|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
44-738 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 761.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 44 FDSVLDLWAACLYRSCLLLGATIGVAKNSAlgpRRLRASWL-VITLVCLFVGIYAMVKLLLFSEVRRPI--RDPWFWALF 120
Cdd:TIGR00958 35 EKGLYVLWLEGTLRLGVLWLGALGILLNKA---GGLLAAVKpLVAALCLATPSLSSLRALAFWEALDPAvrVALGLWSWF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 121 VWTYISLGASFLLWWLLSTvrPGTQALEPgaateaegfpgsgrpPPEQAS-GATLQKLLSYTKPDVAFLVAASFFLIVAA 199
Cdd:TIGR00958 112 VWSYGAALPAAALWAVLSS--AGASEKEA---------------EQGQSEtADLLFRLLGLSGRDWPWLISAFVFLTLSS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 200 LGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDE 279
Cdd:TIGR00958 175 LGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 280 NRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQN 359
Cdd:TIGR00958 255 NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 360 ALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQ 439
Cdd:TIGR00958 335 AVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 440 MTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHT 519
Cdd:TIGR00958 415 VSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDN 599
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVREN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 600 ISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 679
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 680 LIQQAIhgNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 738
Cdd:TIGR00958 655 LLQESR--SRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
169-744 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 598.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 169 ASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGG 248
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 249 IFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQL 328
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 329 SLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAA 408
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 409 YMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPT 488
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 489 MVH-DGSLAPDHLEGRVDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG 567
Cdd:COG1132 324 IPDpPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 568 KPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQ 647
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 648 KQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 727
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*..
gi 767973635 728 LAQGGLYAKLVQRQMLG 744
Cdd:COG1132 562 LARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
191-479 |
0e+00 |
|
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: 528.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767973635 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
174-742 |
1.03e-152 |
|
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: 462.00 E-value: 1.03e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 174 LQKLLSYTKPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLI 253
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLAL---ATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 254 FARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 334 MGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV 413
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 414 WGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYefvlgdcmesVGSVYSGLMQGVG----------AAEKVFEFI 483
Cdd:COG2274 383 TLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNIL----------SGRFLAPVAQLIGllqrfqdakiALERLDDIL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 484 DRQPTMVHDGS-LAPDHLEGRVDFENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGR 562
Cdd:COG2274 453 DLPPEREEGRSkLSLPRLKGDIELENVSFRYPGDS-PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 563 VLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQ 642
Cdd:COG2274 532 ILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSN 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 643 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 722
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDG 691
|
570 580
....*....|....*....|
gi 767973635 723 THQQLLAQGGLYAKLVQRQM 742
Cdd:COG2274 692 THEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
174-741 |
2.42e-150 |
|
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: 451.08 E-value: 2.42e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 174 LQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLI 253
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 254 FARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:TIGR02204 86 GERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 334 MGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV 413
Cdd:TIGR02204 166 LAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 414 WGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTM---V 490
Cdd:TIGR02204 246 AIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIkapA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 491 HDGSLaPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI 570
Cdd:TIGR02204 326 HPKTL-PVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 571 SAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQR 650
Cdd:TIGR02204 405 RQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 651 VAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:TIGR02204 485 IAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
570
....*....|.
gi 767973635 731 GGLYAKLVQRQ 741
Cdd:TIGR02204 565 GGLYARLARLQ 575
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
493-718 |
2.36e-148 |
|
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: 432.67 E-value: 2.36e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 493 GSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA 572
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 573 YDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVA 652
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 718
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
173-737 |
3.73e-141 |
|
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: 427.21 E-value: 3.73e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 173 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQfstaVVIVCLLAIGSSFAAGIRGGIFTL 252
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSV----LWWVPLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 253 IFARLNIR----LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQL 328
Cdd:TIGR02203 77 LLSWVSNKvvrdIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 329 SLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAA 408
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 409 YMYYvwgSGLTLLVVQVS---ILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDr 485
Cdd:TIGR02203 237 GSIS---SPITQLIASLAlavVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 486 QPTMVHDGSLAPDHLEGRVDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL 565
Cdd:TIGR02203 313 SPPEKDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 566 DGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLS 644
Cdd:TIGR02203 392 DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 645 GGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTH 724
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTH 551
|
570
....*....|...
gi 767973635 725 QQLLAQGGLYAKL 737
Cdd:TIGR02203 552 NELLARNGLYAQL 564
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
191-479 |
1.09e-129 |
|
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: 387.28 E-value: 1.09e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767973635 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
504-741 |
2.06e-119 |
|
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: 358.78 E-value: 2.06e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 664 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 741
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
173-741 |
2.50e-115 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 360.49 E-value: 2.50e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 173 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDgiviqksmDQFSTA----VVIVCLLAIGSSFAAGIRGG 248
Cdd:PRK11176 12 TFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLD--------DGFGKAdrsvLKWMPLVVIGLMILRGITSF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 249 IFTLIFA------RLNIRLRncLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMF 322
Cdd:PRK11176 84 ISSYCISwvsgkvVMTMRRR--LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 323 SLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrKLQQVYKLN 402
Cdd:PRK11176 162 YYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK----RFDKVSNRM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 403 RKEAaayMYYVWGSGLTLLVVQ-------VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGA 475
Cdd:PRK11176 238 RQQG---MKMVSASSISDPIIQliaslalAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 476 AEKVFEFIDRQPTmVHDGSLAPDHLEGRVDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF 555
Cdd:PRK11176 315 CQTLFAILDLEQE-KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 556 YPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYST 634
Cdd:PRK11176 393 YDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDT 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 635 ETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH-TVLIIAHRLSTVEHAHLIVVL 713
Cdd:PRK11176 473 VIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALD-ELQKNrTSLVIAHRLSTIEKADEILVV 551
|
570 580
....*....|....*....|....*...
gi 767973635 714 DKGRVVQQGTHQQLLAQGGLYAKLVQRQ 741
Cdd:PRK11176 552 EDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
159-741 |
1.89e-110 |
|
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: 348.73 E-value: 1.89e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 159 PGSGRPPPEQASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLA-- 236
Cdd:COG5265 6 AMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAyg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 237 ---IGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDL---ISRLTSDT-TMVSDLVSQNINVFLR 309
Cdd:COG5265 86 llrLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIERGTKGIeFLLRFLLFNILPTLLE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 310 nTVKVTGVVVFMFSlsWQLSLVTFmgfpiIMMVSNIYgkyYKRLSKEVQNALARASNTAEeTISAMK---------TVRS 380
Cdd:COG5265 166 -IALVAGILLVKYD--WWFALITL-----VTVVLYIA---FTVVVTEWRTKFRREMNEAD-SEANTRavdsllnyeTVKY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 381 FANEEEEAEVYLRKLQqvyklnRKEAAAYMyyVWGSGLTLLVVQ--------VSILYYGGHLVISGQMTSGNLI---AFI 449
Cdd:COG5265 234 FGNEAREARRYDEALA------RYERAAVK--SQTSLALLNFGQaliialglTAMMLMAAQGVVAGTMTVGDFVlvnAYL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 450 IYEFV-LGdcmeSVGSVYSGLMQGVGAAEKVFEFIDRQPTmVHDgslAPD--HL---EGRVDFENVTFTYRtrPHTQVLQ 523
Cdd:COG5265 306 IQLYIpLN----FLGFVYREIRQALADMERMFDLLDQPPE-VAD---APDapPLvvgGGEVRFENVSFGYD--PERPILK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYG 603
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 604 LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQ 683
Cdd:COG5265 456 RPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQA 535
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 684 AIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 741
Cdd:COG5265 536 ALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
504-737 |
1.96e-102 |
|
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: 314.55 E-value: 1.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 664 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 737
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
175-732 |
2.95e-100 |
|
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: 320.55 E-value: 2.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 175 QKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIF 254
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 255 A-RLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTsdtTMVSDL-------VSQNINVFLrntVKVTgVVVFMFSLSW 326
Cdd:COG4988 86 AaRVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLT---EGVEALdgyfaryLPQLFLAAL---VPLL-ILVAVFPLDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 327 QLSLVTFMGFPII---MMvsnIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrklqQVYKLNR 403
Cdd:COG4988 159 LSGLILLVTAPLIplfMI---LVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAE-------RIAEASE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 404 KEAAAYMyyvwG-------SGLTL-LVVQVSI---LYYGGHLVISGQMT--SGNLIAFIIYEFVLGdcMESVGSVYSGLM 470
Cdd:COG4988 229 DFRKRTM----KvlrvaflSSAVLeFFASLSIalvAVYIGFRLLGGSLTlfAALFVLLLAPEFFLP--LRDLGSFYHARA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 471 QGVGAAEKVFEFIDRQPTMVHDGSL-APDHLEGRVDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV 549
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTApLPAAGPPSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 550 NILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQ 629
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 630 DGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHL 709
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADR 540
|
570 580
....*....|....*....|...
gi 767973635 710 IVVLDKGRVVQQGTHQQLLAQGG 732
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
191-479 |
3.04e-96 |
|
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: 300.41 E-value: 3.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKL-NRKEAAAYMYYVWGSGLTLLvVQVSILY 429
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLkDRRDTVRAVYLLVRRVLQLG-VQVLMLY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767973635 430 YGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18590 240 CGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
504-741 |
3.12e-96 |
|
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: 298.38 E-value: 3.12e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 664 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 741
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
502-732 |
8.74e-96 |
|
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: 297.21 E-value: 8.74e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 502 GRVDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 581
Cdd:cd03254 1 GEIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 662 PVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGG 732
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
173-750 |
2.71e-95 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 308.57 E-value: 2.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 173 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMdqfstAVVIVCLLA---IGSSFAAGIRGGI 249
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNL-----PLGLVAGLAaayVGLQLLAAGLHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 250 FTLIFARLNI----RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLS 325
Cdd:PRK10790 85 QSLLFNRAAVgvvqQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 326 WQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrKLQQVyklNRKE 405
Cdd:PRK10790 165 WRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGE----RMGEA---SRSH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 406 AAAYMYYVWGSGLTL--LVVQVSILYYGGHLVI-----SGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEK 478
Cdd:PRK10790 238 YMARMQTLRLDGFLLrpLLSLFSALILCGLLMLfgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 479 VFEFID--RQPTMVHDGSLApdhlEGRVDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY 556
Cdd:PRK10790 318 VFELMDgpRQQYGNDDRPLQ----SGRIDIDNVSFAYRD--DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 557 PLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPtVPFEMVVEAAQKANAHGFIMELQDGYSTET 636
Cdd:PRK10790 392 PLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 637 GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKG 716
Cdd:PRK10790 471 GEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRG 550
|
570 580 590
....*....|....*....|....*....|....
gi 767973635 717 RVVQQGTHQQLLAQGGLYAKLVQRQMLGLQPAAD 750
Cdd:PRK10790 551 QAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAAS 584
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
191-479 |
3.67e-93 |
|
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: 292.54 E-value: 3.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767973635 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
260-740 |
1.31e-92 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 300.53 E-value: 1.31e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDttmVSDLVsqniNVFLR-------NTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVAD---VDALD----NLYLRvllpllvALLVILAAVAFLAFFSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 333 FMGF-------PIIMMVSNiygkyyKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKE 405
Cdd:COG4987 162 ALGLllaglllPLLAARLG------RRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 406 AAAYMyyvWGSGLTLLVVQ---VSILYYGGHLVISGQMtSGNLIAFIIYeFVLGdCMESVGSVySGLMQGVG----AAEK 478
Cdd:COG4987 236 ARLSA---LAQALLQLAAGlavVAVLWLAAPLVAAGAL-SGPLLALLVL-AALA-LFEALAPL-PAAAQHLGrvraAARR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 479 VFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPL 558
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 559 EGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGE 638
Cdd:COG4987 388 QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 639 KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 718
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
490 500
....*....|....*....|..
gi 767973635 719 VQQGTHQQLLAQGGLYAKLVQR 740
Cdd:COG4987 548 VEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
504-741 |
1.24e-90 |
|
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: 283.99 E-value: 1.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03252 1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 664 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 741
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
178-743 |
5.92e-88 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 288.78 E-value: 5.92e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 178 LSYTKPD---VAFLVAASFFLIVAALGEtflPYYTGRAIDgiVIQKSMDQFSTAVVIVCLlaigssfaagirgGIFTLIF 254
Cdd:PRK13657 11 LQYLGAEkrlGILLAVANVLLAAATFAE---PILFGRIID--AISGKGDIFPLLAAWAGF-------------GLFNIIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 255 A--------RLNIRLRNCL----FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVsqnINVFLRNTVKVTGVVVFM- 321
Cdd:PRK13657 73 GvlvarhadRLAHRRRLAVlteyFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLW---LEFMREHLATLVALVVLLp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 322 --FSLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQNAL--------ARASntaeETISAMKTVRSFANEEEEAEVy 391
Cdd:PRK13657 150 laLFMNWRLSLVLV----VLGIVYTLITTLVMRKTKDGQAAVeehyhdlfAHVS----DAIGNVSVVQSYNRIEAETQA- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 392 LRKLqqvykLNRKEAAAYMYYVW---GSGLTLL---VVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSV 465
Cdd:PRK13657 221 LRDI-----ADNLLAAQMPVLSWwalASVLNRAastITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 466 YSGLMQgvgAAEKVFEFIDRQPTM--VHDGSLAPD--HLEGRVDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPS 541
Cdd:PRK13657 296 INQVFM---AAPKLEEFFEVEDAVpdVRDPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 542 GSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANA 621
Cdd:PRK13657 371 GAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 622 HGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRL 701
Cdd:PRK13657 451 HDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL 530
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 767973635 702 STVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQML 743
Cdd:PRK13657 531 STVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGM 572
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
193-479 |
1.79e-86 |
|
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: 275.12 E-value: 1.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 193 FFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQ 272
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 273 ETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKR 352
Cdd:cd18589 83 EIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 353 LSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGG 432
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767973635 433 HLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18589 243 QLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
146-739 |
1.25e-85 |
|
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: 286.07 E-value: 1.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 146 ALEPGaateaEGFPGSGRPPPEQASgatLQKLLSYTKPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQF 225
Cdd:TIGR03796 125 TFEPG-----PEFQKGGRKPSLLRA---LWRRLRGSRGALLYLLLAGLLLVLPGL---VIPAFSQIFVDEILVQGRQDWL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 226 STAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTmVSDLVSQNIN 305
Cdd:TIGR03796 194 RPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNDQ-VAEFLSGQLA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 306 VFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEE 385
Cdd:TIGR03796 273 TTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLES 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 386 EE----AEVYLRKLQQVYKLNRKEAaayMYYVWGSGLTLLVVqVSILYYGGHLVISGQMTSGNLIAFiiyEFVLGDCMES 461
Cdd:TIGR03796 353 DFfsrwAGYQAKLLNAQQELGVLTQ---ILGVLPTLLTSLNS-ALILVVGGLRVMEGQLTIGMLVAF---QSLMSSFLEP 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 462 VGSV--YSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPD--------HLEGRVDFENVTFTY-RTRPHtqVLQNVSFSLS 530
Cdd:TIGR03796 426 VNNLvgFGGTLQELEGDLNRLDDVLRNPVDPLLEEPEGSaatsepprRLSGYVELRNITFGYsPLEPP--LIENFSLTLQ 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 531 PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFE 610
Cdd:TIGR03796 504 PGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDA 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 611 MVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQaihgNLQ 690
Cdd:TIGR03796 584 DLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDD----NLR 659
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 767973635 691 KH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQ 739
Cdd:TIGR03796 660 RRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
191-479 |
4.43e-80 |
|
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: 258.33 E-value: 4.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQ------KSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNC 264
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHsgsggeEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 265 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYvwgSGLTLLVVQ 424
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGF---NGFMGAAAQ 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 425 VSI---LYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18780 238 LAIvlvLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
504-717 |
4.15e-78 |
|
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: 248.45 E-value: 4.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767973635 664 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGR 717
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
191-479 |
6.78e-77 |
|
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: 249.74 E-value: 6.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 191 ASFFLIVAALGETFLPYYTGRAID------GIVIQKSMDQFSTAVVIVCLLAIGSsFAAGIRGGIFTLIFARLNIRLRNC 264
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDvaskesGDIEIFGLSLKTFALALLGVFVVGA-AANFGRVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 265 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQ 424
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 425 VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18573 240 LSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
193-762 |
1.73e-76 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 257.72 E-value: 1.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 193 FFLIVAALGETFLPYYTGRAIDGIviqkSMDQFSTAVVIVCL--LAIGSSFAAGIRGGIFTLIFA---RLNIRLRNCLFR 267
Cdd:PRK10789 2 ALLIIIAMLQLIPPKVVGIIVDGV----TEQHMTTGQILMWIgtMVLIAVVVYLLRYVWRVLLFGasyQLAVELREDFYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFS-LSWQLSLVTFMGFPIIMMVSNIY 346
Cdd:PRK10789 78 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 347 GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANE-------EEEAEVYLRKLQQVYKLN-RKEAAAYMyyvwGSGL 418
Cdd:PRK10789 158 GDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEdrqsalfAADAEDTGKKNMRVARIDaRFDPTIYI----AIGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 419 T-LLVVQvsilyYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPtMVHDGSLAP 497
Cdd:PRK10789 234 AnLLAIG-----GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAP-VVKDGSEPV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 498 DHLEGRVDFENVTFTYrtrPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 575
Cdd:PRK10789 308 PEGRGELDVNIRQFTY---PQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 576 KYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:PRK10789 385 DSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIAR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYA 735
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYR 544
|
570 580
....*....|....*....|....*..
gi 767973635 736 KLVQRQMlgLQPAADFTAGHNEPVANG 762
Cdd:PRK10789 545 DMYRYQQ--LEAALDDAPEIREEAVDA 569
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
181-713 |
2.12e-73 |
|
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: 248.36 E-value: 2.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 181 TKPDVAFLVAASFFLIVAALGETFLpyyTGRAIDGIVIQKS-MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNI 259
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWL---LARVVDGLISAGEpLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQ---LSLVTFMGF 336
Cdd:TIGR02857 78 QLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWIsglILLLTAPLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 337 PIIMMVSniyGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVyLRKLQQVYklnRKEAAAYMYYVWGS 416
Cdd:TIGR02857 158 PIFMILI---GWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA-IRRSSEEY---RERTMRVLRIAFLS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 417 GLTL-----LVVQVSILYYGGHLViSGQMT--SGNLIAFIIYEFVLGdcMESVGSVYSGLMQGVGAAEKVFEFIDRQPTM 489
Cdd:TIGR02857 231 SAVLelfatLSVALVAVYIGFRLL-AGDLDlaTGLFVLLLAPEFYLP--LRQLGAQYHARADGVAAAEALFAVLDAAPRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 490 VHDGSLAPDHLEGRVDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKP 569
Cdd:TIGR02857 308 LAGKAPVTAAPASSLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 570 ISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQ 649
Cdd:TIGR02857 386 LADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQ 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 650 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVL 713
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
189-738 |
1.16e-68 |
|
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: 240.03 E-value: 1.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 189 VAASFFLIVAALGEtflpYYTGRAIDGIVIQKSMDQFStaVVIVCLLA--IGSSFAAGIRGGIFTLIFARLNIRLRNCLF 266
Cdd:TIGR01193 163 IAAIIVTLISIAGS----YYLQKIIDTYIPHKMMGTLG--IISIGLIIayIIQQILSYIQIFLLNVLGQRLSIDIILSYI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 267 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTgVVVFMFSLSWQLSLVTFMGFPIIMMVSNIY 346
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVI-VGLFLVRQNMLLFLLSLLSIPVYAVIIILF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 347 GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE-------EAEVYLRKlqqVYKLNRKEAAAYMYYVwgsgLT 419
Cdd:TIGR01193 316 KRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAEryskidsEFGDYLNK---SFKYQKADQGQQAIKA----VT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 420 LLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFE--FIDRQPTMVHDGSlAP 497
Cdd:TIGR01193 389 KLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEFINKKKRT-EL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 498 DHLEGRVDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY 577
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 578 LHRVISLVSQEPVLFARSITDNISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 656
Cdd:TIGR01193 546 LRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAK 736
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
..
gi 767973635 737 LV 738
Cdd:TIGR01193 705 LI 706
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
139-742 |
8.58e-68 |
|
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: 237.16 E-value: 8.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 139 TVRPGTQALEPGAATEAEGFPgsgRPPPEQASGAT--LQKLLSYTKPDVAFLVAASffLIVAALGeTFLPYYTGRAIDGI 216
Cdd:TIGR03797 93 TRRRVDAAMAATLAPEAYMFY---RPLPDKALGLRdlLRFALRGARRDLLAILAMG--LLGTLLG-MLVPIATGILIGTA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 217 VIQKSMDQfstaVVIVCLLAIGSSFAAGIrggiFTLIFARLNIRLRN--------CLFRSLVSQETSFFDENRTGDLISR 288
Cdd:TIGR03797 167 IPDADRSL----LVQIALALLAAAVGAAA----FQLAQSLAVLRLETrmdaslqaAVWDRLLRLPVSFFRQYSTGDLASR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 289 LTSDTTMVSDLVSQNINVFLRNTVKVTGVVVfMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTA 368
Cdd:TIGR03797 239 AMGISQIRRILSGSTLTTLLSGIFALLNLGL-MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 369 EETIS-------AMKTVRSFAneeEEAEVYLRKLQQVYKLNRkeaaaymyyvWGSGLT-----LLVVQVSILYYgghLVI 436
Cdd:TIGR03797 318 VQLINgisklrvAGAENRAFA---RWAKLFSRQRKLELSAQR----------IENLLTvfnavLPVLTSAALFA---AAI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 437 SGQMTSG-NLIAFIIYEFVLGDCMESVGSVySGLMQGVGAAEKVFEFID---RQPTMVHDGSLAPDHLEGRVDFENVTFT 512
Cdd:TIGR03797 382 SLLGGAGlSLGSFLAFNTAFGSFSGAVTQL-SNTLISILAVIPLWERAKpilEALPEVDEAKTDPGKLSGAIEVDRVTFR 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 513 YRtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLF 592
Cdd:TIGR03797 461 YR-PDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLM 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 593 ARSITDNISYGLPTVPfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:TIGR03797 540 SGSIFENIAGGAPLTL-DEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSA 618
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 673 LDAESEYLIQQAIHGnlQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQM 742
Cdd:TIGR03797 619 LDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQL 686
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
191-479 |
2.34e-64 |
|
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: 216.20 E-value: 2.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFST-AVVIVCLLAIGSSFAAgIRGGIFTLIFARLNIRLRNCLFRSL 269
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQiALLLLGLFLLQAVFSF-FRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 270 VSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKY 349
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 350 YKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILY 429
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767973635 430 YGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18576 240 YGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
421-730 |
2.87e-64 |
|
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: 224.24 E-value: 2.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 421 LVVQVSILYYGGHLVISGQMTSGNLIAFIIyefVLGDCM---ESVGSVYSGLMQGVGAAEKVFEFIDRQPTmvHDGSLAP 497
Cdd:COG4618 250 LLLQSAVLGLGAYLVIQGEITPGAMIAASI---LMGRALapiEQAIGGWKQFVSARQAYRRLNELLAAVPA--EPERMPL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 498 DHLEGRVDFENVTFTY--RTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 575
Cdd:COG4618 325 PRPKGRLSVENLTVVPpgSKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 576 KYLHRVISLVSQEPVLFARSITDNISyGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:COG4618 402 EELGRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
502-722 |
1.25e-61 |
|
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: 206.29 E-value: 1.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 502 GRVDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 581
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 662 PVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 722
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
502-723 |
2.83e-61 |
|
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: 205.42 E-value: 2.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 502 GRVDFENVTFTYRtrPHTQ-VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR 580
Cdd:cd03244 1 GDIEFKNVSLRYR--PNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VISLVSQEPVLFARSITDNISyglptvPF-----EMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PFgeysdEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 723
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
188-479 |
8.24e-61 |
|
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: 206.63 E-value: 8.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeAAAYMYYVWG-SGLTLLVVQVS 426
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR-AARLSALFSPlIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767973635 427 ILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
471-741 |
1.33e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 214.71 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 471 QGVGAAEKVFEFIDRQPTMVHDGSlAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 550
Cdd:PRK11174 316 QAVGAAESLVTFLETPLAHPQQGE-KELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 551 ILENFYPLEGgRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQD 630
Cdd:PRK11174 395 ALLGFLPYQG-SLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 631 GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLI 710
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI 553
|
250 260 270
....*....|....*....|....*....|.
gi 767973635 711 VVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 741
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
188-479 |
4.34e-59 |
|
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: 202.27 E-value: 4.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDqfstAVVIVCLLAIGSSFAAGI--RGGIFTLIFARLNI--RLRN 263
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLE----ALLLVPLAIIGLFLLRGLasYLQTYLMAYVGQRVvrDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAymyyvwgSGLTLLVV 423
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARA-------RALSSPLM 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 424 QV-------SILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18552 230 ELlgaiaiaLVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
416-741 |
2.05e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.53 E-value: 2.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 416 SGLTLLVvqvsILYYGGHLViSGQMTSGNLIAFIIyeFVLGDCMES---VGSVYSGLMQGVGAAEKVFEFIDRQPTMVHD 492
Cdd:PRK11160 255 NGLTVVL----MLWLAAGGV-GGNAQPGALIALFV--FAALAAFEAlmpVAGAFQHLGQVIASARRINEITEQKPEVTFP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 493 GSLAPDHLEGRVDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA 572
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 573 YDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFImELQDGYSTETGEKGAQLSGGQKQRVA 652
Cdd:PRK11160 407 YSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLG 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGG 732
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
....*....
