG--YDWLKEE 242
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
462-664 |
9.38e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.90 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPV--LFAR-SITD 535
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLasLNPRmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGL----PTVPFEMVVEAAQKANAH-GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:PRK15079 120 IIAEPLrtyhPKLSRQEVKDRVKAMMLKvGLLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 611 D----AESEYLIQQaihgnLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 664
Cdd:PRK15079 193 DvsiqAQVVNLLQQ-----LQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
460-677 |
1.16e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.64 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFAR-SITDNIS 538
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YG-LPTVPF--------EMVVEAAQKANAhgfIMELQDgYSTETgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSA 609
Cdd:PRK10253 104 RGrYPHQPLftrwrkedEEAVTKAMQATG---ITHLAD-QSVDT------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 610 LDAESEY-LIQQAIHGNLQK-HTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLAqgglyAKLVQR 677
Cdd:PRK10253 174 LDISHQIdLLELLSELNREKgYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT-----AELIER 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
461-653 |
1.65e-14 |
|
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: 72.66 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILEN--FYPLEGGRVLLDGKPISaydhKYLHRVISLVSQEPVLFarsitdnis 538
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD----KNFQRSTGYVEQQDVHS--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 yglptvPFEMVVEAAQ-KANAHGfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:cd03232 92 ------PNLTVREALRfSALLRG-------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 339895785 618 IQQAIHgNLQKH--TVLIIAHRLSTV--EHAHLIVVLDKG 653
Cdd:cd03232 147 IVRFLK-KLADSgqAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
460-687 |
1.75e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.67 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKS----SCVNILEN---FYPleGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVl 528
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYP--SGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPM- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 529 farsITDNISYGLPTVPFE-------MVVEAAQkanahGFIMELQDgystETGEKGA---------QLSGGQKQRVAMAR 592
Cdd:PRK15134 103 ----VSLNPLHTLEKQLYEvlslhrgMRREAAR-----GEILNCLD----RVGIRQAakrltdyphQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 593 ALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQG 668
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLR-ELQQElnmGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAP 248
|
250
....*....|....*....
gi 339895785 669 glyAKLVQRQMLGLQPAAD 687
Cdd:PRK15134 249 ---THPYTQKLLNSEPSGD 264
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
457-656 |
2.45e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.69 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 457 DCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFAR- 531
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehFGFIFQRYHLLSHl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 SITDNISygLPTVpFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PRK10535 102 TAAQNVE--VPAV-YAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 339895785 612 AESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVV 656
Cdd:PRK10535 177 SHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
438-667 |
3.17e-14 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 73.35 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 438 GQMTSGNLIAfiIYEFVLGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHR 517
Cdd:cd03289 1 GQMTVKDLTA--KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 518 VISLVSQEPVLFARSITDNIS-YGLPTVpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVR 596
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDpYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 597 NPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
461-656 |
3.89e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.20 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAY-DHKYlHRVISLVSQEPVLfarsitdnisy 539
Cdd:COG1101 24 GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEYKR-AKYIGRVFQDPMM----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 540 GlpTVPfEMVVE-----AAQKANAHGFI-------------------MELQDGYSTETGekgaQLSGGQKQRVAMARALV 595
Cdd:COG1101 92 G--TAP-SMTIEenlalAYRRGKRRGLRrgltkkrrelfrellatlgLGLENRLDTKVG----LLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 596 RNPPVLILDEATSALD---AE-----SEYLIQQaihgnlQKHTVLIIAHRLS-TVEHAHLIVVLDKGRVV 656
Cdd:COG1101 165 TKPKLLLLDEHTAALDpktAAlvlelTEKIVEE------NNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
461-667 |
3.91e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI---SAYDHkyLHRVISLVSQE----PVLfarSI 533
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAA--LAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYG-LPTvPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 612
Cdd:PRK11288 97 AENLYLGqLPH-KGGIVNRRLLNYEAREQLEHLGVDIDPDT--PLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 613 -ESEYLIqqAIHGNL--QKHTVLIIAHRLSTV-EHAHLIVVLDKGRVV------QQGTHQQLLAQ 667
Cdd:PRK11288 174 rEIEQLF--RVIRELraEGRVILYVSHRMEEIfALCDAITVFKDGRYVatfddmAQVDRDQLVQA 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
462-664 |
5.93e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.35 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFY---PLEGGRVLLDGKPIS-----AYDHKYLHRVISLVSQEPVLFAR-S 532
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIRKSRANTGYIFQQFNLVNRlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYG-LPTVPFEMVV----EAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:PRK09984 103 VLENVLIGaLGSTPFWRTCfswfTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 608 SALDAESEYLIQQAIHGNLQKH--TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQL 664
Cdd:PRK09984 181 ASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
460-650 |
9.33e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 70.34 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpisaydhkylHRVISLVSQ---EPVLFARSITDN 536
Cdd:NF040873 9 HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVPDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGL---------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:NF040873 78 VAMGRwarrglwrrLTRDDRAAVDDALER------VGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 339895785 608 SALDAESEYLIQQAI---HGnlQKHTVLIIAHRLSTVEHAHLIVVL 650
Cdd:NF040873 148 TGLDAESRERIIALLaeeHA--RGATVVVVTHDLELVRRADPCVLL 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
459-666 |
1.19e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.07 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNIL---ENFYPLEG---------------GRVLLDGKPISAYDHKYLHRVIS 520
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmDQYEPTSGriiyhvalcekcgyvERPSKVGEPCPVCGGTLEPEEVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 521 LVSQEPVLFARsITDNIS---------YGLPTVpFEMVVEAAQKAnahgfimelqdGYSTETGEKGA------------- 578
Cdd:TIGR03269 96 FWNLSDKLRRR-IRKRIAimlqrtfalYGDDTV-LDNVLEALEEI-----------GYEGKEAVGRAvdliemvqlshri 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 579 -----QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEH-AHLIVVL 650
Cdd:TIGR03269 163 thiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWL 242
|
250
....*....|....*.
gi 339895785 651 DKGRVVQQGTHQQLLA 666
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVA 258
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
186-395 |
1.37e-13 |
|
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: 72.18 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 186 AFLVAASFFLIVAA--LGETFLPYYTGRAIDGIViQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIF---TLIFARlniR 260
Cdd:cd18605 1 LILILLSLILMQASrnLIDFWLSYWVSHSNNSFF-NFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFaygGLRAAR---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 261 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTG-VVVFMFSLSWQLSLVtfmgFPII 339
Cdd:cd18605 77 LHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGyLVVICYQLPWLLLLL----LPLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 340 MMVSNIYgKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEEEEAEVYLRKL 395
Cdd:cd18605 153 FIYYRIQ-RYYRATSRELKrlNSVNLSPlyTHFSETLKGLVTIRAFRKQERFLKEYLEKL 211
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
184-448 |
1.50e-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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 71.78 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 184 DVAFlvaASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFST-AVVIVCLLAIGSSFAAgIRGGIFTLIFARLNIRLR 262
Cdd:cd18783 6 DVAI---ASLILHVLAL---APPIFFQIVIDKVLVHQSYSTLYVlTIGVVIALLFEGILGY-LRRYLLLVATTRIDARLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 263 NCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNinvFLRNTVKVTGVVVF---MFSLSWQLSLVTFMGFPII 339
Cdd:cd18783 79 LRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQ---LFGTLLDATSLLVFlpvLFFYSPTLALVVLAFSALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 340 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMyyvWGSGLT 419
Cdd:cd18783 155 ALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSN---WPQTLT 231
|
250 260 270
....*....|....*....|....*....|..
gi 339895785 420 LL---VVQVSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18783 232 GPlekLMTVGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
462-684 |
2.23e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRVIS-LVSQEPVLF--------ARS 532
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAGQPLEAWSAAELARHRAyLSQQQTPPFampvfqylTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNISYGLPTVPFEMVVEAAQkanahgfimeLQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NP--PVLILDE 605
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 606 ATSALDAESEYLIQQAIHGNLQKH-TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLAQGGL---YAKLVQRQML 680
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGiAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENLaqvFGVNFRRLDV 239
|
....
