|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
44-734 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 758.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 44 FDSVLDLWAACLYRSCLLLGATIGVAKNSAlgpRRLRASWL-VITLVCLFVGIYAMAKLLLFSEVRRPI--RDPWFWALF 120
Cdd:TIGR00958 35 EKGLYVLWLEGTLRLGVLWLGALGILLNKA---GGLLAAVKpLVAALCLATPSLSSLRALAFWEALDPAvrVALGLWSWF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 121 VWTYISLAASFLLWGLLATVRPDAEALEPGNEGfhgeggapaeqaSGATLQKLLSYTKPDVAFLVAASFFLIVAALGETF 200
Cdd:TIGR00958 112 VWSYGAALPAAALWAVLSSAGASEKEAEQGQSE------------TADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 201 LPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGD 280
Cdd:TIGR00958 180 IPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 281 LISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARA 360
Cdd:TIGR00958 260 LTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 361 STTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQVSILYYGGHLVISGQMSSGN 440
Cdd:TIGR00958 340 NQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGN 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 441 LIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQN 520
Cdd:TIGR00958 420 LVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKG 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 521 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGL 600
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 601 PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQA 680
Cdd:TIGR00958 580 TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES 659
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 66932952 681 IhgNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 734
Cdd:TIGR00958 660 R--SRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
165-740 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 597.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 165 ASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGG 244
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 245 IFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQL 324
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 325 SLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAA 404
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 405 YMSYVWGSGLTLLVVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPT 484
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 485 MVH-DGSLAPDHLEGRVDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDG 563
Cdd:COG1132 324 IPDpPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 564 KPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQ 643
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 644 KQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQL 723
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*..
gi 66932952 724 LAQGGLYAKLVQRQMLG 740
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 ... |
187-475 |
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: 518.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLV 266
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 267 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 346
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 347 KRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQVSILYY 426
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 66932952 427 GGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
170-738 |
5.55e-151 |
|
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: 457.37 E-value: 5.55e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 170 LQKLLSYTKPDVAFLVAASFFLIVAALgetFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLV 249
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLAL---ATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 250 FARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTF 329
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 330 MGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYV 409
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 410 WGSGLTLLVVQVSILYYGGHLVISGQMSSGNLIAFIIYefvlgdcmesVGSVYSGLMQGVG----------AAEKVFEFI 479
Cdd:COG2274 383 TLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNIL----------SGRFLAPVAQLIGllqrfqdakiALERLDDIL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 480 DRQPTMVHDGS-LAPDHLEGRVDFENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGR 558
Cdd:COG2274 453 DLPPEREEGRSkLSLPRLKGDIELENVSFRYPGDS-PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 559 VLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQ 638
Cdd:COG2274 532 ILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSN 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 639 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQG 718
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDG 691
|
570 580
....*....|....*....|
gi 66932952 719 THQQLLAQGGLYAKLVQRQM 738
Cdd:COG2274 692 THEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
170-737 |
1.77e-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: 451.46 E-value: 1.77e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 170 LQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLV 249
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 250 FARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTF 329
Cdd:TIGR02204 86 GERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 330 MGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYV 409
Cdd:TIGR02204 166 LAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 410 WGSGLTLLVVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTM---V 486
Cdd:TIGR02204 246 AIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIkapA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 487 HDGSLaPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPI 566
Cdd:TIGR02204 326 HPKTL-PVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 567 GAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQR 646
Cdd:TIGR02204 405 RQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 647 VAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:TIGR02204 485 IAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
570
....*....|.
gi 66932952 727 GGLYAKLVQRQ 737
Cdd:TIGR02204 565 GGLYARLARLQ 575
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
489-714 |
3.20e-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: 432.28 E-value: 3.20e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 489 GSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGA 568
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 569 YDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVA 648
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 649 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRV 714
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
169-733 |
1.43e-137 |
|
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: 417.97 E-value: 1.43e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 169 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTL 248
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 249 VFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVT 328
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 329 FMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSY 408
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 409 vwgSGLTLLVVQVS---ILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDrQPTM 485
Cdd:TIGR02203 241 ---SPITQLIASLAlavVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD-SPPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 486 VHDGSLAPDHLEGRVDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKP 565
Cdd:TIGR02203 317 KDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 566 IGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQK 644
Cdd:TIGR02203 396 LADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 645 QRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLL 724
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
....*....
gi 66932952 725 AQGGLYAKL 733
Cdd:TIGR02203 556 ARNGLYAQL 564
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
187-475 |
6.04e-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: 384.97 E-value: 6.04e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLV 266
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 267 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 346
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 347 KRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQVSILYY 426
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 66932952 427 GGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
500-737 |
4.00e-118 |
|
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: 355.31 E-value: 4.00e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 659
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 660 LILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 737
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
169-737 |
5.84e-114 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 357.02 E-value: 5.84e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 169 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYT--------GRAIDSIVIqksmdqfTTAVVVVCLLAIgsslaAG 240
Cdd:PRK11176 12 TFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLkpllddgfGKADRSVLK-------WMPLVVIGLMIL-----RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 241 IRGGIFTL----VFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVF 316
Cdd:PRK11176 80 ITSFISSYciswVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 317 MFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFlrklQQVYK 396
Cdd:PRK11176 160 MFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRF----DKVSN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 397 LNRKEAaayMSYVWGSGLTLLVVQ-------VSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 469
Cdd:PRK11176 236 RMRQQG---MKMVSASSISDPIIQliaslalAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 470 GAAEKVFEFIDRQPTmVHDGSLAPDHLEGRVDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILE 549
Cdd:PRK11176 313 AACQTLFAILDLEQE-KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 550 NFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGY 628
Cdd:PRK11176 391 RFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 629 STETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH-TVLIIAHRLSTVERAHLIV 707
Cdd:PRK11176 471 DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALD-ELQKNrTSLVIAHRLSTIEKADEIL 549
|
570 580 590
....*....|....*....|....*....|
gi 66932952 708 VLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 737
Cdd:PRK11176 550 VVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
168-737 |
1.10e-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: 349.12 E-value: 1.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 168 ATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLA-----IGSSLAAGIR 242
Cdd:COG5265 19 LLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAygllrLLSVLFGELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 243 GGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDL---ISRLTSDttmVSDLVSQNI-NIF--LRNTVKVTGVVVF 316
Cdd:COG5265 99 DALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIERGTKG---IEFLLRFLLfNILptLLEIALVAGILLV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 317 MFSlsWQLSLVTF------MGFPIImmVSNIYGKYYKRLSKEVQSALARAsttaeetISAM---KTVRSFANEEEEAEVF 387
Cdd:COG5265 176 KYD--WWFALITLvtvvlyIAFTVV--VTEWRTKFRREMNEADSEANTRA-------VDSLlnyETVKYFGNEAREARRY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 388 LRKLQqvyklnRKEAAAYMSYvwgSGLTLL-VVQ--------VSILYYGGHLVISGQMSSGNLI---AFIIYEFV-LGdc 454
Cdd:COG5265 245 DEALA------RYERAAVKSQ---TSLALLnFGQaliialglTAMMLMAAQGVVAGTMTVGDFVlvnAYLIQLYIpLN-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 455 meSVGSVYSGLMQGVGAAEKVFEFIDRQPTmVHDgslAPD--HL---EGRVDFENVTFTYRtrPHTQVLQNVSFSLSPGK 529
Cdd:COG5265 314 --FLGFVYREIRQALADMERMFDLLDQPPE-VAD---APDapPLvvgGGEVRFENVSFGYD--PERPILKGVSFEVPAGK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 530 VTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVV 609
Cdd:COG5265 386 TVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 610 EAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHT 689
Cdd:COG5265 466 AAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRT 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 66932952 690 VLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 737
Cdd:COG5265 546 TLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
500-733 |
4.88e-101 |
|
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: 310.70 E-value: 4.88e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 659
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 660 LILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 733
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
171-728 |
8.18e-99 |
|
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: 316.70 E-value: 8.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 171 QKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDSIVI-QKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLV 249
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIgGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 250 FARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTsdtTMVSDL-------VSQninIFLRNTVKVTgVVVFMFSLSW 322
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLT---EGVEALdgyfaryLPQ---LFLAALVPLL-ILVAVFPLDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 323 QLSLVTFMGFPII---MMvsnIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFlrklqqvyklnR 399
Cdd:COG4988 159 LSGLILLVTAPLIplfMI---LVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERI-----------A 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 400 KEAAAY---------MSYVwgSGLTL-LVVQVSI---LYYGGHLVISGQMS--SGNLIAFIIYEFVLGdcMESVGSVYSG 464
Cdd:COG4988 225 EASEDFrkrtmkvlrVAFL--SSAVLeFFASLSIalvAVYIGFRLLGGSLTlfAALFVLLLAPEFFLP--LRDLGSFYHA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 465 LMQGVGAAEKVFEFIDRQPTMVHDGSL-APDHLEGRVDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSS 543
Cdd:COG4988 301 RANGIAAAEKIFALLDAPEPAAPAGTApLPAAGPPSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKST 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 544 CVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIME 623
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 624 LQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERA 703
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
570 580
....*....|....*....|....*
gi 66932952 704 HLIVVLDKGRVVQQGTHQQLLAQGG 728
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
169-742 |
2.61e-96 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 310.88 E-value: 2.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 169 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMdqfttAVVVVCLLAIG----SSLAAGIRGg 244
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNL-----PLGLVAGLAAAyvglQLLAAGLHY- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 245 IFTLVFARLNI----RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSL 320
Cdd:PRK10790 84 AQSLLFNRAAVgvvqQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 321 SWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEeaevFLRKLQQVyklNRK 400
Cdd:PRK10790 164 DWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQAR----FGERMGEA---SRS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 401 EAAAYMSYVWGSGLTL--LVVQVSILYYGGHLVISGQMSSGN-----LIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAE 473
Cdd:PRK10790 237 HYMARMQTLRLDGFLLrpLLSLFSALILCGLLMLFGFSASGTievgvLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 474 KVFEFID--RQPTMVHDGSLApdhlEGRVDFENVTFTYRT-RPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN 550
Cdd:PRK10790 317 RVFELMDgpRQQYGNDDRPLQ----SGRIDIDNVSFAYRDdNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 551 FYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPtVPFEMVVEAAQKANAHGFIMELQDGYST 630
Cdd:PRK10790 390 YYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 631 ETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLD 710
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLH 548
|
570 580 590
....*....|....*....|....*....|..