gi 767973635 733 LYAKLVQRQ 741
Cdd:PRK11160 566 RYYQLKQRL 574
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
188-455 |
2.54e-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: 194.01 E-value: 2.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIG--SSFAAGIRGGIFTLIFARLNIRLRNCL 265
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGlaQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 266 FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNI 345
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 346 YGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQV 425
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|
gi 767973635 426 SILYYGGHLVISGQMTSGNLIAFIIYEFVL 455
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQL 270
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
191-479 |
4.11e-54 |
|
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: 188.46 E-value: 4.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYmyyvwgSGLTLLVVQ------ 424
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRAR------ALLTALVIFlvfgai 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 425 VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18575 235 VFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
421-730 |
4.46e-54 |
|
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: 195.64 E-value: 4.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 421 LVVQVSILYYGGHLVISGQMTSGNLIA-FIIYEFVLGDCMESVGsVYSGLMQGVGAAEKVFEFIDRQPtmvhdgsLAPDH 499
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAgSILVGRALAPIDGAIG-GWKQFSGARQAYKRLNELLANYP-------SRDPA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 500 L-----EGRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD 574
Cdd:TIGR01842 308 MplpepEGHLSVENVTIVP-PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 575 HKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMA 654
Cdd:TIGR01842 387 RETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALA 466
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 655 RALVRNPPVLILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIkALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
175-739 |
1.33e-53 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 201.41 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 175 QKLLSYTKpDVAF-----LVAASFFLIVAALgetfLPYYTGRAIDGIVIQKSMDQFStavVIVCLLAIGSSFAAGIRGGI 249
Cdd:PTZ00265 818 REIFSYKK-DVTIialsiLVAGGLYPVFALL----YAKYVSTLFDFANLEANSNKYS---LYILVIAIAMFISETLKNYY 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 250 FTLIFARLNIRLRNCLFRSLVSQETSFFDE--NRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK--VTGVVVFMFSlS 325
Cdd:PTZ00265 890 NNVIGEKVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLflVSMVMSFYFC-P 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 326 WQLSLVTFMGFpIIMMVSNIYGKYYKrlSKEVQNALARASNTA-----------------EETISAMKTVRSFANEE--- 385
Cdd:PTZ00265 969 IVAAVLTGTYF-IFMRVFAIRARLTA--NKDVEKKEINQPGTVfaynsddeifkdpsfliQEAFYNMNTVIIYGLEDyfc 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 386 ---EEAEVYLRKLQQvyklnRKEAAAYMyyVWG-SGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIiYEFVLgdcmes 461
Cdd:PTZ00265 1046 nliEKAIDYSNKGQK-----RKTLVNSM--LWGfSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSL-FTFLF------ 1111
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 462 VGSVYSGLMQGVGAAEKV-FEFIDRQPTMVH--------DGSLA---PDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSL 529
Cdd:PTZ00265 1112 TGSYAGKLMSLKGDSENAkLSFEKYYPLIIRksnidvrdNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSC 1191
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 530 SPGKVTALVGPSGSGKSSCVNILENFYPLE-------------------------------------------------- 559
Cdd:PTZ00265 1192 DSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedst 1271
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 560 ----GGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTE 635
Cdd:PTZ00265 1272 vfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTN 1351
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 636 TGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK--HTVLIIAHRLSTVEHAHLIVVL 713
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIITIAHRIASIKRSDKIVVF 1431
|
650 660 670
....*....|....*....|....*....|..
gi 767973635 714 DK----GRVVQ-QGTHQQLL-AQGGLYAKLVQ 739
Cdd:PTZ00265 1432 NNpdrtGSFVQaHGTHEELLsVQDGVYKKYVK 1463
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
188-479 |
1.91e-53 |
|
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: 186.87 E-value: 1.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV-WGSGLTLLVVqVS 426
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWpLMDFLSGLQI-VL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767973635 427 ILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18542 240 VLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
188-713 |
7.22e-52 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 196.02 E-value: 7.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFflIVAALGETFLPYYTgrAIDGiVIQKSMDQFSTA-VVIVCLLAIG---------SSFAAGIrggIFTLIFARL 257
Cdd:PTZ00265 61 LLGVSF--VCATISGGTLPFFV--SVFG-VIMKNMNLGENVnDIIFSLVLIGifqfilsfiSSFCMDV---VTTKILKTL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 258 NIRLrnclFRSLVSQETSFFDENRTgdliSRLTSDTTMVSDLVSQNINV----FLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:PTZ00265 133 KLEF----LKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIGTkfitIFTYASAFLGLYIWSLFKNARLTLCIT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 334 MGFPIIMMVSNIYGKYYKrLSKevQNALARASNTA---EETISAMKTVRSFANEEEEAEVY--LRKLQQVY--KLNRKEA 406
Cdd:PTZ00265 205 CVFPLIYICGVICNKKVK-INK--KTSLLYNNNTMsiiEEALVGIRTVVSYCGEKTILKKFnlSEKLYSKYilKANFMES 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 407 -----------AAYMYYVWgSGLTLLVVQVSILY----YGGHLVISgqMTSGNLIAFIIYEFVLGDCMEsvgsvysgLMQ 471
Cdd:PTZ00265 282 lhigmingfilASYAFGFW-YGTRIIISDLSNQQpnndFHGGSVIS--ILLGVLISMFMLTIILPNITE--------YMK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 472 GVGAAEKVFEFIDRQPTMVH--DGSLAPDhlEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV 549
Cdd:PTZ00265 351 SLEATNSLYEIINRKPLVENndDGKKLKD--IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 550 NILENFY-PLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGL------------------------ 604
Cdd:PTZ00265 429 KLIERLYdPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenk 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 605 ---------------------------------PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRV 651
Cdd:PTZ00265 509 nkrnscrakcagdlndmsnttdsneliemrknyQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRI 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 652 AMARALVRNPPVLILDEATSALDAESEYLIQQAIH---GNLQKHTVlIIAHRLSTVEHAHLIVVL 713
Cdd:PTZ00265 589 SIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkGNENRITI-IIAHRLSTIRYANTIFVL 652
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
226-701 |
2.08e-51 |
|
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: 187.95 E-value: 2.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 226 STAVVIVCLLAIGSSFAAGI-RGGIFTLIFARLNiRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 304
Cdd:TIGR02868 53 SVAAVAVRAFGIGRAVFRYLeRLVGHDAALRSLG-ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 305 NVFLRNTVKVTGVVVFMFSLSWQLSLVT--------FMGFPIIMMVSNIYGKYYKRLSKEVQNALARA-SNTAEETIS-A 374
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALILaaglllagFVAPLVSLRAARAAEQALARLRGELAAQLTDAlDGAAELVASgA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 375 MKTVRSfanEEEEAEVYLRKLQQvyklNRKEAAAymyyvWGSGLTLLVVQVSI---LYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:TIGR02868 212 LPAALA---QVEEADRELTRAER----RAAAATA-----LGAALTLLAAGLAVlgaLWAGGPAVADGRLAPVTLAVLVLL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 452 EFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDrQPTMVHDGSLAPDHLEG----RVDFENVTFTYRTRPhtQVLQNVSF 527
Cdd:TIGR02868 280 PLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD-AAGPVAEGSAPAAGAVGlgkpTLELRDLSAGYPGAP--PVLDGVSL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 528 SLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTV 607
Cdd:TIGR02868 357 DLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 608 PFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG 687
Cdd:TIGR02868 437 TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA 516
|
490
....*....|....
gi 767973635 688 NLQKHTVLIIAHRL 701
Cdd:TIGR02868 517 ALSGRTVVLITHHL 530
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
188-479 |
2.75e-49 |
|
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: 174.93 E-value: 2.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMdqfSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSS---GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAaymYYVWGSGLTLLVVQVS- 426
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAK---IEALIGPLMGLAVQLAl 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 427 --ILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18551 235 lvVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
188-451 |
1.25e-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: 170.67 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQK-SMDQFSTAVVIVCLLAIGSsfaAGIR-GGIFTLIFARLNI--RLRN 263
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLI---GIFRfLWRYLIFGASRRIeyDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaayMYYVWG-------- 415
Cdd:cd18541 158 YRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR-----LARVDAlffpligl 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 767973635 416 -SGLTLLVVqvsiLYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18541 233 lIGLSFLIV----LWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
504-730 |
5.13e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 166.74 E-value: 5.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPV--LFARSITDNISYGlPT---VPFEMVVEAAQKA-NAHGfIMELQDgYSTetgekgAQLSGGQKQRVAMARAL 657
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFG-PEnlgLPREEIRERVEEAlELVG-LEHLAD-RPP------HELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 658 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
178-489 |
8.73e-47 |
|
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: 169.17 E-value: 8.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 178 LSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVV---IVCLLAIGSSFAAGIRGGIFTLIF 254
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFwalMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 255 ARLNIRLRNCLFRSLVSQETSFFD--ENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMyy 412
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISG-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 413 vWGSGLT---LLVVQVSILYYGGHLVISGQMTSGNLiaFIIYEFVLGdCMESVGSVYSGL---MQGVGAAEKVFEFIDRQ 486
Cdd:cd18578 239 -LGFGLSqslTFFAYALAFWYGGRLVANGEYTFEQF--FIVFMALIF-GAQSAGQAFSFApdiAKAKAAAARIFRLLDRK 314
|
...
gi 767973635 487 PTM 489
Cdd:cd18578 315 PEI 317
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
219-739 |
1.94e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 176.32 E-value: 1.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 219 QKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMV 296
Cdd:PLN03232 941 QSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAakRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDI 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 297 SDLVSQNINVFLRNTVKVTGVVVFMFSLSwQLSLVTFMgfPIIMMVSNIYgKYYKRLSKEVQ--NALARASNTAE--ETI 372
Cdd:PLN03232 1021 DRNVANLMNMFMNQLWQLLSTFALIGTVS-TISLWAIM--PLLILFYAAY-LYYQSTSREVRrlDSVTRSPIYAQfgEAL 1096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 373 SAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV-----WGSGLTLLVVQVSILYYG---GHLVISGQMtsGN 444
Cdd:PLN03232 1097 NGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTirletLGGVMIWLTATFAVLRNGnaeNQAGFASTM--GL 1174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 445 LIAFIIyefvlgdcmeSVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLE-----------GRVDFENVTFTY 513
Cdd:PLN03232 1175 LLSYTL----------NITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIEnnrpvsgwpsrGSIKFEDVHLRY 1244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 514 RtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLF 592
Cdd:PLN03232 1245 R--PGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLF 1322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 593 ARSITDNISyglptvPFEM-----VVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILD 667
Cdd:PLN03232 1323 SGTVRFNID------PFSEhndadLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 668 EATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLA-QGGLYAKLVQ 739
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSrDTSAFFRMVH 1469
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
188-451 |
2.56e-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: 164.10 E-value: 2.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDqfSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARL--NI--RLRN 263
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGD--LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLgqRIiyDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18544 79 DLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEaaAYMYYVWGSGLTLL-- 421
Cdd:cd18544 159 YLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKS--IKLFALFRPLVELLss 236
|
250 260 270
....*....|....*....|....*....|
gi 767973635 422 VVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18544 237 LALALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
507-718 |
6.82e-45 |
|
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: 158.92 E-value: 6.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTY--RTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISL 584
Cdd:cd03246 4 ENVSFRYpgAEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 585 VSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVL 664
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 665 ILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 718
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
188-479 |
1.24e-44 |
|
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: 162.64 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIV----IQKSMDQFSTAVVIVCL----LAIGSSFAAGIRGGIFTLIFARLNI 259
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsGESSPDEFLDDVNKYALyfvyLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 339
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 340 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMyyvWGSGLT 419
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSG---LGLGLL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 420 LLVVQVSI---LYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18577 238 FFIIFAMYalaFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
506-699 |
2.44e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.44 E-value: 2.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRViSL 584
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQV-AY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 585 VSQEPVLFARSITDNISYglptvPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPV 663
Cdd:COG4619 79 VPQEPALWGGTVRDNLPF-----PFQLRERKFDRERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLLQPDV 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 767973635 664 LILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAH 699
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSH 189
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
234-734 |
6.96e-44 |
|
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: 171.67 E-value: 6.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 234 LLAIGSSFAAGIrGGIFTlifARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 313
Cdd:TIGR00957 1020 FAVFGYSMAVSI-GGIQA---SR---VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFN 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 314 VTGVVVFMFsLSWQLSLVTFMGFPII-MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFaNEEEEAEVyl 392
Cdd:TIGR00957 1093 VIGALIVIL-LATPIAAVIIPPLGLLyFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIH-- 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 393 rklQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVS---ILYYGGHLVISGQMTSGNLIAFII-YEFVLGDCMESVGSVYSG 468
Cdd:TIGR00957 1169 ---QSDLKVDENQKAYYPSIVANRWLAVRLECVGnciVLFAALFAVISRHSLSAGLVGLSVsYSLQVTFYLNWLVRMSSE 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 469 LMQGVGAAEKVFEF--IDRQPTMVHDGSLAPDHL--EGRVDFENvtFTYRTRPHTQ-VLQNVSFSLSPGKVTALVGPSGS 543
Cdd:TIGR00957 1246 METNIVAVERLKEYseTEKEAPWQIQETAPPSGWppRGRVEFRN--YCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGA 1323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 544 GKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPF-----EMVVEAAQK 618
Cdd:TIGR00957 1324 GKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD------PFsqysdEEVWWALEL 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 619 ANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIA 698
Cdd:TIGR00957 1398 AHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIA 1477
|
490 500 510
....*....|....*....|....*....|....*.
gi 767973635 699 HRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLY 734
Cdd:TIGR00957 1478 HRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
497-723 |
8.00e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 157.19 E-value: 8.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 497 PDHleGRVDFENVTFTYRtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 575
Cdd:cd03369 2 PEH--GEIEVENLSVRYA--PDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 576 KYLHRVISLVSQEPVLFARSITDNISyglptvPFEMVVEAAqkanahgfIMElqdgySTETGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSNLD------PFDEYSDEE--------IYG-----ALRVSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 723
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
446-730 |
2.42e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 164.31 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 446 IAFIIYEFVLGDCMESVGSV---YSGLMQGVGAAEKVFEFIDR---QPTMVHDGSLAPDHLEGR---VDFENVTFTYRTR 516
Cdd:COG1123 194 TTVLLITHDLGVVAEIADRVvvmDDGRIVEDGPPEEILAAPQAlaaVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 517 P--HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH---KYLHRVISLVSQEPV- 590
Cdd:COG1123 274 GkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYs 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 -LFAR-SITDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:COG1123 354 sLNPRmTVGDIIAEPL------RLHGLLSRAERRERVAELLErvGLPPDLADRyPHELSGGQRQRVAIARALALEPKLLI 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973635 666 LDEATSALDaeseYLIQQAIHGNLQK------HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:COG1123 428 LDEPTSALD----VSVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
504-717 |
3.23e-43 |
|
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: 155.32 E-value: 3.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgrvlldgkpisaydHKYLHR 580
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSG--------------SVSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VISLVSQEPVLFARSITDNISYGLPTVP--FEMVVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARAL 657
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPFDEerYEKVIKACAlEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973635 658 VRNPPVLILDEATSALDAE-SEYLIQQAIHGNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGR 717
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
506-717 |
3.71e-43 |
|
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: 155.32 E-value: 3.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:cd03225 2 LKNLSFSYPDGA-RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEP--VLFARSITDNISYGLP--TVPFEMVVEAAQKANAHGFIMELQDgYSTETgekgaqLSGGQKQRVAMARALVRNP 661
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALELVGLEGLRD-RSPFT------LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 662 PVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGR 717
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
504-721 |
5.92e-43 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 154.94 E-value: 5.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTR-PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkyLHRVI 582
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEPVLFA-RSITDNISYGLptvpfEM--VVEAAQKANAHGFImelqdgysTETGEKGA------QLSGGQKQRVAM 653
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL-----ELqgVPKAEARERAEELL--------ELVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 654 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLStvEHAHL---IVVLDK--GRVVQQ 721
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDID--EAVFLadrVVVLSArpGRIVAE 215
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
256-450 |
8.38e-43 |
|
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: 157.32 E-value: 8.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 256 RLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDttmVSDLVS---QNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSsfkQCVSQGLRSVTQTVGCVVSLYLISPKLTLLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYY 412
Cdd:cd18574 149 LVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIF 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 767973635 413 VWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18574 229 QGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
504-730 |
1.08e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.84 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvIS 583
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNIS-----YGLPTVPFEMVVEAAQKAnahgfiMELQDgystETGEKGAQLSGGQKQRVAMARAL 657
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEARERIDELLEL------FGLTD----AADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 658 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
188-451 |
4.63e-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: 154.93 E-value: 4.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeAAAYMYYVWGS-GLTLLVVQVS 426
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMR-AVRLNALFWPLvELISALGTAL 240
|
250 260
....*....|....*....|....*
gi 767973635 427 ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGY 265
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
504-727 |
2.16e-41 |
|
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: 150.79 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLE--GGRVLLDGKPISAYDHK-- 576
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPGApdEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 577 YLHRVISLVSQEPVLFARSITDNISYGLP-------TVPFEMVVEAAQKANAHGFIMELQDGYStetgekgaqLSGGQKQ 649
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 650 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 727
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
189-451 |
2.57e-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: 153.05 E-value: 2.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 189 VAASFFLIVAAlgeTFL----PYYTGRAIDGIVIQKSMDQFSTAVVIVCL----LAIGSSFAAGIRGGIFTLIFARLNIR 260
Cdd:cd18563 1 LILGFLLMLLG---TALglvpPYLTKILIDDVLIQLGPGGNTSLLLLLVLglagAYVLSALLGILRGRLLARLGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 261 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaAAYMYYVWGSGLTL 420
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR--AEKLWATFFPLLTF 235
|
250 260 270
....*....|....*....|....*....|...
gi 767973635 421 LVV--QVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18563 236 LTSlgTLIVWYFGGRQVLSGTMTLGTLVAFLSY 268
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
507-728 |
3.89e-41 |
|
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: 150.96 E-value: 3.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 586
Cdd:COG1120 5 ENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPVL-FARSITDNISYG-LPTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMAR 655
Cdd:COG1120 82 QEPPApFGLTVRELVALGrYPHLGLfgrpsaedrEAVEEALERTG----LEHLADRPVDE-------LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLL 728
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
250-739 |
5.35e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 162.60 E-value: 5.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 250 FTLIFARLNI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSwQ 327
Cdd:PLN03130 975 YWLIMSSLYAakRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVS-T 1053
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 328 LSLVTFMgfPIIMMVSNIYgKYYKRLSKEVQ--NALARASNTAE--ETISAMKTVRSFANEEEEAEVYLRKLQQvyklNR 403
Cdd:PLN03130 1054 ISLWAIM--PLLVLFYGAY-LYYQSTAREVKrlDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDN----NI 1126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 404 KEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFI 483
Cdd:PLN03130 1127 RFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAV 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 484 DRQPTMVHDGSLAPDHLE-----------GRVDFENVTFTYRTR--PhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 550
Cdd:PLN03130 1207 ERVGTYIDLPSEAPLVIEnnrpppgwpssGSIKFEDVVLRYRPElpP---VLHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 551 ILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQKANAHGFI 625
Cdd:PLN03130 1284 ALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD------PFNEhndadLWESLERAHLKDVI 1357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 626 MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVE 705
Cdd:PLN03130 1358 RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTII 1437
|
490 500 510
....*....|....*....|....*....|....*
gi 767973635 706 HAHLIVVLDKGRVVQQGTHQQLLA-QGGLYAKLVQ 739
Cdd:PLN03130 1438 DCDRILVLDAGRVVEFDTPENLLSnEGSAFSKMVQ 1472
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
506-722 |
8.84e-41 |
|
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: 147.46 E-value: 8.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYrtrPH--TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDhKYLHRVIS 583
Cdd:cd03247 3 INNVSFSY---PEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 664 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 722
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
504-722 |
1.60e-40 |
|
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: 148.42 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRP-HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYLH 579
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 RVISLVSQEPVL---FARSITDNISYGLptVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 656
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIAEPL--RIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 722
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLK-KLQEElglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
501-719 |
2.91e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 148.70 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 501 EGRVDFENVTFTYRTRP-HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylh 579
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 rvISLVSQEPVLFA-RSITDNISYGLptvpfEMVVEAAQKANAHgfIMELQDgystETGEKGA------QLSGGQKQRVA 652
Cdd:COG1116 82 --RGVVFQEPALLPwLTVLDNVALGL-----ELRGVPKAERRER--ARELLE----LVGLAGFedayphQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAH------RLSTVehahlIVVLDK--GRVV 719
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHdvdeavFLADR-----VVVLSArpGRIV 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
522-671 |
1.03e-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: 143.56 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFAR-SITDNI 600
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 601 SYGLptvPFEMVVEAAQKANAHGFI--MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 671
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
504-730 |
1.62e-39 |
|
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: 145.80 E-value: 1.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfYPLEGgRVLLDGKPISAYDHKYL- 578
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLE--RPTSG-SVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 --HRVISLVSQEPVLF-ARSITDNISYglptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAM 653
Cdd:cd03258 79 kaRRRIGMIFQHFNLLsSRTVFENVAL-----PLE--IAGVPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 654 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLR-DINRElglTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 767973635 730 Q 730
Cdd:cd03258 231 N 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
504-722 |
2.87e-39 |
|
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: 144.58 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVI 582
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpER---RNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEPVLFA-RSITDNISYGLPtvpfEMVVEAAQKANAHGFIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:cd03259 75 GMVFQDYALFPhLTVAENIAFGLK----LRGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 662 PVLILDEATSALDAESEYLIQ---QAIHGNLQKhTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQG 722
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELReelKELQRELGI-TTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
506-717 |
3.56e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 142.00 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQepvlfarsitdnisyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 665
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767973635 666 LDEATSALDAESEYLIQQAIHGNLQKH-TVLIIAHRLSTVEHA-HLIVVLDKGR 717
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGrTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
188-479 |
5.31e-39 |
|
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: 146.39 E-value: 5.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIV------IQKSMDQFSTAVVIVCLLAIGSSfaagirggIFTLIFARLNI-- 259
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIeglgggGGVDFSGLLRILLLLLGLYLLSA--------LFSYLQNRLMArv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 260 ------RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:cd18547 73 sqrtvyDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 334 MGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaAYMYyv 413
Cdd:cd18547 153 VTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK---AQFY-- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 414 wgSGLTL-------LVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18547 228 --SGLLMpimnfinNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
504-730 |
1.17e-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: 150.82 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG---GRVLLDGKPISAYDHKYLHR 580
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VISLVSQEP--VLFARSITDNISYGL--PTVPFEMVVEAAQKANAHGFIMELQDGYStetgekgAQLSGGQKQRVAMARA 656
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALenLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
507-732 |
1.18e-38 |
|
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: 143.84 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvISLVS 586
Cdd:COG4555 5 ENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPVLFAR-SITDNISY-----GLPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRN 660
Cdd:COG4555 81 DERGLYDRlTVRENIRYfaelyGLFDEELKKRIEELIEL------LGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 661 PPVLILDEATSALDAESEYLIQQAI--HGNlQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGG 732
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILraLKK-EGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
504-723 |
7.80e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.86 E-value: 7.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS---AYdhkylHR 580
Cdd:COG3842 6 LELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPE-----KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VISLVSQEPVLFA-RSITDNISYGLptvpfEM--VVEAAQKANAHGFI--MELqDGYStetGEKGAQLSGGQKQRVAMAR 655
Cdd:COG3842 78 NVGMVFQDYALFPhLTVAENVAFGL-----RMrgVPKAEIRARVAELLelVGL-EGLA---DRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKH---TVLIIAHRLS---TVehAHLIVVLDKGRVVQQGT 723
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREEL-RRLQRElgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
504-718 |
1.02e-37 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 140.32 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK----YL 578
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 HRVISLVSQEPVLFAR-SITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVE--LP-----LLLAGVPKKERRERAEELLErvGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 718
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
506-730 |
1.07e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.66 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRTRPhtqvlQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVISL 584
Cdd:COG3840 4 LDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAE---RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 585 VSQEPVLFAR-SITDNISYGL-----PTVP-FEMVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAMARAL 657
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGLrpglkLTAEqRAQVEQALERVGLAGLL-----------DRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 658 VRNPPVLILDEATSALD----AESEYLIQQaIHGNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:COG3840 145 VRKRPILLLDEPFSALDpalrQEMLDLVDE-LCRERGL-TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
507-729 |
1.20e-36 |
|
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: 138.01 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:COG1124 5 RNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEP--VLFAR-SITDNIS-----YGLPTVPfEMVVEAAQKanahgfiMELQDGYSTEtgeKGAQLSGGQKQRVAMARAL 657
Cdd:COG1124 85 FQDPyaSLHPRhTVDRILAeplriHGLPDRE-ERIAELLEQ-------VGLPPSFLDR---YPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 658 VRNPPVLILDEATSALDAeseyLIQ----------QAIHGNlqkhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQ 726
Cdd:COG1124 154 ILEPELLLLDEPTSALDV----SVQaeilnllkdlREERGL----TYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
...
gi 767973635 727 LLA 729
Cdd:COG1124 226 LLA 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
504-723 |
3.57e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 139.44 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEGgRVLLDGKPISAYDHKYLH 579
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER--PTSG-SVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 RV---ISLVSQEPVLF-ARSITDNISYglptvPFEMV----VEAAQKANahgfimELQD--GYStetgEKG----AQLSG 645
Cdd:COG1135 79 AArrkIGMIFQHFNLLsSRTVAENVAL-----PLEIAgvpkAEIRKRVA------ELLElvGLS----DKAdaypSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 646 GQKQRVAMARALVRNPPVLILDEATSALDAESEY----LIQQaIHGNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQ 720
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKD-INRELGL-TIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 767973635 721 QGT 723
Cdd:COG1135 222 QGP 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
507-718 |
1.04e-35 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 132.91 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvISLVS 586
Cdd:cd03230 4 RNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPVLfarsitdnisyglptvpfemvveaaqkanahgfimelqdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:cd03230 80 EEPSL----------------------------------------YENLTVRENLKLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767973635 667 DEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRV 718
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
188-479 |
1.21e-35 |
|
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: 136.84 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQnINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaAAYMYYVWGSGLTLL--VVQV 425
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLR--AARLRARFWPLLEALpeLGLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767973635 426 SILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18543 238 AVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
507-722 |
1.90e-35 |
|
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: 132.56 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 586
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QepvlfarsitdnisyglptvpfemVVEAAQKAN-AHGFIMElqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 665
Cdd:cd03214 80 Q------------------------ALELLGLAHlADRPFNE---------------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 666 LDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQG 722
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLR-RLARErgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
504-717 |
2.87e-35 |
|
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: 131.93 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD--HKYLHRV 581
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ISLVSQEPVLFAR-SITDNISYGLptvpfemvveaaqkanahgfimelqdgystetgekgaqlSGGQKQRVAMARALVRN 660
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALGL---------------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 661 PPVLILDEATSALDAESEYLIQ---QAIHGNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGR 717
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRallKSLQAQLGI-TVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
504-721 |
4.85e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.86 E-value: 4.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfypleG-------GRVLLDGKPISAYDH 575
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL-------GgldrptsGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 576 KYLHRV----ISLVSQEPVLFAR-SITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQK 648
Cdd:COG1136 78 RELARLrrrhIGFVFQFFNLLPElTALENVA--LP-----LLLAGVSRKERRERARELLErvGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 649 QRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQ 721
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
504-730 |
5.33e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.20 E-value: 5.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAyDHKYLHR 580
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLE---EPDSGTITVDGEDLTD-SKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 V---ISLVSQEPVLFA-RSITDNISYGLptvpfeMVV------EAAQKAnahgfiMEL---------QDGYStetgekgA 641
Cdd:COG1126 75 LrrkVGMVFQQFNLFPhLTVLENVTLAP------IKVkkmskaEAEERA------MELlervgladkADAYP-------A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 642 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAE--SEYL--IQQAIHGNLqkhTVLIIAHRLS---TVehAHLIVVLD 714
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElvGEVLdvMRDLAKEGM---TMVVVTHEMGfarEV--ADRVVFMD 210
|
250
....*....|....*.