gi 339895785 681 GLQP 684
Cdd:PRK03695 240 EGHP 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
459-667 |
2.93e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.89 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY-LHRVISLVSQEP--VLFARSITD 535
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNPdnQIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYG---LPTVPFEM---VVEAAQKANAHGFimelqdgystetgEKGAQ--LSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:PRK13633 106 DVAFGpenLGIPPEEIrerVDESLKKVGMYEY-------------RRHAPhlLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 608 SALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
460-656 |
4.53e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVS----QEPVLF 529
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAG-----IAYVPedrkGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 530 ARSITDNISygLPTVP----FEMVVEAAQKANAHGFIMELQ---DGYSTETGekgaQLSGGQKQRVAMARALVRNPPVLI 602
Cdd:COG1129 344 DLSIRENIT--LASLDrlsrGGLLDRRRERALAEEYIKRLRiktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 603 LDEATSALDAESEYLIQQAIHgNL--QKHTVLII----------AHRlstvehahlIVVLDKGRVV 656
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIR-ELaaEGKAVIVIsselpellglSDR---------ILVMREGRIV 473
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
443-659 |
6.89e-13 |
|
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: 68.90 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 443 GNLIAFIIYEFVLGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 522
Cdd:cd03267 21 GSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 523 SQE-------PVLFARSITDNIsYGLPTVPFemvveaaqKANAHGF--IMELQDGYSTETgekgAQLSGGQKQRVAMARA 593
Cdd:cd03267 101 GQKtqlwwdlPVIDSFYLLAAI-YDLPPARF--------KKRLDELseLLDLEELLDTPV----RQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895785 594 LVRNPPVLILDEATSALDAESeyliQQAIHGNLQ------KHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVA----QENIRNFLKeynrerGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-636 |
8.62e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.72 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 471 VTALVGPSGSGKSSCVNILENFYPLEG-----GRVLLDGKPISAYDHKYLH--RVISLVSQEPVLFAR-SITDNISYGL- 541
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEvrREVGMVFQYPNPFPHlTIYDNVAIGVk 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 542 ------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 615
Cdd:PRK14267 112 lnglvkSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
170 180
....*....|....*....|.
gi 339895785 616 YLIQQAIHGNLQKHTVLIIAH 636
Cdd:PRK14267 186 AKIEELLFELKKEYTIVLVTH 206
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
459-660 |
9.14e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.09 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--------GRVLLDGKPISAYDHKYLHRVISLVSQ--EPVl 528
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 529 FARSITDNISYGLptvpFEMVVEAAQKANAHGFI----MELQDGySTETGEKGAQLSGGQKQRVAMARAL---------V 595
Cdd:PRK13547 96 FAFSAREIVLLGR----YPHARRAGALTHRDGEIawqaLALAGA-TALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 596 RNPPVLILDEATSALDAESEYLIQQAIHGNLQKHT--VLIIAHRLS-TVEHAHLIVVLDKGRVVQQGT 660
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
459-647 |
9.54e-13 |
|
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: 71.32 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYdhkylhrvislVSQEPVLFARSITDNIS 538
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY-----------VPQRPYMTLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YglPTVPFEMVVEAAQKANAHGFIMELQDGY--STETGEKGAQ-----LSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:TIGR00954 537 Y--PDSSEDMKRRGLSDKDLEQILDNVQLTHilEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180 190
....*....|....*....|....*....|....*....
gi 339895785 612 AESEyliqQAIHGNLQKH--TVLIIAHRLSTVE-HAHLI 647
Cdd:TIGR00954 615 VDVE----GYMYRLCREFgiTLFSVSHRKSLWKyHEYLL 649
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
459-636 |
1.14e-12 |
|
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: 65.93 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVlldgkpisaydhkylhrvislvsqepvlfARSITDNIS 538
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------------------------TWGSTVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 YglptvpFEmvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES-EYL 617
Cdd:cd03221 67 Y------FE-------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESiEAL 109
|
170 180
....*....|....*....|.
gi 339895785 618 IQQaihgnLQKH--TVLIIAH 636
Cdd:cd03221 110 EEA-----LKEYpgTVILVSH 125
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
459-690 |
1.22e-12 |
|
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: 71.48 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgRVLLDGKpisaydhkylhrvISLVSQEPVLFARSITDNI 537
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEG-KIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVPFEM--VVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 615
Cdd:TIGR01271 508 IFGLSYDEYRYtsVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 616 YLI-QQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKlvqrQMLGLQPAADFTA 690
Cdd:TIGR01271 585 KEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSS----LLLGLEAFDNFSA 656
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
440-664 |
1.76e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.25 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 440 MTSGNLIAFIIYEFVLGD--CMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR 517
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNrcIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 518 V---ISLVSQEPVLFAR-SITDNISY------GLPTVPFEMVVeaaqkanahgfIMELQdgystETGEKGA------QLS 581
Cdd:PRK11831 82 VrkrMSMLFQSGALFTDmNVFDNVAYplrehtQLPAPLLHSTV-----------MMKLE-----AVGLRGAaklmpsELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 582 GGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKH---TVLIIAHR----LSTVEHAHliVVLDKgR 654
Cdd:PRK11831 146 GGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLI-SELNSAlgvTCVVVSHDvpevLSIADHAY--IVADK-K 221
|
250
....*....|
gi 339895785 655 VVQQGTHQQL 664
Cdd:PRK11831 222 IVAHGSAQAL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
459-638 |
1.84e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SITDN 536
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQlTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL-DAES 614
Cdd:PRK10762 100 IFLGReFVNRFGRIDWKKMYAEADKLLARLNLRFSSDK--LVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET 177
|
170 180
....*....|....*....|....
gi 339895785 615 EYLIQQAIHGNLQKHTVLIIAHRL 638
Cdd:PRK10762 178 ESLFRVIRELKSQGRGIVYISHRL 201
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
455-659 |
3.39e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.36 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 455 LGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENF-YPLEG-----GRVLLD-GKPISAYDHKylhRVISLVSQEPV 527
Cdd:PRK11144 10 LGDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLtRPQKGrivlnGRVLFDaEKGICLPPEK---RRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 LFAR-SITDNISYGLptvpfemvveaAQKANAHgF--------IMELQDGYStetgekgAQLSGGQKQRVAMARALVRNP 598
Cdd:PRK11144 87 LFPHyKVRGNLRYGM-----------AKSMVAQ-FdkivallgIEPLLDRYP-------GSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 599 PVLILDEATSALDAESE-----YLIQQAIHGNLqkhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 659
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKrellpYLERLAREINI---PILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
459-670 |
3.58e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHK---YLHRVISLVSQEP--VLFARSI 533
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRgllALRQQVATVFQDPeqQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISYGLPT--VPFEMVV----EAAQKANAHGFIME-LQdgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEA 606
Cdd:PRK13638 96 DSDIAFSLRNlgVPEAEITrrvdEALTLVDAQHFRHQpIQ------------CLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 607 TSALD----AESEYLIQQAIHgnlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGL 670
Cdd:PRK13638 164 TAGLDpagrTQMIAIIRRIVA---QGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
460-659 |
5.36e-12 |
|
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: 65.24 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPI---SAYDhkylhRV---ISLVSQEPVLFar 531
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDItdlPPEE-----RArlgIFLAFQYPPEI-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 sitdnisyglPTVPFEMvveaaqkanahgFIMELQDGystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:cd03217 90 ----------PGVKNAD------------FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 339895785 612 AESEYLIQQAIhGNL--QKHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQG 659
Cdd:cd03217 137 IDALRLVAEVI-NKLreEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
468-652 |
7.10e-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: 63.55 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 468 PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL-LDGKPISAYDHKYLHRVIslvsqepvlfarsitdnisyglptvpf 546
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 547 emvveaaqkanahgfimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNL 626
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180 190
....*....|....*....|....*....|...