gi 66932952 711 KGRVVQQGTHQQLLAQGGLYAKLVQRQMLGLE 742
Cdd:PRK10790 549 RGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
500-737 |
3.16e-95 |
|
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: 295.68 E-value: 3.16e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 659
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 660 LILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 737
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
187-475 |
6.87e-95 |
|
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: 296.94 E-value: 6.87e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLV 266
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 267 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 346
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 347 KRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQVSILYY 426
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 66932952 427 GGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18590 241 GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
498-728 |
3.37e-94 |
|
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: 292.98 E-value: 3.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 498 GRVDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV 577
Cdd:cd03254 1 GEIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 657
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 658 PVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGG 728
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
187-475 |
6.85e-94 |
|
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: 294.47 E-value: 6.85e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLV 266
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 267 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 346
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 347 KRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQVSILYY 426
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 66932952 427 GGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
256-736 |
2.23e-92 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 299.76 E-value: 2.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 256 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLvsqniniFLR-------NTVKVTGVVVFMFSLSWQLSLVT 328
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL-------YLRvllpllvALLVILAAVAFLAFFSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 329 FMGF-------PIIMMVSNiygkyyKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKE 401
Cdd:COG4987 162 ALGLllaglllPLLAARLG------RRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 402 AAAYMsyvWGSGLTLLVVQ---VSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEF 478
Cdd:COG4987 236 ARLSA---LAQALLQLAAGlavVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 479 IDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGR 558
Cdd:COG4987 313 LDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 559 VLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQ 638
Cdd:COG4987 392 ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 639 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQG 718
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
490
....*....|....*...
gi 66932952 719 THQQLLAQGGLYAKLVQR 736
Cdd:COG4987 552 THEELLAQNGRYRQLYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
500-737 |
1.98e-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: 283.22 E-value: 1.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:cd03252 1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 659
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 660 LILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 737
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
189-475 |
6.71e-88 |
|
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: 278.59 E-value: 6.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 189 FFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLVSQ 268
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 269 ETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKR 348
Cdd:cd18589 83 EIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 349 LSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQVSILYYGG 428
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 66932952 429 HLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18589 243 QLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
174-744 |
8.96e-88 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 288.40 E-value: 8.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 174 LSYTKPD---VAFLVAASFFLIVAALGEtflPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSS---------LAAGI 241
Cdd:PRK13657 11 LQYLGAEkrlGILLAVANVLLAAATFAE---PILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAGvlvarhadrLAHRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 242 RGGIFTLVFARLnirlrnclfrslVSQETSFFDENRTGDLISRLTSDTTMVSDLVsqnINIFLRNTVKVTGVVVFM---F 318
Cdd:PRK13657 88 RLAVLTEYFERI------------IQLPLAWHSQRGSGRALHTLLRGTDALFGLW---LEFMREHLATLVALVVLLplaL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 319 SLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQSAL--------ARASttaeETISAMKTVRSFANEEEEAEVfLRK 390
Cdd:PRK13657 153 FMNWRLSLVLV----VLGIVYTLITTLVMRKTKDGQAAVeehyhdlfAHVS----DAIGNVSVVQSYNRIEAETQA-LRD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 391 LqqvykLNRKEAAAYMSYVW---GSGLTLL---VVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSG 464
Cdd:PRK13657 224 I-----ADNLLAAQMPVLSWwalASVLNRAastITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 465 LMQgvgAAEKVFEFIDRQPTM--VHDGSLAPD--HLEGRVDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSG 540
Cdd:PRK13657 299 VFM---AAPKLEEFFEVEDAVpdVRDPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 541 KSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGF 620
Cdd:PRK13657 374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDF 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 621 IMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTV 700
Cdd:PRK13657 454 IERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTV 533
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 66932952 701 ERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLGLEHP 744
Cdd:PRK13657 534 RNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQEDE 577
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
146-735 |
5.79e-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: 284.14 E-value: 5.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 146 ALEPGnEGFHGEGGAPAEQASgatLQKLLSYTKPDVAFLVAASFFLIVAALgetFLPYYTGRAIDSIVIQKSMDQFTTav 225
Cdd:TIGR03796 125 TFEPG-PEFQKGGRKPSLLRA---LWRRLRGSRGALLYLLLAGLLLVLPGL---VIPAFSQIFVDEILVQGRQDWLRP-- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 226 vvvclLAIGSSLAAGIRGGiFTLVFARLNIRLRNCLFRSLVSQ--------ETSFFDENRTGDLISRLTSDTTmVSDLVS 297
Cdd:TIGR03796 196 -----LLLGMGLTALLQGV-LTWLQLYYLRRLEIKLAVGMSARflwhilrlPVRFFAQRHAGDIASRVQLNDQ-VAEFLS 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 298 QNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSF 377
Cdd:TIGR03796 269 GQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKAS 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 378 ANEEEeaevFLRKL--QQVYKLNRKE----AAAYMSYVwGSGLTLLVVqVSILYYGGHLVISGQMSSGNLIAFiiyEFVL 451
Cdd:TIGR03796 349 GLESD----FFSRWagYQAKLLNAQQelgvLTQILGVL-PTLLTSLNS-ALILVVGGLRVMEGQLTIGMLVAF---QSLM 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 452 GDCMESVGSV--YSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPD--------HLEGRVDFENVTFTY-RTRPHtqVLQN 520
Cdd:TIGR03796 420 SSFLEPVNNLvgFGGTLQELEGDLNRLDDVLRNPVDPLLEEPEGSaatsepprRLSGYVELRNITFGYsPLEPP--LIEN 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 521 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGL 600
Cdd:TIGR03796 498 FSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWD 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 601 PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQa 680
Cdd:TIGR03796 578 PTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDD- 656
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 681 ihgNLQRH--TVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQ 735
Cdd:TIGR03796 657 ---NLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
187-475 |
7.59e-79 |
|
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: 254.87 E-value: 7.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIVIQ------KSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNC 260
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHsgsggeEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 261 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 340
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 341 IYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYvwgSGLTLLVVQ 420
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGF---NGFMGAAAQ 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 421 VSI---LYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18780 238 LAIvlvLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
500-713 |
3.54e-77 |
|
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: 245.76 E-value: 3.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPV 659
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 66932952 660 LILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGR 713
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
187-475 |
1.19e-76 |
|
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: 248.97 E-value: 1.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIV------IQKSMDQFTTAVVVVCLLAIGSsLAAGIRGGIFTLVFARLNIRLRNC 260
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASkesgdiEIFGLSLKTFALALLGVFVVGA-AANFGRVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 261 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 340
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 341 IYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQ 420
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 421 VSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18573 240 LSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
189-746 |
3.95e-74 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 251.17 E-value: 3.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 189 FFLIVAALGETFLPYYTGRAIDSIviqkSMDQFTTAVVVVCL--LAIGSSLAAGIRGGIFTLVFA---RLNIRLRNCLFR 263
Cdd:PRK10789 2 ALLIIIAMLQLIPPKVVGIIVDGV----TEQHMTTGQILMWIgtMVLIAVVVYLLRYVWRVLLFGasyQLAVELREDFYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFS-LSWQLSLVTFMGFPIIMMVSNIY 342
Cdd:PRK10789 78 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 343 GKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeaAAYMSYVWGSGLTLLVVQVS 422
Cdd:PRK10789 158 GDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMR--VARIDARFDPTIYIAIGMAN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 423 ILYYGG--HLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPtMVHDGSLAPDHLEGRV 500
Cdd:PRK10789 236 LLAIGGgsWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAP-VVKDGSEPVPEGRGEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 501 DFENVTFTYrtrPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVI 578
Cdd:PRK10789 315 DVNIRQFTY---PQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPP 658
Cdd:PRK10789 392 AVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 659 VLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQM 738
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQ 551
|
....*...
gi 66932952 739 lgLEHPLD 746
Cdd:PRK10789 552 --LEAALD 557
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
177-709 |
1.78e-72 |
|
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: 245.66 E-value: 1.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 177 TKPDVAFLVAASFFLIVAALGETFLpyyTGRAIDSIVIQKS-MDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNI 255
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWL---LARVVDGLISAGEpLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 256 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI-NIFLRNTVKVTgVVVFMFSLSWQ---LSLVTFMG 331
Cdd:TIGR02857 78 QLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLpQLVLAVIVPLA-ILAAVFPQDWIsglILLLTAPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 332 FPIIMMVSniyGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVfLRKLQQVYklnRKEAAAYMSYVWG 411
Cdd:TIGR02857 157 IPIFMILI---GWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA-IRRSSEEY---RERTMRVLRIAFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 412 SGLTL-----LVVQVSILYYGGHLViSGQM--SSGNLIAFIIYEFVLGdcMESVGSVYSGLMQGVGAAEKVFEFIDRQPT 484
Cdd:TIGR02857 230 SSAVLelfatLSVALVAVYIGFRLL-AGDLdlATGLFVLLLAPEFYLP--LRQLGAQYHARADGVAAAEALFAVLDAAPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 485 MVHDGSLAPDHLEGRVDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGK 564
Cdd:TIGR02857 307 PLAGKAPVTAAPASSLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 565 PIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQK 644
Cdd:TIGR02857 385 PLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQA 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 645 QRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVL 709
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
185-734 |
7.05e-70 |
|
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: 243.11 E-value: 7.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 185 VAASFFLIVAALGEtflpYYTGRAIDSIVIQKSMDqfTTAVVVVCLLA--IGSSLAAGIRGGIFTLVFARLNIRLRNCLF 262
Cdd:TIGR01193 163 IAAIIVTLISIAGS----YYLQKIIDTYIPHKMMG--TLGIISIGLIIayIIQQILSYIQIFLLNVLGQRLSIDIILSYI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 263 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTgVVVFMFSLSWQLSLVTFMGFPIIMMVSNIY 342
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVI-VGLFLVRQNMLLFLLSLLSIPVYAVIIILF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 343 GKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEE-------EAEVFLRKlQQVYKLNRKEAAAYMSyvwgsgLT 415
Cdd:TIGR01193 316 KRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAEryskidsEFGDYLNK-SFKYQKADQGQQAIKA------VT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 416 LLVVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFE--FIDRQPTMVHDGSlAP 493
Cdd:TIGR01193 389 KLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEFINKKKRT-EL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 494 DHLEGRVDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKY 573
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 574 LHRVISLVSQEPVLFARSITDNISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 652
Cdd:TIGR01193 546 LRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 653 LVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAK 732
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
..