gi 767973635 715 KGRVVQQGTHQQLLAQ 730
Cdd:COG1126 211 GGRIVEEGPPEEFFEN 226
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
189-451 |
1.25e-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: 133.76 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 189 VAASFFLIVA-ALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18550 1 LALVLLLILLsALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 348 KYYKRLSKEVQNALARASNTAEET--ISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQV 425
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260
....*....|....*....|....*.
gi 767973635 426 SILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTAL 266
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
504-718 |
1.98e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhrvIS 583
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEpVLFARS--IT--DNISYGL-PTVPF---------EMVVEAAQKANAHGF----ImelqdgystetgekgAQLSG 645
Cdd:COG1121 79 YVPQR-AEVDWDfpITvrDVVLMGRyGRRGLfrrpsradrEAVDEALERVGLEDLadrpI---------------GELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 646 GQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRV 718
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRREgkTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
195-451 |
1.56e-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: 130.65 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 195 LIVAALgETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQET 274
Cdd:cd18549 12 VLIAAL-DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 275 SFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLS 354
Cdd:cd18549 91 SFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 355 KEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQvYKLNRKEAAAYM-YYVWGSGLTLLVVQVSILYYGGH 433
Cdd:cd18549 171 RRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR-FLESKKKAYKAMaYFFSGMNFFTNLLNLVVLVAGGY 249
|
250
....*....|....*...
gi 767973635 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 |
1.58e-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: 131.09 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQK---------------SMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTL 252
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKplpgllglapllgpdPLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 253 IFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYY 412
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 767973635 413 VWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
522-730 |
5.57e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 128.53 E-value: 5.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFA-RSI 596
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 597 TDNISYGLPT--VP----FEMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:cd03294 120 LENVAFGLEVqgVPraerEERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 671 SALDA------ESEYLiqqAIHGNLQKhTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:cd03294 189 SALDPlirremQDELL---RLQAELQK-TIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
504-729 |
8.15e-33 |
|
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: 127.03 E-value: 8.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFA-RSITDNISyglpTVP-FEMVVEAAQKANAHGFI-------MELQDGYStetgekgAQLSGGQKQRVAMA 654
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIA----LVPkLLKWPKEKIRERADELLalvgldpAEFADRYP-------HELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 655 RALVRNPPVLILDEATSALDA------ESEYL-IQQAIHgnlqkHTVLIIAHRL-STVEHAHLIVVLDKGRVVQQGTHQQ 726
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPitrdqlQEEFKrLQQELG-----KTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDE 222
|
...
gi 767973635 727 LLA 729
Cdd:cd03295 223 ILR 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
504-729 |
9.01e-33 |
|
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: 126.46 E-value: 9.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-- 581
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 -ISLVSQEPVLF-ARSITDNISYGL---PTVPFEMVVE-AAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMAR 655
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPLrehTRLSEEEIREiVLEKLEAVG-LRGAEDLYP-------AELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIR-SLKKElglTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
504-731 |
1.48e-32 |
|
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: 127.16 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-KPISAYDHKYLHRVI 582
Cdd:TIGR04520 1 IEVENVSFSY-PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALV 658
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEALK---LVGMEDFRDREP----HLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 659 RNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQG 731
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIR-KLNKEegiTVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
504-728 |
1.70e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.03 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEP--VLFARSITDNISYGLPTV---PFEM---VVEAAQKANAHGFImelqdgystetgEKGAQ-LSGGQKQRVAMA 654
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKkvpPKKMkdiIDDLAKKVGMEDYL------------DKEPQnLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 655 RALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLL 728
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMV-DLRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
507-730 |
2.44e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.73 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfYPLE---GGRVLLDGKPISAyDHKYLHRVIS 583
Cdd:COG1118 6 RNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AGLEtpdSGRIVLNGRDLFT-NLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFaR--SITDNISYGLPTVPfemVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRN 660
Cdd:COG1118 79 FVFQHYALF-PhmTVAENIAFGLRVRP---PSKAEIRARVEELLELVQlEGLA---DRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 661 PPVLILDEATSALDAESEYLIQQ---AIHGNLQkHTVLIIAH-RLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRwlrRLHDELG-GTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
188-451 |
2.45e-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: 127.13 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSsFAAGIRGGIF-TLIFARLNIRLRNCLF 266
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLG-LIAGILAGYFaAKASQGFGRDLRKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 267 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIY 346
Cdd:cd18548 80 EKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 347 GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaAYMYYVWGSGLTLLVVQVS 426
Cdd:cd18548 160 MKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLK---AGRLMALLNPLMMLIMNLA 236
|
250 260
....*....|....*....|....*...
gi 767973635 427 ---ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18548 237 ivaILWFGGHLINAGSLQVGDLVAFINY 264
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
188-479 |
3.54e-32 |
|
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: 126.83 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMdqfsTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIR----LRN 263
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDL----GVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERllydLRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18546 77 RVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYlRKLQQVYKLNRKEAAAYMyYVWGSGLTLL-- 421
Cdd:cd18546 157 RWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF-AELSDDYRDARLRAQRLV-AIYFPGVELLgn 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 422 VVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18546 235 LATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
504-727 |
3.80e-32 |
|
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: 124.66 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVI 582
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPpHK---RPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEPVLFAR-SITDNISYGLPTvpfEMVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRN 660
Cdd:cd03300 75 NTVFQNYALFPHlTVFENIAFGLRL---KKLPKAEIKERVAEALDLVQlEGYA---NRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 661 PPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLS---TVehAHLIVVLDKGRVVQQGTHQQL 727
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELK-RLQKElgiTFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
494-701 |
6.30e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.76 E-value: 6.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 494 SLAPDHLEGRVDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP---LEgGRVLLDG 567
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPgarVE-GEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 568 KPIsaYDHKY----LHRVISLVSQEPVLFARSITDNISYGL-------PTVPFEMVVEAAQKANahgfimeLQDgystET 636
Cdd:COG1117 78 EDI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiksKSELDEIVEESLRKAA-------LWD----EV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 637 ----GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES----EYLIQQaihgnL-QKHTVLIIAHRL 701
Cdd:COG1117 145 kdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELILE-----LkKDYTIVIVTHNM 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
520-718 |
1.21e-31 |
|
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: 122.64 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFyplEGGRVLLDGKPISAyDHKYLHRV---ISLVSQEPVLFA 593
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEEP---DSGTIIIDGLKLTD-DKKNINELrqkVGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 594 -RSITDNISYGLPTVPFEMVVEAAQKAnahgfiMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:cd03262 90 hLTVLENITLAPIKVKGMSKAEAEERA------LELLEkvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767973635 671 SALDAE--SEYL--IQQAIHgnlQKHTVLIIAHRLSTVEH-AHLIVVLDKGRV 718
Cdd:cd03262 164 SALDPElvGEVLdvMKDLAE---EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
502-727 |
1.28e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.73 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 502 GRVDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRV 581
Cdd:COG3839 2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ISLVSQEPVLF-ARSITDNISYGLptvpfEM-----------VVEAAQkanahgfIMELQDgYStetGEKGAQLSGGQKQ 649
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPL-----KLrkvpkaeidrrVREAAE-------LLGLED-LL---DRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 650 RVAMARALVRNPPVLILDEATSALDAE------SEylIQQaIHGNLqKHTVLIiahrlstVEH--------AHLIVVLDK 715
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKlrvemrAE--IKR-LHRRL-GTTTIY-------VTHdqveamtlADRIAVMND 209
|
250
....*....|..
gi 767973635 716 GRVVQQGTHQQL 727
Cdd:COG3839 210 GRIQQVGTPEEL 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
507-699 |
2.38e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 121.60 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhKYLHRVISLVS 586
Cdd:cd03226 3 ENISFSYK--KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEP--VLFARSITDNISYGLPTVPfemvvEAAQKANAhgfIMELQDGYSTEtgEKGAQ-LSGGQKQRVAMARALVRNPPV 663
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELD-----AGNEQAET---VLKDLDLYALK--ERHPLsLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 767973635 664 LILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAH 699
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIrELAAQGKAVIVITH 184
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
519-729 |
2.48e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 122.16 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SI 596
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 597 TDNIsyglptvpfEMVVEAAQKANAHgFIME--------LQDGYSTetgeKGAQLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:cd03224 93 EENL---------LLGAYARRRAKRK-ARLErvyelfprLKERRKQ----LAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 669 ATSALdaeSEYLIQQ---AIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:cd03224 159 PSEGL---APKIVEEifeAIRElRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
506-727 |
2.67e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.86 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAYDHKYLHRV- 581
Cdd:COG3638 5 LRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTllrCLNGLV---EPTSGEILVDGQDVTALRGRALRRLr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 --ISLVSQEPVLFAR-SITDNISYG-LPTVPF----EMVVEAAQKANAHGFI--MELQDgystETGEKGAQLSGGQKQRV 651
Cdd:COG3638 80 rrIGMIFQQFNLVPRlSVLTNVLAGrLGRTSTwrslLGLFPPEDRERALEALerVGLAD----KAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 652 AMARALVRNPPVLILDEATSALDAES-----EYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQ 725
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTarqvmDLLRRIAREDGI---TVVVNLHQVDLArRYADRIIGLRDGRVVFDGPPA 232
|
..
gi 767973635 726 QL 727
Cdd:COG3638 233 EL 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
506-722 |
3.16e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.49 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhrvISLV 585
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVL---FARSITDNISYGL-PTVPFEMVVEAAQKANahgfIMELQDgySTETGEKG----AQLSGGQKQRVAMARAL 657
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLyGHKGLFRRLSKADKAK----VDEALE--RVGLSELAdrqiGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 658 VRNPPVLILDEATSALDAESeyliQQAIHGNLQK-----HTVLIIAHRLSTV-EHAHLIVVLDKgRVVQQG 722
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKT----QEDIYELLRElrregMTILVVTHDLGLVlEYFDRVLLLNR-TVVASG 213
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
187-479 |
5.55e-31 |
|
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: 123.36 E-value: 5.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 187 FLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVI-VCLLAIgssFAAGIRGGIFT--LIFARLNIRLRN 263
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLyLGLILI---QALSVFLFIRLagKIEMGVSYDLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18540 80 KAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 344 NIygkYYKRLSKevQNALARASN---TA--EETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaAAYMyyvwgSGL 418
Cdd:cd18540 160 IY---FQKKILK--AYRKVRKINsriTGafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVR--AARL-----SAL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 419 TLLVVQV-------SILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18540 228 FLPIVLFlgsiataLVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
504-747 |
5.61e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 122.55 E-value: 5.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRT-RPHTqvLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI 582
Cdd:PRK13648 8 IVFKNVSFQYQSdASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEPV-LFARSITD-NISYGLP--TVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAqLSGGQKQRVAMARALV 658
Cdd:PRK13648 86 GIVFQNPDnQFVGSIVKyDVAFGLEnhAVPYDEMHRRVSEA------LKQVDMLERADYEPNA-LSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 659 RNPPVLILDEATSALDAES-EYLIQQAIHGNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT------HQQLLAQ 730
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDArQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTpteifdHAEELTR 238
|
250
....*....|....*....
gi 767973635 731 GGLYAKLVQR--QMLGLQP 747
Cdd:PRK13648 239 IGLDLPFPIKinQMLGHQT 257
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
504-719 |
8.11e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.54 E-value: 8.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLHR 580
Cdd:COG2884 2 IRFENVSKRYPGGR--EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VISLVSQE-PVLFARSITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARAL 657
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVA--LP-----LRVTGKSRKEIRRRVREVLDlvGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 658 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEHA-HLIVVLDKGRVV 719
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATHDLELVDRMpKRVLELEDGRLV 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
504-729 |
8.62e-31 |
|
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: 121.24 E-value: 8.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-- 581
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 -ISLVSQEPVLFArSIT--DNISYGL---PTVPFEMVVEAAqkanahgfIMELQdgystETGEKGA------QLSGGQKQ 649
Cdd:COG1127 83 rIGMLFQGGALFD-SLTvfENVAFPLrehTDLSEAEIRELV--------LEKLE-----LVGLPGAadkmpsELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 650 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQ 725
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIR-ELRDElglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
....
gi 767973635 726 QLLA 729
Cdd:COG1127 228 ELLA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
521-723 |
1.92e-30 |
|
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: 119.85 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITD 598
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 599 NI---------SYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEA 669
Cdd:cd03219 95 NVmvaaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 670 TSAL-DAESEYLIQ--QAIhgNLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 723
Cdd:cd03219 171 AAGLnPEETEELAEliREL--RERGITVLLVEHDMDVVmSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
524-722 |
2.35e-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: 118.94 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 524 NVSFSLsPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKylhRVISLVSQEPVLFAR-S 595
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQ---RKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 596 ITDNISYGLPTV-PFEMVVEAAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:cd03297 92 VRENLAFGLKRKrNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767973635 675 AESEYLIQ---QAIHGNLQKHtVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 722
Cdd:cd03297 164 RALRLQLLpelKQIKKNLNIP-VIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
188-479 |
2.76e-30 |
|
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: 121.10 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAID-GIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGgIFTLIFA-RLNIRLRNCL 265
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDlVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRI-YLNHVAEqKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 266 FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNI 345
Cdd:cd18778 80 YDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 346 YGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLN---RKEAAAY---MYYVWGSGlT 419
Cdd:cd18778 160 YSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQlraMKLWAIFhplMEFLTSLG-T 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 420 LLVvqvsiLYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18778 239 VLV-----LGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
504-722 |
2.92e-30 |
|
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: 118.75 E-value: 2.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTQVLQnvsfsLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 583
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT-----FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISYGL-PTVPFEMVVEAAQKANAHgfimelQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLsPGLKLTAEDRQAIEVALA------RVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 662 PVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 722
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
504-719 |
3.50e-30 |
|
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: 116.76 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkylhrvis 583
Cdd:cd03216 1 LELRGITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 lvsqepvlfaRSITDNISYGLPTVPfemvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03216 67 ----------ASPRDARRAGIAMVY---------------------------------QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 664 LILDEATSAL-DAESEYLIqqAIHGNLQK--HTVLIIAHRLSTV-EHAHLIVVLDKGRVV 719
Cdd:cd03216 104 LILDEPTAALtPAEVERLF--KVIRRLRAqgVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
503-714 |
5.26e-30 |
|
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: 117.58 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 503 RVDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVI 582
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEPVLFAR-SITDNIS-----YGLPtVPFEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 656
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEAVG----LAGLAD-------LPVRQLSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIA-HRLSTVEHAHLIVVLD 714
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDLGD 204
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
500-742 |
6.08e-30 |
|
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: 119.24 E-value: 6.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 500 LEGRVDFENVTFTYRT--RPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY 577
Cdd:cd03288 16 LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 578 LHRVISLVSQEPVLFARSITDNISyglP--TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNLD---PecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ-GGLY 734
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVF 249
|
....*...
gi 767973635 735 AKLVQRQM 742
Cdd:cd03288 250 ASLVRTDK 257
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
504-731 |
6.20e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.73 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 581
Cdd:PRK13635 6 IRVEHISFRY---PDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ISLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHgfiMELQDGYSTETgekgAQLSGGQKQRVAMARAL 657
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLENigVPREEMVERVDQALRQ---VGMEDFLNREP----HRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 658 VRNPPVLILDEATSALDAESEYLIQQAIH-----GNLqkhTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQG 731
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRqlkeqKGI---TVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
504-728 |
6.58e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 118.66 E-value: 6.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGkpISAYDHKYLHR 580
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLE---EITSGDLIVDG--LKVNDPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VI----SLVSQEPVLFAR-SITDNISYGlptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAM 653
Cdd:PRK09493 74 LIrqeaGMVFQQFYLFPHlTALENVMFG----PLR--VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 654 ARALVRNPPVLILDEATSALDAE--SEYL--IQQ-AIHGnlqkHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 727
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPElrHEVLkvMQDlAEEG----MTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVL 223
|
.
gi 767973635 728 L 728
Cdd:PRK09493 224 I 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
503-722 |
9.04e-30 |
|
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: 116.50 E-value: 9.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 503 RVDFENVTFT---YRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--GRVLLDGKPISAYDHKY 577
Cdd:cd03213 3 TLSFRNLTVTvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 578 LhrvISLVSQEPVLFARSitdnisyglpTVpFEMVVEAAqkanahgfimELQdgystetgekgaQLSGGQKQRVAMARAL 657
Cdd:cd03213 83 I---IGYVPQDDILHPTL----------TV-RETLMFAA----------KLR------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 658 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLST--VEHAHLIVVLDKGRVVQQG 722
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
521-728 |
1.98e-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: 117.05 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SITDN 599
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 600 ISYGL-------PTVPfEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:cd03299 92 IAYGLkkrkvdkKEIE-RKVLEIAEMLG----IDHLLN-------RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 673 LDAESE----YLIQQAIHGNlqKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLL 728
Cdd:cd03299 160 LDVRTKeklrEELKKIRKEF--GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
182-449 |
2.27e-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: 118.70 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRL 261
Cdd:cd18570 1 KKLLILILLLSLLITLLGI---AGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 262 RNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQN-INVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18570 78 ILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFL-DLLMVIISGIILFFYNWKLFLITLLIIPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTL 420
Cdd:cd18570 156 LIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLIS 235
|
250 260
....*....|....*....|....*....
gi 767973635 421 LVVQVSILYYGGHLVISGQMTSGNLIAFI 449
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFN 264
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
507-761 |
2.69e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.42 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 586
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPvLFARSIT--DNISYGL-PTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMA 654
Cdd:PRK11231 83 QHH-LTPEGITvrELVAYGRsPWLSLwgrlsaednARVNQAMEQTR----INHLADRRLTD-------LSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 655 RALVRNPPVLILDEATSALD----AESEYLIQQAihgNLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT 227
|
250 260 270
....*....|....*....|....*....|..
gi 767973635 730 QGGLyaklvqRQMLGLQpaadfTAGHNEPVAN 761
Cdd:PRK11231 228 PGLL------RTVFDVE-----AEIHPEPVSG 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
506-727 |
2.78e-29 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 116.90 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAYDHKYLHRV- 581
Cdd:cd03256 3 VENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTllrCLNGLV---EPTSGSVLIDGTDINKLKGKALRQLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 --ISLVSQEPVLFAR-SITDNISYG-LPTVP-----FEMVVEAA-QKANAhgfIMElQDGYSTETGEKGAQLSGGQKQRV 651
Cdd:cd03256 78 rqIGMIFQQFNLIERlSVLENVLSGrLGRRStwrslFGLFPKEEkQRALA---ALE-RVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 652 AMARALVRNPPVLILDEATSALDAES-----EYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQ 725
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASsrqvmDLLKRINREEGI---TVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPA 230
|
..
gi 767973635 726 QL 727
Cdd:cd03256 231 EL 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
520-723 |
6.44e-29 |
|
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: 116.29 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SIT 597
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIARLGIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 598 DNI--------SYGLPTVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILD 667
Cdd:COG0411 98 ENVlvaaharlGRGLLAALLRLPRARREEREARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 668 EATSAL-DAESEYLIQ--QAIHGNlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 723
Cdd:COG0411 178 EPAAGLnPEETEELAEliRRLRDE-RGITILLIEHDMDLVmGLADRIVVLDFGRVIAEGT 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
504-723 |
8.48e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 118.36 E-value: 8.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPlEGGRVLLDGKPISAYDHKYL- 578
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER--P-TSGRVLVDGQDLTALSEKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 --HRVISLVSQE-PVLFARSITDNISYglptvPFEMVVEAAQKANAHgfIMELQD--GYSTETGEKGAQLSGGQKQRVAM 653
Cdd:PRK11153 79 kaRRQIGMIFQHfNLLSSRTVFDNVAL-----PLELAGTPKAEIKAR--VTELLElvGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 654 ARALVRNPPVLILDEATSALDAESeyliQQAIHGNLQK------HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGT 723
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPAT----TRSILELLKDinrelgLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
504-718 |
9.14e-29 |
|
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: 114.43 E-value: 9.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQV-LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLH 579
Cdd:cd03292 1 IEFINVTKTY---PNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 RVISLVSQE-PVLFARSITDNisyglptVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARA 656
Cdd:cd03292 78 RKIGVVFQDfRLLPDRNVYEN-------VAFALEVTGVPPREIRKRVPAALElvGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRV 718
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
504-722 |
1.13e-28 |
|
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: 114.27 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 583
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRN 660
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKLrkVPKDEIDERVREVAELLQIEHLLD-------RKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 661 PPVLILDEATSALDAESEYLIQQAI---HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 722
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELkrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
504-704 |
2.81e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.75 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG-----GRVLLDGKPIsaYDHKY- 577
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI--YERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 578 ---LHRVISLVSQEPVLFARSITDNISYGL------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAQLSGGQK 648
Cdd:PRK14258 83 lnrLRRQVSMVHPKPNLFPMSVYDNVAYGVkivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 649 QRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTV 704
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQV 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
504-745 |
3.56e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.83 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALVR 659
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEALE---LVGMQDFKEREP----ARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 660 NPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGlyaKL 737
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN---DL 234
|
....*...
gi 767973635 738 VQrqmLGL 745
Cdd:PRK13650 235 LQ---LGL 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
504-722 |
4.32e-28 |
|
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: 112.29 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGkVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVIS 583
Cdd:cd03264 1 LQLENLTKRY---GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL-RRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISY-----GLP--TVPfEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPskEVK-ARVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 656 ALVRNPPVLILDEATSALDAES-----EYLIQQAihgnlQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVVQQG 722
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEErirfrNLLSELG-----EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
504-727 |
5.84e-28 |
|
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: 112.21 E-value: 5.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsAYDHKYLHRVIS 583
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISY-----GLPTVPFEMVVEAAQKanahgfIMELQDGYSTETGekgaQLSGGQKQRVAMARAL 657
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 658 VRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 727
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
507-730 |
6.47e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 115.15 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP---LEGGRVLLDGKPISAYDHKYLHRV- 581
Cdd:COG0444 5 RNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKIr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ---ISLVSQE------PVLfarsitdnisyglpTVpFEMVVEAaqkanahgfiMELQDGYSTETGEKGA----------- 641
Cdd:COG0444 85 greIQMIFQDpmtslnPVM--------------TV-GDQIAEP----------LRIHGGLSKAEARERAiellervglpd 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 642 ----------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQKH---TVLIIAHRLSTVE 705
Cdd:COG0444 140 perrldryphELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQILNllkDLQRElglAILFITHDLGVVA 215
|
250 260
....*....|....*....|....*.
gi 767973635 706 H-AHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:COG0444 216 EiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
519-713 |
6.77e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 112.50 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITD 598
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 599 NISYglptvPFEMvveAAQKANAHGFIMELQD-GYSTETGEKG-AQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:PRK10247 100 NLIF-----PWQI---RNQQPDPAIFLDDLERfALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 767973635 677 SEYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVL 713
Cdd:PRK10247 172 NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
507-728 |
7.10e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.29 E-value: 7.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 586
Cdd:COG4559 5 ENLSVRLGGR---TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 Q-----------EPVLFARsitdnISYGLPTVPFEMVVEAAqkanahgfiMELqdgysTETGEKGA----QLSGGQKQRV 651
Cdd:COG4559 82 QhsslafpftveEVVALGR-----APHGSSAAQDRQIVREA---------LAL-----VGLAHLAGrsyqTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 652 AMARAL------VRNPP-VLILDEATSALDaeseyLIQQaihgnlqkHTVLIIAHRLS-------TVEH--------AHL 709
Cdd:COG4559 143 QLARVLaqlwepVDGGPrWLFLDEPTSALD-----LAHQ--------HAVLRLARQLArrgggvvAVLHdlnlaaqyADR 209
|
250
....*....|....*....
gi 767973635 710 IVVLDKGRVVQQGTHQQLL 728
Cdd:COG4559 210 ILLLHQGRLVAQGTPEEVL 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
517-719 |
1.47e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVSQEPV 590
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdAQAAG-----IAIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 LFA-RSITDNISYG-LPTVPF-----EMVVEAAQKANAHGFIMELqdgySTETGEkgaqLSGGQKQRVAMARALVRNPPV 663
Cdd:COG1129 90 LVPnLSVAENIFLGrEPRRGGlidwrAMRRRARELLARLGLDIDP----DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 664 LILDEATSAL-DAESEYLIqqAIHGNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVV 719
Cdd:COG1129 162 LILDEPTASLtEREVERLF--RIIRRLKAQgvAIIYISHRLDEVfEIADRVTVLRDGRLV 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
507-722 |
2.10e-27 |
|
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: 110.38 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVS 586
Cdd:cd03268 4 NDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 qEPVLF-ARSITDNISYglptvpfemvveaaqKANAHGF----IMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVR 659
Cdd:cd03268 80 -APGFYpNLTARENLRL---------------LARLLGIrkkrIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 660 NPPVLILDEATSALDAESEYLIQQAIHgNLQK--HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 722
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELIL-SLRDqgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
524-741 |
2.70e-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: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsaYD---------HKylhRVISLVSQEPVLFA- 593
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDsargiflppHR---RRIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 594 RSITDNISYGL-------PTVPFEMVVEAAQkanahgfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:COG4148 92 LSVRGNLLYGRkrapraeRRISFDEVVELLG-------IGHLLDRRP-------ATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 667 DEATSALDAES-----EYLIQqaihgnLQKHT---VLIIAHrlSTVEHAHL---IVVLDKGRVVQQGTHQQLLAQGGLYA 735
Cdd:COG4148 158 DEPLAALDLARkaeilPYLER------LRDELdipILYVSH--SLDEVARLadhVVLLEQGRVVASGPLAEVLSRPDLLP 229
|
....*.