gi 339895785 627 QKH-------TVLIIAHRLSTVEHAHLIVVLDK 652
Cdd:smart00382 108 LLLlkseknlTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
462-666 |
8.34e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH----KYLHRVISLVSQE----PVLFARsi 533
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaKLRAKHVGFVFQSfmliPTLNAL-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 tDNISygLPTVpfeMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATsaldae 613
Cdd:PRK10584 107 -ENVE--LPAL---LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT------ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 614 seyliqqaihGNLQKHTVLIIAHRLSTVEHAH---LIVVldkgrvvqqgTHQQLLA 666
Cdd:PRK10584 175 ----------GNLDRQTGDKIADLLFSLNREHgttLILV----------THDLQLA 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
459-667 |
9.51e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.91 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGR--VLLDGKPISAYDHKYLHR-----VISLVSQEPVLFA- 530
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRgrakrYIGILHQEYDLYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 531 RSITDNI--SYGLpTVPFEM-VVEAAQKANAHGFimelQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLILDEA 606
Cdd:TIGR03269 380 RTVLDNLteAIGL-ELPDELaRMKAVITLKMVGF----DEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 607 TSALDAESEYLIQQAIHGNLQK--HTVLIIAHRLSTVehahlIVVLDK------GRVVQQGTHQQLLAQ 667
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFV-----LDVCDRaalmrdGKIVKIGDPEEIVEE 518
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
185-447 |
1.10e-11 |
|
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: 65.98 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 185 VAFLVAASFFLIVAalgetflPYYTGRAIDGIVIQKSMDQFSTAVVIVC--LLAIGSSFAAGIRGGIFTLIFARLNIRLR 262
Cdd:cd18582 2 LLLLVLAKLLNVAV-------PFLLKYAVDALSAPASALLAVPLLLLLAygLARILSSLFNELRDALFARVSQRAVRRLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 263 NCLFRSLVSQETSFFDENRTGDL---ISRLTSDTTMVSDLVSQNInvfLRNTVKVTGVVVFMFSL-SWQLSLVTFMGFPI 338
Cdd:cd18582 75 LRVFRHLHSLSLRFHLSRKTGALsraIERGTRGIEFLLRFLLFNI---LPTILELLLVCGILWYLyGWSYALITLVTVAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 339 IMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGL 418
Cdd:cd18582 152 YVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQAL 231
|
250 260
....*....|....*....|....*....
gi 339895785 419 TLLVVQVSILYYGGHLVISGQMTSGNLIA 447
Cdd:cd18582 232 IISLGLTAIMLLAAQGVVAGTLTVGDFVL 260
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
459-667 |
1.56e-11 |
|
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: 65.65 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCV-NILENFYPLEGgRVLLDGKpisaydhkylhrvISLVSQEPVLFARSITDNI 537
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELEPSEG-KIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLP--TVPFEMVVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 615
Cdd:cd03291 119 IFGVSydEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 339895785 616 YLIQQAIHGNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 667
Cdd:cd03291 196 KEIFESCVCKLMANkTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
438-671 |
1.63e-11 |
|
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: 68.01 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 438 GQMTSGNLIAfiIYEFVLGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHR 517
Cdd:TIGR01271 1216 GQMDVQGLTA--KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-EIQIDGVSWNSVTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 518 VISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 592
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGTFRKNLD------PYEQwsdeeIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLAR 1366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 593 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLY 671
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
460-665 |
1.80e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.95 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKpisaydHKYLHRVISLVSQEPVLFARS----ITD 535
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------DGQLRDLYALSEAERRRLLRTewgfVHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGLptvpfEMVVEA---------AQKANAHGFI----------MELQdgySTETGEKGAQLSGGQKQRVAMARALVR 596
Cdd:PRK11701 97 HPRDGL-----RMQVSAggnigerlmAVGARHYGDIratagdwlerVEID---AARIDDLPTTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339895785 597 NPPVLILDEATSALD----AESEYLIQQAIHgNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLL 665
Cdd:PRK11701 169 HPRLVFMDEPTGGLDvsvqARLLDLLRGLVR-ELGL-AVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
449-664 |
2.37e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 449 IIYEFVLGDCME-----NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRV---LLDGKPISAYDH-------- 512
Cdd:PRK13651 8 IVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 513 -------------KYLHRVISLVSQ--EPVLFARSITDNISYGlptvPFEMVV---EAAQKANAHGFIMELQDGYStetg 574
Cdd:PRK13651 88 viqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVskeEAKKRAAKYIELVGLDESYL---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 575 EKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALDAES--EYLiqqAIHGNLQKH--TVLIIAHRLSTV-EHAHLIV 648
Cdd:PRK13651 160 QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGvkEIL---EIFDNLNKQgkTIILVTHDLDNVlEWTKRTI 236
|
250
....*....|....*..
gi 339895785 649 VLDKGRVVQQG-THQQL 664
Cdd:PRK13651 237 FFKDGKIIKDGdTYDIL 253
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
467-666 |
3.08e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 467 SPGKVTALVGPSGSGKSSCVNILENFYPLEG--GRVLLDGKPISaydhKYLHRVISLVSQEPVLFAR-SITDNISY-GLP 542
Cdd:PLN03211 92 SPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILYPHlTVRETLVFcSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 543 TVPFEMVVEAAQKAnAHGFIMEL--QDGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQ 619
Cdd:PLN03211 168 RLPKSLTKQEKILV-AESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 339895785 620 QAIHGNLQK-HTVLIIAHRLST--VEHAHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PLN03211 247 LTLGSLAQKgKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
460-660 |
4.94e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.76 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKS-SCVNILENF-YPlegGRVL-----LDGKPISAYDHKYLHRVI----SLVSQEPVl 528
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIdYP---GRVMaekleFNGQDLQRISEKERRNLVgaevAMIFQDPM- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 529 farsITDNISYglpTVPFEM-----VVEAAQKANAHGFIMEL--QDGYSTETGEKGA---QLSGGQKQRVAMARALVRNP 598
Cdd:PRK11022 100 ----TSLNPCY---TVGFQImeaikVHQGGNKKTRRQRAIDLlnQVGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 599 PVLILDEATSALDAEseylIQQAIHG---NLQKH---TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 660
Cdd:PRK11022 173 KLLIADEPTTALDVT----IQAQIIElllELQQKenmALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
457-664 |
5.41e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.65 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 457 DCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK----------PISAYDHKYLHRV----ISLV 522
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVrgadMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 523 SQEPVL-----------FARSItdNISYGLPTvpfEMVVEAAQKANAHGFIMELQdgysTETGEKGAQLSGGQKQRVAMA 591
Cdd:PRK10261 110 FQEPMTslnpvftvgeqIAESI--RLHQGASR---EEAMVEAKRMLDQVRIPEAQ----TILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 592 RALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKHT---VLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQL 664
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMsmgVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQI 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
459-680 |
7.00e-11 |
|
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: 65.23 E-value: 7.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE-GGRVLLDGKPISAYD-HKYLHRVISLVSQE-------PVLf 529
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPIL- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 530 arSITDNISYG-LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:TIGR02633 355 --GVGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 609 ALDAESEYLIQQAIhGNLQKHTVLIIahrLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGlyakLVQRQML 680
Cdd:TIGR02633 433 GVDVGAKYEIYKLI-NQLAQEGVAII---VVSSELAEVLGLSDRVLVIGEGKLKGDFVNHA----LTQEQVL 496
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
440-659 |
7.27e-11 |
|
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: 62.28 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 440 MTSGNLIAFIIYEFVLGDCMENVSFSLSPGKVTALVGPSGSGKSS----CVNILENFYPLEGgRVLLDGKPISAYDHKYl 515
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVEG-DIHYNGIPYKEFAEKY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 516 HRVISLVSQEPVLFarsitdnisyglPTVPFEMVVEAAQKANAHGFImelqdgystetgeKGaqLSGGQKQRVAMARALV 595
Cdd:cd03233 82 PGEIIYVSEEDVHF------------PTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 596 RNPPVLILDEATSALDAESEYLIQQAIH--GNLQKHTVLIIAHRLStVEHAHL---IVVLDKGRVVQQG 659
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRtmADVLKTTTFVSLYQAS-DEIYDLfdkVLVLYEGRQIYYG 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
460-656 |
1.11e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLdGKPIS-AY---DHKYLHRvislvsqepvlfARSITD 535
Cdd:COG0488 332 DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKiGYfdqHQEELDP------------DKTVLD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NISYGLPTvpfemvveaAQKANAHGFimeLQD-GYSTETGEKG-AQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:COG0488 399 ELRDGAPG---------GTEQEVRGY---LGRfLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 339895785 614 SEYLIQQAihgnLQKH--TVLIIAH-R--LSTVehAHLIVVLDKGRVV 656
Cdd:COG0488 467 TLEALEEA----LDDFpgTVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
459-659 |
2.38e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLhrvISLVSQE-------PVLfar 531
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 sITDNISYG---------LPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLI 602
Cdd:PRK15056 97 -VEDVVMMGryghmgwlrRAKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 603 LDEATSALDAESEYLIqQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 659
Cdd:PRK15056 166 LDEPFTGVDVKTEARI-ISLLRELRDEgkTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
459-617 |
5.16e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY-LHRVISLVSQE-PVLFARSITDN 536
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYG-LPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL-DAES 614
Cdd:PRK10982 94 MWLGrYPTKGM-FVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEKEV 170
|
...