gi 66932952 733 LV 734
Cdd:TIGR01193 705 LI 706
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
180-738 |
9.24e-67 |
|
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: 234.08 E-value: 9.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 180 DVAFLVAASffLIVAALGeTFLPYYTGRAIDSIVIQKSMDQfttaVVVVCLLAIGSSLAAGIrggiFTLVFARLNIRLRN 259
Cdd:TIGR03797 137 DLLAILAMG--LLGTLLG-MLVPIATGILIGTAIPDADRSL----LVQIALALLAAAVGAAA----FQLAQSLAVLRLET 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 260 --------CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVfMFSLSWQLSLVTFMG 331
Cdd:TIGR03797 206 rmdaslqaAVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGL-MFYYSWKLALVAVAL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 332 FPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETIS-------AMKTVRSFAneeEEAEVFLRKLQQVYKLNRkeaaa 404
Cdd:TIGR03797 285 ALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINgisklrvAGAENRAFA---RWAKLFSRQRKLELSAQR----- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 405 ymsyvWGSGLT-----LLVVQVSILYY-GGHLVISGQMSSGNLIAFiiyefvlgdcMESVGSVYSGLMQGVGAAEKVFEF 478
Cdd:TIGR03797 357 -----IENLLTvfnavLPVLTSAALFAaAISLLGGAGLSLGSFLAF----------NTAFGSFSGAVTQLSNTLISILAV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 479 I---DR-QPTM-----VHDGSLAPDHLEGRVDFENVTFTYRtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILE 549
Cdd:TIGR03797 422 IplwERaKPILealpeVDEAKTDPGKLSGAIEVDRVTFRYR-PDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLL 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 550 NFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPfEMVVEAAQKANAHGFIMELQDGYS 629
Cdd:TIGR03797 501 GFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTL-DEAWEAARMAGLAEDIRAMPMGMH 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 630 TETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGnlQRHTVLIIAHRLSTVERAHLIVVL 709
Cdd:TIGR03797 580 TVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVL 657
|
570 580
....*....|....*....|....*....
gi 66932952 710 DKGRVVQQGTHQQLLAQGGLYAKLVQRQM 738
Cdd:TIGR03797 658 DAGRVVQQGTYDELMAREGLFAQLARRQL 686
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
187-475 |
1.92e-65 |
|
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: 219.28 E-value: 1.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTT-AVVVVCLLAIgSSLAAGIRGGIFTLVFARLNIRLRNCLFRSL 265
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQiALLLLGLFLL-QAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 266 VSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKY 345
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 346 YKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEA---AAYMSYVwgsGLTLLVVQVS 422
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRArirALFSSFI---IFLLFGAIVA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 66932952 423 ILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18576 237 VLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
417-726 |
2.15e-63 |
|
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: 221.93 E-value: 2.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 417 LVVQVSILYYGGHLVISGQMSSGNLIAFIIyefVLGDCM---ESVGSVYSGLMQGVGAAEKVFEFIDRQPTmvHDGSLAP 493
Cdd:COG4618 250 LLLQSAVLGLGAYLVIQGEITPGAMIAASI---LMGRALapiEQAIGGWKQFVSARQAYRRLNELLAAVPA--EPERMPL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 494 DHLEGRVDFENVTFTY--RTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDH 571
Cdd:COG4618 325 PRPKGRLSVENLTVVPpgSKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 572 KYLHRVISLVSQEPVLFARSITDNISyGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 651
Cdd:COG4618 402 EELGRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQR-HTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
498-718 |
2.09e-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: 205.90 E-value: 2.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 498 GRVDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV 577
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 657
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 658 PVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQG 718
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
184-475 |
2.26e-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: 208.17 E-value: 2.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFR 263
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 343
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 344 KYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeAAAYMSYVWG-SGLTLLVVQVS 422
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR-AARLSALFSPlIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 66932952 423 ILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
467-737 |
4.96e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 213.17 E-value: 4.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 467 QGVGAAEKVFEFIDRQPTMVHDGSlAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 546
Cdd:PRK11174 316 QAVGAAESLVTFLETPLAHPQQGE-KELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 547 ILENFYPLQGgRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQD 626
Cdd:PRK11174 395 ALLGFLPYQG-SLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 627 GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLI 706
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI 553
|
250 260 270
....*....|....*....|....*....|.
gi 66932952 707 VVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 737
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
184-475 |
6.27e-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: 201.50 E-value: 6.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDqfttAVVVVCLLAIGSSLAAGI--RGGIFTLVFARLNI--RLRN 259
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLE----ALLLVPLAIIGLFLLRGLasYLQTYLMAYVGQRVvrDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 260 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 339
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 340 NIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAymsyvwgSGLTLLVV 419
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARA-------RALSSPLM 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 420 QV-------SILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18552 230 ELlgaiaiaLVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
498-719 |
6.63e-59 |
|
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: 198.87 E-value: 6.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 498 GRVDFENVTFTYRtrPHTQ-VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHR 576
Cdd:cd03244 1 GDIEFKNVSLRYR--PNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VISLVSQEPVLFARSITDNISyglptvPF-----EMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 651
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PFgeysdEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGT 719
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
412-737 |
1.83e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 205.83 E-value: 1.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 412 SGLTLLVvqvsILYYGGHLViSGQMSSGNLIAFIIyeFVLGDCMES---VGSVYSGLMQGVGAAEKVFEFIDRQPTMVHD 488
Cdd:PRK11160 255 NGLTVVL----MLWLAAGGV-GGNAQPGALIALFV--FAALAAFEAlmpVAGAFQHLGQVIASARRINEITEQKPEVTFP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 489 GSLAPDHLEGRVDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGA 568
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 569 YDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFImELQDGYSTETGEKGAQLSGGQKQRVA 648
Cdd:PRK11160 407 YSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLG 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 649 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGG 728
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
....*....
gi 66932952 729 LYAKLVQRQ 737
Cdd:PRK11160 566 RYYQLKQRL 574
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
184-475 |
1.16e-56 |
|
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: 195.34 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFR 263
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 343
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 344 KYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEA---AAYMSYVWGSGLTLLVVq 420
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAkllAKYWPLMDFLSGLQIVL- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 421 vsILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18542 240 --VLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
184-451 |
1.42e-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: 194.78 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIG--SSLAAGIRGGIFTLVFARLNIRLRNCL 261
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGlaQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 262 FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNI 341
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 342 YGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQV 421
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|
gi 66932952 422 SILYYGGHLVISGQMSSGNLIAFIIYEFVL 451
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 ... |
187-475 |
2.89e-55 |
|
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: 191.54 E-value: 2.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLV 266
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 267 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 346
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 347 KRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYmsyvwgSGLTLLVVQ------ 420
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRAR------ALLTALVIFlvfgai 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 421 VSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18575 235 VFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
171-735 |
6.40e-54 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 202.18 E-value: 6.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 171 QKLLSYTKpDVAF-----LVAASFFLIVAALgetfLPYYTGRAIDSIVIQKSMDQFTTAVVVVcllAIGSSLAAGIRGGI 245
Cdd:PTZ00265 818 REIFSYKK-DVTIialsiLVAGGLYPVFALL----YAKYVSTLFDFANLEANSNKYSLYILVI---AIAMFISETLKNYY 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 246 FTLVFARLNIRLRNCLFRSLVSQETSFFDE--NRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVK--VTGVVVFMFSlS 321
Cdd:PTZ00265 890 NNVIGEKVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLflVSMVMSFYFC-P 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 322 WQLSLVTFMGFpIIMMVSNIYGKYYKrlSKEVQSALARASTTA-----------------EETISAMKTVRSFANEEEEA 384
Cdd:PTZ00265 969 IVAAVLTGTYF-IFMRVFAIRARLTA--NKDVEKKEINQPGTVfaynsddeifkdpsfliQEAFYNMNTVIIYGLEDYFC 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 385 EVFLRKLQQVYKlNRKEAAAYMSYVWG-SGLTLLVVQVSILYYGGHLVISGQMSSGNLIAFIiYEFVLgdcmesVGSVYS 463
Cdd:PTZ00265 1046 NLIEKAIDYSNK-GQKRKTLVNSMLWGfSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSL-FTFLF------TGSYAG 1117
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 464 GLMQGVGAAEKV-FEFIDRQPTMVH--------DGSLA---PDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVT 531
Cdd:PTZ00265 1118 KLMSLKGDSENAkLSFEKYYPLIIRksnidvrdNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTT 1197
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 532 ALVGPSGSGKSSCVNILENFYPLQ------------------------------------------------------GG 557
Cdd:PTZ00265 1198 AIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSG 1277
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 558 RVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGA 637
Cdd:PTZ00265 1278 KILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGK 1357
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 638 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG--NLQRHTVLIIAHRLSTVERAHLIVVLDK---- 711
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikDKADKTIITIAHRIASIKRSDKIVVFNNpdrt 1437
|
650 660
....*....|....*....|....*.