gi 767973635 736 KLVQRQ 741
Cdd:COG4148 230 LAGGEE 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
514-727 |
2.79e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.29 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYL---HRVISLVSQEPv 590
Cdd:COG4608 26 RTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 lFA-----RSITDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGA-QLSGGQKQRVAMARALVRNPP 662
Cdd:COG4608 105 -YAslnprMTVGDIIAEPL------RIHGLASKAERRERVAELLElvGLRPEHADRYPhEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 663 VLILDEATSALDAeSeylIQ-QAIhgN----LQK---HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 727
Cdd:COG4608 178 LIVCDEPVSALDV-S---IQaQVL--NlledLQDelgLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
507-730 |
3.91e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 110.44 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPhtqvlqnVSFSLS--PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKpisayDHKYL---HRV 581
Cdd:PRK10771 5 TDITWLYHHLP-------MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ISLVSQEPVLFAR-SITDNISYGL-PTVPF-----EMVVEAAQKANAHGFIMELQdgystetgekgAQLSGGQKQRVAMA 654
Cdd:PRK10771 73 VSMLFQENNLFSHlTVAQNIGLGLnPGLKLnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 655 RALVRNPPVLILDEATSALD----AESEYLIQQAIHGnlQKHTVLIIAHRLstvEHAHLI----VVLDKGRVVQQGTHQQ 726
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSL---EDAARIaprsLVVADGRIAWDGPTDE 216
|
....
gi 767973635 727 LLAQ 730
Cdd:PRK10771 217 LLSG 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
504-727 |
5.31e-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: 110.12 E-value: 5.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVIS 583
Cdd:cd03296 3 IEVRNVSKRF---GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISYGLPTVP-FEMVVEAAQKANAHGFIMELQ-DGYSTETGekgAQLSGGQKQRVAMARALVRN 660
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPrSERPPEAEIRAKVHELLKLVQlDWLADRYP---AQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 661 PPVLILDEATSALDAESEYLIQ---QAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 727
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRrwlRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
512-728 |
1.97e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.09 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 512 TYRtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVL 591
Cdd:PRK13548 9 SVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 592 -FARSITDNISYGL-----PTVPFEMVVEAAqkanahgfiMELQD--GYStetGEKGAQLSGGQKQRVAMARALVR---- 659
Cdd:PRK13548 88 sFPFTVEEVVAMGRaphglSRAEDDALVAAA---------LAQVDlaHLA---GRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 660 --NPPVLILDEATSALDaeseyLIQQaihgnlqkHTVLIIAHRLST--------VEH--------AHLIVVLDKGRVVQQ 721
Cdd:PRK13548 156 dgPPRWLLLDEPTSALD-----LAHQ--------HHVLRLARQLAHerglavivVLHdlnlaaryADRIVLLHQGRLVAD 222
|
....*..
gi 767973635 722 GTHQQLL 728
Cdd:PRK13548 223 GTPAEVL 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
504-729 |
2.95e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.03 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVR 659
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973635 660 NPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
507-744 |
3.70e-26 |
|
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: 107.63 E-value: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV 585
Cdd:cd03218 4 ENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVLFAR-SITDNISYGLPTVPFEmvvEAAQKANAHGFIMELQdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 664
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLS---KKEREEKLEELLEEFH--ITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 665 ILDEATSALDAESEYLIQQAIHgNLQKHT--VLIIAHR----LSTVEHAHLIVvldKGRVVQQGTHQQLLAQgglyaKLV 738
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIK-ILKDRGigVLITDHNvretLSITDRAYIIY---EGKVLAEGTPEEIAAN-----ELV 226
|
....*.
gi 767973635 739 QRQMLG 744
Cdd:cd03218 227 RKVYLG 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
514-730 |
6.97e-26 |
|
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: 112.47 E-value: 6.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSC----VNILENfypleGGRVLLDGKPISAYDHKYLHRV---ISLVS 586
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRALRPLrrrMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPvlFA-----RSITDNISYGLpTVPF---------EMVVEAAQKAnahGFIMELQDGYSTEtgekgaqLSGGQKQRVA 652
Cdd:COG4172 369 QDP--FGslsprMTVGQIIAEGL-RVHGpglsaaerrARVAEALEEV---GLDPAARHRYPHE-------FSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 653 MARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQ 725
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDV----SVQAQILDllrDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTE 511
|
....*
gi 767973635 726 QLLAQ 730
Cdd:COG4172 512 QVFDA 516
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
518-727 |
8.62e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.40 E-value: 8.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaydhkYLH---RVISLVSQEPVLFaR 594
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-----RLHardRKVGFVFQHYALF-R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 SIT--DNISYGLPTVPfemvveAAQKANAHGF---IMELQDGYSTE--TGEKGAQLSGGQKQRVAMARALVRNPPVLILD 667
Cdd:PRK10851 88 HMTvfDNIAFGLTVLP------RRERPNAAAIkakVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 668 EATSALDAE-----SEYLIQqaIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 727
Cdd:PRK10851 162 EPFGALDAQvrkelRRWLRQ--LHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
514-749 |
1.33e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.08 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYLHRVISLVSQEP- 589
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 590 --VLFARSITDNIsyGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTEtgeKGAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:PRK10419 100 saVNPRKTVREII--REPLRHLLSLDKAERLARASEMLraVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 666 LDEATSALDaeseyLIQQA----IHGNLQKHT---VLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 737
Cdd:PRK10419 175 LDEAVSNLD-----LVLQAgvirLLKKLQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTFSSPAGRV 249
|
250
....*....|..
gi 767973635 738 VQRQMLGLQPAA 749
Cdd:PRK10419 250 LQNAVLPAFPVR 261
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
502-727 |
1.53e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 113.72 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 502 GRVDFENVTFTYRT-RPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR 580
Cdd:PTZ00243 1307 GSLVFEGVQMRYREgLP--LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VISLVSQEPVLFARSITDNISYGLPTVPFEmVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRN 660
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 661 PPVLIL-DEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 727
Cdd:PTZ00243 1464 GSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
504-745 |
1.62e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.19 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY---PLEGGRVLLDGKPISAYDHKYLHR 580
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VISLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDGystetgeKGAQLSGGQKQRVAMARA 656
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLADVGMLDYIDS-------EPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT------HQQL 727
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIR-KLKKKnnlTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifsKVEM 236
|
250
....*....|....*...
gi 767973635 728 LAQGGLYAKLVQRQMLGL 745
Cdd:PRK13640 237 LKEIGLDIPFVYKLKNKL 254
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
520-729 |
1.90e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.99 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEG----GRVLLDG-KPISAYDH--KYLHRVISLVSQEP 589
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ--PEAGtirvGDITIDTaRSLSQQKGliRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 590 VLFA-RSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:PRK11264 95 NLFPhRTVLENIIEG----PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 669 ATSALDAESEYLIQQAIHGNLQ-KHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
504-746 |
5.18e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 5.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEP--VLFARSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQDGYstETGEKGA-QLSGGQKQRVAMARALVRN 660
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFG----PVNMGLDKDEVERRVEEALKAVRMW--DFRDKPPyHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 661 PPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQG-----THQQLLAQGGL 733
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGL 236
|
250
....*....|...
gi 767973635 734 YAKLVQRQMLGLQ 746
Cdd:PRK13647 237 RLPLVAQIFEDLP 249
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
507-762 |
6.38e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 111.75 E-value: 6.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGGRVLLDGKpisaydhkylhrvISLV 585
Cdd:PLN03130 618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVLFARSITDNISYGLPTVP--FEMVVEAAqkANAHGFIMeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:PLN03130 685 PQVSWIFNATVRDNILFGSPFDPerYERAIDVT--ALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 664 LILDEATSALDAE-SEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQR-- 740
Cdd:PLN03130 762 YIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENag 841
|
250 260
....*....|....*....|....*
gi 767973635 741 QMLGLQPAADFTAGHNE---PVANG 762
Cdd:PLN03130 842 KMEEYVEENGEEEDDQTsskPVANG 866
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
465-738 |
6.39e-25 |
|
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: 111.58 E-value: 6.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 465 VYSGLMQGVGAAEKVFEFIDRQptmvhdgSLAPDHLEGR---------VDFENVTFTY-RTRPHTqvLQNVSFSLSPGKV 534
Cdd:TIGR00957 596 VISSIVQASVSLKRLRIFLSHE-------ELEPDSIERRtikpgegnsITVHNATFTWaRDLPPT--LNGITFSIPEGAL 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 535 TALVGPSGSGKSSCVN-ILENFYPLEGgrvlldgkpisaydHKYLHRVISLVSQEPVLFARSITDNISYGLPTVP--FEM 611
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSaLLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEkyYQQ 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 612 VVEAAqkanahGFIMELQ---DGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE-SEYLIQQAI-- 685
Cdd:TIGR00957 733 VLEAC------ALLPDLEilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgp 806
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767973635 686 HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 738
Cdd:TIGR00957 807 EGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
522-701 |
8.43e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.48 E-value: 8.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP---LEGgRVLLDGKPISA--YDHKYLHRVISLVSQEPVLFA 593
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPgfrVEG-KVTFHGKNLYApdVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 594 RSITDNISYGlPTV-----PFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:PRK14243 105 KSIYDNIAYG-ARIngykgDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|...
gi 767973635 669 ATSALDAESEYLIQQAIHGNLQKHTVLIIAHRL 701
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
514-729 |
9.73e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYL---HRVISLVSQEP- 589
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 590 -VLFAR-SITDNISYGLPTvpFEMVVEAAQKANAHGFIMElQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:PRK15134 373 sSLNPRlNVLQIIEEGLRV--HQPTLSAAQREQQVIAVME-EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 667 DEATSALDAESEYLIQQAIHGNLQKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
518-745 |
1.04e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.52 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-S 595
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 596 ITDNISYGLPTVPFEMVVEAAQKanahgFIMEL---------QdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRADLE-----RVYELfprlkerrrQ---------RAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 667 DEATSALDAeseyLIQQAIHGNLQK-----HTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGlyaklVQR 740
Cdd:COG0410 161 DEPSLGLAP----LIVEEIFEIIRRlnregVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLADPE-----VRE 231
|
....*
gi 767973635 741 QMLGL 745
Cdd:COG0410 232 AYLGV 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
525-733 |
1.14e-24 |
|
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: 106.35 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 525 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKylhRVISLVSQEPVLFAR-SI 596
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEK---RRIGYVFQEARLFPHlSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 597 TDNISYGL--PTVPFEMVVEAAqkanahgfIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:TIGR02142 93 RGNLRYGMkrARPSERRISFER--------VIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 675 AESEYLIQQAIHgNLQKHT---VLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGGL 733
Cdd:TIGR02142 164 DPRKYEILPYLE-RLHAEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
506-727 |
1.40e-24 |
|
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: 103.15 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfypLEGGRVLLDGKPISAYDHKYLHRV- 581
Cdd:TIGR02315 4 VENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTllrCINRLVE---PSSGSILLEGTDITKLRGKKLRKLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 --ISLVSQEPVLFAR-SITDNISYG----LPTVP--FEMVVEAaQKANAhgfiMELQD--GYSTETGEKGAQLSGGQKQR 650
Cdd:TIGR02315 79 rrIGMIFQHYNLIERlTVLENVLHGrlgyKPTWRslLGRFSEE-DKERA----LSALErvGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 651 VAMARALVRNPPVLILDEATSALDAES-----EYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTH 724
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTskqvmDYLKRINKEDGI---TVIINLHQVDLAkKYADRIVGLKAGEIVFDGAP 230
|
...
gi 767973635 725 QQL 727
Cdd:TIGR02315 231 SEL 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
522-719 |
1.69e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.19 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVSQEPVLFAR- 594
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdAIALG-----IGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 SITDNISYGLPTVPFEMV--VEAAQKanahgfIMELQDGYstetG------EKGAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLdrKAARAR------IRELSERY----GldvdpdAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 667 DEATSAL-DAESEYLIqqAIHGNL--QKHTVLIIAHRLSTV-EHAHLIVVLDKGRVV 719
Cdd:COG3845 166 DEPTAVLtPQEADELF--EILRRLaaEGKSIIFITHKLREVmAIADRVTVLRRGKVV 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
507-722 |
3.03e-24 |
|
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: 101.68 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYR-TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-----KPISAydhkylHR 580
Cdd:cd03266 5 DALTKRFRdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEA------RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VISLVSQEPVLFAR-SITDNISY-----GLptvpfemvveaaQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVA 652
Cdd:cd03266 79 RLGFVSDSTGLYDRlTARENLEYfaglyGL------------KGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 722
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIrQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
517-716 |
3.59e-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: 101.25 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV-NILENFYPLEG----GRVLLDGKPISAYDHKYLHRViSLVSQEPVL 591
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRYSV-AYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 592 FARSITDNISYGLP--TVPFEMVVEAAqkaNAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 669
Cdd:cd03290 91 LNATVEENITFGSPfnKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767973635 670 TSALDAE-SEYLIQQAIHGNLQ--KHTVLIIAHRLSTVEHAHLIVVLDKG 716
Cdd:cd03290 168 FSALDIHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
511-736 |
4.24e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.78 E-value: 4.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 511 FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-------------ILENFY---PLEGGRVLLDGKPISAYD 574
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigdKKNNHELITNPYSKKIKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 575 HKYLHRVISLVSQEP--VLFARSITDNISYGlPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGekgAQLSGGQKQRVA 652
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSYLERSP---FGLSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTD 266
|
....*.
gi 767973635 731 GGLYAK 736
Cdd:PRK13631 267 QHIINS 272
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
507-721 |
5.13e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.25 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTY-RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRviSLV 585
Cdd:COG4525 7 RHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---R--GVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVLFA-RSITDNISYGLPtvpFEMVVEAAQKANAHGFI--MELQDgysteTGEKG-AQLSGGQKQRVAMARALVRNP 661
Cdd:COG4525 82 FQKDALLPwLNVLDNVAFGLR---LRGVPKAERRARAEELLalVGLAD-----FARRRiWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 662 PVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHrlsTVEHAHL----IVVLDK--GRVVQQ 721
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH---SVEEALFlatrLVVMSPgpGRIVER 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
520-701 |
6.48e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP--LEGGRVLLDGKPISA--YDHKYLHRVISLVSQEPVLF 592
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 593 ARSITDNISYGL------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:PRK14239 99 PMSIYENVVYGLrlkgikDKQVLDEAVEKSLKGAS------IWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 767973635 667 DEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRL 701
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
507-730 |
7.63e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.08 E-value: 7.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKYLHRV---IS 583
Cdd:PRK13639 3 ETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVrktVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfiMElqdGYstetgEKGA--QLSGGQKQRVAMA 654
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGplnlgLSKEEVEKRVKEALKAVG----ME---GF-----ENKPphHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 655 RALVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
510-730 |
7.83e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 101.84 E-value: 7.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 510 TFTYRT----RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPvlfarsitdNISYGlPTVPFEMVVEAAQKANAH-----------------GFIMELQDGYSTEtgekgaqLSGGQK 648
Cdd:COG4167 93 FQDP---------NTSLN-PRLNIGQILEEPLRLNTDltaeereerifatlrlvGLLPEHANFYPHM-------LSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 649 QRVAMARALVRNPPVLILDEATSALDAEseyLIQQAIhgNL-----QKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVQ 720
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMS---VRSQII--NLmlelqEKLGIsyIYVSQHLGIVKHiSDKVLVMHQGEVVE 230
|
250
....*....|
gi 767973635 721 QGTHQQLLAQ 730
Cdd:COG4167 231 YGKTAEVFAN 240
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
235-462 |
8.21e-24 |
|
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: 102.74 E-value: 8.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 235 LAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKV 314
Cdd:cd18558 68 IGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 315 TGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRK 394
Cdd:cd18558 148 GTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQN 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973635 395 LQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLI----AFIIYEFVLGDCMESV 462
Cdd:cd18558 228 LEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLtvffSVLIGAFSAGQQVPSI 299
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
256-739 |
8.42e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 108.14 E-value: 8.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 256 RLNIRLRNCLFRSLVSQETSFFDENR----TGDLISRLTSDTTMVSdLVSQNINVFLRNTVKVTgvvVFMFSLSWQLSLV 331
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDANALQ-QIAEQLHGLWSAPFRII---VSMVLLYQQLGVA 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 332 TFMGFPIIMMV---SNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE----------EAEVYLRKLQQV 398
Cdd:PLN03232 443 SLFGSLILFLLiplQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSfesriqgirnEELSWFRKAQLL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 399 YKLNrkeaaAYMyyvwgsgLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEK 478
Cdd:PLN03232 523 SAFN-----SFI-------LNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 479 VFE-FIDRQPTMVHDGSLAPDhlEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFY 556
Cdd:PLN03232 591 IEElLLSEERILAQNPPLQPG--APAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELS 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 557 PLEGGRVLLDGKpisaydhkylhrvISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGfiMELQDGYS-TE 635
Cdd:PLN03232 669 HAETSSVVIRGS-------------VAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTE 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 636 TGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE-SEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLD 714
Cdd:PLN03232 734 IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVS 813
|
490 500
....*....|....*....|....*
gi 767973635 715 KGRVVQQGTHQQLLAQGGLYAKLVQ 739
Cdd:PLN03232 814 EGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
188-450 |
8.55e-24 |
|
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: 102.25 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18568 7 ILLASLLLQLLGL---ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18568 84 HLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE-----EAEvYLRKLQQVYKLNRKEAAAYMyyvwGSGLTLLV 422
Cdd:cd18568 163 PKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPirwrwENK-FAKALNTRFRGQKLSIVLQL----ISSLINHL 237
|
250 260
....*....|....*....|....*...
gi 767973635 423 VQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18568 238 GTIAVLWYGAYLVISGQLTIGQLVAFNM 265
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
508-747 |
8.63e-24 |
|
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: 101.42 E-value: 8.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 508 NVTFTYRT------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYL 578
Cdd:TIGR02769 7 DVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 HRVISLVSQE-PVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGfIMELQDGYSTETGEKGAQLSGGQKQRVAMARAL 657
Cdd:TIGR02769 87 RRDVQLVFQDsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAE-LLDMVGLRSEDADKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 658 VRNPPVLILDEATSALDaeseYLIQQAIHGNLQK------HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafgTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSF 241
|
250
....*....|....*..
gi 767973635 731 GGLYAKLVQRQMLGLQP 747
Cdd:TIGR02769 242 KHPAGRNLQSAVLPEHP 258
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
185-448 |
1.24e-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: 101.82 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 185 VAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNC 264
Cdd:cd18555 4 LISILLLSLLLQLLTL---LIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 265 LFRSLVSQETSFFDENRTGDLISRLTSdTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANS-NVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQ 424
Cdd:cd18555 160 LTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAP 239
|
250 260
....*....|....*....|....
gi 767973635 425 VSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18555 240 LLILWIGAYLVINGELTLGELIAF 263
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
188-451 |
2.54e-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: 101.49 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKS---------------MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTL 252
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEAsflplvpaslgpadpRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 253 IFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvYLRKLQQVYKLNRKEA----AA 408
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERE-RVADASEEYRDANWRAirlrAA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767973635 409 Y---MYYVWGSGLtllvvqVSILYYGGHLVISG------QMTSGNLIAFIIY 451
Cdd:cd18565 240 FfpvIRLVAGAGF------VATFVVGGYWVLDGpplftgTLTVGTLVTFLFY 285
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
504-729 |
3.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSScvnILENFYPL---EGGRVLLDGKPISAYDH--- 575
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKST---LMQHFNALlkpSSGTITIAGYHITPETGnkn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 576 -KYLHRVISLVSQ--EPVLFARSITDNISYGLPTVPFEmvvEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRV 651
Cdd:PRK13641 80 lKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFS---EDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 652 AMARALVRNPPVLILDEATSALDAESEYLIQQaIHGNLQK--HTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLL 728
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKagHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIF 233
|
.
gi 767973635 729 A 729
Cdd:PRK13641 234 S 234
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
182-451 |
3.85e-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: 100.23 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRL 261
Cdd:cd18567 1 KRALLQILLLSLALELFAL---ASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 262 RNCLFRSLVSQETSFFdENR-TGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18567 78 TSNLFRHLLRLPLSYF-EKRhLGDIVSRFGSLDEIQQTLTTGFVEALL-DGLMAILTLVMMFLYSPKLALIVLAAVALYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTL 420
Cdd:cd18567 156 LLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLF 235
|
250 260 270
....*....|....*....|....*....|.
gi 767973635 421 LVVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18567 236 GLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
507-676 |
4.27e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.94 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE---GGRVLLDGKPISAYdhKYLHRVIS 583
Cdd:COG4136 5 ENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISYGLP-TVPFE----MVVEAAQKANAHGFimelqdgystetGEKG-AQLSGGQKQRVAMARA 656
Cdd:COG4136 80 ILFQDDLLFPHlSVGENLAFALPpTIGRAqrraRVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRA 147
|
170 180
....*....|....*....|
gi 767973635 657 LVRNPPVLILDEATSALDAE 676
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAA 167
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
505-730 |
5.18e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 103.61 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 505 DFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGKPISAYDHKYLH 579
Cdd:COG4172 8 SVEDLSVAFGQGGGtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 RV----ISLVSQEPV-----LFarSITDNISYGLptvpfeMVVEAAQKANAHGFIMELQDgystETGEKGA--------- 641
Cdd:COG4172 88 RIrgnrIAMIFQEPMtslnpLH--TIGKQIAEVL------RLHRGLSGAAARARALELLE----RVGIPDPerrldayph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 642 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQKHT---VLIIAHRLSTVEH-AHLIVVLD 714
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQAQILDllkDLQRELgmaLLLITHDLGVVRRfADRVAVMR 231
|
250
....*....|....*.
gi 767973635 715 KGRVVQQGTHQQLLAQ 730
Cdd:COG4172 232 QGEIVEQGPTAELFAA 247
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
521-737 |
9.33e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 104.86 E-value: 9.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDgkpisaydhkylhRVISLVSQEPVLFARSITDNI 600
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 601 SYGLPTVPFEM--VVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE- 676
Cdd:PTZ00243 742 LFFDEEDAARLadAVRVSQlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHv 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 677 SEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQlLAQGGLYAKL 737
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATL 877
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
519-722 |
1.01e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.06 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILENFYPLE--GGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFA 593
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 594 R-SITDNISYGLP--------TVPFEMVVEAAQKAnahgfimELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 664
Cdd:PRK14247 96 NlSIFENVALGLKlnrlvkskKELQERVRWALEKA-------QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 665 ILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAH------RLSTvehahLIVVLDKGRVVQQG 722
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRISD-----YVAFLYKGQIVEWG 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
504-728 |
1.36e-22 |
|
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: 97.46 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL--ENfYPLEGGRVLLDGKPISAYDHKYLHRV 581
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgDL-PPTYGNDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ISLVSQEpvlFARSITDNIsyglpTVpFEMV-------------VEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQK 648
Cdd:COG1119 80 IGLVSPA---LQLRFPRDE-----TV-LDVVlsgffdsiglyrePTDEQRERARELLELL--GLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 649 QRVAMARALVRNPPVLILDEATSALDAES-EYLIQ--QAIHGNLQKHTVLiIAHRL----STVEHAhliVVLDKGRVVQQ 721
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGArELLLAllDKLAAEGAPTLVL-VTHHVeeipPGITHV---LLLKDGRVVAA 224
|
....*..
gi 767973635 722 GTHQQLL 728
Cdd:COG1119 225 GPKEEVL 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
504-731 |
1.88e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.31 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA-YDHKYLHR 580
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 V---ISLVSQ--EPVLFARSITDNISYGLPTvpFEMVVEAAqKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMA 654
Cdd:PRK13646 83 VrkrIGMVFQfpESQLFEDTVEREIIFGPKN--FKMNLDEV-KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 655 RALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQ---KHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLK-SLQtdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 767973635 731 G 731
Cdd:PRK13646 237 K 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
518-723 |
2.61e-22 |
|
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: 96.44 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-S 595
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 596 ITDNISYGLPTVPfemvveaAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 675
Cdd:TIGR03410 92 VEENLLTGLAALP-------RRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767973635 676 ESEYLIQQAIhGNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGT 723
Cdd:TIGR03410 165 SIIKDIGRVI-RRLRAEggmAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
189-448 |
2.67e-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: 97.95 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 189 VAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMdqfSTAVVIVCLLAIGSSFAA---GIRGGIFTLIFARLNIRLRNCL 265
Cdd:cd18588 8 LLASLFLQLFALV---TPLFFQVIIDKVLVHRSL---STLDVLAIGLLVVALFEAvlsGLRTYLFSHTTNRIDAELGARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 266 FRSLVSQETSFFDENRTGDLISR----------LTSDT-TMVSDLVSqnINVFLrntvkvtgvvVFMFSLSWQLSLVTFM 334
Cdd:cd18588 82 FRHLLRLPLSYFESRQVGDTVARvrelesirqfLTGSAlTLVLDLVF--SVVFL----------AVMFYYSPTLTLIVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 335 GFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVW 414
Cdd:cd18588 150 SLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQ 229
|
250 260 270
....*....|....*....|....*....|....