gi 339895785 615 EYL 617
Cdd:PRK10982 171 NHL 173
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
460-675 |
5.52e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.26 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILEN-FYPlEGGRVLLDGKPISAYDHKYLHRvISLV----SQ----EPVL-- 528
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGYVPFKRRKEFARR-IGVVfgqrSQlwwdLPAIds 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 529 FA--RSItdnisYGLPTVPF----EMVVEaaqkanahgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALVRNPPVLI 602
Cdd:COG4586 117 FRllKAI-----YRIPDAEYkkrlDELVE----------LLDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 603 LDEATSALDAESeyliQQAIHGNL----QKH--TVLIIAHRLSTVEhaHL---IVVLDKGRVVQQGTHQQLLAQGGLYAK 673
Cdd:COG4586 178 LDEPTIGLDVVS----KEAIREFLkeynRERgtTILLTSHDMDDIE--ALcdrVIVIDHGRIIYDGSLEELKERFGPYKT 251
|
..
gi 339895785 674 LV 675
Cdd:COG4586 252 IV 253
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
463-674 |
6.85e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 463 SFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvisLVSQEpvlFARSITDNIS---- 538
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDE---WQRNNTDMLSpged 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 -YGLPTVpfEMVVEAAqKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:PRK10938 97 dTGRTTA--EIIQDEV-KDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 339895785 618 IQQAIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQgGLYAKL 674
Cdd:PRK10938 174 LAELLASlHQSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ-ALVAQL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
456-622 |
7.77e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 456 GDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEP----VLFA 530
Cdd:PRK10762 265 GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 531 RSITDNISY-GLPTVPFEMVV--EAAQKANAHGFImelqDGYSTETGEKGAQ---LSGGQKQRVAMARALVRNPPVLILD 604
Cdd:PRK10762 345 MSVKENMSLtALRYFSRAGGSlkHADEQQAVSDFI----RLFNIKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILD 420
|
170
....*....|....*...
gi 339895785 605 EATSALDAESEYLIQQAI 622
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLI 438
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
461-634 |
1.28e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPleG---GRVLLDGKPIS------AYDHKylhrvISLVSQE------ 525
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKirnpqqAIAQG-----IAMVPEDrkrdgi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 526 -PVLfarSITDNISYG-LPTVPFEMVV-EAAQKANAHGFIMELQdgYSTETGE-KGAQLSGGQKQRVAMARALVRNPPVL 601
Cdd:PRK13549 353 vPVM---GVGKNITLAaLDRFTGGSRIdDAAELKTILESIQRLK--VKTASPElAIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190
....*....|....*....|....*....|...
gi 339895785 602 ILDEATSALDAESEYLIQQAIhGNLQKHTVLII 634
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLI-NQLVQQGVAII 459
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
458-654 |
1.37e-09 |
|
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: 61.10 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 458 CMENVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFypleggrvllDGKPISAYDHKylhrvISLVSQEPVL-FARS 532
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdKDF----------NGEARPQPGIK-----VGYLPQEPQLdPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 533 ITDNI-------------------SYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GE-KGAQ 579
Cdd:TIGR03719 85 VRENVeegvaeikdaldrfneisaKYAEPDADFDKLAAEQAELQE---IIDAADAWDLDSqleiamdalrcppWDaDVTK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 580 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGnlQKHTVLIIAH-R--LSTVehAHLIVVLDKGR 654
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPGTVVAVTHdRyfLDNV--AGWILELDRGR 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
459-641 |
1.45e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.36 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLvsqePVLFARSITDNis 538
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTL----PLTVNRFLRLR-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 yglPTVPFEMVVEAAQKANA-HGFIMELQdgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:PRK09544 94 ---PGTKKEDILPALKRVQAgHLIDAPMQ------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|....*..
gi 339895785 618 IQQAIHgNLQKH---TVLIIAHRLSTV 641
Cdd:PRK09544 159 LYDLID-QLRREldcAVLMVSHDLHLV 184
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
230-605 |
1.47e-09 |
|
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: 60.97 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 230 VIVCLLAIGSSFAAGIRggiFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSqNINVFLR 309
Cdd:COG4615 55 AGLLVLLLLSRLASQLL---LTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 310 NTVKVTGVVVFMFSLSWQLSLVT--FMGFPIIM-------------MVSNIYGKYYKRLS------KEV----------- 357
Cdd:COG4615 131 SVALVLGCLAYLAWLSPPLFLLTlvLLGLGVAGyrllvrrarrhlrRAREAEDRLFKHFRallegfKELklnrrrrraff 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 358 QNALARASNTAEETISAMKTVRSFANEEEEAEVY------LRKLQQVYKLNRKEAAAY---MYYVWG--SGL-----TLL 421
Cdd:COG4615 211 DEDLQPTAERYRDLRIRADTIFALANNWGNLLFFaligliLFLLPALGWADPAVLSGFvlvLLFLRGplSQLvgalpTLS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 422 VVQVSI-------------LYYGGHLVISGQMTSGNLIAF--IIYE---------FVLGdcmeNVSFSLSPGKVTALVGP 477
Cdd:COG4615 291 RANVALrkieelelalaaaEPAAADAAAPPAPADFQTLELrgVTYRypgedgdegFTLG----PIDLTIRRGELVFIVGG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 478 SGSGKSSCVNILENFYPLEGGRVLLDGKPISA--YDHkYLHRvISLVSQEPVLFARsitdniSYGLPTVPfemvveAAQK 555
Cdd:COG4615 367 NGSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREA-YRQL-FSAVFSDFHLFDR------LLGLDGEA------DPAR 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 556 ANAHGFIMELQ------DGYSTETgekgaQLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:COG4615 433 ARELLERLELDhkvsveDGRFSTT-----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
188-449 |
1.93e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 59.48 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18779 7 ILLASLLLQLLGLA---LPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTfMGFPII----MMVS 343
Cdd:cd18779 84 HLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALL-DGTLVLGYLALLFAQSPLLGLVV-LGLAALqvalLLAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 344 NiygKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKL--QQVYKLNRKEAAAYMyyvwGSGLTLL 421
Cdd:cd18779 162 R---RRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFvdQLNASLRRGRLDALV----DALLATL 234
|
250 260 270
....*....|....*....|....*....|
gi 339895785 422 --VVQVSILYYGGHLVISGQMTSGNLIAFI 449
Cdd:cd18779 235 rlAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
461-683 |
2.23e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.18 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSpgKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVSQEPVLFARSitdnisyg 540
Cdd:TIGR01257 950 NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHL-------- 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 lpTVPFEMVVEAAQKANAH---GFIME--LQD-GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 614
Cdd:TIGR01257 1019 --TVAEHILFYAQLKGRSWeeaQLEMEamLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 615 EYLIQQAIHGNLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVVQQGTHQQL--LAQGGLYAKLVqRQMLGLQ 683
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLknCFGTGFYLTLV-RKMKNIQ 1167
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
460-657 |
2.51e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlEG---GRVLLDGKP-----ISAYDHkylhRVISLVSQE----PV 527
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEVcrfkdIRDSEA----LGIVIIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 LfarSITDNISYGLPTVPF------EMVVEAAQKANAHGfimeLQDGYSTETGEKGAqlsgGQKQRVAMARALVRNPPVL 601
Cdd:NF040905 93 L---SIAENIFLGNERAKRgvidwnETNRRARELLAKVG----LDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 602 ILDEATSAL-DAESEYLIQQAIHgnLQKH--TVLIIAHRLSTVEH-AHLIVVLDKGRVVQ 657
Cdd:NF040905 162 ILDEPTAALnEEDSAALLDLLLE--LKAQgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
461-653 |
3.80e-09 |
|
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: 56.56 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNilENFYplEGGRVLLDGKPiSAYDHKYLHRVISLvsqepvlfaRSITDNisyG 540
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLISFL-PKFSRNKLIFIDQL---------QFLIDV---G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 LptvpfemvveaaqkanahgfimelqdGYSTeTGEKGAQLSGGQKQRVAMARALVRNPP--VLILDEATSALDAESEYLI 618
Cdd:cd03238 76 L--------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190
....*....|....*....|....*....|....*.