gi 66932952 712 GRVVQ-QGTHQQLL-AQGGLYAKLVQ 735
Cdd:PTZ00265 1438 GSFVQaHGTHEELLsVQDGVYKKYVK 1463
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
417-726 |
4.05e-53 |
|
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: 192.95 E-value: 4.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 417 LVVQVSILYYGGHLVISGQMSSGNLIA-FIIYEFVLGDCMESVGsVYSGLMQGVGAAEKVFEFIDRQPtmvhdgsLAPDH 495
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAgSILVGRALAPIDGAIG-GWKQFSGARQAYKRLNELLANYP-------SRDPA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 496 L-----EGRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD 570
Cdd:TIGR01842 308 MplpepEGHLSVENVTIVP-PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 571 HKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMA 650
Cdd:TIGR01842 387 RETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALA 466
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 651 RALVRNPPVLILDEATSALDAESEYLIQQAI-HGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIkALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
222-697 |
3.67e-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: 187.18 E-value: 3.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 222 TTAVVVVCLLAIGSSLAAGI-RGGIFTLVFARLNiRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 300
Cdd:TIGR02868 53 SVAAVAVRAFGIGRAVFRYLeRLVGHDAALRSLG-ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 301 NIFLRNTVKVTGVVVFMFSLSWQLSLVT--------FMGFPIIMMVSNIYGKYYKRLSKEVQSALARA-STTAEETIS-A 370
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALILaaglllagFVAPLVSLRAARAAEQALARLRGELAAQLTDAlDGAAELVASgA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 371 MKTVRSfanEEEEAEVFLRKLQQvyklNRKEAAAymsyvWGSGLTLLVVQVSI---LYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:TIGR02868 212 LPAALA---QVEEADRELTRAER----RAAAATA-----LGAALTLLAAGLAVlgaLWAGGPAVADGRLAPVTLAVLVLL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 448 EFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDrQPTMVHDGSLAPDHLEG----RVDFENVTFTYRTRPhtQVLQNVSF 523
Cdd:TIGR02868 280 PLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD-AAGPVAEGSAPAAGAVGlgkpTLELRDLSAGYPGAP--PVLDGVSL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 524 SLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTV 603
Cdd:TIGR02868 357 DLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 604 PFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG 683
Cdd:TIGR02868 437 TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA 516
|
490
....*....|....
gi 66932952 684 NLQRHTVLIIAHRL 697
Cdd:TIGR02868 517 ALSGRTVVLITHHL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
184-709 |
2.87e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 191.40 E-value: 2.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFflIVAALGETFLPYYTgraidSI--VIQKSM---DQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLR 258
Cdd:PTZ00265 61 LLGVSF--VCATISGGTLPFFV-----SVfgVIMKNMnlgENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 259 NCLFRSLVSQETSFFDENRTgdliSRLTSDTTMVSDLVSQNI-----NIFLRnTVKVTGVVVFMFSLSWQLSLVTFMGFP 333
Cdd:PTZ00265 134 LEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIgtkfiTIFTY-ASAFLGLYIWSLFKNARLTLCITCVFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 334 IIMMVSNIYGKYYKrLSKEVqSALARASTTA--EETISAMKTVRSFANEEEEAEVF--LRKLQQVY--KLNRKEAA---- 403
Cdd:PTZ00265 209 LIYICGVICNKKVK-INKKT-SLLYNNNTMSiiEEALVGIRTVVSYCGEKTILKKFnlSEKLYSKYilKANFMESLhigm 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 404 ----AYMSYVWG--SGLTLLVVQVSILY----YGGHLVISgqMSSGNLIAFIIYEFVLGDCMEsvgsvysgLMQGVGAAE 473
Cdd:PTZ00265 287 ingfILASYAFGfwYGTRIIISDLSNQQpnndFHGGSVIS--ILLGVLISMFMLTIILPNITE--------YMKSLEATN 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 474 KVFEFIDRQPTMVH--DGSLAPDhlEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF 551
Cdd:PTZ00265 357 SLYEIINRKPLVENndDGKKLKD--IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 552 Y-PLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGL------------------------------ 600
Cdd:PTZ00265 435 YdPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnsc 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 601 ---------------------------PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARAL 653
Cdd:PTZ00265 515 rakcagdlndmsnttdsneliemrknyQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAI 594
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIH---GNLQRHTVlIIAHRLSTVERAHLIVVL 709
Cdd:PTZ00265 595 IRNPKILILDEATSSLDNKSEYLVQKTINnlkGNENRITI-IIAHRLSTIRYANTIFVL 652
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
184-475 |
9.69e-50 |
|
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: 176.47 E-value: 9.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMdqfTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFR 263
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSS---GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 343
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 344 KYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEaAAYMSYVWG-SGLTLLVVQVS 422
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKA-AKIEALIGPlMGLAVQLALLV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 66932952 423 ILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18551 237 VLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
184-447 |
5.14e-48 |
|
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: 171.83 E-value: 5.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQK-SMDQFTTAVVVVCLLAIGSslaagirgGIFTlVFARLNI------- 255
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLI--------GIFR-FLWRYLIfgasrri 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 256 --RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFP 333
Cdd:cd18541 72 eyDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 334 IIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeaaayMSYVWG-- 411
Cdd:cd18541 152 LLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR-----LARVDAlf 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 66932952 412 -------SGLTLLVVqvsiLYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:cd18541 227 fpligllIGLSFLIV----LWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
500-726 |
1.93e-46 |
|
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: 165.20 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPV--LFARSITDNISYGlPT---VPFEMVVEAAQKA-NAHGfIMELQDgYSTetgekgAQLSGGQKQRVAMARAL 653
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFG-PEnlgLPREEIRERVEEAlELVG-LEHLAD-RPP------HELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
184-447 |
7.89e-46 |
|
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: 165.64 E-value: 7.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDqfTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARL--NI--RLRN 259
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGD--LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLgqRIiyDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 260 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 339
Cdd:cd18544 79 DLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 340 NIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKE---AAAYMSYV-WGSGLT 415
Cdd:cd18544 159 YLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSiklFALFRPLVeLLSSLA 238
|
250 260 270
....*....|....*....|....*....|..
gi 66932952 416 LlvvqVSILYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:cd18544 239 L----ALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
174-485 |
1.30e-45 |
|
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: 165.70 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 174 LSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVV---VVCLLAIGSSLAAGIRGGIFTLVF 250
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFwalMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 251 ARLNIRLRNCLFRSLVSQETSFFD--ENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVT 328
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 329 FMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSy 408
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 409 vwGSGLT---LLVVQVSILYYGGHLVISGQMSSGNLiaFIIYEFVLGdCMESVGSVYSGL---MQGVGAAEKVFEFIDRQ 482
Cdd:cd18578 240 --GFGLSqslTFFAYALAFWYGGRLVANGEYTFEQF--FIVFMALIF-GAQSAGQAFSFApdiAKAKAAAARIFRLLDRK 314
|
...