gi 767973635 415 GSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18588 230 IVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
521-730 |
2.88e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNI---LENfyPLEGgRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SI 596
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLvagLEK--PTEG-QIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 597 TDNISYGLPT--VPFE----MVVEAAQKANAHGFimelQDGYSTetgekgaQLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:PRK11432 96 GENVGYGLKMlgVPKEerkqRVKEALELVDLAGF----EDRYVD-------QISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 671 SALDAESEYLIQQAIHgNLQKH---TVLIIAHRLS---TVEHAhlIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:PRK11432 165 SNLDANLRRSMREKIR-ELQQQfniTSLYVTHDQSeafAVSDT--VIVMNKGKIMQIGSPQELYRQ 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
507-729 |
3.16e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.25 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV 585
Cdd:COG1137 7 ENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVLFaRSIT--DNIsyglptvpfEMVVE------AAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARAL 657
Cdd:COG1137 84 PQEASIF-RKLTveDNI---------LAVLElrklskKEREERLEELLEEFGITHLRKS--KAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 658 VRNPPVLILDEATSALD--AESEylIQQAIHgNLQKH--TVLIIAHR----LSTVEHAHLIvvlDKGRVVQQGTHQQLLA 729
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiAVAD--IQKIIR-HLKERgiGVLITDHNvretLGICDRAYII---SEGKVLAEGTPEEILN 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
513-730 |
3.25e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.61 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 513 YRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHK---YLHRVISLVSQEP 589
Cdd:PRK13636 13 YNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmKLRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 590 --VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:PRK13636 92 dnQLFSASVYQDVSFGAVNlkLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 666 LDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVE-HAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLV-EMQKElglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
506-699 |
3.60e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpisaydhkylHRVISLV 585
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVLFA-RSITDNISYGLPTV-------------PFEMVVEAAQKANAHGfIMELQDGYSTET--------------- 636
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELraleaeleeleakLAEPDEDLERLAELQE-EFEALGGWEAEAraeeilsglgfpeed 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 637 -GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES-----EYLIQqaihgnlQKHTVLIIAH 699
Cdd:COG0488 146 lDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN-------YPGTVLVVSH 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
501-716 |
9.08e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 501 EGRVDFENVTFTyrtRPHTQVL-QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL-DGKPISaydhkyl 578
Cdd:COG4178 360 DGALALEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 hrvisLVSQEPVLFARSITDNISYGLPTVPF--EMVVEAAQKANAHGFIMELQdgystETGEKGAQLSGGQKQRVAMARA 656
Cdd:COG4178 430 -----FLPQRPYLPLGTLREALLYPATAEAFsdAELREALEAVGLGHLAERLD-----EEADWDQVLSLGEQQRLAFARL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKG 716
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
504-723 |
1.26e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.71 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 583
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISYGL--PTVPFE----MVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAMARA 656
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGLrmQKTPAAeitpRVMEALRMVQLEEFA-----------QRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIHGnLQKH---TVLIIAH----RLSTVEHahlIVVLDKGRVVQQGT 723
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKA-LQRKlgiTFVFVTHdqeeALTMSDR---IVVMRDGRIEQDGT 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
507-675 |
1.53e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRVIsLVS 586
Cdd:PRK11248 5 SHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGV-VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPVLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfimelqdgystETGEKGA------QLSGGQKQRVAMARALV 658
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLagVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIARALA 144
|
170
....*....|....*..
gi 767973635 659 RNPPVLILDEATSALDA 675
Cdd:PRK11248 145 ANPQLLLLDEPFGALDA 161
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
507-718 |
1.60e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.74 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkyLHRVISLVS 586
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPVLFA-RSITDNISYGLptvpfemvvEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGL---------KGQWRDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 666 LDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLS-TVEHAHLIVVLDKGRV 718
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
506-708 |
1.75e-21 |
|
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: 91.83 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFtyRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVlldgkpisaydHKYLHRVISLV 585
Cdd:cd03223 3 LENLSL--ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVLFARSITDNISYglptvPFEMVveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 665
Cdd:cd03223 70 PQRPYLPLGTLREQLIY-----PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767973635 666 LDEATSALDAESEyliqQAIHGNLQKH--TVLIIAHRlSTVEHAH 708
Cdd:cd03223 115 LDEATSALDEESE----DRLYQLLKELgiTVISVGHR-PSLWKFH 154
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
507-723 |
1.82e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.38 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 586
Cdd:COG4604 5 KNVSKRYGG---KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPVLFAR-SITDNISYG-------LPTVPFEMVVEAAqkanahgfI-----MELQDGYSTEtgekgaqLSGGQKQR--V 651
Cdd:COG4604 82 QENHINSRlTVRELVAFGrfpyskgRLTAEDREIIDEA--------IayldlEDLADRYLDE-------LSGGQRQRafI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 652 AMarALVRNPPVLILDEATSALD----AESEYLIQQAIHgNLQKhTVLIIAHRL---STveHAHLIVVLDKGRVVQQGT 723
Cdd:COG4604 147 AM--VLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLAD-ELGK-TVVIVLHDInfaSC--YADHIVAMKDGRVVAQGT 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
516-730 |
2.73e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.80 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 516 RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH---KYLHRVISLVSQ--- 587
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQnpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 588 --------------EPVLfarsITDNISyglptvpfemVVEAAQKANAhgfiMELQDGYSTE-TGEKGAQLSGGQKQRVA 652
Cdd:PRK11308 103 gslnprkkvgqileEPLL----INTSLS----------AAERREKALA----MMAKVGLRPEhYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 653 MARALVRNPPVLILDEATSALDAEseylIQQAIHG---NLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQ 725
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVS----VQAQVLNlmmDLQQElglSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKE 240
|
....*
gi 767973635 726 QLLAQ 730
Cdd:PRK11308 241 QIFNN 245
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
521-698 |
4.21e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.24 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK----YL-HRVislvSQEPVLfarS 595
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHRN----AMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 596 ITDNIS-----YGlptvPFEMVVEAAQKANAHGFIMELQDGYstetgekgaqLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:PRK13539 90 VAENLEfwaafLG----GEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 767973635 671 SALDAESEYLIQQAIHGNLQKHTVLIIA 698
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
504-723 |
6.95e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.91 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 583
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISYGLPT--VP----FEMVVEAAQkanahgfIMELQ---DgystetgEKGAQLSGGQKQRVAM 653
Cdd:PRK11650 80 MVFQNYALYPHmSVRENMAYGLKIrgMPkaeiEERVAEAAR-------ILELEpllD-------RKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 654 ARALVRNPPVLILDEATSALDA--------EseylIQQaihgnLQKhtvliiahRLST----VEH--------AHLIVVL 713
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAklrvqmrlE----IQR-----LHR--------RLKTtslyVTHdqveamtlADRVVVM 208
|
250
....*....|
gi 767973635 714 DKGRVVQQGT 723
Cdd:PRK11650 209 NGGVAEQIGT 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
521-729 |
7.67e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.24 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEG----GRVLLDGKPISAY-DHKYLHRVISLVSQEPVLFAR 594
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 SITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 675 AESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
504-747 |
9.17e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.13 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpISAYDHKYLH--- 579
Cdd:PRK13644 2 IRLENVSYSY---PDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQgir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 RVISLVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAqkanahgfIMELQDGYSTETGEKgaQLSGGQKQRVA 652
Cdd:PRK13644 77 KLVGIVFQNPetQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRA--------LAEIGLEKYRHRSPK--TLSGGQGQCVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQG 731
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
250
....*....|....*.
gi 767973635 732 GLyaklvqrQMLGLQP 747
Cdd:PRK13644 227 SL-------QTLGLTP 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
504-722 |
9.53e-21 |
|
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: 91.19 E-value: 9.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHkylHRvIS 583
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR---NR-IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLF-ARSITDNISY-----GLPTvpfemvvEAAQKANAHGF----IMELQDgystetgEKGAQLSGGQKQRVAM 653
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlaqlkGLKK-------EEARRRIDEWLerleLSEYAN-------KRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 654 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 722
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
507-723 |
1.74e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.42 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY--LHRVI 582
Cdd:PRK13637 6 ENLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEP--VLFARSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQdGYSTET-GEKGA-QLSGGQKQRVAMARALV 658
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAFG----PINLGLSEEEIENRVKRAMNIV-GLDYEDyKDKSPfELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 659 RNPPVLILDEATSALD--AESEYLIQ-QAIHGNlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 723
Cdd:PRK13637 161 MEPKILILDEPTAGLDpkGRDEILNKiKELHKE-YNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
521-722 |
1.76e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.50 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SITD 598
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 599 NISYGLPTVPfemvvEAAQKANAhgFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD-AES 677
Cdd:PRK15439 106 NILFGLPKRQ-----ASMQKMKQ--LLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767973635 678 EYLIQQaIHGNLQK-HTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQG 722
Cdd:PRK15439 177 ERLFSR-IRELLAQgVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
507-720 |
1.80e-20 |
|
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: 90.96 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENfypLE---GGRVLLDGKPISAYDHKYLHRV- 581
Cdd:COG4181 12 RGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG---LDrptSGTVRLAGQDLFALDEDARARLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ---ISLVSQE----PVLFARsitDNIsyglpTVPFEM--VVEAAQKANAhgfimELQD-GYSTETGEKGAQLSGGQKQRV 651
Cdd:COG4181 89 arhVGFVFQSfqllPTLTAL---ENV-----MLPLELagRRDARARARA-----LLERvGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 652 AMARALVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIA-HRLSTVEHAHLIVVLDKGRVVQ 720
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFElNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
504-732 |
2.87e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKylhRVIS 583
Cdd:COG4152 2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDR---RRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISY-----GLPtvpfemvvEAAQKANAHGFI--MELQDgYSTETGEKgaqLSGGQKQRVAMAR 655
Cdd:COG4152 75 YLPEERGLYPKmKVGEQLVYlarlkGLS--------KAEAKRRADEWLerLGLGD-RANKKVEE---LSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIhgnLQKH----TVLIIAHRLSTVE----HahlIVVLDKGRVVQQGTHQQL 727
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVI---RELAakgtTVIFSSHQMELVEelcdR---IVIINKGRKVLSGSVDEI 216
|
....*
gi 767973635 728 LAQGG 732
Cdd:COG4152 217 RRQFG 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
510-729 |
3.21e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.39 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 510 TFTYRT----RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:PRK15112 13 TFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPvlfARSITDNISYG-LPTVPFEMVVEAAQKANAHGFIMEL-QDGYSTE-TGEKGAQLSGGQKQRVAMARALVRNPP 662
Cdd:PRK15112 93 FQDP---STSLNPRQRISqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 663 VLILDEATSALDAEseyLIQQAIHGNL---QKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PRK15112 170 VIIADEALASLDMS---MRSQLINLMLelqEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
505-728 |
3.39e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 505 DFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG------GRVLLDGKPISAYDHKYL 578
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 HRVISLVSQEPVLFAR-SITDNISYGLPTVPFE-------MVVEAAQKAnahGFIMELQDGYSTetgeKGAQLSGGQKQR 650
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKekreikkIVEECLRKV---GLWKEVYDRLNS----PASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 651 VAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLL 728
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
507-684 |
3.58e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 90.19 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENV--TFTYRTRPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSS---CvnILENFYPlEGGRVLL--DGKPI---SAYD 574
Cdd:COG4778 8 ENLskTFTLHLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTllkC--IYGNYLP-DSGSILVrhDGGWVdlaQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 575 HKYLH---RVISLVSQepvlFARSItdnisyglPTVP-FEMVVEAAqkanahgfimeLQDGYSTETG-EKGAQL------ 643
Cdd:COG4778 85 REILAlrrRTIGYVSQ----FLRVI--------PRVSaLDVVAEPL-----------LERGVDREEArARARELlarlnl 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 644 ------------SGGQKQRVAMARALVRNPPVLILDEATSALDAESE----YLIQQA 684
Cdd:COG4778 142 perlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEA 198
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
504-736 |
5.58e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.63 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13652 4 IETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 656
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpinlgLDEETVAHRVSSALHMLG---LEELRD-------RVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGL 733
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
...
gi 767973635 734 YAK 736
Cdd:PRK13652 232 LAR 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
504-723 |
1.20e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.80 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAY----DHKY 577
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 578 LHRVISLVSQ--EPVLFARSITDNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMA 654
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQN--FGVSQEEAEALAREKLALV---GISESLFEKNPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 655 RALVRNPPVLILDEATSALDA----ESEYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 723
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPkgrkELMTLFKKLHQSGM---TIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
514-734 |
1.55e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.19 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP---LEGGRVLLDGKPIsayDHKYLHRVISLVSQepv 590
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI---DAKEMRAISAYVQQ--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 lfarsitDNISYGLPTVPFEMVVEAAQKANAHGFI-------------MELQDGYSTETGEKGAQ--LSGGQKQRVAMAR 655
Cdd:TIGR00955 107 -------DDLFIPTLTVREHLMFQAHLRMPRRVTKkekrervdevlqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLST--VEHAHLIVVLDKGRVVQQGTHQQL---LA 729
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAvpfFS 259
|
....*
gi 767973635 730 QGGLY 734
Cdd:TIGR00955 260 DLGHP 264
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
521-698 |
1.65e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 87.55 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsAYDHKYLHRVISLVSQEPVLFAR-SITDN 599
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 600 ISYGLPTVPFEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 679
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNGF-----------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170
....*....|....*....
gi 767973635 680 LIQQAIHGNLQKHTVLIIA 698
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLT 181
|
|
| 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 |
1.82e-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: 89.56 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18566 7 VLLASLFINILALA---TPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrntvKVTGVVVF---MFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18566 84 HLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALL----DLPFVLIFlglIWYLGGKLVLVPLVLLGLFVLVAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQ----VYKLNRKEAAAYMyyvwGSGLTL 420
Cdd:cd18566 160 LLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANaayaGFKVAKINAVAQT----LGQLFS 235
|
250 260 270
....*....|....*....|....*....|
gi 767973635 421 LVVQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18566 236 QVSMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
516-698 |
2.17e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 87.03 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 516 RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVISLVSQEPVLFAR- 594
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 SITDNISYGLPTVPFE--MVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:TIGR01189 89 SALENLHFWAAIHGGAqrTIEDALAAVGLTGF-----------EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 767973635 673 LDAESEYLIQQAIHGNLQKHTVLIIA 698
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLT 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 |
2.62e-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: 89.19 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRL 261
Cdd:cd18782 1 RRALIEVLALSFVVQLLGL---ANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 262 RNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 341
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 342 VSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEE----EEAEVYLRKLQQVYKLNRKEAAAYMYyvwgSG 417
Cdd:cd18782 157 LTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELkarwRWQNRYARSLGEGFKLTVLGTTSGSL----SQ 232
|
250 260 270
....*....|....*....|....*....|...
gi 767973635 418 LTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18782 233 FLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRI 265
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
504-724 |
2.87e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 87.76 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILEnfYPLEGGRVLLDGK-----PISAYDH 575
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLrvlNLLE--TPDSGQLNIAGHQfdfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 576 KYLHRVISLVSQEPVLFA-RSITDNISYGlPTVPFEMVVEAAQ-KANAHGFIMELQDgystETGEKGAQLSGGQKQRVAM 653
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPhLTVMENLIEA-PCKVLGLSKEQAReKAMKLLARLRLTD----KADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 654 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRlstVEHAHLI----VVLDKGRVVQQGTH 724
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIR-ELSQTgiTQVIVTHE---VEFARKVasqvVYMEKGRIIEQGDA 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
507-744 |
2.94e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV 585
Cdd:PRK10895 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVLFAR-SITDNIsygLPTVPFEMVVEAAQKANAHGFIME------LQDGYstetgekGAQLSGGQKQRVAMARALV 658
Cdd:PRK10895 84 PQEASIFRRlSVYDNL---MAVLQIRDDLSAEQREDRANELMEefhiehLRDSM-------GQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 659 RNPPVLILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHR----LSTVEHAHLIvvlDKGRVVQQGTHQQLLAQggl 733
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIeHLRDSGLGVLITDHNvretLAVCERAYIV---SQGHLIAHGTPTEILQD--- 227
|
250
....*....|.
gi 767973635 734 yaKLVQRQMLG 744
Cdd:PRK10895 228 --EHVKRVYLG 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
521-727 |
5.33e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SITDN 599
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 600 ISYGLPTVPFEMVvEAAQKANAHGFIMELQDGysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 679
Cdd:PRK11607 112 IAFGLKQDKLPKA-EIASRVNEMLGLVHMQEF----AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767973635 680 LIQQAIHGNLQK--HTVLIIAH-RLSTVEHAHLIVVLDKGRVVQQGTHQQL 727
Cdd:PRK11607 187 RMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
518-723 |
6.88e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.41 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI----SAYDHKYLHRVISLVSQepvlFA 593
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRNQKLGFIYQ----FH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 594 RSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK11629 97 HLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767973635 674 DAESEYLIQQAIhGNL---QKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 723
Cdd:PRK11629 177 DARNADSIFQLL-GELnrlQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
522-728 |
7.12e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.71 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFAR-SI 596
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 597 TDNISYG--LPTVPFEMVVEAAQKANAHGFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK10070 124 LDNTAFGmeLAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 675 A------ESEYLIQQAIHgnlqKHTVLIIAHRL-STVEHAHLIVVLDKGRVVQQGTHQQLL 728
Cdd:PRK10070 197 PlirtemQDELVKLQAKH----QRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
520-722 |
7.71e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.17 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN---FYPLEGGRVLLDGKPISAYDHKYlhrVISLVSQEPVlFARSI 596
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQK---CVAYVRQDDI-LLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 597 T--DNISYglpTVPFEMVVEA--AQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:cd03234 97 TvrETLTY---TAILRLPRKSsdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 673 LDAESEYLI----QQAIHGNlqkHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQG 722
Cdd:cd03234 174 LDSFTALNLvstlSQLARRN---RIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
504-727 |
8.27e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 85.88 E-value: 8.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVIS 583
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLfARSIT--DNIS-----YGLPTvpfemvVEAAQKanahgfIMELQDGYstETGEKGAQL----SGGQKQRVA 652
Cdd:cd03265 77 IVFQDLSV-DDELTgwENLYiharlYGVPG------AERRER------IDELLDFV--GLLEAADRLvktySGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 727
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
522-728 |
9.41e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.43 E-value: 9.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRVIS-LVSQEPVLFARSITDNI 600
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQG-EILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 601 SYGLPTVPFEMVVEA--AQKANAhgfiMELQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NPP--VLILDEATS 671
Cdd:COG4138 91 ALHQPAGASSEAVEQllAQLAEA----LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 672 ALDaeseyLIQQAIHGNL------QKHTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLL 728
Cdd:COG4138 163 SLD-----VAQQAALDRLlrelcqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
504-751 |
1.07e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.10 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRP--HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEGGRVLLDGKPISAYDHKYLHR 580
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 V---ISLVSQEP--VLFARSITDNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMA 654
Cdd:PRK13643 82 VrkkVGVVFQFPesQLFEETVLKDVAFGPQN--FGIPKEKAEKIAAEKLEMV---GLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 655 RALVRNPPVLILDEATSALDAESEYLIQ---QAIHGNLQkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQSGQ--TVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE 234
|
250 260
....*....|....*....|.
gi 767973635 731 gglyAKLVQRQMLGLQPAADF 751
Cdd:PRK13643 235 ----VDFLKAHELGVPKATHF 251
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
507-725 |
1.35e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.84 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILEnfYPLEG-----GRVLLDGKPISAYDHKYL 578
Cdd:PRK11124 6 NGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLrvlNLLE--MPRSGtlniaGNHFDFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 HRVISLVSQEPVLFAR-SITDNisygLPTVPfeMVVEAAQKANAHGFIMELQDGYS-TETGEK-GAQLSGGQKQRVAMAR 655
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHlTVQQN----LIEAP--CRVLGLSKDQALARAEKLLERLRlKPYADRfPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH-TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQ 725
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
504-728 |
2.54e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydHKYLHRV-I 582
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARArI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQ----EPVLFARsitDNI-----SYGLPTVPFEMVV----EAAQ---KANAhgfimelqdgystetgeKGAQLSGG 646
Cdd:PRK13536 117 GVVPQfdnlDLEFTVR---ENLlvfgrYFGMSTREIEAVIpsllEFARlesKADA-----------------RVSDLSGG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 647 QKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTH 724
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRP 256
|
....
gi 767973635 725 QQLL 728
Cdd:PRK13536 257 HALI 260
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
230-668 |
2.77e-18 |
|
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: 89.09 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 230 VIVCLLAIGSSFAAGIRggiFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSqNINVFLR 309
Cdd:COG4615 55 AGLLVLLLLSRLASQLL---LTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 310 NTVKVTGVVVFMFSLSWQLSLVTFmgfpiIMMVSNIYGkyYKRLSKEVQNALARASNTAEETISAMKTV----------- 378
Cdd:COG4615 131 SVALVLGCLAYLAWLSPPLFLLTL-----VLLGLGVAG--YRLLVRRARRHLRRAREAEDRLFKHFRALlegfkelklnr 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 379 ---RSFANEEeeaevYLRKLQQVYKLNRKEAAAYMYYV-WGSgLTLLVVQVSILYYGGHLV-ISGQMTSGnlIAFIIYeF 453
Cdd:COG4615 204 rrrRAFFDED-----LQPTAERYRDLRIRADTIFALANnWGN-LLFFALIGLILFLLPALGwADPAVLSG--FVLVLL-F 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 454 VLGDcMESVGSVYSGLMQGVGAAEKVFEF---IDRQPTMVHDGSLAPDHLE-GRVDFENVTFTYRTRPHTQ--VLQNVSF 527
Cdd:COG4615 275 LRGP-LSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDEgfTLGPIDL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 528 SLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA--YDHkYLHRvISLVSQEPVLFARsitdniSYGLP 605
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREA-YRQL-FSAVFSDFHLFDR------LLGLD 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 606 TVPfemvveAAQKANAHGFIMELQ------DGYSTETgekgaQLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:COG4615 426 GEA------DPARARELLERLELDhkvsveDGRFSTT-----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
504-729 |
3.03e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 L-----------VSQEPVLFARSitdnisYGLPT------VPfeMVVEAA---QKANAhgfimelqdgystetgeKGAQL 643
Cdd:PRK13537 85 VpqfdnldpdftVRENLLVFGRY------FGLSAaaaralVP--PLLEFAkleNKADA-----------------KVGEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 644 SGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQ 721
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAE 219
|
....*...
gi 767973635 722 GTHQQLLA 729
Cdd:PRK13537 220 GAPHALIE 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
502-737 |
3.14e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 502 GRVDFENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA-----YD 574
Cdd:PRK13645 5 KDIILDNVSYTYakKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 575 HKYLHRVISLVSQEP--VLFARSITDNISYGlptvPFEMvveAAQKANAHGFIMELQDGYS--TETGEKGA-QLSGGQKQ 649
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFG----PVNL---GENKQEAYKKVPELLKLVQlpEDYVKRSPfELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 650 RVAMARALVRNPPVLILDEATSALD--AESEYL-IQQAIHGNlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQ 725
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDpkGEEDFInLFERLNKE-YKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPF 236
|
250
....*....|..
gi 767973635 726 QLLAQGGLYAKL 737
Cdd:PRK13645 237 EIFSNQELLTKI 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
507-728 |
5.16e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR-VISLV 585
Cdd:PRK10575 15 RNVSFRV---PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVLFARSITDNISYGlpTVPF------------EMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAM 653
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIG--RYPWhgalgrfgaadrEKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 654 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLL 728
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
522-699 |
6.17e-18 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 83.67 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLhrvisLVSQEPVLFA-RSITDNI 600
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 601 SYGLPTVPFEMVVEAAQKANAHGFIMElqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 680
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALV---GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|.
gi 767973635 681 IQQAIHGNLQKH--TVLIIAH 699
Cdd:TIGR01184 153 LQEELMQIWEEHrvTVLMVTH 173
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
522-747 |
6.60e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE--GGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SIT 597
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 598 DNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALdAES 677
Cdd:PRK13549 101 ENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPAT--PVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TES 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 678 EYLIQQAIHGNLQKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVqqGTH-QQLLAQGGLYAKLVQRQMLGLQP 747
Cdd:PRK13549 178 ETAVLLDIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGRHI--GTRpAAGMTEDDIITMMVGRELTALYP 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
504-723 |
6.91e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.53 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-I 582
Cdd:PRK09700 6 ISMAGIGKSF---GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQE-PVLFARSITDNISYG-LPT-----VPF----EMVVEAAqkanahgfIMELQDGYSTETGEKGAQLSGGQKQRV 651
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGrHLTkkvcgVNIidwrEMRVRAA--------MMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 652 AMARALVRNPPVLILDEATSAL-DAESEYLIqqAIHGNLQKH--TVLIIAHRLstvehAHLIVVLDKGRVVQQGT 723
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRKEgtAIVYISHKL-----AEIRRICDRYTVMKDGS 222
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
261-451 |
1.51e-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: 84.01 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 261 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAaymyyvWgSGLTL 420
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTR------W-NAKTF 233
|
170 180 190
....*....|....*....|....*....|....*...
gi 767973635 421 LVVQVS-------ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18554 234 SAVNTItdlapllVIGFAAYLVIEGNLTVGTLVAFVGY 271
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
503-722 |
1.92e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.83 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 503 RVDFENVTFTyrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKS-SCVNILENFYP---LEGGRVLLDGKPISAYDHKyl 578
Cdd:PRK10418 4 QIELRNIALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVAPCALR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 HRVISLVSQEPvlfaRSITDNI----SYGLPTvpfemvVEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQ 649
Cdd:PRK10418 78 GRKIATIMQNP----RSAFNPLhtmhTHARET------CLALGKPADDATLTAALEAVGLENAARVLKLypfemSGGMLQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 650 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHT--VLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 722
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
506-731 |
2.37e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA----YDHKYLH 579
Cdd:PRK13634 5 FQKVEHRYqyKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 RVISLVSQ--EPVLFARSITDNISYGlPT---VPFEmvvEAAQKANAhgfIMELQdGYSTETGEKGA-QLSGGQKQRVAM 653
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFG-PMnfgVSEE---DAKQKARE---MIELV-GLPEELLARSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 654 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFY-KLHKEkglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
..
gi 767973635 730 QG 731
Cdd:PRK13634 236 DP 237
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
506-716 |
2.60e-17 |
|
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: 80.75 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN--FYPLEGGRVLLDGKPISaydhKYLHRVI 582
Cdd:cd03232 6 WKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD----KNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEPVLFarsitdnisyglptvPFEMVVEAAQ-KANAHGfimelqdgystetgekgaqLSGGQKQRVAMARALVRNP 661
Cdd:cd03232 82 GYVEQQDVHS---------------PNLTVREALRfSALLRG-------------------LSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 662 PVLILDEATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRLSTV--EHAHLIVVLDKG 716
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLK-KLADSgqAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
508-730 |
2.68e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 508 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEGGrVLLDGKPIS----------AYD 574
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK--PSEGS-IVVNGQTINlvrdkdgqlkVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 575 HKYLHRV---ISLVSQEPVLFAR-SITDNISYGLPTVPFEMVVEAAQKA----NAHGFIMELQDGYStetgekgAQLSGG 646
Cdd:PRK10619 84 KNQLRLLrtrLTMVFQHFNLWSHmTVLENVMEAPIQVLGLSKQEARERAvkylAKVGIDERAQGKYP-------VHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 647 QKQRVAMARALVRNPPVLILDEATSALDAE--SEYL-IQQAIHGnlQKHTVLIIAHRLSTVEH--AHLIvVLDKGRVVQQ 721
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPElvGEVLrIMQQLAE--EGKTMVVVTHEMGFARHvsSHVI-FLHQGKIEEE 233
|
....*....