gi 339895785 619 QQAIHGNL-QKHTVLIIAHRLSTVEHAHLIVVLDKG 653
Cdd:cd03238 129 LEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
459-656 |
4.06e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILenfypleGGRVLLD-GKPISAYDhkylhRVISLVSQEPvlfARSITDN- 536
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQD-----LIVARLQQDP---PRNVEGTv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 --------------------ISYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GEKGAQLSGG 583
Cdd:PRK11147 84 ydfvaegieeqaeylkryhdISHLVETDPSEKNLNELAKLQE---QLDHHNLWQLENrinevlaqlgldpDAALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 584 QKQRVAMARALVRNPPVLILDEATSALDAES-EYLiqqaiHGNLQ--KHTVLIIAHRLSTVEH-AHLIVVLDKGRVV 656
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL-----EGFLKtfQGSIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
461-657 |
8.71e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLEGGRVLLDGKpisaydhkylhrvislVSQEpvlfaRSITDNI 537
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTllrLLAGALKGTPVAGCVDVPDNQ----------------FGRE-----ASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 sygLPTVPFEMVVEAAqkaNAHGfimeLQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 617
Cdd:COG2401 107 ---GRKGDFKDAVELL---NAVG----LSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 339895785 618 IQQAIHGNLQKH--TVLIIAHRlSTVEHA---HLIVVLDKGRVVQ 657
Cdd:COG2401 175 VARNLQKLARRAgiTLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
461-659 |
1.06e-08 |
|
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: 56.00 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaydhkylhrVISL-VSQEPVLFARsitDNIS- 538
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---------LLGLgGGFNPELTGR---ENIYl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 539 ----YGLPTVpfemvvEAAQKANahgFIMELqdgysTETGEKGAQ----LSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:cd03220 108 ngrlLGLSRK------EIDEKID---EIIEF-----SELGDFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 339895785 611 DAESEYLIQQAIHGNLQKHTVLIIA-HRLSTV-EHAHLIVVLDKGRVVQQG 659
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVsHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
461-660 |
1.75e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.86 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpisaydhkylhRVISLVSqepvL---FARSIT--D 535
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------RVSALLE----LgagFHPELTgrE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 536 NIS-----YGLPTVP----FEMVVEAAqkanahgfimELQD-------GYSTetgekgaqlsgGQKQRVAMARALVRNPP 599
Cdd:COG1134 108 NIYlngrlLGLSRKEidekFDEIVEFA----------ELGDfidqpvkTYSS-----------GMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 600 VLILDEATSALDAE----SEYLIQQaihgnLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 660
Cdd:COG1134 167 ILLVDEVLAVGDAAfqkkCLARIRE-----LRESgrTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGD 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
459-666 |
1.99e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR-VISLVSQEPVLFAR-SITDN 536
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMReAVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGlptvpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALdaeSEY 616
Cdd:PRK11614 101 LAMG------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---API 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 617 LIQQaIHGNLQK-----HTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK11614 172 IIQQ-IFDTIEQlreqgMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
461-660 |
2.69e-08 |
|
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: 55.70 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNilENFYPLEGGRVLLDGKPISAYD----HKYLHRVIsLVSQEPV--------- 527
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNHDriegLEHIDKVI-VIDQSPIgrtprsnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 -----------LF------AR--SITDNISYGLPTVP--FEMVVEAAQK-----ANAHGFIMELQD---GYSTeTGEKGA 578
Cdd:cd03271 90 tytgvfdeireLFcevckgKRynRETLEVRYKGKSIAdvLDMTVEEALEffeniPKIARKLQTLCDvglGYIK-LGQPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 579 QLSGGQKQRVAMARALVR---NPPVLILDEATSALDAESeylIQQAIHGnLQK-----HTVLIIAHRLSTVEHAHLIVVL 650
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHD---VKKLLEV-LQRlvdkgNTVVVIEHNLDVIKCADWIIDL 244
|
250
....*....|....*.
gi 339895785 651 -----DK-GRVVQQGT 660
Cdd:cd03271 245 gpeggDGgGQVVASGT 260
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
456-655 |
3.76e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 456 GDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK-YLHRVISLVS---QEPVLFAR 531
Cdd:PRK15439 276 GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYLPedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 S-ITDNI-SYGLPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATS 608
Cdd:PRK15439 356 ApLAWNVcALTHNRRGF-WIKPARENAVLERYRRAL--NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 339895785 609 ALDAESEYLIQQAIHGNLQKHT-VLIIAHRLSTVEH-AHLIVVLDKGRV 655
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
462-654 |
5.90e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 462 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNisygl 541
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPE----- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 542 ptvPFEMVVEAAQKANAH---GFIMELQDGYSTETgekgaQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:PRK10522 417 ---GKPANPALVEKWLERlkmAHKLELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895785 619 QQAIHGNLQK--HTVLIIAHRLSTVEHAHLIVVLDKGR 654
Cdd:PRK10522 489 YQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
564-698 |
6.32e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 564 ELQDGYS-TET-GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLST 640
Cdd:NF000106 127 ELLERFSlTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEE 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 641 VEH-AHLIVVLDKGRVVQQGTHQQLLAQGG--------LYAKLVQRQM-----LGLQPAADFTAGHNEPVAN 698
Cdd:NF000106 207 AEQlAHELTVIDRGRVIADGKVDELKTKVGgrtlqirpAHAAELDRMVgaiaqAGLDGIAGATADHEDGVVN 278
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
578-654 |
6.92e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 578 AQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQaiHgnLQKH--TVLIIAH-R--LSTVehAHLIVVLDK 652
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ--F--LHDYpgTVVAVTHdRyfLDNV--AGWILELDR 235
|
..
gi 339895785 653 GR 654
Cdd:PRK11819 236 GR 237
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
459-660 |
8.65e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVL------- 528
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEipgvsna 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 529 -FARSI--TDNISYGLPTV-PFEMVVEAAQKANahgfIMELQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPPVLILD 604
Cdd:CHL00131 103 dFLRLAynSKRKFQGLPELdPLEFLEIINEKLK----LVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 605 EATSALDAESEYLIQQAIHgNL--QKHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQGT 660
Cdd:CHL00131 177 ETDSGLDIDALKIIAEGIN-KLmtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
182-447 |
8.75e-08 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 54.15 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 182 KPDVAFLVAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMdqfSTAVVIvCLLAIGSSFAAGI----RGGIFTLIFARL 257
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALA---PPIFMLQVYDRVLPSGSL---STLLGL-TLGMVVLLAFDGLlrqvRSRILQRVGLRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 258 NIRLRNCLFRSLVSQETsffdENRTGDLISRLTSDTTMVSDLVSQN--INVFLRNTVKVTGVVVFMFSlSWqLSLVTFMG 335
Cdd:cd18586 74 DVELGRRVFRAVLELPL----ESRPSGYWQQLLRDLDTLRNFLTGPslFAFFDLPWAPLFLAVIFLIH-PP-LGWVALVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 336 FPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKL-NRKEAAAYMYYVW 414
Cdd:cd18586 148 APVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELqIRASDLAGAISAI 227
|
250 260 270
....*....|....*....|....*....|...
gi 339895785 415 GSGLTlLVVQVSILYYGGHLVISGQMTSGNLIA 447
Cdd:cd18586 228 GKTLR-MALQSLILGVGAYLVIDGELTIGALIA 259
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
460-665 |
9.22e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV----SQEPVLFARSIT 534
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAGIMLCpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DN--ISYGLPTVPFEMVVEAAQKA-NAHGFIMELQdgYSTETGE-KGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 610
Cdd:PRK11288 350 DNinISARRHHLRAGCLINNRWEAeNADRFIRSLN--IKTPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 611 D--AESEylIQQAIHgNL--QKHTVLIIAHRLSTVEH-AHLIVVLDKGRVV-----QQGTHQQLL 665
Cdd:PRK11288 428 DvgAKHE--IYNVIY-ELaaQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgelarEQATERQAL 489
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
463-639 |
1.04e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.52 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 463 SFSL------SPGKVTALVGPSGSGKSSCVNILENFYPLEGGRvlLDGKP-----ISAYD----HKYLHRVIS------- 520
Cdd:cd03236 14 SFKLhrlpvpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRgselQNYFTKLLEgdvkviv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 521 ---LVSQEPVLFARSITDNISYGLPTVPFEMVVEAaqkanahgfiMELQDGYSTETgekgAQLSGGQKQRVAMARALVRN 597
Cdd:cd03236 92 kpqYVDLIPKAVKGKVGELLKKKDERGKLDELVDQ----------LELRHVLDRNI----DQLSGGELQRVAIAAALARD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 339895785 598 PPVLILDEATSALDAESEYLIQQAIHGnLQKHT--VLIIAHRLS 639
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRE-LAEDDnyVLVVEHDLA 200
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
464-667 |
1.04e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 464 FSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG---GRVLLDGKPISAYDHKYLHRV----ISLVSQEPVlfaRSITDN 536
Cdd:PRK09473 37 FSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNKLraeqISMIFQDPM---TSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 537 ISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PRK09473 114 MRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphefSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895785 612 AESEYLIQQAIhgNLQKH----TVLIIAHRLSTVehAHL---IVVLDKGRVVQQGTHQQLLAQ 667
Cdd:PRK09473 194 VTVQAQIMTLL--NELKRefntAIIMITHDLGVV--AGIcdkVLVMYAGRTMEYGNARDVFYQ 252
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
465-636 |
1.27e-07 |
|
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: 53.18 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 465 SLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKYLHRVISLVSQEpvlFARSITDnisyGLPTV 544
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGTVRD---LLSSITK----DFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 545 PFeMVVEAAQKanahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG 624
Cdd:cd03237 93 PY-FKTEIAKP-------LQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170
....*....|....