gi 66932952 483 PTM 485
Cdd:cd18578 315 PEI 317
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
184-475 |
2.64e-45 |
|
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: 164.18 E-value: 2.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIV----IQKSMDQFTTAVVVVCL----LAIGSSLAAGIRGGIFTLVFARLNI 255
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsGESSPDEFLDDVNKYALyfvyLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 256 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 335
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 336 MMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeaaayMSYVWG--SG 413
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIK-----KGLVSGlgLG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 414 LTLLVVQVSI---LYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18577 236 LLFFIIFAMYalaFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
503-714 |
3.03e-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: 159.69 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTY--RTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISL 580
Cdd:cd03246 4 ENVSFRYpgAEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 581 VSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVL 660
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 661 ILDEATSALDAESEYLIQQAI-HGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRV 714
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
256-735 |
8.64e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 174.39 E-value: 8.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 256 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSwQLSLVTFMgfPII 335
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS-TISLWAIM--PLL 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 336 MMVSNIYgKYYKRLSKEVQ--SALARASTTAE--ETISAMKTVRSFaneeeEAEVFLRKLQQVYKLN--RKEAAAYMSYV 409
Cdd:PLN03232 1061 ILFYAAY-LYYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY-----KAYDRMAKINGKSMDNniRFTLANTSSNR 1134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 410 W--------GSGLTLLVVQVSILYYG---GHLVISGQMssGNLIAFIIyefvlgdcmeSVGSVYSGLMQGVGAAEKVFEF 478
Cdd:PLN03232 1135 WltirletlGGVMIWLTATFAVLRNGnaeNQAGFASTM--GLLLSYTL----------NITTLLSGVLRQASKAENSLNS 1202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 479 IDRQPTMVHDGSLAPDHLE-----------GRVDFENVTFTYRtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 546
Cdd:PLN03232 1203 VERVGNYIDLPSEATAIIEnnrpvsgwpsrGSIKFEDVHLRYR--PGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLN 1280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 547 ILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQKANAHGFI 621
Cdd:PLN03232 1281 ALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID------PFSEhndadLWEALERAHIKDVI 1354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 622 MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVE 701
Cdd:PLN03232 1355 DRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTII 1434
|
490 500 510
....*....|....*....|....*....|....*
gi 66932952 702 RAHLIVVLDKGRVVQQGTHQQLLA-QGGLYAKLVQ 735
Cdd:PLN03232 1435 DCDKILVLSSGQVLEYDSPQELLSrDTSAFFRMVH 1469
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
502-714 |
1.07e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.60 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRViSL 580
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQV-AY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 581 VSQEPVLFARSITDNISYglptvPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPV 659
Cdd:COG4619 79 VPQEPALWGGTVRDNLPF-----PFQLRERKFDRERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 660 LILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTVER-AHLIVVLDKGRV 714
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
184-447 |
1.79e-44 |
|
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: 161.87 E-value: 1.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFR 263
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 343
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 344 KYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeAAAYMSYVWGS-GLTLLVVQVS 422
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMR-AVRLNALFWPLvELISALGTAL 240
|
250 260
....*....|....*....|....*
gi 66932952 423 ILYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGY 265
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
230-730 |
3.88e-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: 172.44 E-value: 3.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 230 LLAIGSSLAAGIrGGIFTlvfARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVK 309
Cdd:TIGR00957 1020 FAVFGYSMAVSI-GGIQA---SR---VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFN 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 310 VTGVVVFMFsLSWQLSLVTFmgfPIIMMVSNIYGKYYKRLSKEVQ--SALARASTTAE--ETISAMKTVRSFaneeEEAE 385
Cdd:TIGR00957 1093 VIGALIVIL-LATPIAAVII---PPLGLLYFFVQRFYVASSRQLKrlESVSRSPVYSHfnETLLGVSVIRAF----EEQE 1164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 386 VFLrkLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQVS---ILYYGGHLVISGQMSSGNLIAFII-YEFVLGDCMESVGSV 461
Cdd:TIGR00957 1165 RFI--HQSDLKVDENQKAYYPSIVANRWLAVRLECVGnciVLFAALFAVISRHSLSAGLVGLSVsYSLQVTFYLNWLVRM 1242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 462 YSGLMQGVGAAEKVFEF--IDRQPTMVHDGSLAPDHL--EGRVDFENvtFTYRTRPHTQ-VLQNVSFSLSPGKVTALVGP 536
Cdd:TIGR00957 1243 SSEMETNIVAVERLKEYseTEKEAPWQIQETAPPSGWppRGRVEFRN--YCLRYREDLDlVLRHINVTIHGGEKVGIVGR 1320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 537 SGSGKSSCVNILENFYPLQGGRVLLDG---KPIGAYDhkyLHRVISLVSQEPVLFARSITDNISyglptvPF-----EMV 608
Cdd:TIGR00957 1321 TGAGKSSLTLGLFRINESAEGEIIIDGlniAKIGLHD---LRFKITIIPQDPVLFSGSLRMNLD------PFsqysdEEV 1391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 609 VEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH 688
Cdd:TIGR00957 1392 WWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC 1471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 66932952 689 TVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLY 730
Cdd:TIGR00957 1472 TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
252-446 |
3.81e-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: 158.09 E-value: 3.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 252 RLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDttmVSDLVS---QNINIFLRNTVKVTGVVVFMFSLSWQLSLVT 328
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSsfkQCVSQGLRSVTQTVGCVVSLYLISPKLTLLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 329 FMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSY 408
Cdd:cd18574 149 LVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIF 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 66932952 409 VWGSGLTLLVVQVSILYYGGHLVISGQMSSGNLIAFII 446
Cdd:cd18574 229 QGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
500-726 |
3.94e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.99 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRvIS 579
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNIS-----YGLPTVPFEMVVEAAQKAnahgfiMELQDgystETGEKGAQLSGGQKQRVAMARAL 653
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEARERIDELLEL------FGLTD----AADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
500-717 |
1.40e-42 |
|
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: 154.17 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTR-PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAydhkyLHRVI 578
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFA-RSITDNISYGLptvpfEM--VVEAAQKANAHGFImelqdgysTETGEKGA------QLSGGQKQRVAM 649
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL-----ELqgVPKAEARERAEELL--------ELVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 650 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLStvERAHL---IVVLDK--GRVVQQ 717
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDID--EAVFLadrVVVLSArpGRIVAE 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
442-726 |
1.48e-42 |
|
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: 161.99 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 442 IAFIIYEFVLGDCMESVGSV---YSGLMQGVGAAEKVFEFIDR---QPTMVHDGSLAPDHLEGR---VDFENVTFTYRTR 512
Cdd:COG1123 194 TTVLLITHDLGVVAEIADRVvvmDDGRIVEDGPPEEILAAPQAlaaVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 513 P--HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDH---KYLHRVISLVSQEPV- 586
Cdd:COG1123 274 GkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYs 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 -LFAR-SITDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLI 661
Cdd:COG1123 354 sLNPRmTVGDIIAEPL------RLHGLLSRAERRERVAELLErvGLPPDLADRyPHELSGGQRQRVAIARALALEPKLLI 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 662 LDEATSALDaeseYLIQQAIHG---NLQR---HTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:COG1123 428 LDEPTSALD----VSVQAQILNllrDLQRelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
502-713 |
1.80e-42 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 153.39 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLV 581
Cdd:cd03225 2 LKNLSFSYPDGA-RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEP--VLFARSITDNISYGLP--TVPFEMVVEAAQKANAHGFIMELQDgYSTETgekgaqLSGGQKQRVAMARALVRNP 657
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALELVGLEGLRD-RSPFT------LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 658 PVLILDEATSALDAESEYLIQQAIHG-NLQRHTVLIIAHRLSTVER-AHLIVVLDKGR 713
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
500-723 |
1.84e-42 |
|
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: 153.88 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLQ--GGRVLLDGKPIGAYDHK-- 572
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPGApdEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 573 YLHRVISLVSQEPVLFARSITDNISYGLP-------TVPFEMVVEAAQKANAHGFIMELQDGYStetgekgaqLSGGQKQ 645
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 646 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQL 723
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
493-719 |
2.09e-42 |
|
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: 152.95 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 493 PDHleGRVDFENVTFTYRtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDH 571
Cdd:cd03369 2 PEH--GEIEVENLSVRYA--PDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 572 KYLHRVISLVSQEPVLFARSITDNISyglptvPFEMVVEAAqkanahgfIMElqdgySTETGEKGAQLSGGQKQRVAMAR 651
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSNLD------PFDEYSDEE--------IYG-----ALRVSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGT 719
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
500-713 |
3.07e-42 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 152.62 E-value: 3.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVlldgkpigaydhkYLHRV 577
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEPVLFARSITDNISYGLPTVP--FEMVVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALV 654
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEerYEKVIKACAlEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 655 RNPPVLILDEATSALDAE-SEYLIQQAIHGNLQRH-TVLIIAHRLSTVERAHLIVVLDKGR 713
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
185-447 |
3.09e-42 |
|
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: 155.75 E-value: 3.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 185 VAASFFLIVAAlgeTFL----PYYTGRAIDSIVIQKSMDQFTTAVVVVCL----LAIGSSLAAGIRGGIFTLVFARLNIR 256
Cdd:cd18563 1 LILGFLLMLLG---TALglvpPYLTKILIDDVLIQLGPGGNTSLLLLLVLglagAYVLSALLGILRGRLLARLGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 257 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 336
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 337 MVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeaAAYMSYVWGSGLTL 416
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR--AEKLWATFFPLLTF 235
|
250 260 270
....*....|....*....|....*....|...
gi 66932952 417 LVV--QVSILYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:cd18563 236 LTSlgTLIVWYFGGRQVLSGTMTLGTLVAFLSY 268
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
246-735 |
5.11e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 162.60 E-value: 5.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 246 FTLVFARLNI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSwQ 323
Cdd:PLN03130 975 YWLIMSSLYAakRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVS-T 1053
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 324 LSLVTFMgfPIIMMVSNIYgKYYKRLSKEVQ--SALARASTTAE--ETISAMKTVRSFANEEEEAEVFLRKLQQvyklNR 399
Cdd:PLN03130 1054 ISLWAIM--PLLVLFYGAY-LYYQSTAREVKrlDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDN----NI 1126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 400 KEAAAYMSYVWGSGLTLLVVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFI 479
Cdd:PLN03130 1127 RFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAV 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 480 DRQPTMVHDGSLAPDHLE-----------GRVDFENVTFTYRTR--PhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 546
Cdd:PLN03130 1207 ERVGTYIDLPSEAPLVIEnnrpppgwpssGSIKFEDVVLRYRPElpP---VLHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 547 ILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQKANAHGFI 621
Cdd:PLN03130 1284 ALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD------PFNEhndadLWESLERAHLKDVI 1357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 622 MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVE 701
Cdd:PLN03130 1358 RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTII 1437
|
490 500 510
....*....|....*....|....*....|....*
gi 66932952 702 RAHLIVVLDKGRVVQQGTHQQLLA-QGGLYAKLVQ 735
Cdd:PLN03130 1438 DCDRILVLDAGRVVEFDTPENLLSnEGSAFSKMVQ 1472
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
503-724 |
2.59e-40 |
|
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: 148.65 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVS 582
Cdd:COG1120 5 ENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPVL-FARSITDNISYG-LPTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMAR 651
Cdd:COG1120 82 QEPPApFGLTVRELVALGrYPHLGLfgrpsaedrEAVEEALERTG----LEHLADRPVDE-------LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHG--NLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLL 724
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
184-475 |
2.65e-40 |
|
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: 150.25 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIV------IQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRL 257
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIeglgggGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 258 RNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 337
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 338 VSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeaAAYMSYVWGSGLTLL 417
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK--AQFYSGLLMPIMNFI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 418 --VVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18547 239 nnLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
497-715 |