gi 767973635 722 GTHQQLLAQ 730
Cdd:PRK10619 234 GAPEQLFGN 242
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
504-719 |
5.12e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLHR 580
Cdd:PRK10908 2 IRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 VISLVSQEP-VLFARSITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARAL 657
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVA--IP-----LIIAGASGDDIRRRVSAALDkvGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 658 VRNPPVLILDEATSALD-AESEYLIQQAIHGNLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVV 719
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDdALSEGILRLFEEFNRVGVTVLMATHDIGLISrRSYRMLTLSDGHLH 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
522-747 |
7.76e-17 |
|
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: 84.11 E-value: 7.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP--LEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SIT 597
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 598 DNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGaQLSGGQKQRVAMARALVRNPPVLILDEATSAL-DA 675
Cdd:TIGR02633 97 ENIFLGNEiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEK 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 676 ESEYLIQqaIHGNLQKHTV--LIIAHRLSTVEhahliVVLDKGRVVQQGTH-----QQLLAQGGLYAKLVQRQMLGLQP 747
Cdd:TIGR02633 176 ETEILLD--IIRDLKAHGVacVYISHKLNEVK-----AVCDTICVIRDGQHvatkdMSTMSEDDIITMMVGREITSLYP 247
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
515-750 |
1.23e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 515 TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPvlfar 594
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 sitdnisyglpTVPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ------------------LSGGQKQRVAMARA 656
Cdd:PRK09536 87 -----------SLSFEFDVRQVVEMGRTPHRSRF--DTWTETDRAAVEramertgvaqfadrpvtsLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 657 LVRNPPVLILDEATSALD--------------AESEYLIQQAIHGnlqkhtvLIIAHRlstveHAHLIVVLDKGRVVQQG 722
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDinhqvrtlelvrrlVDDGKTAVAAIHD-------LDLAAR-----YCDELVLLADGRVRAAG 221
|
250 260
....*....|....*....|....*...
gi 767973635 723 THQQLLAQGGLYAKLVQRQMLGLQPAAD 750
Cdd:PRK09536 222 PPADVLTADTLRAAFDARTAVGTDPATG 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
232-753 |
1.39e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 84.58 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 232 VCLLAIGSSFAagIRGGIFTL--IFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISrltsdttmvsdLVSQNINVF-- 307
Cdd:TIGR01271 128 LCLLFIVRTLL--LHPAIFGLhhLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVS-----------LLSNNLNKFde 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 308 ---LRNTVKVTGV-VVFMFSLSWQL---SLVTFMGFPIIMMV-----SNIYGKYYKRLSKEVQNALARASntaeETISAM 375
Cdd:TIGR01271 195 glaLAHFVWIAPLqVILLMGLIWELlevNGFCGLGFLILLALfqaclGQKMMPYRDKRAGKISERLAITS----EIIENI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 376 KTVRSFAnEEEEAEVYLRKLQQV-YKLNRKeaAAYMYYVWGSGL---TLLVVQVSILYYGghlvISGQMTSGNLIAFIIY 451
Cdd:TIGR01271 271 QSVKAYC-WEEAMEKIIKNIRQDeLKLTRK--IAYLRYFYSSAFffsGFFVVFLSVVPYA----LIKGIILRRIFTTISY 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 452 EFVLgdcMESVGSVYSGLMQ----GVGAAEKVFEFIDRQPTMVHDGSLAPDHLEgrvdFENVT----------------- 510
Cdd:TIGR01271 344 CIVL---RMTVTRQFPGAIQtwydSLGAITKIQDFLCKEEYKTLEYNLTTTEVE----MVNVTaswdegigelfekikqn 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 511 --------------FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgRVLLDGKpisaydh 575
Cdd:TIGR01271 417 nkarkqpngddglfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEG-KIKHSGR------- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 576 kylhrvISLVSQEPVLFARSITDNISYGLPTVPFEM--VVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQRVAM 653
Cdd:TIGR01271 489 ------ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYtsVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISL 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 654 ARALVRNPPVLILDEATSALDAESEYLI-QQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGG 732
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP 639
|
570 580
....*....|....*....|.
gi 767973635 733 LYAKlvqrQMLGLQPAADFTA 753
Cdd:TIGR01271 640 DFSS----LLLGLEAFDNFSA 656
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
514-722 |
1.99e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI---SAYDHKYLHRVISLVSQEPV 590
Cdd:PRK10261 332 RVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 --LFAR-SITDNISYGLpTVPFEMVVEAAQKANAH-----GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPP 662
Cdd:PRK10261 412 asLDPRqTVGDSIMEPL-RVHGLLPGKAAAARVAWllervGLLPEHAWRYPHE-------FSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 663 VLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 722
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLL-DLQRDfgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
506-730 |
2.01e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 506 FENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI---SAYDHkyLHRVI 582
Cdd:PRK11288 7 FDGIGKTF---PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAA--LAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQE----PVLfarSITDNISYG-LPTvPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARAL 657
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGqLPH-KGGIVNRRLLNYEAREQLEHLGVDIDPDT--PLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 658 VRNPPVLILDEATSALDA-ESEYLIqqAIHGNL--QKHTVLIIAHRLSTV-EHAHLIVVLDKGRVV------QQGTHQQL 727
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSArEIEQLF--RVIRELraEGRVILYVSHRMEEIfALCDAITVFKDGRYVatfddmAQVDRDQL 233
|
...
gi 767973635 728 LAQ 730
Cdd:PRK11288 234 VQA 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
504-699 |
2.11e-16 |
|
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: 76.72 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVlldgkpisaydhkylhrvis 583
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 lvsqepvlfARSITDNISYglptvpFEmvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03221 58 ---------TWGSTVKIGY------FE-------------------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*....
gi 767973635 664 LILDEATSALDAES-EYLIQQaihgnLQKH--TVLIIAH 699
Cdd:cd03221 92 LLLDEPTNHLDLESiEALEEA-----LKEYpgTVILVSH 125
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
504-722 |
2.49e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.61 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVIS 583
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFAR-SITDNISYGLPTVPFEMVvEAAQKANAHGFImeLQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPP 662
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGLKLAGAKKE-EINQRVNQVAEV--LQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 663 VLILDEATSALDAESEylIQQAI-----HGNLQKhTVLIIAHrlSTVEH---AHLIVVLDKGRVVQQG 722
Cdd:PRK11000 154 VFLLDEPLSNLDAALR--VQMRIeisrlHKRLGR-TMIYVTH--DQVEAmtlADKIVVLDAGRVAQVG 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
520-740 |
3.22e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.96 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPV------ 590
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSpDERARAGIFLAFQYPVeipgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 --LFARSITDNISYGLPTVPfEMVVEAAQKANAHGFIMELQDGYSTETgekgaqLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:COG0396 94 vsNFLRTALNARRGEELSAR-EFLKLLKEKMKELGLDEDFLDRYVNEG------FSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 669 ATSALDAE-----SEYLiqQAIHGnlQKHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQGTH---QQLLAQGglYAKLV 738
Cdd:COG0396 167 TDSGLDIDalrivAEGV--NKLRS--PDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKelaLELEEEG--YDWLK 240
|
..
gi 767973635 739 QR 740
Cdd:COG0396 241 EE 242
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
505-750 |
6.67e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 505 DFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILEN---FYPleGGRVLLDGKPISAYDHK 576
Cdd:PRK15134 7 AIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYP--SGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 577 YLHRV----ISLVSQEPVlfarsITDNISYGLPTVPFEMVV--EAAQKANAHGFIMELQDgystETGEKGA--------- 641
Cdd:PRK15134 85 TLRGVrgnkIAMIFQEPM-----VSLNPLHTLEKQLYEVLSlhRGMRREAARGEILNCLD----RVGIRQAakrltdyph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 642 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGR 717
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLR-ELQQElnmGLLFITHNLSIVRKlADRVAVMQNGR 234
|
250 260 270
....*....|....*....|....*....|...
gi 767973635 718 VVQQGTHQQLLAQGglyAKLVQRQMLGLQPAAD 750
Cdd:PRK15134 235 CVEQNRAATLFSAP---THPYTQKLLNSEPSGD 264
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
508-719 |
8.44e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.20 E-value: 8.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 508 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAY-DHKYlHRVISLVS 586
Cdd:COG1101 8 SKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEYKR-AKYIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPVLfarsitdnisyGlpTVPfEMVVE-----AAQKANAHGFI-------------------MELQDGYSTETGekgaQ 642
Cdd:COG1101 87 QDPMM-----------G--TAP-SMTIEenlalAYRRGKRRGLRrgltkkrrelfrellatlgLGLENRLDTKVG----L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 643 LSGGQKQRVAMARALVRNPPVLILDEATSALD---AE-----SEYLIQQaihgnlQKHTVLIIAHRLS-TVEHAHLIVVL 713
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAAlvlelTEKIVEE------NNLTTLMVTHNMEqALDYGNRLIMM 222
|
....*.
gi 767973635 714 DKGRVV 719
Cdd:COG1101 223 HEGRII 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
260-734 |
8.81e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 81.88 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVvFMFSLSWQLSLVTFMGFPII 339
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAI-FVVSVLQPYIFIAAIPVAVI 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 340 MMVSNIYgkyYKRLSKEVQNALARA-SNTAEETISAMK---TVRSFANEEeeaevYLRKLqqVYK-LNRKEAAAYMYYVW 414
Cdd:TIGR01271 1038 FIMLRAY---FLRTSQQLKQLESEArSPIFSHLITSLKglwTIRAFGRQS-----YFETL--FHKaLNLHTANWFLYLST 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 415 GSGLTLLVVQVSILYYGGHLVIS---GQMTSGNL-IAFIIYEFVLGDCMESVGSVYS--GLMQGVgaaEKVFEFIDRQP- 487
Cdd:TIGR01271 1108 LRWFQMRIDIIFVFFFIAVTFIAigtNQDGEGEVgIILTLAMNILSTLQWAVNSSIDvdGLMRSV---SRVFKFIDLPQe 1184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 488 ---------------TMVHDGSLAPDHL--EGRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 550
Cdd:TIGR01271 1185 eprpsggggkyqlstVLVIENPHAQKCWpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 551 ILENFYPLEGgRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQKANAHGFI 625
Cdd:TIGR01271 1264 ALLRLLSTEG-EIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD------PYEQwsdeeIWKVAEEVGLKSVI 1336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 626 MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVE 705
Cdd:TIGR01271 1337 EQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALL 1416
|
490 500
....*....|....*....|....*....
gi 767973635 706 HAHLIVVLDKGRVVQQGTHQQLLAQGGLY 734
Cdd:TIGR01271 1417 ECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
519-719 |
1.12e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.92 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFAR 594
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 -SITDNISygLPTVpFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK10535 101 lTAAQNVE--VPAV-YAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767973635 674 DAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVV 719
Cdd:PRK10535 176 DSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
514-727 |
1.15e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY---PLEGGRVLLDGKPIS-----AYDHKYLHRVISLV 585
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIRKSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQEPVLFAR-SITDNISYG-LPTVPFEMVV----EAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVR 659
Cdd:PRK09984 92 FQQFNLVNRlSVLENVLIGaLGSTPFWRTCfswfTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 660 NPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQL 727
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
521-718 |
1.97e-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: 75.16 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEP----VLFARS 595
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 596 ITDNISYGlptvpfemvveaaqkanahgfimelqdgystetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 675
Cdd:cd03215 95 VAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767973635 676 ESeyliQQAIHGNLQK-----HTVLIIAHRLSTVEH-AHLIVVLDKGRV 718
Cdd:cd03215 138 GA----KAEIYRLIREladagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
513-713 |
2.93e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.58 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 513 YRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpisaydhkylHRVISLVSQ---EP 589
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 590 VLFARSITDNISYGL---------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRN 660
Cdd:NF040873 68 DSLPLTVRDLVAMGRwarrglwrrLTRDDRAAVDDALER------VGLADLAGRQLGE----LSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 661 PPVLILDEATSALDAESEYLIQQAI---HGnlQKHTVLIIAHRLSTVEHAHLIVVL 713
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLaeeHA--RGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
188-395 |
3.12e-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: 77.16 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVtfmgFPIIMMVSNIYG 347
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV----LPPLLVVYYLLQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767973635 348 KYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEEEEAEVYLRKL 395
Cdd:cd18580 157 RYYLRTSRQLRrlESESRSPlySHFSETLSGLSTIRAFGWQERFIEENLRLL 208
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
502-730 |
3.55e-15 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 76.43 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 502 GRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRV 581
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 ISLVSQEPVLFARSITDNIS-YGLPTVpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRN 660
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 661 PPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
503-740 |
3.79e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 503 RVDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI 582
Cdd:PRK10253 7 RLRGEQLTLGYGKY---TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEPVLFAR-SITDNISYG-LPTVPF--------EMVVEAAQKANAhgfIMELQDgYSTETgekgaqLSGGQKQRVA 652
Cdd:PRK10253 84 GLLAQNATTPGDiTVQELVARGrYPHQPLftrwrkedEEAVTKAMQATG---ITHLAD-QSVDT------LSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEY-LIQQAIHGNLQK-HTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIdLLELLSELNREKgYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
250
....*....|.
gi 767973635 730 qgglyAKLVQR 740
Cdd:PRK10253 234 -----AELIER 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
504-730 |
6.17e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTQ---VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY-LH 579
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 RVISLVSQEP--VLFARSITDNISYG---LPTVPFEM---VVEAAQKANAHGFimelqdgystetgEKGAQ--LSGGQKQ 649
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpenLGIPPEEIrerVDESLKKVGMYEY-------------RRHAPhlLSGGQKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 650 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 727
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
...
gi 767973635 728 LAQ 730
Cdd:PRK13633 232 FKE 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
523-737 |
7.64e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 7.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 523 QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI----------SLVSQEPVLF 592
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpgiktELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 593 ARSITDNISYglptvpfEMVVEAAQKANAHGFiMELqdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:PRK13538 98 YQRLHGPGDD-------EALWEALAQVGLAGF-EDV----------PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 673 LDaeseyliqqaihgnlqKHTVLIIAHRLStvEHAhlivvlDKGRVVQQGTHQQLLAQGGLYAKL 737
Cdd:PRK13538 160 ID----------------KQGVARLEALLA--QHA------EQGGMVILTTHQDLPVASDKVRKL 200
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
525-727 |
1.06e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.90 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 525 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPV--LFAR-SITD 598
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLasLNPRmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 599 NISYGL----PTVPFEMVVEAAQKANAH-GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK15079 120 IIAEPLrtyhPKLSRQEVKDRVKAMMLKvGLLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973635 674 D----AESEYLIQQaihgnLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 727
Cdd:PRK15079 193 DvsiqAQVVNLLQQ-----LQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
516-723 |
1.18e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.86 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 516 RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--------GRVLLDGKPISAYDHKYLHRVISLVSQ 587
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 588 --EPVlFARSITDNISYGLptvpFEMVVEAAQKANAHGFI----MELQDGySTETGEKGAQLSGGQKQRVAMARAL---- 657
Cdd:PRK13547 91 aaQPA-FAFSAREIVLLGR----YPHARRAGALTHRDGEIawqaLALAGA-TALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 658 -----VRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHT--VLIIAHRLS-TVEHAHLIVVLDKGRVVQQGT 723
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
524-727 |
1.31e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.26 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA--------------YDHKYLHRVISLVsqEP 589
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpghqiarmgvvrtFQHVRLFREMTVI--EN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 590 VLFA--RSITDNISYGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTETGekgaQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:PRK11300 101 LLVAqhQQLKTGLFSGLLKTPAFRRAESEALDRAATWLerVGLLEHANRQAG----NLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 666 LDEATSALDAESEYLIQQAIhGNLQKH---TVLIIAHRLSTV----EHahlIVVLDKGRVVQQGTHQQL 727
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELI-AELRNEhnvTVLLIEHDMKLVmgisDR---IYVVNQGTPLANGTPEEI 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
504-729 |
1.36e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.15 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL---ENFYPLEG---------------GRVLL 565
Cdd:TIGR03269 1 IEVKNLTKKFDGK---EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmDQYEPTSGriiyhvalcekcgyvERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 566 DGKPISAYDHKYLHRVISLVSQEPVLFARsITDNIS---------YGLPTVpFEMVVEAAQKAnahgfimelqdGYSTET 636
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFWNLSDKLRRR-IRKRIAimlqrtfalYGDDTV-LDNVLEALEEI-----------GYEGKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 637 GEKGA------------------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLI 696
Cdd:TIGR03269 145 AVGRAvdliemvqlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVL 224
|
250 260 270
....*....|....*....|....*....|....
gi 767973635 697 IAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:TIGR03269 225 TSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
501-710 |
5.80e-14 |
|
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: 75.56 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 501 EGRVDFENVTFTyrtRPHTQVL-QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYdhkylh 579
Cdd:TIGR00954 449 DNGIKFENIPLV---TPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY------ 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 rvislVSQEPVLFARSITDNISYglPTVPFEMVVEAAQKANAHGFIMELQDGY--STETGEKGAQ-----LSGGQKQRVA 652
Cdd:TIGR00954 520 -----VPQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDKDLEQILDNVQLTHilEREGGWSAVQdwmdvLSGGEKQRIA 592
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEyliqQAIHGNLQKH--TVLIIAHRLSTVE-HAHLI 710
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREFgiTLFSVSHRKSLWKyHEYLL 649
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
507-722 |
6.65e-14 |
|
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: 71.98 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRT----------------RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK 568
Cdd:cd03267 4 SNLSKSYRVyskepgligslkslfkRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 569 PISAYDHKYLHRVISLVSQE-------PVLFARSITDNIsYGLPTVPFemvveaaqKANAHGF--IMELQDGYSTETgek 639
Cdd:cd03267 84 VPWKRRKKFLRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-YDLPPARF--------KKRLDELseLLDLEELLDTPV--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 640 gAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESeyliQQAIHGNLQ------KHTVLIIAHRLSTVEH-AHLIVV 712
Cdd:cd03267 152 -RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA----QENIRNFLKeynrerGTTVLLTSHYMKDIEAlARRVLV 226
|
250
....*....|
gi 767973635 713 LDKGRVVQQG 722
Cdd:cd03267 227 IDKGRLLYDG 236
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
186-395 |
7.29e-14 |
|
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: 72.95 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 186 AFLVAASFFLIVAA--LGETFLPYYTGRAIDGIViQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIF---TLIFARlniR 260
Cdd:cd18605 1 LILILLSLILMQASrnLIDFWLSYWVSHSNNSFF-NFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFaygGLRAAR---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 261 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTG-VVVFMFSLSWQLSLVtfmgFPII 339
Cdd:cd18605 77 LHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGyLVVICYQLPWLLLLL----LPLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 340 MMVSNIYgKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEEEEAEVYLRKL 395
Cdd:cd18605 153 FIYYRIQ-RYYRATSRELKrlNSVNLSPlyTHFSETLKGLVTIRAFRKQERFLKEYLEKL 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
511-733 |
8.49e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 8.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 511 FTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHK---YLHRVISLVSQ 587
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRgllALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 588 EP--VLFARSITDNISYGLPT--VPFEMVV----EAAQKANAHGFIME-LQdgystetgekgaQLSGGQKQRVAMARALV 658
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRNlgVPEAEITrrvdEALTLVDAQHFRHQpIQ------------CLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 659 RNPPVLILDEATSALD----AESEYLIQQAIHgnlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGL 733
Cdd:PRK13638 153 LQARYLLLDEPTAGLDpagrTQMIAIIRRIVA---QGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
504-719 |
9.88e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 9.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLdGKPIS-AY---DHKYLH 579
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKiGYfdqHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 RvislvsqepvlfARSITDNISYGLPTvpfemvveaAQKANAHGFimeLQD-GYSTETGEKG-AQLSGGQKQRVAMARAL 657
Cdd:COG0488 392 P------------DKTVLDELRDGAPG---------GTEQEVRGY---LGRfLFSGDDAFKPvGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 658 VRNPPVLILDEATSALDAESEYLIQQAihgnLQKH--TVLIIAH-R--LSTVehAHLIVVLDKGRVV 719
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEA----LDDFpgTVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
504-727 |
1.05e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-- 581
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 -ISLVSQEPVLFAR-SITDNISY------GLPTVPFEMVVeaaqkanahgfIMELQdgystETGEKGA------QLSGGQ 647
Cdd:PRK11831 85 rMSMLFQSGALFTDmNVFDNVAYplrehtQLPAPLLHSTV-----------MMKLE-----AVGLRGAaklmpsELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 648 KQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKH---TVLIIAHR----LSTVEHAHliVVLDKgRVVQ 720
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLI-SELNSAlgvTCVVVSHDvpevLSIADHAY--IVADK-KIVA 224
|
....*..
gi 767973635 721 QGTHQQL 727
Cdd:PRK11831 225 HGSAQAL 231
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
184-448 |
1.08e-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: 72.55 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 184 DVAFlvaASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFST-AVVIVCLLAIGSSFAAgIRGGIFTLIFARLNIRLR 262
Cdd:cd18783 6 DVAI---ASLILHVLAL---APPIFFQIVIDKVLVHQSYSTLYVlTIGVVIALLFEGILGY-LRRYLLLVATTRIDARLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 263 NCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNinvFLRNTVKVTGVVVF---MFSLSWQLSLVTFMGFPII 339
Cdd:cd18783 79 LRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQ---LFGTLLDATSLLVFlpvLFFYSPTLALVVLAFSALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 340 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMyyvWGSGLT 419
Cdd:cd18783 155 ALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSN---WPQTLT 231
|
250 260 270
....*....|....*....|....*....|..
gi 767973635 420 LL---VVQVSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18783 232 GPlekLMTVGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
521-719 |
1.68e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.51 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVS----QEPV 590
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAG-----IAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 LFARSITDNISygLPTVP----FEMVVEAAQKANAHGFIMELQ---DGYSTETGekgaQLSGGQKQRVAMARALVRNPPV 663
Cdd:COG1129 342 VLDLSIRENIT--LASLDrlsrGGLLDRRRERALAEEYIKRLRiktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 664 LILDEATSALDAESEYLIQQAIHgNL--QKHTVLII----------AHRlstvehahlIVVLDKGRVV 719
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIR-ELaaEGKAVIVIsselpellglSDR---------ILVMREGRIV 473
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-699 |
1.71e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG-----GRVLLDGKPISAYDHKYLH--RVISLVSQEPVLF 592
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEvrREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 593 AR-SITDNISYGL-------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 664
Cdd:PRK14267 98 PHlTIYDNVAIGVklnglvkSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 767973635 665 ILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAH 699
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
508-730 |
2.22e-13 |
|
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: 71.43 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 508 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV-NILENFYPLEGgRVLLDGKpisaydhkylhrvISLVS 586
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELEPSEG-KIKHSGR-------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPVLFARSITDNISYGLP--TVPFEMVVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 664
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSydEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 665 ILDEATSALDAESEYLIQQAIHGNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 730
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFESCVCKLMANkTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
517-701 |
2.29e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR- 594
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 SITDNISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK10762 95 TIAENIFLGReFVNRFGRIDWKKMYAEADKLLARLNLRFSSDK--LVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180
....*....|....*....|....*....
gi 767973635 674 -DAESEYLIQQAIHGNLQKHTVLIIAHRL 701
Cdd:PRK10762 173 tDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
525-747 |
2.29e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 525 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRVIS-LVSQEPVLF--------ARS 595
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAGQPLEAWSAAELARHRAyLSQQQTPPFampvfqylTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 596 ITDNISYGLPTVPFEMVVEAAQkanahgfimeLQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NP--PVLILDE 668
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 669 ATSALDAESEYLIQQAIHGNLQKH-TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLAQGGL---YAKLVQRQML 743
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGiAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENLaqvFGVNFRRLDV 239
|
....
gi 767973635 744 GLQP 747
Cdd:PRK03695 240 EGHP 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
508-727 |
2.45e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 508 NVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRV---LLDGKPISAYDH------- 575
Cdd:PRK13651 7 NIVKIFnkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 576 --------------KYLHRVISLVSQ--EPVLFARSITDNISYGlptvPFEMVV---EAAQKANAHGFIMELQDGYStet 636
Cdd:PRK13651 87 lviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVskeEAKKRAAKYIELVGLDESYL--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 637 gEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALDAES--EYLiqqAIHGNLQKH--TVLIIAHRLSTV-EHAHLI 710
Cdd:PRK13651 160 -QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGvkEIL---EIFDNLNKQgkTIILVTHDLDNVlEWTKRT 235
|
250
....*....|....*...
gi 767973635 711 VVLDKGRVVQQG-THQQL 727
Cdd:PRK13651 236 IFFKDGKIIKDGdTYDIL 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
520-722 |
2.60e-13 |
|
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: 69.48 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPI---SAYDhkylhRV---ISLVSQEPVL 591
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDItdlPPEE-----RArlgIFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 592 FarsitdnisyglPTVPFEMvveaaqkanahgFIMELQDGystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATS 671
Cdd:cd03217 89 I------------PGVKNAD------------FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 672 ALDAESEYLIQQAIhGNL--QKHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQG 722
Cdd:cd03217 134 GLDIDALRLVAEVI-NKLreEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
505-730 |
3.95e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.09 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 505 DFENVTFTYRTrPH--TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGK---PISAYD- 574
Cdd:COG4170 5 DIRNLTIEIDT-PQgrVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIdllKLSPREr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 575 HKYLHRVISLVSQEPVLF---ARSITDNISYGLPTVPFE---MVVEAAQKANA-----------HGFIMelqDGYSTEtg 637
Cdd:COG4170 84 RKIIGREIAMIFQEPSSCldpSAKIGDQLIEAIPSWTFKgkwWQRFKWRKKRAiellhrvgikdHKDIM---NSYPHE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 638 ekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESeyliQQAIH------GNLQKHTVLIIAHRLSTVEH-AHLI 710
Cdd:COG4170 159 -----LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTT----QAQIFrllarlNQLQGTSILLISHDLESISQwADTI 229
|
250 260
....*....|....*....|
gi 767973635 711 VVLDKGRVVQQGTHQQLLAQ 730
Cdd:COG4170 230 TVLYCGQTVESGPTEQILKS 249
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
507-743 |
5.12e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.16 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE-GGRVLLDGKPISAYD-HKYLHRVISL 584
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 585 VSQE-------PVLfarSITDNISYG-LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 656
Cdd:TIGR02633 341 VPEDrkrhgivPIL---GVGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKM 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 657 LVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKHTVLIIahrLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGlyak 736
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEIYKLI-NQLAQEGVAII---VVSSELAEVLGLSDRVLVIGEGKLKGDFVNHA---- 489
|
....*..