gi 339895785 625 NLQKH--TVLIIAH 636
Cdd:cd03237 161 FAENNekTAFVVEH 174
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
464-627 |
2.53e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 464 FSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRVISLVSQEPVLFAR-SITDNISY--G 540
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKADlSTLENLHFlcG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 541 LPTVpfemvvEAAQKANAHGFIMELQDGYSTETgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQ 620
Cdd:PRK13543 109 LHGR------RAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNR 178
|
....*..
gi 339895785 621 AIHGNLQ 627
Cdd:PRK13543 179 MISAHLR 185
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
225-381 |
2.59e-07 |
|
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: 52.99 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 225 FSTAVVIVCLLAIGSSFAAGIRGgiftlifARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 304
Cdd:cd18602 59 LSLGAVILSLVTNLAGELAGLRA-------AR---RLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 305 NVFLRNTVKV-TGVVVFMFSLSWQLslvtFMGFPIImMVSNIYGKYYKRLSKEVQ--NALARA---SNTAeETISAMKTV 378
Cdd:cd18602 129 ERLLRFLLLClSAIIVNAIVTPYFL----IALIPII-IVYYFLQKFYRASSRELQrlDNITKSpvfSHFS-ETLGGLTTI 202
|
...
gi 339895785 379 RSF 381
Cdd:cd18602 203 RAF 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
466-638 |
4.77e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 466 LSPGKVTALVGPSGSGKSSCVNILE-----NFyplegGRVllDGKP-----ISAYDHKYLHRVISLVSQEPVLFARSI-- 533
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgelipNL-----GDY--EEEPswdevLKRFRGTELQNYFKKLYNGEIKVVHKPqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNIsyglPTVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PRK13409 169 VDLI----PKVFKGKVRELLKKVDERGKLDEVVErlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*..
gi 339895785 612 AESEYLIQQAIHGNLQKHTVLIIAHRL 638
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
191-451 |
6.15e-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: 51.84 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFS--TAVVIVCLLAIGSSFAAGIRggifTLIFARLN----IRLRNC 264
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESavTLILLYALLRFSSKLLKELR----SLLYRRVQqnayRELSLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 265 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSqninVFLRNTVK-----VTGVVVFMFSLSWQLSLVTFMGFpII 339
Cdd:cd18560 77 TFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLS----YLVFYLVPtllelIVVSVVFAFHFGAWLALIVFLSV-LL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 340 MMVSNIYG-KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGL 418
Cdd:cd18560 152 YGVFTIKVtEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQL 231
|
250 260 270
....*....|....*....|....*....|...
gi 339895785 419 TLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18560 232 IIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTY 264
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
460-659 |
6.31e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK-PISAYDHkylHRVISL-VSQEPVLFarsitdnI 537
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQ---HHVDGLdLSSNPLLY-------M 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 538 SYGLPTVPfemvveaAQKANAH----GFI--MELQDGYStetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PLN03073 596 MRCFPGVP-------EQKLRAHlgsfGVTgnLALQPMYT---------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 339895785 612 AES-EYLIQQAIhgnLQKHTVLIIAHrlstveHAHLIV-VLDKGRVVQQG 659
Cdd:PLN03073 660 LDAvEALIQGLV---LFQGGVLMVSH------DEHLISgSVDELWVVSEG 700
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
459-641 |
7.60e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILE---NFYPLEGGRVLLDGKPISAYdhkyLHRVISLVSQEPVLFARS-IT 534
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLDSS----FQRSIGYVQQQDLHLPTStVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNISYG----LP-TVPFEM---VVEAAQKanahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLI-LDE 605
Cdd:TIGR00956 855 ESLRFSaylrQPkSVSKSEkmeYVEEVIK------LLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895785 606 ATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRLSTV 641
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMR-KLADHgqAILCTIHQPSAI 965
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
461-656 |
1.06e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEP-----VLfARSIT 534
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRlgrglVP-DMSVA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 535 DNI----SYGLPTVPFEMVVEAAQKANAHGFIMELQ---DGYSTETGekgaQLSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:COG3845 355 ENLilgrYRRPPFSRGGFLDRKAIRAFAEELIEEFDvrtPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPT 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 608 SALDAESeyliQQAIHGNLQKH-----TVLIIAHRLSTV-EHAHLIVVLDKGRVV 656
Cdd:COG3845 431 RGLDVGA----IEFIHQRLLELrdagaAVLLISEDLDEIlALSDRIAVMYEGRIV 481
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
465-642 |
1.13e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 465 SLSPGKVTALVGPSGSGKSscvNILenfypleggrvlldgkpisaydhkylhRVISLVsqepVLFARSITDNISYGLPTV 544
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKS---TIL---------------------------DAIGLA----LGGAQSATRRRSGVKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 545 PfemvvEAAQKANAHGFIMelqdgystetgekgaQLSGGQKQRVAMARAL----VRNPPVLILDEATSALDAESEYLIQQ 620
Cdd:cd03227 63 I-----VAAVSAELIFTRL---------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180
....*....|....*....|...
gi 339895785 621 AIHGNLQKH-TVLIIAHRLSTVE 642
Cdd:cd03227 123 AILEHLVKGaQVIVITHLPELAE 145
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
461-665 |
1.52e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK---PISAYDHkyLHRVISLVSQ---EPVLFAR-SI 533
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDA--VKKGMAYITEsrrDNGFFPNfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDN--ISYGLPTVPFEMVV------EAAQKANAHGFIMELQdgySTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 605
Cdd:PRK09700 359 AQNmaISRSLKDGGYKGAMglfhevDEQRTAENQRELLALK---CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895785 606 ATSALD--AESE-YLIQQAIHGnlQKHTVLIIAHRLStvehaHLIVVLDKGRVVQQGTHQQLL 665
Cdd:PRK09700 436 PTRGIDvgAKAEiYKVMRQLAD--DGKVILMVSSELP-----EIITVCDRIAVFCEGRLTQIL 491
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
459-664 |
2.06e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.17 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVN-----ILENFypLEGGRVLLD-GKPISAYDHkyLHRVISlVSQEPV----- 527
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypALANR--LNGAKTVPGrYTSIEGLEH--LDKVIH-IDQSPIgrtpr 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 ---------------LFARS--------------------------------ITDNIsygLPT--VP------------- 545
Cdd:TIGR00630 699 snpatytgvfdeireLFAETpeakvrgytpgrfsfnvkggrceacqgdgvikIEMHF---LPDvyVPcevckgkrynret 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 546 -------------FEMVVEAAQK-----ANAHGFIMELQD---GYSTeTGEKGAQLSGGQKQRVAMARALVR---NPPVL 601
Cdd:TIGR00630 776 levkykgkniadvLDMTVEEAYEffeavPSISRKLQTLCDvglGYIR-LGQPATTLSGGEAQRIKLAKELSKrstGRTLY 854
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895785 602 ILDEATSALDAES----EYLIQQAIHgnlQKHTVLIIAHRLSTVEHAHLIVVL-----DK-GRVVQQGTHQQL 664
Cdd:TIGR00630 855 ILDEPTTGLHFDDikklLEVLQRLVD---KGNTVVVIEHNLDVIKTADYIIDLgpeggDGgGTVVASGTPEEV 924
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
459-634 |
2.19e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQE----------PV 527
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyaylDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 LFARSITDNISYglpTVPFEMVVEAAQKANAHGFI--MELQD-GYSTETGekgaQLSGGQKQRVAMARALVRNPPVLILD 604
Cdd:PRK10982 344 GFNSLISNIRNY---KNKVGLLDNSRMKSDTQWVIdsMRVKTpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190
....*....|....*....|....*....|
gi 339895785 605 EATSALDAESEYLIQQAIHGNLQKHTVLII 634
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
460-611 |
2.31e-06 |
|
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: 50.94 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENvSFSL------SPGKVTALVGPSGSGKSSCVNILE-----NFyplegGRVllDGKP-----ISAYD----HKYLHRVI 519
Cdd:COG1245 85 EN-GFRLyglpvpKKGKVTGILGPNGIGKSTALKILSgelkpNL-----GDY--DEEPswdevLKRFRgtelQDYFKKLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 520 S---LVSQEP--VlfarsitDNIsyglPTVPFEMVVEAAQKANAHGFIMELQDGYSTET--GEKGAQLSGGQKQRVAMAR 592
Cdd:COG1245 157 NgeiKVAHKPqyV-------DLI----PKVFKGTVRELLEKVDERGKLDELAEKLGLENilDRDISELSGGELQRVAIAA 225
|
170
....*....|....*....