5.35e-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: 147.93 E-value: 5.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 497 EGRVDFENVTFTYRTRP-HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKylh 575
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 rvISLVSQEPVLFA-RSITDNISYGLptvpfEMVVEAAQKANAHgfIMELQDgystETGEKGA------QLSGGQKQRVA 648
Cdd:COG1116 82 --RGVVFQEPALLPwLTVLDNVALGL-----ELRGVPKAERRER--ARELLE----LVGLAGFedayphQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 649 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAH------RLSTveRahlIVVLDK--GRVV 715
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHdvdeavFLAD--R---VVVLSArpGRIV 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
500-718 |
1.01e-39 |
|
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: 146.11 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRP-HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD---HKYLH 575
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RVISLVSQEPVL---FARSITDNISYGLptVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 652
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIAEPL--RIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 653 LVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLK-KLQEElglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
518-667 |
1.39e-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: 143.17 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFAR-SITDNI 596
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 597 SYGLptvPFEMVVEAAQKANAHGFI--MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 667
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
502-718 |
1.55e-39 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 143.99 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYrtrPH--TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDhKYLHRVIS 579
Cdd:cd03247 3 INNVSFSY---PEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekGAQLSGGQKQRVAMARALVRNPPV 659
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 660 LILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQG 718
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
500-726 |
2.29e-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: 145.42 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfYPLQGgRVLLDGKPIGAYDHKYL- 574
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLE--RPTSG-SVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 575 --HRVISLVSQEPVLF-ARSITDNISYglptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAM 649
Cdd:cd03258 79 kaRRRIGMIFQHFNLLsSRTVFENVAL-----PLE--IAGVPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 650 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLR-DINRElglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 66932952 726 Q 726
Cdd:cd03258 231 N 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
502-713 |
4.76e-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: 141.61 E-value: 4.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLV 581
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQepvlfarsitdnisyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 661
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 66932952 662 LDEATSALDAESEYLIQQAIHGNLQRH-TVLIIAHRLSTVERA-HLIVVLDKGR 713
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGrTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
500-726 |
1.40e-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: 150.44 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKS---SCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHR 576
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKStlaLALMGLLPHGGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VISLVSQEP--VLFARSITDNISYGL--PTVPFEMVVEAAQKANAHGFIMELQDGYStetgekgAQLSGGQKQRVAMARA 652
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALenLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 653 LVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLR-ELQRErgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
500-718 |
1.91e-38 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 142.27 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKylhRVI 578
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpER---RNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFA-RSITDNISYGLPtvpfEMVVEAAQKANAHGFIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNP 657
Cdd:cd03259 75 GMVFQDYALFPhLTVAENIAFGLK----LRGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 658 PVLILDEATSALDAESEYLIQ---QAIHGNLQRhTVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELReelKELQRELGI-TTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
184-475 |
2.27e-38 |
|
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: 144.55 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFR 263
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQnINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 343
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 344 KYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeaAAYMSYVWGSGLTLL--VVQV 421
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLR--AARLRARFWPLLEALpeLGLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 66932952 422 SILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18543 238 AVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
503-728 |
3.31e-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: 142.30 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRvISLVS 582
Cdd:COG4555 5 ENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPVLFAR-SITDNISY-----GLPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRN 656
Cdd:COG4555 81 DERGLYDRlTVRENIRYfaelyGLFDEELKKRIEELIEL------LGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 657 PPVLILDEATSALDAESeyliQQAIHGNLQRH-----TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQGG 728
Cdd:COG4555 151 PKVLLLDEPTNGLDVMA----RRLLREILRALkkegkTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
502-726 |
4.23e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.82 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRTRPhtqvlQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKylhRVISL 580
Cdd:COG3840 4 LDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAE---RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 581 VSQEPVLFAR-SITDNISYGL-----PTVP-FEMVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAMARAL 653
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGLrpglkLTAEqRAQVEQALERVGLAGLL-----------DRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 654 VRNPPVLILDEATSALD----AESEYLIQQaIHGNLQRhTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:COG3840 145 VRKRPILLLDEPFSALDpalrQEMLDLVDE-LCRERGL-TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
500-714 |
2.76e-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: 138.78 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHK----YL 574
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 575 HRVISLVSQEPVLFAR-SITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMAR 651
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVE--LP-----LLLAGVPKKERRERAEELLErvGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHG--NLQRHTVLIIAHRLSTVERAHLIVVLDKGRV 714
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
500-719 |
1.05e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.39 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIG---AYdhkylHR 576
Cdd:COG3842 6 LELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPE-----KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VISLVSQEPVLFA-RSITDNISYGLptvpfEM--VVEAAQKANAHGFI--MELqDGYStetGEKGAQLSGGQKQRVAMAR 651
Cdd:COG3842 78 NVGMVFQDYALFPhLTVAENVAFGL-----RMrgVPKAEIRARVAELLelVGL-EGLA---DRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQRH---TVLIIAHRLS---TVerAHLIVVLDKGRVVQQGT 719
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREEL-RRLQRElgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
503-714 |
1.27e-36 |
|
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: 135.60 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRvISLVS 582
Cdd:cd03230 4 RNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPVLfarsitdnisyglptvpfemvveaaqkanahgfimelqdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL 662
Cdd:cd03230 80 EEPSL----------------------------------------YENLTVRENLKLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 66932952 663 DEATSALDAESEYLIQQAIHG-NLQRHTVLIIAHRLSTVER-AHLIVVLDKGRV 714
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
503-725 |
1.80e-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: 137.63 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLV 581
Cdd:COG1124 5 RNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEP--VLFAR-SITDNIS-----YGLPTVPfEMVVEAAQKanahgfiMELQDGYSTEtgeKGAQLSGGQKQRVAMARAL 653
Cdd:COG1124 85 FQDPyaSLHPRhTVDRILAeplriHGLPDRE-ERIAELLEQ-------VGLPPSFLDR---YPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 654 VRNPPVLILDEATSALDAeseylIQQAIHGNL-----QRH--TVLIIAHRLSTVerAHL---IVVLDKGRVVQQGTHQQL 723
Cdd:COG1124 154 ILEPELLLLDEPTSALDV-----SVQAEILNLlkdlrEERglTYLFVSHDLAVV--AHLcdrVAVMQNGRIVEELTVADL 226
|
..
gi 66932952 724 LA 725
Cdd:COG1124 227 LA 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
500-719 |
1.86e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 140.21 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFyplQGGRVLLDGKPIGAYDHKYLH 575
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RV---ISLVSQEPVLF-ARSITDNISYglptvPFEMV----VEAAQKANahgfimELQD--GYStetgEKG----AQLSG 641
Cdd:COG1135 79 AArrkIGMIFQHFNLLsSRTVAENVAL-----PLEIAgvpkAEIRKRVA------ELLElvGLS----DKAdaypSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 642 GQKQRVAMARALVRNPPVLILDEATSALDAESeyliQQAIHGNLQR------HTVLIIAHRLSTVER-AHLIVVLDKGRV 714
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPET----TRSILDLLKDinrelgLTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 66932952 715 VQQGT 719
Cdd:COG1135 220 VEQGP 224
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
191-447 |
5.12e-36 |
|
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: 137.97 E-value: 5.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 191 LIVAALgETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLVSQET 270
Cdd:cd18549 12 VLIAAL-DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 271 SFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLS 350
Cdd:cd18549 91 SFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 351 KEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQvYKLNRKEAAAYMSYvWGSGLTLL--VVQVSILYYGG 428
Cdd:cd18549 171 RRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR-FLESKKKAYKAMAY-FFSGMNFFtnLLNLVVLVAGG 248
|
250
....*....|....*....
gi 66932952 429 HLVISGQMSSGNLIAFIIY 447
Cdd:cd18549 249 YFIIKGEITLGDLVAFLLY 267
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
500-726 |
1.00e-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: 135.12 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLQGGRVLLDGKPIGAyDHKYLHR 576
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLE---EPDSGTITVDGEDLTD-SKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 V---ISLVSQEPVLFA-RSITDNISYGLptvpfeMVV------EAAQKAnahgfiMEL---------QDGYStetgekgA 637
Cdd:COG1126 75 LrrkVGMVFQQFNLFPhLTVLENVTLAP------IKVkkmskaEAEERA------MELlervgladkADAYP-------A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 638 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAE--SEYL--IQQAIHGNLqrhTVLIIAHRLSTVER-AHLIVVLDKG 712
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElvGEVLdvMRDLAKEGM---TMVVVTHEMGFAREvADRVVFMDGG 212
|
250
....*....|....
gi 66932952 713 RVVQQGTHQQLLAQ 726
Cdd:COG1126 213 RIVEEGPPEEFFEN 226
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
185-447 |
1.27e-35 |
|
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: 136.84 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 185 VAASFFLIVA-ALGETFLPYYTGRAIDSIVIQKSMDqfttavvVVCLLAIGSsLAAGIRGGIFTLVFARLNIR------- 256
Cdd:cd18550 1 LALVLLLILLsALLGLLPPLLLREIIDDALPQGDLG-------LLVLLALGM-VAVAVASALLGVVQTYLSARigqgvmy 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 257 -LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 335
Cdd:cd18550 73 dLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 336 MMVSNIYGKYYKRLSKEVQSALARASTTAEET--ISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSG 413
Cdd:cd18550 153 VLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALG 232
|
250 260 270
....*....|....*....|....*....|....
gi 66932952 414 LTLLVVQVSILYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:cd18550 233 LFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTAL 266
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
184-447 |
1.79e-35 |
|
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: 136.49 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQK---------------SMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTL 248
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKplpgllglapllgpdPLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 249 VFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVT 328
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 329 FMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSY 408
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 66932952 409 VWGSGLTLLVVQVSILYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
500-713 |
5.40e-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: 131.16 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD--HKYLHRV 577
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEPVLFAR-SITDNISYGLptvpfemvveaaqkanahgfimelqdgystetgekgaqlSGGQKQRVAMARALVRN 656
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALGL---------------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 657 PPVLILDEATSALDAESEYLIQ---QAIHGNLQRhTVLIIAHRLSTVER-AHLIVVLDKGR 713
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRallKSLQAQLGI-TVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
500-717 |
8.58e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.09 E-value: 8.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV- 577
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ---ISLVSQEPVLFAR-SITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMAR 651
Cdd:COG1136 85 rrhIGFVFQFFNLLPElTALENVA--LP-----LLLAGVSRKERRERARELLErvGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQR---HTVLIIAHRLSTVERAHLIVVLDKGRVVQQ 717
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLR-ELNRelgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
184-447 |
1.31e-34 |
|
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: 133.68 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSsLAAGIRGGIF-TLVFARLNIRLRNCLF 262
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLG-LIAGILAGYFaAKASQGFGRDLRKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 263 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIY 342
Cdd:cd18548 80 EKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 343 GKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeAAAYMSyvWGSGLTLLVVQVS 422
Cdd:cd18548 160 MKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLK-AGRLMA--LLNPLMMLIMNLA 236
|
250 260
....*....|....*....|....*...