gi 767973635 737 LVQRQML 743
Cdd:TIGR02633 490 LTQEQVL 496
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
521-674 |
6.17e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH----KYLHRVISLVSQE----PVLF 592
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaKLRAKHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 593 ARsitDNISygLPTVpfeMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:PRK10584 105 AL---ENVE--LPAL---LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
..
gi 767973635 673 LD 674
Cdd:PRK10584 177 LD 178
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
504-722 |
1.49e-12 |
|
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: 67.29 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYR-TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS----CVNILENFYPLEGgRVLLDGKPISAYDHKYl 578
Cdd:cd03233 4 LSWRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVEG-DIHYNGIPYKEFAEKY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 HRVISLVSQEPVLFarsitdnisyglPTVPFEMVVEAAQKANAHGFImelqdgystetgeKGaqLSGGQKQRVAMARALV 658
Cdd:cd03233 82 PGEIIYVSEEDVHF------------PTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 659 RNPPVLILDEATSALDAESEYLIQQAIH--GNLQKHTVLIIAHRLStVEHAHL---IVVLDKGRVVQQG 722
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRtmADVLKTTTFVSLYQAS-DEIYDLfdkVLVLYEGRQIYYG 202
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
185-473 |
1.84e-12 |
|
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: 68.68 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 185 VAFLVAASFFLIVAalgetflPYYTGRAIDGIVIQKSMDQFSTAVVIVC--LLAIGSSFAAGIRGGIFTLIFARLNIRLR 262
Cdd:cd18582 2 LLLLVLAKLLNVAV-------PFLLKYAVDALSAPASALLAVPLLLLLAygLARILSSLFNELRDALFARVSQRAVRRLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 263 NCLFRSLVSQETSFFDENRTGDL---ISRLTSDTTMVSDLVSQNInvfLRNTVKVTGVVVFMFSL-SWQLSLVTFMGFPI 338
Cdd:cd18582 75 LRVFRHLHSLSLRFHLSRKTGALsraIERGTRGIEFLLRFLLFNI---LPTILELLLVCGILWYLyGWSYALITLVTVAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 339 IMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGL 418
Cdd:cd18582 152 YVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQAL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 419 TLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 473
Cdd:cd18582 232 IISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
507-722 |
1.85e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTrPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLhrvISLVS 586
Cdd:PRK15056 10 NDVTVTWRN-GHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QE-------PVLfarsITDNISYG---------LPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQR 650
Cdd:PRK15056 85 QSeevdwsfPVL----VEDVVMMGryghmgwlrRAKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 651 VAMARALVRNPPVLILDEATSALDAESEYLIqQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 722
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARI-ISLLRELRDEgkTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
504-704 |
4.03e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LvsqePVLFARSITDNisyglPTVPFEMVVEAAQKANA-HGFIMELQdgystetgekgaQLSGGQKQRVAMARALVRNPP 662
Cdd:PRK09544 82 L----PLTVNRFLRLR-----PGTKKEDILPALKRVQAgHLIDAPMQ------------KLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767973635 663 VLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTV 704
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLID-QLRREldcAVLMVSHDLHLV 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
499-697 |
4.24e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 499 HLEGRVDFE--NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPleG---GRVLLDGKPIS-- 571
Cdd:PRK13549 253 HTIGEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKir 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 572 ----AYDHKylhrvISLVSQE-------PVLfarSITDNISYG-LPTVPFEMVV-EAAQKANAHGFIMELQdgYSTETGE 638
Cdd:PRK13549 331 npqqAIAQG-----IAMVPEDrkrdgivPVM---GVGKNITLAaLDRFTGGSRIdDAAELKTILESIQRLK--VKTASPE 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 639 -KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKHTVLII 697
Cdd:PRK13549 401 lAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI-NQLVQQGVAII 459
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
531-715 |
5.58e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 64.32 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 531 PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL-LDGKPISAYDHKYLHRVIslvsqepvlfarsitdnisyglptvpf 609
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 610 emvveaaqkanahgfimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNL 689
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180 190
....*....|....*....|....*....|...
gi 767973635 690 QKH-------TVLIIAHRLSTVEHAHLIVVLDK 715
Cdd:smart00382 108 LLLlkseknlTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
521-729 |
9.27e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--GRVLLDGKPISaydhKYLHRVISLVSQEPVLFAR-SIT 597
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 598 DNISY-GLPTVPFEMVVEAAQKAnAHGFIMEL--QDGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PLN03211 159 ETLVFcSLLRLPKSLTKQEKILV-AESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 674 DAESEYLIQQAIHGNLQK-HTVLIIAHRLST--VEHAHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKgKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
524-730 |
1.47e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.52 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGR--VLLDGKPISAYDHKYLHR-----VISLVSQEPVLFA-RS 595
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRgrakrYIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 596 ITDNI--SYGLpTVPFEM-VVEAAQKANAHGFimelQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLILDEATS 671
Cdd:TIGR03269 382 VLDNLteAIGL-ELPDELaRMKAVITLKMVGF----DEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 672 ALDAESEYLIQQAIHGNLQK--HTVLIIAHRLSTVehahlIVVLDK------GRVVQQGTHQQLLAQ 730
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFV-----LDVCDRaalmrdGKIVKIGDPEEIVEE 518
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
534-722 |
1.48e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 534 VTALVGPSGSGKSSCVNILENF-YPLEG-----GRVLLD-GKPISAYDHKylhRVISLVSQEPVLFAR-SITDNISYGLp 605
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLtRPQKGrivlnGRVLFDaEKGICLPPEK---RRIGYVFQDARLFPHyKVRGNLRYGM- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 606 tvpfemvveaAQKANAHgF--------IMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 677
Cdd:PRK11144 102 ----------AKSMVAQ-FdkivallgIEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767973635 678 E-----YLIQQAIHGNLqkhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 722
Cdd:PRK11144 164 KrellpYLERLAREINI---PILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
508-727 |
1.53e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 508 NVTFtYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK----------PISAYDHKY 577
Cdd:PRK10261 19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 578 LHRV----ISLVSQEPVL-----------FARSItdNISYGLPTvpfEMVVEAAQKANAHGFIMELQdgysTETGEKGAQ 642
Cdd:PRK10261 98 MRHVrgadMAMIFQEPMTslnpvftvgeqIAESI--RLHQGASR---EEAMVEAKRMLDQVRIPEAQ----TILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 643 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKHT---VLIIAHRLSTV-EHAHLIVVLDKGRV 718
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMsmgVIFITHDMGVVaEIADRVLVMYQGEA 247
|
....*....
gi 767973635 719 VQQGTHQQL 727
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
507-728 |
1.55e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKpisaydHKYLHRVISLVS 586
Cdd:PRK11701 10 RGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------DGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 587 QEPVLFARS----ITDNISYGLptvpfEMVVEA---------AQKANAHGFI----------MELQdgySTETGEKGAQL 643
Cdd:PRK11701 81 AERRRLLRTewgfVHQHPRDGL-----RMQVSAggnigerlmAVGARHYGDIratagdwlerVEID---AARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 644 SGGQKQRVAMARALVRNPPVLILDEATSALD----AESEYLIQQAIHgNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGRV 718
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVR-ELGL-AVVIVTHDLAVARLlAHRLLVMKQGRV 230
|
250
....*....|
gi 767973635 719 VQQGTHQQLL 728
Cdd:PRK11701 231 VESGLTDQVL 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
504-723 |
6.43e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPHTQVlQNVSFSLSPGKVTALVGPSGSGKS-SCVNILENF-YPlegGRVL-----LDGKPISAYDHK 576
Cdd:PRK11022 6 VDKLSVHFGDESAPFRAV-DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIdYP---GRVMaekleFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 577 YLHRVI----SLVSQEPVlfarsITDNISYglpTVPFEM-----VVEAAQKANAHGFIMEL--QDGYSTETGEKGA---Q 642
Cdd:PRK11022 82 ERRNLVgaevAMIFQDPM-----TSLNPCY---TVGFQImeaikVHQGGNKKTRRQRAIDLlnQVGIPDPASRLDVyphQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 643 LSGGQKQRVAMARALVRNPPVLILDEATSALDAEseylIQQAIHG---NLQKH---TVLIIAHRLSTV-EHAHLIVVLDK 715
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT----IQAQIIElllELQQKenmALVLITHDLALVaEAAHKIIVMYA 229
|
....*...
gi 767973635 716 GRVVQQGT 723
Cdd:PRK11022 230 GQVVETGK 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
504-723 |
1.02e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.79 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRT-------------------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL 564
Cdd:COG1134 5 IEVENVSKSYRLyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 565 LDGkpisaydhkylhRVISLVSqepvL---FARSIT--DNIS-----YGLPTVP----FEMVVEAAqkanahgfimELQD 630
Cdd:COG1134 85 VNG------------RVSALLE----LgagFHPELTgrENIYlngrlLGLSRKEidekFDEIVEFA----------ELGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 631 -------GYSTetgekgaqlsgGQKQRVAMARALVRNPPVLILDEATSALDAE----SEYLIQQaihgnLQKH--TVLII 697
Cdd:COG1134 139 fidqpvkTYSS-----------GMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE-----LRESgrTVIFV 202
|
250 260
....*....|....*....|....*..
gi 767973635 698 AHRLSTV-EHAHLIVVLDKGRVVQQGT 723
Cdd:COG1134 203 SHSMGAVrRLCDRAIWLEKGRLVMDGD 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
517-680 |
1.07e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY-LHRVISLVSQE-PVLFAR 594
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 SITDNISYG-LPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK10982 89 SVMDNMWLGrYPTKGM-FVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
....*...
gi 767973635 674 -DAESEYL 680
Cdd:PRK10982 166 tEKEVNHL 173
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
519-737 |
1.14e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvisLVSQEpvlFARSITD 598
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDE---WQRNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 599 NIS-----YGLPTVpfEMVVEAAqKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK10938 90 MLSpgeddTGRTTA--EIIQDEV-KDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 674 DAESEYLIQQAIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQgGLYAKL 737
Cdd:PRK10938 167 DVASRQQLAELLASlHQSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ-ALVAQL 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
516-738 |
1.36e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.18 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 516 RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVN----ILenfYPlEGGRVLLDGKPISAYDHKYLHRvISLV---- 585
Cdd:COG4586 30 REYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgIL---VP-TSGEVRVLGYVPFKRRKEFARR-IGVVfgqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 586 SQ----EPVL--FA--RSItdnisYGLPTVPF----EMVVEaaqkanahgfIMELQDGYSTETgekgAQLSGGQKQRVAM 653
Cdd:COG4586 105 SQlwwdLPAIdsFRllKAI-----YRIPDAEYkkrlDELVE----------LLDLGELLDTPV----RQLSLGQRMRCEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 654 ARALVRNPPVLILDEATSALDAESeyliQQAIHGNL----QKH--TVLIIAHRLSTVEhaHL---IVVLDKGRVVQQGTH 724
Cdd:COG4586 166 AAALLHRPKILFLDEPTIGLDVVS----KEAIREFLkeynRERgtTILLTSHDMDDIE--ALcdrVIVIDHGRIIYDGSL 239
|
250
....*....|....
gi 767973635 725 QQLLAQGGLYAKLV 738
Cdd:COG4586 240 EELKERFGPYKTIV 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
517-717 |
1.40e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.57 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFypleggrvllDGKPISAYDHKylhrvISLVSQEPVL- 591
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdKDF----------NGEARPQPGIK-----VGYLPQEPQLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 592 FARSITDNI-------------------SYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GE- 638
Cdd:TIGR03719 81 PTKTVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAAEQAELQE---IIDAADAWDLDSqleiamdalrcppWDa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 639 KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGnlQKHTVLIIAH-R--LSTVehAHLIVVLDK 715
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPGTVVAVTHdRyfLDNV--AGWILELDR 233
|
..
gi 767973635 716 GR 717
Cdd:TIGR03719 234 GR 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
504-722 |
1.86e-10 |
|
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: 61.39 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRT-------------------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL 564
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 565 LDGKPISaydhkylhrVISL-VSQEPVLFARsitDNIS-----YGLPTvpfemvVEAAQKANahgFIMELqdgysTETGE 638
Cdd:cd03220 81 VRGRVSS---------LLGLgGGFNPELTGR---ENIYlngrlLGLSR------KEIDEKID---EIIEF-----SELGD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 639 KGAQ----LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIA-HRLSTV-EHAHLIVV 712
Cdd:cd03220 135 FIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIkRLCDRALV 214
|
250
....*....|
gi 767973635 713 LDKGRVVQQG 722
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
522-716 |
2.29e-10 |
|
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: 60.03 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNilENFYplEGGRVLLDGKPiSAYDHKYLHRVISLvsqepvlfaRSITDNis 601
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLISFL-PKFSRNKLIFIDQL---------QFLIDV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 602 yGLptvpfemvveaaqkanahgfimelqdGYSTeTGEKGAQLSGGQKQRVAMARALVRNPP--VLILDEATSALDAESEY 679
Cdd:cd03238 75 -GL--------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 767973635 680 LIQQAIHGNL-QKHTVLIIAHRLSTVEHAHLIVVLDKG 716
Cdd:cd03238 127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
522-720 |
2.52e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlEG---GRVLLDGKP-----ISAYDHkylhRVISLVSQE----P 589
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEVcrfkdIRDSEA----LGIVIIHQElaliP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 590 VLfarSITDNISYGLPTVPF------EMVVEAAQKANAHGfimeLQDGYSTETGEKGAqlsgGQKQRVAMARALVRNPPV 663
Cdd:NF040905 92 YL---SIAENIFLGNERAKRgvidwnETNRRARELLAKVG----LDESPDTLVTDIGV----GKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973635 664 LILDEATSAL-DAESEYLIQQAIHgnLQKH--TVLIIAHRLSTVEH-AHLIVVLDKGRVVQ 720
Cdd:NF040905 161 LILDEPTAALnEEDSAALLDLLLE--LKAQgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
503-717 |
4.26e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 503 RVDFENVTFTYrtrphtqvlQNVSFSLSP-------GKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 575
Cdd:PRK10522 322 TLELRNVTFAY---------QDNGFSVGPinltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 576 KYLHRVISLVSQEPVLFARSITDNisyglptvPFEMVVEAAQKANAH---GFIMELQDGYSTETgekgaQLSGGQKQRVA 652
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFDQLLGPE--------GKPANPALVEKWLERlkmAHKLELEDGRISNL-----KLSKGQKKRLA 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK--HTVLIIAHRLSTVEHAHLIVVLDKGR 717
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
522-719 |
4.48e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfypleGGRVLLD-GKPISAYDhkylhRVISLVSQEPvlfARSITDN- 599
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQD-----LIVARLQQDP---PRNVEGTv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 600 --------------------ISYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GEKGAQLSGG 646
Cdd:PRK11147 84 ydfvaegieeqaeylkryhdISHLVETDPSEKNLNELAKLQE---QLDHHNLWQLENrinevlaqlgldpDAALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 647 QKQRVAMARALVRNPPVLILDEATSALDAES-EYLiqqaiHGNLQ--KHTVLIIAHRLSTVEH-AHLIVVLDKGRVV 719
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL-----EGFLKtfQGSIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
518-720 |
6.13e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLEGGRVLLDGKpisaydhkylhrvislVSQEpvlfaR 594
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTllrLLAGALKGTPVAGCVDVPDNQ----------------FGRE-----A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 SITDNIsygLPTVPFEMVVEAaqkANAHGfimeLQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:COG2401 101 SLIDAI---GRKGDFKDAVEL---LNAVG----LSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767973635 675 AESEYLIQQAIHGNLQKH--TVLIIAHRlSTVEHA---HLIVVLDKGRVVQ 720
Cdd:COG2401 169 RQTAKRVARNLQKLARRAgiTLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
504-729 |
6.25e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR-VI 582
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMReAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SLVSQEPVLFAR-SITDNISYGlptvpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMG------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 662 PVLILDEATSALdaeSEYLIQQaIHGNLQK-----HTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLA 729
Cdd:PRK11614 157 RLLLLDEPSLGL---APIIIQQ-IFDTIEQlreqgMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
188-449 |
1.24e-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: 60.25 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18779 7 ILLASLLLQLLGLA---LPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTfMGFPII----MMVS 343
Cdd:cd18779 84 HLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALL-DGTLVLGYLALLFAQSPLLGLVV-LGLAALqvalLLAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 344 NiygKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKL--QQVYKLNRKEAAAYMyyvwGSGLTLL 421
Cdd:cd18779 162 R---RRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFvdQLNASLRRGRLDALV----DALLATL 234
|
250 260 270
....*....|....*....|....*....|
gi 767973635 422 --VVQVSILYYGGHLVISGQMTSGNLIAFI 449
Cdd:cd18779 235 rlAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
524-685 |
1.62e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEP----VLFARSITD 598
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 599 NISY-GLPTVPFEMVV--EAAQKANAHGFImelqDGYSTETGEKGAQ---LSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:PRK10762 350 NMSLtALRYFSRAGGSlkHADEQQAVSDFI----RLFNIKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170
....*....|...
gi 767973635 673 LDAESEYLIQQAI 685
Cdd:PRK10762 426 VDVGAKKEIYQLI 438
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
516-746 |
1.66e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.57 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 516 RPHTQVLqNVSFSLSpgKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVSQEPVLFARS 595
Cdd:TIGR01257 943 RPAVDRL-NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 596 itdnisyglpTVPFEMVVEAAQKANAH---GFIME--LQD-GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 669
Cdd:TIGR01257 1019 ----------TVAEHILFYAQLKGRSWeeaQLEMEamLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 670 TSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVVQQGTHQQL--LAQGGLYAKLVqRQMLGLQ 746
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLknCFGTGFYLTLV-RKMKNIQ 1167
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
522-723 |
2.11e-09 |
|
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: 59.17 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNilENFYPLEGGRVLLDGKPISAYD----HKYLHRVIsLVSQEPV------- 590
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNHDriegLEHIDKVI-VIDQSPIgrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 -------------LF------AR--SITDNISYGLPTVP--FEMVVEAAQK-----ANAHGFIMELQD---GYSTeTGEK 639
Cdd:cd03271 88 patytgvfdeireLFcevckgKRynRETLEVRYKGKSIAdvLDMTVEEALEffeniPKIARKLQTLCDvglGYIK-LGQP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 640 GAQLSGGQKQRVAMARALVR---NPPVLILDEATSALDAESeylIQQAIHGnLQK-----HTVLIIAHRLSTVEHAHLIV 711
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHD---VKKLLEV-LQRlvdkgNTVVVIEHNLDVIKCADWII 242
|
250
....*....|....*...
gi 767973635 712 VL-----DK-GRVVQQGT 723
Cdd:cd03271 243 DLgpeggDGgGQVVASGT 260
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
519-723 |
3.29e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVL---- 591
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEipgv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 592 ----FARSI--TDNISYGLPTV-PFEMVVEAAQKANahgfIMELQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPPVL 664
Cdd:CHL00131 100 snadFLRLAynSKRKFQGLPELdPLEFLEIINEKLK----LVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 665 ILDEATSALDAESEYLIQQAIHgNL--QKHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQGT 723
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGIN-KLmtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
517-717 |
5.92e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFyplEGGRVLLDGKPISaydhkYLhrvislvSQEPVL- 591
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdKEF---EGEARPAPGIKVG-----YL-------PQEPQLd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 592 FARSITDNISYGLPTVpfemvVEAAQKANAHGFIMELQDGYSTETGEKGAQ----------------------------- 642
Cdd:PRK11819 83 PEKTVRENVEEGVAEV-----KAALDRFNEIYAAYAEPDADFDALAAEQGElqeiidaadawdldsqleiamdalrcppw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 643 ------LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQaiHgnLQKH--TVLIIAH-R--LSTVehAHLIV 711
Cdd:PRK11819 158 dakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ--F--LHDYpgTVVAVTHdRyfLDNV--AGWIL 231
|
....*.
gi 767973635 712 VLDKGR 717
Cdd:PRK11819 232 ELDRGR 237
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
464-728 |
2.37e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 464 SVYSGLMQGVGAAEKVF-----EFIDRQPTMVHdgslAPDHLEGRVDFE--NVTFTYRTRphtqvLQNVSFSLSPGKVTA 536
Cdd:PRK09700 223 SVCSGMVSDVSNDDIVRlmvgrELQNRFNAMKE----NVSNLAHETVFEvrNVTSRDRKK-----VRDISFSVCRGEILG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 537 LVGPSGSGKSSCVNILENFYPLEGGRVLLDGK---PISAYDHkyLHRVISLVSQ---EPVLFAR-SITDN--ISYGLPTV 607
Cdd:PRK09700 294 FAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDA--VKKGMAYITEsrrDNGFFPNfSIAQNmaISRSLKDG 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 608 PFEMVV------EAAQKANAHGFIMELQdgySTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD--AESE- 678
Cdd:PRK09700 372 GYKGAMglfhevDEQRTAENQRELLALK---CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAEi 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767973635 679 YLIQQAIHGnlQKHTVLIIAHRLStvehaHLIVVLDKGRVVQQGTHQQLL 728
Cdd:PRK09700 449 YKVMRQLAD--DGKVILMVSSELP-----EIITVCDRIAVFCEGRLTQIL 491
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
191-473 |
2.98e-08 |
|
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: 55.69 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFS--TAVVIVCLLAIGSSFAAGIRggifTLIFARLN----IRLRNC 264
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESavTLILLYALLRFSSKLLKELR----SLLYRRVQqnayRELSLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 265 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSqninVFLRNTVK-----VTGVVVFMFSLSWQLSLVTFMGFpII 339
Cdd:cd18560 77 TFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLS----YLVFYLVPtllelIVVSVVFAFHFGAWLALIVFLSV-LL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 340 MMVSNIYG-KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGL 418
Cdd:cd18560 152 YGVFTIKVtEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767973635 419 TLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 473
Cdd:cd18560 232 IIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
513-728 |
4.01e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 513 YRTRPHTQVL------------QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLH 579
Cdd:PRK11288 248 YRPRPLGEVRlrldglkgpglrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 580 RVISLV----SQEPVLFARSITDN--ISYGLPTVPFEMVVEAAQKA-NAHGFIMELQdgYSTETGE-KGAQLSGGQKQRV 651
Cdd:PRK11288 328 AGIMLCpedrKAEGIIPVHSVADNinISARRHHLRAGCLINNRWEAeNADRFIRSLN--IKTPSREqLIMNLSGGNQQKA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 652 AMARALVRNPPVLILDEATSALD--AESEylIQQAIHgNL--QKHTVLIIAHRLSTVEH-AHLIVVLDKGRVV-----QQ 721
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDvgAKHE--IYNVIY-ELaaQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgelarEQ 482
|
....*..
gi 767973635 722 GTHQQLL 728
Cdd:PRK11288 483 ATERQAL 489
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
524-718 |
4.63e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK-YLHRVISLVS---QEPVLFARS-ITD 598
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYLPedrQSSGLYLDApLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 599 NI-SYGLPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:PRK15439 361 NVcALTHNRRGF-WIKPARENAVLERYRRAL--NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767973635 677 SEYLIQQAIHGNLQKHT-VLIIAHRLSTVEH-AHLIVVLDKGRV 718
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
182-447 |
5.29e-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: 54.92 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 182 KPDVAFLVAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMdqfSTAVVIvCLLAIGSSFAAGI----RGGIFTLIFARL 257
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALA---PPIFMLQVYDRVLPSGSL---STLLGL-TLGMVVLLAFDGLlrqvRSRILQRVGLRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 258 NIRLRNCLFRSLVSQETsffdENRTGDLISRLTSDTTMVSDLVSQN--INVFLRNTVKVTGVVVFMFSlSWqLSLVTFMG 335
Cdd:cd18586 74 DVELGRRVFRAVLELPL----ESRPSGYWQQLLRDLDTLRNFLTGPslFAFFDLPWAPLFLAVIFLIH-PP-LGWVALVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 336 FPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKL-NRKEAAAYMYYVW 414
Cdd:cd18586 148 APVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELqIRASDLAGAISAI 227
|
250 260 270
....*....|....*....|....*....|...
gi 767973635 415 GSGLTlLVVQVSILYYGGHLVISGQMTSGNLIA 447
Cdd:cd18586 228 GKTLR-MALQSLILGVGAYLVIDGELTIGALIA 259
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
518-704 |
5.79e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILE---NFYPLEGGRVLLDGKPISAydhkYLHRVISLVSQEPVLFAR 594
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLDS----SFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 S-ITDNISYG----LP-TVPFE---MVVEAAQKanahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:TIGR00956 851 StVRESLRFSaylrQPkSVSKSekmEYVEEVIK------LLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLL 924
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767973635 666 -LDEATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRLSTV 704
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLMR-KLADHgqAILCTIHQPSAI 965
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
515-690 |
6.03e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 515 TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRVISLVSQEPVLFAR 594
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 -SITDNISY--GLPTVpfemvvEAAQKANAHGFIMELQDGYSTETgekgAQLSGGQKQRVAMARALVRNPPVLILDEATS 671
Cdd:PRK13543 97 lSTLENLHFlcGLHGR------RAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170
....*....|....*....
gi 767973635 672 ALDAESEYLIQQAIHGNLQ 690
Cdd:PRK13543 167 NLDLEGITLVNRMISAHLR 185
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
627-761 |
7.09e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 627 ELQDGYS-TET-GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLST 703
Cdd:NF000106 127 ELLERFSlTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEE 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973635 704 VEH-AHLIVVLDKGRVVQQGTHQQLLAQGG--------LYAKLVQRQM-----LGLQPAADFTAGHNEPVAN 761
Cdd:NF000106 207 AEQlAHELTVIDRGRVIADGKVDELKTKVGgrtlqirpAHAAELDRMVgaiaqAGLDGIAGATADHEDGVVN 278
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
508-730 |
8.07e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.73 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 508 NVTFTYRTRPHTQVlQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG---GRVLLDGKPISAYDHKYLHRV--- 581
Cdd:PRK09473 19 RVTFSTPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNKLrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 582 -ISLVSQEPVlfaRSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQRVAMAR 655
Cdd:PRK09473 98 qISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphefSGGMRQRVMIAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 656 ALVRNPPVLILDEATSALDAESEYLIQQAIhgNLQKH----TVLIIAHRLSTVehAHL---IVVLDKGRVVQQGTHQQLL 728
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLL--NELKRefntAIIMITHDLGVV--AGIcdkVLVMYAGRTMEYGNARDVF 250
|
..