gi 339895785 593 ALVRNPPVLILDEATSALD 611
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLD 244
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
234-422 |
3.30e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 49.40 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 234 LLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 313
Cdd:cd18606 43 GLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 314 VTGVVVfmfslswqLSLVTF----MGFPIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEe 385
Cdd:cd18606 123 IIGTFI--------LIIIYLpwfaIALPPLLVLYYFIANYYRASSRELKrlESILRSFvyANFSESLSGLSTIRAYGAQ- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 339895785 386 eeaEVYLRKLQqvYKLNRKEAAAYMYYV---W--------GSGLTLLV 422
Cdd:cd18606 194 ---DRFIKKNE--KLIDNMNRAYFLTIAnqrWlairldllGSLLVLIV 236
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
459-636 |
8.34e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLsPGKV--------------TALVGPSGSGKSSCVNI-LENFYPlEGGRVLLDGKPISAY-DHkylHRVIslv 522
Cdd:PRK11147 322 MENVNYQI-DGKQlvkdfsaqvqrgdkIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHCGTKLEVAYfDQ---HRAE--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 523 sQEPvlfARSITDNISYGLPTVpfeMVveAAQKANAHGFimeLQD----GYSTETGEKGaqLSGGQKQRVAMARALVRNP 598
Cdd:PRK11147 394 -LDP---EKTVMDNLAEGKQEV---MV--NGRPRHVLGY---LQDflfhPKRAMTPVKA--LSGGERNRLLLARLFLKPS 459
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895785 599 PVLILDEATSALDAESEYLIQQAIHGnlQKHTVLIIAH 636
Cdd:PRK11147 460 NLLILDEPTNDLDVETLELLEELLDS--YQGTVLLVSH 495
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
459-678 |
1.13e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNIL--ENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPV-------- 527
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeipgvsnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 LFARSITDNI-SY----GLPTVPFEMVVEAAQKanahgfIMELQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPPVLI 602
Cdd:PRK09580 97 FFLQTALNAVrSYrgqePLDRFDFQDLMEEKIA------LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 603 LDEATSALDAESEYLIQQAIHgNLQ--KHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQGTH---QQLLAQGglYAKLV 675
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVN-SLRdgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQG--YGWLT 245
|
...
gi 339895785 676 QRQ 678
Cdd:PRK09580 246 EQQ 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
463-636 |
1.60e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 463 SFSLS-------PGKVTALVGPSGSGKSSCVNILE-NFYPLEGGrvlLDGKPISAYDHKYlhrvISLVSQEPV-LFARSI 533
Cdd:PRK13409 352 DFSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAgVLKPDEGE---VDPELKISYKPQY----IKPDYDGTVeDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNISyglpTVPFEmvVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:PRK13409 425 TDDLG----SSYYK--SEIIKPLQ----LERLLDKNVKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*
gi 339895785 614 SEYLIQQAI--HGNLQKHTVLIIAH 636
Cdd:PRK13409 488 QRLAVAKAIrrIAEEREATALVVDH 512
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
229-413 |
1.78e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 47.08 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 229 VVIVCLLAIGSSFAAGIRGGIFTL--------IFARLnirlrnclFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLV 300
Cdd:cd18604 46 LGIYALISLLSVLLGTLRYLLFFFgslrasrkLHERL--------LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 301 SQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMK 376
Cdd:cd18604 118 ADSLSSLLESTLSLLVILIAIVVVSPAFLLPAV----VLAALYVYIGRLYLRASRELKrlESVARSPilSHFGETLAGLV 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 339895785 377 TVRSFANEeeeaEVYLRKLQQvyKLNRKEAAAYMYYV 413
Cdd:cd18604 194 TIRAFGAE----ERFIEEMLR--RIDRYSRAFRYLWN 224
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
182-448 |
2.39e-05 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 46.70 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFStavvivcLLAIGSSFAAGIRGgIFTLIFARLNIRL 261
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGL---VIPVFSRIFIDDILVGGLPDWLR-------PLLLGMALTALLQG-LLTWLQQYYLLRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 262 RNCLfrSLVSQET----------SFFDENRTGDLISRLTSDTTmVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLV 331
Cdd:cd18569 70 ETKL--ALSSSSRffwhvlrlpvEFFSQRYAGDIASRVQSNDR-VANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 332 TFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEeaevYLRKL--QQVYKLNRKEAAAY 409
Cdd:cd18569 147 GIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESD----FFSRWagYQAKVLNAQQELGR 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 339895785 410 MYYVWGSGLTLL--VVQVSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18569 223 TNQLLGALPTLLsaLTNAAILGLGGLLVMDGALTIGMLVAF 263
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
459-666 |
3.79e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI----SLVSQEP---V 527
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRERRKLVghnvSMIFQEPqscL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 528 LFARSITDNISYGLP----------------TVPFEMVVEAAQKAnaHGFIMElqdGYSTEtgekgaqLSGGQKQRVAMA 591
Cdd:PRK15093 103 DPSERVGRQLMQNIPgwtykgrwwqrfgwrkRRAIELLHRVGIKD--HKDAMR---SFPYE-------LTEGECQKVMIA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 592 RALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 666
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
460-636 |
4.16e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENfyPLE--GGRVLLD-----GKpIS----AYDHkylHRVISLV--SQEP 526
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGG--DLEpsAGNVSLDpnerlGK-LRqdqfAFEE---FTVLDTVimGHTE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 527 VLFARSITDNIsYGLPtvpfEMVVEAAQKAnahgfiMELQ------DGYSTET--GE--KGA------------QLSGGQ 584
Cdd:PRK15064 92 LWEVKQERDRI-YALP----EMSEEDGMKV------ADLEvkfaemDGYTAEAraGEllLGVgipeeqhyglmsEVAPGW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 339895785 585 KQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhgNLQKHTVLIIAH 636
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL--NERNSTMIIISH 210
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
318-450 |
4.72e-05 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 45.89 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 318 VVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFAneeeeAE-VYLRKLQ 396
Cdd:cd18587 132 LAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALG-----AEgRMQRRWE 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 397 Q-VYKLNRKEAAAYMYYVWGSGLTLLVVQ---VSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18587 207 EaVAALARSSLKSRLLSSSATNFAQFVQQlvtVAIVIVGVYLISDGELTMGGLIACVI 264
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
580-653 |
8.11e-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: 43.71 E-value: 8.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 580 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQ--KHTVLIIAHRLSTVEHAHLIVVLDKG 653
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
450-669 |
8.96e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.16 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 450 IYEFVLGDCMENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVSQ----- 524
Cdd:TIGR01257 1946 VYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfdaid 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 525 -------EPVLFARsitdnisygLPTVPFEMVVEAAQKAnahgfIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRN 597
Cdd:TIGR01257 2025 dlltgreHLYLYAR---------LRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339895785 598 PPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGG 669
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
580-636 |
1.01e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 1.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895785 580 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAI-----HGNLQkhtVLIIAH 636
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdvlisEGETQ---LLFVSH 460
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
457-659 |
1.30e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 457 DCMENVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFYPLEGGRVLLDGKPISAYDHKYLHRVI----------SLV 522
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVynaetdvhfpHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 523 SQEPVLF-ARSITDNISYGLPTvpfeMVVEAAQKANAHGFIMELQDGYSTETGE---KGaqLSGGQKQRVAMARALVRNP 598
Cdd:TIGR00956 155 VGETLDFaARCKTPQNRPDGVS----REEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895785 599 PVLILDEATSALDAESEYLIQQAIH--GNLQKHTVLIIAHRLS--TVEHAHLIVVLDKGRVVQQG 659
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKtsANILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
461-611 |
1.61e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 461 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV------ISL-----VSQEPVLF 529
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVgymsqaFSLygeltVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 530 ARSitdnisYGLP--TVPfEMVVEAAQKanahgFimELQDgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 607
Cdd:NF033858 364 ARL------FHLPaaEIA-ARVAEMLER-----F--DLAD----VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 339895785 608 SALD 611
Cdd:NF033858 426 SGVD 429
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
578-669 |
1.85e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 578 AQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES-----EyLIQQaIHGNLQKHTVLIiahrlST--VEHA----HL 646
Cdd:NF033858 135 GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSrrqfwE-LIDR-IRAERPGMSVLV-----ATayMEEAerfdWL 207
|
90 100
....*....|....*....|...