gi 66932952 423 ---ILYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:cd18548 237 ivaILWFGGHLINAGSLQVGDLVAFINY 264
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
503-718 |
1.34e-34 |
|
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: 129.86 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVS 582
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QepvlfarsitdnisyglptvpfemVVEAAQKAN-AHGFIMElqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 661
Cdd:cd03214 80 Q------------------------ALELLGLAHlADRPFNE---------------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 662 LDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLR-RLARErgkTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
500-714 |
2.42e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.36 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKylhrvIS 579
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEpVLFARS--IT--DNISYGL-PTVPF---------EMVVEAAQKANAHGF----ImelqdgystetgekgAQLSG 641
Cdd:COG1121 79 YVPQR-AEVDWDfpITvrDVVLMGRyGRRGLfrrpsradrEAVDEALERVGLEDLadrpI---------------GELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 642 GQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH--TVLIIAHRLSTVER-AHLIVVLDKGRV 714
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRREgkTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
184-475 |
2.55e-34 |
|
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: 133.00 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSmdqfTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIR----LRN 259
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGD----LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERllydLRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 260 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 339
Cdd:cd18546 77 RVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 340 NIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFlRKLQQVYKLNRKEAAAYMSyVWGSGLTLL-- 417
Cdd:cd18546 157 RWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF-AELSDDYRDARLRAQRLVA-IYFPGVELLgn 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 418 VVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18546 235 LATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
184-475 |
7.65e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 128.81 E-value: 7.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVI-QKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLF 262
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIgSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 263 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIY 342
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 343 GKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLN---RKEAAAY---MSYVWGSGlTL 416
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQlraMKLWAIFhplMEFLTSLG-TV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 417 LVvqvsiLYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18778 240 LV-----LGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
500-725 |
7.95e-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: 126.85 E-value: 7.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV-- 577
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 -ISLVSQEPVLF-ARSITDNISYGL---PTVPFEMVVE-AAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMAR 651
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPLrehTRLSEEEIREiVLEKLEAVG-LRGAEDLYP-------AELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIR-SLKKElglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
518-726 |
1.60e-32 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 126.99 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV----ISLVSQEPVLFA-RSI 592
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 TDNISYGLPT--VP----FEMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEAT 666
Cdd:cd03294 120 LENVAFGLEVqgVPraerEERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 667 SALDA------ESEYLiqqAIHGNLQRhTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQ 726
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 ... |
500-725 |
2.10e-32 |
|
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: 125.88 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFA-RSITDNISyglpTVP-FEMVVEAAQKANAHGFI-------MELQDGYStetgekgAQLSGGQKQRVAMA 650
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIA----LVPkLLKWPKEKIRERADELLalvgldpAEFADRYP-------HELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 651 RALVRNPPVLILDEATSALDA------ESEYL-IQQAIHgnlqrHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQ 722
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPitrdqlQEEFKrLQQELG-----KTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDE 222
|
...
gi 66932952 723 LLA 725
Cdd:cd03295 223 ILR 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
500-723 |
2.13e-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: 125.43 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKylhRVI 578
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPpHK---RPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFAR-SITDNISYGLPTvpfEMVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRN 656
Cdd:cd03300 75 NTVFQNYALFPHlTVFENIAFGLRL---KKLPKAEIKERVAEALDLVQlEGYA---NRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 657 PPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAH----RLSTVERahlIVVLDKGRVVQQGTHQQL 723
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELK-RLQKElgiTFVFVTHdqeeALTMSDR---IAVMNKGKIQQIGTPEEI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
503-726 |
2.60e-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: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNI---LEnfYPlQGGRVLLDGKPIGAyDHKYLHRVIS 579
Cdd:COG1118 6 RNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLE--TP-DSGRIVLNGRDLFT-NLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFaR--SITDNISYGLPTVPfemVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRN 656
Cdd:COG1118 79 FVFQHYALF-PhmTVAENIAFGLRVRP---PSKAEIRARVEELLELVQlEGLA---DRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 657 PPVLILDEATSALDAESEYLIQQ---AIHGNLQrHTVLIIAH------RLStvERahlIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRwlrRLHDELG-GTTVFVTHdqeealELA--DR---VVVMNQGRIEQVGTPDEVYDR 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
500-724 |
3.53e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.26 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEP--VLFARSITDNISYGLPTV---PFEM---VVEAAQKANAHGFImelqdgystetgEKGAQ-LSGGQKQRVAMA 650
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKkvpPKKMkdiIDDLAKKVGMEDYL------------DKEPQnLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 651 RALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLL 724
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMV-DLRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
183-475 |
5.71e-32 |
|
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: 126.05 E-value: 5.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 183 FLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVV-VCLLAIgssLAAGIRGGIFT--LVFARLNIRLRN 259
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLyLGLILI---QALSVFLFIRLagKIEMGVSYDLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 260 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 339
Cdd:cd18540 80 KAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 340 NIYGK---YYKRLSKEVQSALarastTA--EETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeaAAYMSYVWGSGL 414
Cdd:cd18540 160 IYFQKkilKAYRKVRKINSRI-----TGafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVR--AARLSALFLPIV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 415 TLL--VVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18540 233 LFLgsIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
490-697 |
7.50e-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: 7.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 490 SLAPDHLEGRVDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLQ--GGRVLLDGK 564
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGArvEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 565 PIgaYDHKY----LHRVISLVSQEPVLFARSITDNISYGL-------PTVPFEMVVEAAQKANahgfimeLQDgystET- 632
Cdd:COG1117 79 DI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiksKSELDEIVEESLRKAA-------LWD----EVk 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 633 ---GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES----EYLIQQaihgnL-QRHTVLIIAHRL 697
Cdd:COG1117 146 drlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELILE-----LkKDYTIVIVTHNM 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
516-714 |
7.97e-32 |
|
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: 123.02 E-value: 7.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 516 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFyplQGGRVLLDGKPIGAyDHKYLHRV---ISLVSQEPVLFA 589
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEEP---DSGTIIIDGLKLTD-DKKNINELrqkVGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 590 -RSITDNISYGLPTVPFEMVVEAAQKAnahgfiMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 666
Cdd:cd03262 90 hLTVLENITLAPIKVKGMSKAEAEERA------LELLEkvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 66932952 667 SALDAE--SEYL--IQQAIHGNLqrhTVLIIAHRLSTV-ERAHLIVVLDKGRV 714
Cdd:cd03262 164 SALDPElvGEVLdvMKDLAEEGM---TMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
500-744 |
1.20e-31 |
|
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: 124.46 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDG-KPIGAYDHKYLHRVI 578
Cdd:TIGR04520 1 IEVENVSFSY-PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALV 654
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEALK---LVGMEDFRDREP----HLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 655 RNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGglyA 731
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIR-KLNKEegiTVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV---E 228
|
250
....*....|...
gi 66932952 732 KLVQrqmLGLEHP 744
Cdd:TIGR04520 229 LLKE---IGLDVP 238
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
502-718 |
1.33e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 122.64 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKylhrvISLV 581
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPVL---FARSITDNISYGL-PTVPFEMVVEAAQKANahgfIMELQDgySTETGEKG----AQLSGGQKQRVAMARAL 653
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLyGHKGLFRRLSKADKAK----VDEALE--RVGLSELAdrqiGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIhGNLQR--HTVLIIAHRLSTVERAHLIVVLDKGRVVQQG 718
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELL-RELRRegMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
178-445 |
2.69e-31 |
|
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: 124.10 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 178 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRL 257
Cdd:cd18570 1 KKLLILILLLSLLITLLGI---AGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 258 RNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQN-INIFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 336
Cdd:cd18570 78 ILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFL-DLLMVIISGIILFFYNWKLFLITLLIIPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 337 MVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTL 416
Cdd:cd18570 156 LIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLIS 235
|
250 260
....*....|....*....|....*....
gi 66932952 417 LVVQVSILYYGGHLVISGQMSSGNLIAFI 445
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFN 264
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
500-725 |
5.34e-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: 121.63 E-value: 5.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV-- 577
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 -ISLVSQEPVLFArSIT--DNISYGL---PTVPFEMVVEAAqkanahgfIMELQdgystETGEKGA------QLSGGQKQ 645
Cdd:COG1127 83 rIGMLFQGGALFD-SLTvfENVAFPLrehTDLSEAEIRELV--------LEKLE-----LVGLPGAadkmpsELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 646 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQ 721
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIR-ELRDElglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
....
gi 66932952 722 QLLA 725
Cdd:COG1127 228 ELLA 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
500-715 |
9.04e-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: 9.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHK---YLHR 576
Cdd:COG2884 2 IRFENVSKRYPGGR--EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VISLVSQE-PVLFARSITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARAL 653
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVA--LP-----LRVTGKSRKEIRRRVREVLDlvGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH--TVLIIAHRLSTVERA-HLIVVLDKGRVV 715
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLE-EINRRgtTVLIATHDLELVDRMpKRVLELEDGRLV 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
498-719 |
1.41e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.64 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 498 GRVDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKylHRV 577
Cdd:COG3839 2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEPVLF-ARSITDNISYGLptvpfEM-----------VVEAAQkanahgfIMELQDgYStetGEKGAQLSGGQKQ 645
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPL-----KLrkvpkaeidrrVREAAE-------LLGLED-LL---DRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 646 RVAMARALVRNPPVLILDEATSALDAE------SEylIQQaihgnLQR---HTVLIIAH------RLstverAHLIVVLD 710
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKlrvemrAE--IKR-----LHRrlgTTTIYVTHdqveamTL-----ADRIAVMN 208
|
....*....