gi 767973635 729 AQ 730
Cdd:PRK09473 251 YQ 252
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
504-722 |
8.95e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK-PISAYDHkylHRVI 582
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQ---HHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 SL-VSQEPVLFarsitdnISYGLPTVPfemvveaAQKANAH----GFI--MELQDGYStetgekgaqLSGGQKQRVAMAR 655
Cdd:PLN03073 584 GLdLSSNPLLY-------MMRCFPGVP-------EQKLRAHlgsfGVTgnLALQPMYT---------LSGGQKSRVAFAK 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 656 ALVRNPPVLILDEATSALDAES-EYLIQQAIhgnLQKHTVLIIAHrlstveHAHLIV-VLDKGRVVQQG 722
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAvEALIQGLV---LFQGGVLMVSH------DEHLISgSVDELWVVSEG 700
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
526-702 |
1.15e-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: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 526 SFSL------SPGKVTALVGPSGSGKSSCVNILENFYPLEGGRvlLDGKP-----ISAYD----HKYLHRVIS------- 583
Cdd:cd03236 14 SFKLhrlpvpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRgselQNYFTKLLEgdvkviv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 ---LVSQEPVLFARSITDNISYGLPTVPFEMVVEAaqkanahgfiMELQDGYSTETgekgAQLSGGQKQRVAMARALVRN 660
Cdd:cd03236 92 kpqYVDLIPKAVKGKVGELLKKKDERGKLDELVDQ----------LELRHVLDRNI----DQLSGGELQRVAIAAALARD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767973635 661 PPVLILDEATSALDAESEYLIQQAIHGnLQKHT--VLIIAHRLS 702
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRE-LAEDDnyVLVVEHDLA 200
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
528-699 |
1.41e-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: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 528 SLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKYLHRVISLVSQEpvlFARSITDnisyGLPTV 607
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGTVRD---LLSSITK----DFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 608 PFeMVVEAAQKanahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG 687
Cdd:cd03237 93 PY-FKTEIAKP-------LQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170
....*....|....
gi 767973635 688 NLQKH--TVLIIAH 699
Cdd:cd03237 161 FAENNekTAFVVEH 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
512-719 |
1.48e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.65 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 512 TYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEP- 589
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 590 ----VLfARSITDNI----SYGLPTVPFEMVVEAAQKANAHGFIMELQ---DGYSTETGekgaQLSGGQKQRVAMARALV 658
Cdd:COG3845 344 grglVP-DMSVAENLilgrYRRPPFSRGGFLDRKAIRAFAEELIEEFDvrtPGPDTPAR----SLSGGNQQKVILARELS 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 659 RNPPVLILDEATSALDAESeyliQQAIHGNLQKH-----TVLIIAHRLSTV-EHAHLIVVLDKGRVV 719
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGA----IEFIHQRLLELrdagaAVLLISEDLDEIlALSDRIAVMYEGRIV 481
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
225-381 |
1.69e-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: 53.76 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 225 FSTAVVIVCLLAIGSSFAAGIRGgiftlifARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 304
Cdd:cd18602 59 LSLGAVILSLVTNLAGELAGLRA-------AR---RLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 305 NVFLRNTVKV-TGVVVFMFSLSWQLslvtFMGFPIImMVSNIYGKYYKRLSKEVQ--NALARA---SNTAeETISAMKTV 378
Cdd:cd18602 129 ERLLRFLLLClSAIIVNAIVTPYFL----IALIPII-IVYYFLQKFYRASSRELQrlDNITKSpvfSHFS-ETLGGLTTI 202
|
...
gi 767973635 379 RSF 381
Cdd:cd18602 203 RAF 205
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
522-727 |
2.23e-07 |
|
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: 54.63 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVN-----ILENFypLEGGRVLLD-GKPISAYDHkyLHRVISlVSQEPV----- 590
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypALANR--LNGAKTVPGrYTSIEGLEH--LDKVIH-IDQSPIgrtpr 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 ---------------LFARS--------------------------------ITDNIsygLPT--VP------------- 608
Cdd:TIGR00630 699 snpatytgvfdeireLFAETpeakvrgytpgrfsfnvkggrceacqgdgvikIEMHF---LPDvyVPcevckgkrynret 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 609 -------------FEMVVEAAQK-----ANAHGFIMELQD---GYSTeTGEKGAQLSGGQKQRVAMARALVR---NPPVL 664
Cdd:TIGR00630 776 levkykgkniadvLDMTVEEAYEffeavPSISRKLQTLCDvglGYIR-LGQPATTLSGGEAQRIKLAKELSKrstGRTLY 854
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973635 665 ILDEATSALDAES----EYLIQQAIHgnlQKHTVLIIAHRLSTVEHAHLIVVL-----DK-GRVVQQGTHQQL 727
Cdd:TIGR00630 855 ILDEPTTGLHFDDikklLEVLQRLVD---KGNTVVVIEHNLDVIKTADYIIDLgpeggDGgGTVVASGTPEEV 924
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
495-699 |
2.44e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 495 LAPDhlEGRVDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlEG--------GRVLLD 566
Cdd:PRK10938 254 LPAN--EPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-QGysndltlfGRRRGS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 567 GKPIsaYDHKylhRVISLVSQEPVLFAR---SITDNI------SYGLptvpFEMVVEAAQKanahgFIMELQD--GYSTE 635
Cdd:PRK10938 328 GETI--WDIK---KHIGYVSSSLHLDYRvstSVRNVIlsgffdSIGI----YQAVSDRQQK-----LAQQWLDilGIDKR 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 636 TGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAI-----HGNLQkhtVLIIAH 699
Cdd:PRK10938 394 TADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdvlisEGETQ---LLFVSH 460
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
504-700 |
3.53e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYstetgekgaqLSGGQKQRVAMARALVRNPPV 663
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 767973635 664 LILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHR 700
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKgGAVLLTSHQ 186
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
522-697 |
4.52e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQE----------PV 590
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyaylDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 LFARSITDNISYglpTVPFEMVVEAAQKANAHGFI--MELQD-GYSTETGekgaQLSGGQKQRVAMARALVRNPPVLILD 667
Cdd:PRK10982 344 GFNSLISNIRNY---KNKVGLLDNSRMKSDTQWVIdsMRVKTpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190
....*....|....*....|....*....|
gi 767973635 668 EATSALDAESEYLIQQAIHGNLQKHTVLII 697
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
529-701 |
5.38e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 529 LSPGKVTALVGPSGSGKSSCVNILE-----NFyplegGRVllDGKP-----ISAYDHKYLHRVISLVSQEPVLFARSI-- 596
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgelipNL-----GDY--EEEPswdevLKRFRGTELQNYFKKLYNGEIKVVHKPqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 597 TDNIsyglPTVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK13409 169 VDLI----PKVFKGKVRELLKKVDERGKLDEVVErlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*..
gi 767973635 675 AESEYLIQQAIHGNLQKHTVLIIAHRL 701
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
528-705 |
1.09e-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: 49.28 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 528 SLSPGKVTALVGPSGSGKSscvNILenfypleggrvlldgkpisaydhkylhRVISLVsqepVLFARSITDNISYGLPTV 607
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKS---TIL---------------------------DAIGLA----LGGAQSATRRRSGVKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 608 PfemvvEAAQKANAHGFIMelqdgystetgekgaQLSGGQKQRVAMARAL----VRNPPVLILDEATSALDAESEYLIQQ 683
Cdd:cd03227 63 I-----VAAVSAELIFTRL---------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180
....*....|....*....|...
gi 767973635 684 AIHGNLQKH-TVLIIAHRLSTVE 705
Cdd:cd03227 123 AILEHLVKGaQVIVITHLPELAE 145
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
519-741 |
2.02e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL--ENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPV----- 590
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 591 ---LFARSITDNI-SY----GLPTVPFEMVVEAAQKanahgfIMELQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPP 662
Cdd:PRK09580 94 snqFFLQTALNAVrSYrgqePLDRFDFQDLMEEKIA------LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 663 VLILDEATSALDAESEYLIQQAIHgNLQ--KHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQGTH---QQLLAQGglYA 735
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVN-SLRdgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQG--YG 242
|
....*.
gi 767973635 736 KLVQRQ 741
Cdd:PRK09580 243 WLTEQQ 248
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
234-422 |
2.35e-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: 50.17 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 234 LLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 313
Cdd:cd18606 43 GLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 314 VTGVVVfmfslswqLSLVTF----MGFPIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEe 385
Cdd:cd18606 123 IIGTFI--------LIIIYLpwfaIALPPLLVLYYFIANYYRASSRELKrlESILRSFvyANFSESLSGLSTIRAYGAQ- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767973635 386 eeaEVYLRKLQqvYKLNRKEAAAYMYYV---W--------GSGLTLLV 422
Cdd:cd18606 194 ---DRFIKKNE--KLIDNMNRAYFLTIAnqrWlairldllGSLLVLIV 236
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
505-699 |
2.56e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 505 DFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNI-LENFYPlEGGRVLLDGKPISAY-DHkylHRVI 582
Cdd:PRK11147 321 EMENVNYQI---DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHCGTKLEVAYfDQ---HRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 slvsQEPvlfARSITDNISYGLPTVpfeMVveAAQKANAHGFimeLQD----GYSTETGEKGaqLSGGQKQRVAMARALV 658
Cdd:PRK11147 394 ----LDP---EKTVMDNLAEGKQEV---MV--NGRPRHVLGY---LQDflfhPKRAMTPVKA--LSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767973635 659 RNPPVLILDEATSALDAESEYLIQQAIHGnlQKHTVLIIAH 699
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDS--YQGTVLLVSH 495
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
526-674 |
2.88e-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: 50.55 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 526 SFSL------SPGKVTALVGPSGSGKSSCVNILE-----NFyplegGRVllDGKP-----ISAYD----HKYLHRVIS-- 583
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKILSgelkpNL-----GDY--DEEPswdevLKRFRgtelQDYFKKLANge 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 584 -LVSQEP--VlfarsitDNIsyglPTVPFEMVVEAAQKANAHGFIMELQDGYSTET--GEKGAQLSGGQKQRVAMARALV 658
Cdd:COG1245 160 iKVAHKPqyV-------DLI----PKVFKGTVRELLEKVDERGKLDELAEKLGLENilDRDISELSGGELQRVAIAAALL 228
|
170
....*....|....*.
gi 767973635 659 RNPPVLILDEATSALD 674
Cdd:COG1245 229 RDADFYFFDEPSSYLD 244
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
260-479 |
6.50e-06 |
|
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: 48.82 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 339
Cdd:cd18561 70 HLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 340 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAymyYVWGSGLT 419
Cdd:cd18561 150 PLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAV---SLLSSGIM 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 420 LLVVQVSI---LYYGGHLVISGQMTSGNLIAFIiyeFVLGDC---MESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18561 227 GLATALGTalaLGVGALRVLGGQLTLSSLLLIL---FLSREFfrpLRDLGAYWHAGYQGISAADSI 289
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
504-729 |
7.63e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGKPISAYDHKYL 578
Cdd:PRK15093 4 LDIRNLTIEFKTSDGwVKAVDRVSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 579 HRVI----SLVSQEP---VLFARSITDNISYGLP----------------TVPFEMVVEAAQKAnaHGFIMElqdGYSTE 635
Cdd:PRK15093 84 RKLVghnvSMIFQEPqscLDPSERVGRQLMQNIPgwtykgrwwqrfgwrkRRAIELLHRVGIKD--HKDAMR---SFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 636 tgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEH-AHLIVV 712
Cdd:PRK15093 159 -------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINV 231
|
250
....*....|....*..
gi 767973635 713 LDKGRVVQQGTHQQLLA 729
Cdd:PRK15093 232 LYCGQTVETAPSKELVT 248
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
511-722 |
1.37e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 511 FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFYPLEGGRVLLDGKPISAYDHKYLHRVI---- 582
Cdd:TIGR00956 66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVynae 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 ------SLVSQEPVLF-ARSITDNISYGLPTvpfeMVVEAAQKANAHGFIMELQDGYSTETGE---KGaqLSGGQKQRVA 652
Cdd:TIGR00956 146 tdvhfpHLTVGETLDFaARCKTPQNRPDGVS----REEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVS 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973635 653 MARALVRNPPVLILDEATSALDAESEYLIQQAIH--GNLQKHTVLIIAHRLS--TVEHAHLIVVLDKGRVVQQG 722
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKtsANILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
229-413 |
1.39e-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: 47.85 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 229 VVIVCLLAIGSSFAAGIRGGIFTL--------IFARLnirlrnclFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLV 300
Cdd:cd18604 46 LGIYALISLLSVLLGTLRYLLFFFgslrasrkLHERL--------LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 301 SQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMK 376
Cdd:cd18604 118 ADSLSSLLESTLSLLVILIAIVVVSPAFLLPAV----VLAALYVYIGRLYLRASRELKrlESVARSPilSHFGETLAGLV 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 767973635 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 |
1.72e-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: 47.47 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFStavvivcLLAIGSSFAAGIRGgIFTLIFARLNIRL 261
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGL---VIPVFSRIFIDDILVGGLPDWLR-------PLLLGMALTALLQG-LLTWLQQYYLLRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 262 RNCLfrSLVSQET----------SFFDENRTGDLISRLTSDTTmVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLV 331
Cdd:cd18569 70 ETKL--ALSSSSRffwhvlrlpvEFFSQRYAGDIASRVQSNDR-VANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 332 TFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEeaevYLRKL--QQVYKLNRKEAAAY 409
Cdd:cd18569 147 GIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESD----FFSRWagYQAKVLNAQQELGR 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767973635 410 MYYVWGSGLTLL--VVQVSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18569 223 TNQLLGALPTLLsaLTNAAILGLGGLLVMDGALTIGMLVAF 263
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
526-699 |
1.79e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 526 SFSLS-------PGKVTALVGPSGSGKSSCVNILE-NFYPLEGGrvlLDGKPISAYDHKYlhrvISLVSQEPV-LFARSI 596
Cdd:PRK13409 352 DFSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAgVLKPDEGE---VDPELKISYKPQY----IKPDYDGTVeDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 597 TDNISyglpTVPFEmvVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:PRK13409 425 TDDLG----SSYYK--SEIIKPLQ----LERLLDKNVKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*
gi 767973635 677 SEYLIQQAI--HGNLQKHTVLIIAH 699
Cdd:PRK13409 488 QRLAVAKAIrrIAEEREATALVVDH 512
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
318-450 |
3.92e-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: 46.28 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 318 VVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFAneeeeAE-VYLRKLQ 396
Cdd:cd18587 132 LAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALG-----AEgRMQRRWE 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 397 Q-VYKLNRKEAAAYMYYVWGSGLTLLVVQ---VSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18587 207 EaVAALARSSLKSRLLSSSATNFAQFVQQlvtVAIVIVGVYLISDGELTMGGLIACVI 264
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
517-681 |
7.93e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 517 PHTQVLQNVSFSLSPGKVTALVGPSGSG----------KSSCVNIlenfypleGGRVLLDGKPIS------AYDHKylhr 580
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGrtelamsvfgRSYGRNI--------SGTVFKDGKEVDvstvsdAIDAG---- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 581 vISLVSQepvlfarsitDNISYGL---PTVPFEMVVEAAQKANAHGFI---MELQ--DGY-------STETGEKGAQLSG 645
Cdd:NF040905 339 -LAYVTE----------DRKGYGLnliDDIKRNITLANLGKVSRRGVIdenEEIKvaEEYrkkmnikTPSVFQKVGNLSG 407
|
170 180 190
....*....|....*....|....*....|....*.
gi 767973635 646 GQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEI 443
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
643-716 |
9.13e-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: 9.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 643 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQ--KHTVLIIAHRLSTVEHAHLIVVLDKG 716
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
520-702 |
1.01e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENfyPLEGGRVLLDGKpISAYDHKylhrvislvsQEPvlFAR----- 594
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKK----------QET--FARisgyc 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 595 ----------SITDNISY-GLPTVPFEmvVEAAQKANAHGFIMEL------QDGYSTETGEKGaqLSGGQKQRVAMARAL 657
Cdd:PLN03140 959 eqndihspqvTVRESLIYsAFLRLPKE--VSKEEKMMFVDEVMELveldnlKDAIVGLPGVTG--LSTEQRKRLTIAVEL 1034
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767973635 658 VRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLS 702
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTgRTVVCTIHQPS 1080
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
531-732 |
1.06e-04 |
|
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: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 531 PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVSQ------------EPVLFARsitd 598
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfdaiddlltgreHLYLYAR---- 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 599 nisygLPTVPFEMVVEAAQKAnahgfIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 678
Cdd:TIGR01257 2039 -----LRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 679 YLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGG 732
Cdd:TIGR01257 2107 RMLWNTIVSIIREgRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
193-450 |
1.27e-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: 44.74 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 193 FFLIVAALGETFLPYYTGRAID-GIViQKSMDqFSTAVVIVCL-LAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18571 9 LGLLLGSLLQLIFPFLTQSIVDkGIN-NKDLN-FIYLILIAQLvLFLGSTSIEFIRSWILLHISSRINISIISDFLIKLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 271 SQETSFFDENRTGDLISR----------LTSDT--TMVSDLvsqNINVFlrntvkvtGVVVFMFSlsWQLSLVTFMGFPI 338
Cdd:cd18571 87 RLPISFFDTKMTGDILQRindhsriesfLTSSSlsILFSLL---NLIVF--------SIVLAYYN--LTIFLIFLIGSVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 339 IMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFAneeeeAEVYLR----KLQ-QVYKLNRKEAAAYMYYV 413
Cdd:cd18571 154 YILWILLFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNN-----SERQKRweweRIQaKLFKINIKSLKLDQYQQ 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 767973635 414 WGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIA--FII 450
Cdd:cd18571 229 IGALFINQLKNILITFLAAKLVIDGEITLGMMLAiqYII 267
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
504-676 |
1.27e-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: 45.31 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL-DGKPISAYDHkylhrvi 582
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQ------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 583 slvSQEPVLFARSITDNISYGLPTVpfeMV--VEAAQKANAHGFIMELQDgysteTGEKGAQLSGGQKQRVAMARALVRN 660
Cdd:TIGR03719 393 ---SRDALDPNKTVWEEISGGLDII---KLgkREIPSRAYVGRFNFKGSD-----QQKKVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....*.
gi 767973635 661 PPVLILDEATSALDAE 676
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVE 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
500-699 |
1.29e-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: 45.55 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 500 LEGRVDFENVTF-----TYRTRPHTQVLQNV-------------SFSLS-------PGKVTALVGPSGSGKSSCVNILEN 554
Cdd:COG1245 309 LDGYLPEENVRIrdepiEFEVHAPRREKEEEtlveypdltksygGFSLEveggeirEGEVLGIVGPNGIGKTTFAKILAG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 555 FYPLEGGRVLLDGKpISaYDHKYlhrvISLVSQEPV--LFARSITDNIsyglPTVPFEmvVEAAQKANahgfIMELQDGY 632
Cdd:COG1245 389 VLKPDEGEVDEDLK-IS-YKPQY----ISPDYDGTVeeFLRSANTDDF----GSSYYK--TEIIKPLG----LEKLLDKN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 633 STEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAI--HGNLQKHTVLIIAH 699
Cdd:COG1245 453 VKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIrrFAENRGKTAMVVDH 514
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
524-674 |
1.63e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV------ISL-----VSQEPVLF 592
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVgymsqaFSLygeltVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 593 ARSitdnisYGLP--TVPfEMVVEAAQKanahgFimELQDgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:NF033858 364 ARL------FHLPaaEIA-ARVAEMLER-----F--DLAD----VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 767973635 671 SALD 674
Cdd:NF033858 426 SGVD 429
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
508-699 |
1.96e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 508 NVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENfyPLE--GGRVLLD-----GKpIS----AYDHk 576
Cdd:PRK15064 6 NITMQFGAKP---LFENISVKFGGGNRYGLIGANGCGKSTFMKILGG--DLEpsAGNVSLDpnerlGK-LRqdqfAFEE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 577 ylHRVISLV--SQEPVLFARSITDNIsYGLPtvpfEMVVEAAQKAnahgfiMELQ------DGYSTET--GE--KGA--- 641
Cdd:PRK15064 79 --FTVLDTVimGHTELWEVKQERDRI-YALP----EMSEEDGMKV------ADLEvkfaemDGYTAEAraGEllLGVgip 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 642 ---------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhgNLQKHTVLIIAH 699
Cdd:PRK15064 146 eeqhyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL--NERNSTMIIISH 210
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
245-385 |
2.47e-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: 43.85 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 245 IRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSL 324
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973635 325 S-WqlslvTFMGFPIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEE 385
Cdd:cd18601 158 NpW-----VLIPVIPLVILFLFLRRYYLKTSREVKriEGTTRSPvfSHLSSTLQGLWTIRAYSAQE 218
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
643-713 |
2.84e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973635 643 LSGGQKQRVAMARAL---VRNPPVLILDEATSALDAESeylIQQAIHGNL----QKHTVLIIAHRLSTVEHAHLIVVL 713
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHD---IKALIYVLQslthQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
643-729 |
3.13e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 643 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI----QQAIHgnLQKHTVLI--IAHRLSTVEHAHLIVVLDKG 716
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIvkclQQIVH--LTEATVLMslLQPAPETFDLFDDIILLSEG 414
|
90
....*....|...
gi 767973635 717 RVVQQGTHQQLLA 729
Cdd:PLN03140 415 QIVYQGPRDHILE 427
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
187-473 |
4.30e-04 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 43.01 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 187 FLVAASFFLIVAALGETFLPYYTGRAIDGIV--IQKSMDQFST-AVVIVCLLAIG--SSFAAGIrggIFTLIFARLNIRL 261
Cdd:cd18556 3 LFFSILFISLLSSILISISPVILAKITDLLTssSSDSYNYIVVlAALYVITISATklLGFLSLY---LQSSLRVELIISI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 262 RNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 341
Cdd:cd18556 80 SSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFLLYAVLFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 342 VSNIY----------------GKYYKRLSKEVQNALARASNTAEETIsaMKTVRSFANEEEEAevylrklQQVY-KLNRK 404
Cdd:cd18556 160 INNTIftkkivslrndlmdagRKSYSLLTDSVKNIVAAKQNNAFDFL--FKRYEATLTNDRNS-------QKRYwKLTFK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973635 405 EAAAymyyvwgSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 473
Cdd:cd18556 231 MLIL-------NSLLNVILFGLSFFYSLYGVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
226-412 |
4.83e-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: 42.94 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 226 STAVVIVCLLAIgssfaagiRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNIN 305
Cdd:cd18599 66 GSILVILLLSLI--------RGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 306 VFLRNTVKVTGVVVF-MFSLSWQLslvtfMGFPIIMMVSNIYGKYYKRLSKEvqnaLARASNTAE--------ETISAMK 376
Cdd:cd18599 138 NFLQNVLLVVFSLIIiAIVFPWFL-----IALIPLAIIFVFLSKIFRRAIRE----LKRLENISRsplfshltATIQGLS 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 767973635 377 TVRSFANEEEeaevYLRKLQQVykLNRKEAAAYMYY 412
Cdd:cd18599 209 TIHAFNKEKE----FLSKFKKL--LDQNSSAFFLFN 238
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
642-674 |
2.30e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 2.30e-03
10 20 30
....*....|....*....|....*....|...
gi 767973635 642 QLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
642-711 |
2.87e-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: 2.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973635 642 QLSGGQKQRVAMarALV-----RNP-PVLILDEATSALDAESEYLIQQAIHgNLQKHT-VLIIAHRLSTVEHAHLIV 711
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 ... |
642-677 |
4.89e-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: 4.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767973635 642 QLSGGQKQ------RVAMARALVRNPPVLILDEATSALDAES 677
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
520-714 |
6.07e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKYLHRVISLVSQEPVLF 592
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIGHNLGLKLEMTVFENLKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 593 ARSITDNISyglpTVPfemvveaaqkANAHGFimELQDGYStetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:PRK13541 94 WSEIYNSAE----TLY----------AAIHYF--KLHDLLD----EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767973635 673 LDAESEYLIQQ--AIHGNlQKHTVLIIAHRLSTVEHAhLIVVLD 714
Cdd:PRK13541 154 LSKENRDLLNNliVMKAN-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 |
6.84e-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: 39.15 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 188 LVAASFFLIVAALGEtflPYYTGRAIDGIVIQKSmdqfstavvIVCLLAIGSSF-AAGIRGGIFTLIFA-RLNIRLRNCL 265
Cdd:cd18562 4 LALANVALAGVQFAE---PVLFGRVVDALSSGGD---------AFPLLALWAALgLFSILAGVLVALLAdRLAHRRRLAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 266 ----FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 341
Cdd:cd18562 72 masyFEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 342 VSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVyklnrkEAAAYMYYVWGSGLTLL 421
Cdd:cd18562 152 LNRLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRL------LAAQYPVLNWWALASVL 225
|
250 260 270
....*....|....*....|....*....|....
gi 767973635 422 ------VVQVSILYYGGHLVISGQMTSGNLIAFI 449
Cdd:cd18562 226 traastLTMVAIFALGAWLVQRGELTVGEIVSFV 259
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
192-451 |
9.09e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 38.66 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 192 SFFLIVAALGETFL-PYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSsfaagirGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18583 1 CFLCLLAERVLNVLvPRQLGIIVDSLSGGSGKSPWKEIGLYVLLRFLQS-------GGGLGLLRSWLWIPVEQYSYRALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 271 --------SQETSFFDENRTGDL---ISRLTSDTTMVSDLVSQNINVFLRNTVkvtGVVVFMFSLSWQLSLVTFMgFPII 339
Cdd:cd18583 74 taafnhvmNLSMDFHDSKKSGEVlkaIEQGSSINDLLEQILFQIVPMIIDLVI---AIVYLYYLFDPYMGLIVAV-VMVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973635 340 MMVSNIY-GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQqvyklnRKEAAAYMYYVWGSGL 418
Cdd:cd18583 150 YVWSTIKlTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVK------NYQKAERKYLFSLNLL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767973635 419 TLlvVQVSILYYG--------GHLVISGQMTSGNLIAFIIY 451
Cdd:cd18583 224 NA--VQSLILTLGllagcflaAYQVSQGQATVGDFVTLLTY 262
|
|
| |