gi 339895785 647 iVVLDKGRVVQQGTHQQLLAQGG 669
Cdd:NF033858 208 -VAMDAGRVLATGTPAELLARTG 229
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
193-450 |
2.07e-04 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC 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: 350015 [Multi-domain] Cd Length: 294 Bit Score: 43.97 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 193 FFLIVAALGETFLPYYTGRAID-GIViQKSMDqFSTAVVIVCL-LAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18571 9 LGLLLGSLLQLIFPFLTQSIVDkGIN-NKDLN-FIYLILIAQLvLFLGSTSIEFIRSWILLHISSRINISIISDFLIKLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 271 SQETSFFDENRTGDLISR----------LTSDT--TMVSDLvsqNINVFlrntvkvtGVVVFMFSlsWQLSLVTFMGFPI 338
Cdd:cd18571 87 RLPISFFDTKMTGDILQRindhsriesfLTSSSlsILFSLL---NLIVF--------SIVLAYYN--LTIFLIFLIGSVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 339 IMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGL 418
Cdd:cd18571 154 YILWILLFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALF 233
|
250 260 270
....*....|....*....|....*....|....
gi 339895785 419 TLLVVQVSILYYGGHLVISGQMTSGNLIA--FII 450
Cdd:cd18571 234 INQLKNILITFLAAKLVIDGEITLGMMLAiqYII 267
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
580-650 |
2.54e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895785 580 LSGGQKQRVAMARAL---VRNPPVLILDEATSALDAESeylIQQAIHGNL----QKHTVLIIAHRLSTVEHAHLIVVL 650
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHD---IKALIYVLQslthQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
463-636 |
2.63e-04 |
|
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: 44.39 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 463 SFSLS-------PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKpISaYDHKYlhrvISLVSQEPV--LFARSI 533
Cdd:COG1245 353 GFSLEveggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-IS-YKPQY----ISPDYDGTVeeFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 534 TDNIsyglPTVPFEmvVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:COG1245 427 TDDF----GSSYYK--TEIIKPLG----LEKLLDKNVKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180
....*....|....*....|....*
gi 339895785 614 SEYLIQQAI--HGNLQKHTVLIIAH 636
Cdd:COG1245 490 QRLAVAKAIrrFAENRGKTAMVVDH 514
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
245-385 |
2.67e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), 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: 350045 [Multi-domain] Cd Length: 314 Bit Score: 43.46 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 245 IRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSL 324
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895785 325 S-WqlslvTFMGFPIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEE 385
Cdd:cd18601 158 NpW-----VLIPVIPLVILFLFLRRYYLKTSREVKriEGTTRSPvfSHLSSTLQGLWTIRAYSAQE 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
580-666 |
2.85e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 580 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI----QQAIHgnLQKHTVLI--IAHRLSTVEHAHLIVVLDKG 653
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIvkclQQIVH--LTEATVLMslLQPAPETFDLFDDIILLSEG 414
|
90
....*....|...
gi 339895785 654 RVVQQGTHQQLLA 666
Cdd:PLN03140 415 QIVYQGPRDHILE 427
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
260-450 |
3.01e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 43.42 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 339
Cdd:cd18561 70 HLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 340 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAymyYVWGSGLT 419
Cdd:cd18561 150 PLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAV---SLLSSGIM 226
|
170 180 190
....*....|....*....|....*....|....
gi 339895785 420 LLVVQVSI---LYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18561 227 GLATALGTalaLGVGALRVLGGQLTLSSLLLILF 260
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
460-613 |
4.83e-04 |
|
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: 43.39 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 460 ENVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL-DGKPISAYDHkylhrvislvSQEPVLFARSITDNIS 538
Cdd:TIGR03719 339 DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQ----------SRDALDPNKTVWEEIS 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 539 YGLPTVpfeMV--VEAAQKANAHGFIMELQDgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 613
Cdd:TIGR03719 409 GGLDII---KLgkREIPSRAYVGRFNFKGSD-----QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
226-412 |
5.85e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging 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: 350043 [Multi-domain] Cd Length: 313 Bit Score: 42.55 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 226 STAVVIVCLLAIgssfaagiRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNIN 305
Cdd:cd18599 66 GSILVILLLSLI--------RGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 306 VFLRNTVKVTGVVVF-MFSLSWQLslvtfMGFPIIMMVSNIYGKYYKRLSKEvqnaLARASNTAE--------ETISAMK 376
Cdd:cd18599 138 NFLQNVLLVVFSLIIiAIVFPWFL-----IALIPLAIIFVFLSKIFRRAIRE----LKRLENISRsplfshltATIQGLS 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 339895785 377 TVRSFANEEEeaevYLRKLQQVykLNRKEAAAYMYY 412
Cdd:cd18599 209 TIHAFNKEKE----FLSKFKKL--LDQNSSAFFLFN 238
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
579-611 |
1.91e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|...
gi 339895785 579 QLSGGQKQRVAMARALVRNPPVLILDEATSALD 611
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
459-639 |
2.05e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 459 MENVSFSLSPGKVTALVGPSGSGKSSCVNILENfyPLEGGRVLLDGKpISAYDHKylhrvislvsQEPvlFAR------- 531
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKK----------QET--FARisgyceq 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 532 --------SITDNISY-GLPTVPFEmvVEAAQKANAHGFIMEL------QDGYSTETGEKGaqLSGGQKQRVAMARALVR 596
Cdd:PLN03140 961 ndihspqvTVRESLIYsAFLRLPKE--VSKEEKMMFVDEVMELveldnlKDAIVGLPGVTG--LSTEQRKRLTIAVELVA 1036
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 339895785 597 NPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLS 639
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTgRTVVCTIHQPS 1080
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
579-648 |
2.58e-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: 41.11 E-value: 2.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895785 579 QLSGGQKQRVAMarALV-----RNP-PVLILDEATSALDAESEYLIQQAIHgNLQKHT-VLIIAHRLSTVEHAHLIV 648
Cdd:pfam02463 1077 LLSGGEKTLVAL--ALIfaiqkYKPaPFYLLDEIDAALDDQNVSRVANLLK-ELSKNAqFIVISLREEMLEKADKLV 1150
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
579-614 |
4.67e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 4.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 339895785 579 QLSGGQKQ------RVAMARALVRNPPVLILDEATSALDAES 614
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
575-618 |
4.68e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 4.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 339895785 575 EKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 618
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEI 443
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
440-651 |
7.86e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 440 MTSGNLIAFIIYEFVLGDcmenVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDH 512
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD----LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 513 KYLHRVISLVSQEPVLFARSITDNISyglpTVPfemvveaaqkANAHGFimELQDGYStetgEKGAQLSGGQKQRVAMAR 592
Cdd:PRK13541 77 HNLGLKLEMTVFENLKFWSEIYNSAE----TLY----------AAIHYF--KLHDLLD----EKCYSLSSGMQKIVAIAR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895785 593 ALVRNPPVLILDEATSALDAESEYLIQQ--AIHGNlQKHTVLIIAHRLSTVEHAhLIVVLD 651
Cdd:PRK13541 137 LIACQSDLWLLDEVETNLSKENRDLLNNliVMKAN-SGGIVLLSSHLESSIKSA-QILQLD 195
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
188-449 |
8.11e-03 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350006 [Multi-domain] Cd Length: 289 Bit Score: 38.76 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 188 LVAASFFLIVAALGEtflPYYTGRAIDGIVIQKSmdqfstavvIVCLLAIGSSF-AAGIRGGIFTLIFA-RLNIRLRNCL 265
Cdd:cd18562 4 LALANVALAGVQFAE---PVLFGRVVDALSSGGD---------AFPLLALWAALgLFSILAGVLVALLAdRLAHRRRLAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 266 ----FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 341
Cdd:cd18562 72 masyFEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895785 342 VSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVyklnrkEAAAYMYYVWGSGLTLL 421
Cdd:cd18562 152 LNRLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRL------LAAQYPVLNWWALASVL 225
|
250 260 270
....*....|....*....|....*....|....
gi 339895785 422 ------VVQVSILYYGGHLVISGQMTSGNLIAFI 449
Cdd:cd18562 226 traastLTMVAIFALGAWLVQRGELTVGEIVSFV 259
|
|
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