gi 66932952 711 KGRVVQQGT 719
Cdd:COG3839 209 DGRIQQVGT 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
515-725 |
2.68e-30 |
|
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: 119.08 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 515 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPI-GAYDHKYLHRVISLVSQEPVLFAR-SI 592
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHERARAGIGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 TDNIsyglptvpfEMVVEAAQKANAHgFIME--------LQDGYSTetgeKGAQLSGGQKQRVAMARALVRNPPVLILDE 664
Cdd:cd03224 93 EENL---------LLGAYARRRAKRK-ARLErvyelfprLKERRKQ----LAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 665 ATSALdaeSEYLIQQ---AIHG-NLQRHTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:cd03224 159 PSEGL---APKIVEEifeAIRElRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
503-695 |
2.75e-30 |
|
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: 118.51 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAydhKYLHRVISLVS 582
Cdd:cd03226 3 ENISFSYK--KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEP--VLFARSITDNISYGLPTVPfemvvEAAQKANAhgfIMELQDGYSTEtgEKGAQ-LSGGQKQRVAMARALVRNPPV 659
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELD-----AGNEQAET---VLKDLDLYALK--ERHPLsLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 66932952 660 LILDEATSALDAESEYLIQQAI-HGNLQRHTVLIIAH 695
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIrELAAQGKAVIVITH 184
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
500-718 |
2.93e-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: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTQVLQnvsfsLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKylHRVIS 579
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT-----FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISYGL-PTVPFEMVVEAAQKANAHgfimelQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 657
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLsPGLKLTAEDRQAIEVALA------RVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 658 PVLILDEATSALDAESEYLIQQAIHG--NLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
520-718 |
2.97e-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: 118.55 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 520 NVSFSLsPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgaYD-HKYLH-----RVISLVSQEPVLFAR-SI 592
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDsRKKINlppqqRKIGLVFQQYALFPHlNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 TDNISYGLPTV-PFEMVVEAAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 671
Cdd:cd03297 93 RENLAFGLKRKrNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 66932952 672 ESEYLIQ---QAIHGNLQRHtVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:cd03297 165 ALRLQLLpelKQIKKNLNIP-VIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
500-724 |
3.27e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.43 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLQGGRVLLDGKPI--GAYDHKYL 574
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLE---EITSGDLIVDGLKVndPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 575 HRVISLVSQEPVLFAR-SITDNISYGlptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMAR 651
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHlTALENVMFG----PLR--VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 652 ALVRNPPVLILDEATSALDAEseyliqqaihgnlQRHTVL--------------IIAHRLSTVER-AHLIVVLDKGRVVQ 716
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPE-------------LRHEVLkvmqdlaeegmtmvIVTHEIGFAEKvASRLIFIDKGRIAE 216
|
....*...
gi 66932952 717 QGTHQQLL 724
Cdd:PRK09493 217 DGDPQVLI 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
503-758 |
3.34e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.73 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVS 582
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPvLFARSIT--DNISYGL-PTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMA 650
Cdd:PRK11231 83 QHH-LTPEGITvrELVAYGRsPWLSLwgrlsaednARVNQAMEQTR----INHLADRRLTD-------LSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 651 RALVRNPPVLILDEATSALD----AESEYLIQQAihgNLQRHTVLIIAHRLSTVER--AHLiVVLDKGRVVQQGTHQQLL 724
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNQASRycDHL-VVLANGHVMAQGTPEEVM 226
|
250 260 270
....*....|....*....|....*....|....
gi 66932952 725 AQGGLyaklvqRQMLGLEhpldyTASHKEPPSNT 758
Cdd:PRK11231 227 TPGLL------RTVFDVE-----AEIHPEPVSGT 249
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
502-723 |
3.35e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.78 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLQGGRVLLDGKPIGAYDHKYLHRV- 577
Cdd:COG3638 5 LRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTllrCLNGLV---EPTSGEILVDGQDVTALRGRALRRLr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 --ISLVSQEPVLFAR-SITDNISYG-LPTVPF----EMVVEAAQKANAHGFI--MELQDgystETGEKGAQLSGGQKQRV 647
Cdd:COG3638 80 rrIGMIFQQFNLVPRlSVLTNVLAGrLGRTSTwrslLGLFPPEDRERALEALerVGLAD----KAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 648 AMARALVRNPPVLILDEATSALDAES-----EYLIQQAIHGNLqrhTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQ 721
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTarqvmDLLRRIAREDGI---TVVVNLHQVDLARRyADRIIGLRDGRVVFDGPPA 232
|
..
gi 66932952 722 QL 723
Cdd:COG3638 233 EL 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
500-744 |
4.19e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.51 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV 577
Cdd:PRK13635 6 IRVEHISFRY---PDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHgfiMELQDGYSTETgekgAQLSGGQKQRVAMARAL 653
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLENigVPREEMVERVDQALRQ---VGMEDFLNREP----HRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIH--GNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGlya 731
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH--- 232
|
250
....*....|...
gi 66932952 732 KLVQrqmLGLEHP 744
Cdd:PRK13635 233 MLQE---IGLDVP 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
517-719 |
7.66e-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: 118.31 E-value: 7.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQEPVLFAR-SITD 594
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 595 NI---------SYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEA 665
Cdd:cd03219 95 NVmvaaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 666 TSAL-DAESEYLIQ--QAIhgNLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGT 719
Cdd:cd03219 171 AAGLnPEETEELAEliREL--RERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
499-710 |
1.17e-29 |
|
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: 116.81 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 499 RVDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYlHRVI 578
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFAR-SITDNIS-----YGLPtVPFEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 652
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEAVG----LAGLAD-------LPVRQLSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 653 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIA-HRLSTVERAHLIVVLD 710
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDLGD 204
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
500-760 |
1.19e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.68 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPlQGGRVLLDGKPIGAYDHKYL- 574
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER--P-TSGRVLVDGQDLTALSEKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 575 --HRVISLVSQE-PVLFARSITDNISYglptvPFEMVVEAAQKANAHgfIMELQD--GYSTETGEKGAQLSGGQKQRVAM 649
Cdd:PRK11153 79 kaRRQIGMIFQHfNLLSSRTVFDNVAL-----PLELAGTPKAEIKAR--VTELLElvGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 650 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQG------T 719
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLK-DINRElglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGtvsevfS 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 66932952 720 H-QQLLAQgglyaKLVQRQmLGLEHPLDYTASHKEPPSNTEH 760
Cdd:PRK11153 231 HpKHPLTR-----EFIQST-LHLDLPEDYLARLQAEPTTGSG 266
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
499-718 |
2.73e-29 |
|
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: 115.34 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 499 RVDFENVTFT---YRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN--FYPLQGGRVLLDGKPIGAYDHKY 573
Cdd:cd03213 3 TLSFRNLTVTvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 574 LhrvISLVSQEPVLFARSitdnisyglpTVpFEMVVEAAqkanahgfimELQdgystetgekgaQLSGGQKQRVAMARAL 653
Cdd:cd03213 83 I---IGYVPQDDILHPTL----------TV-RETLMFAA----------KLR------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQRHTVLIIAHRLST--VERAHLIVVLDKGRVVQQG 718
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
500-740 |
2.90e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.54 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRT-RPHTqvLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVI 578
Cdd:PRK13648 8 IVFKNVSFQYQSdASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPV-LFARSITD-NISYGLP--TVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAqLSGGQKQRVAMARALV 654
Cdd:PRK13648 86 GIVFQNPDnQFVGSIVKyDVAFGLEnhAVPYDEMHRRVSEA------LKQVDMLERADYEPNA-LSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 655 RNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIA--HRLSTVERAHLIVVLDKGRVVQQGT------HQQLLAQ 726
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTpteifdHAEELTR 238
|
250
....*....|....*.
gi 66932952 727 GGLYAKLVQR--QMLG 740
Cdd:PRK13648 239 IGLDLPFPIKinQMLG 254
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
500-702 |
4.32e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 117.06 E-value: 4.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQG-----GRVLLDGKPIgaYDHKY- 573
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI--YERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 574 ---LHRVISLVSQEPVLFARSITDNISYGL------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAQLSGGQK 644
Cdd:PRK14258 83 lnrLRRQVSMVHPKPNLFPMSVYDNVAYGVkivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 645 QRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTVER 702
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQVSR 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
496-738 |
5.26e-29 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 116.55 E-value: 5.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 496 LEGRVDFENVTFTYRT--RPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKY 573
Cdd:cd03288 16 LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 574 LHRVISLVSQEPVLFARSITDNISyglP--TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 651
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNLD---PecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQ-GGLY 730
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVF 249
|
....*...
gi 66932952 731 AKLVQRQM 738
Cdd:cd03288 250 ASLVRTDK 257
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
500-715 |
9.18e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 112.52 E-value: 9.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPigaydhkylhrvis 579
Cdd:cd03216 1 LELRGITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 lvsqepVLFArSITDNISYGLPTVPfemvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPV 659
Cdd:cd03216 64 ------VSFA-SPRDARRAGIAMVY---------------------------------QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 660 LILDEATSAL-DAESEYLIqqAIHGNLQR--HTVLIIAHRLSTVER-AHLIVVLDKGRVV 715
Cdd:cd03216 104 LILDEPTAALtPAEVERLF--KVIRRLRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
500-723 |
1.96e-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: 113.75 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgAYDHKYLHRVIS 579
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISY-----GLPTVPFEMVVEAAQKanahgfIMELQDGYSTETGekgaQLSGGQKQRVAMARAL 653
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQL 723
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
516-719 |
2.15e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 114.75 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 516 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgayDHKYLHRVISL-VS---QEPVLFAR- 590
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI---TGLPPHRIARLgIArtfQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SITDNI--------SYGLPTVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 660
Cdd:COG0411 95 TVLENVlvaaharlGRGLLAALLRLPRARREEREARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 661 ILDEATSAL-DAESEYLIQ--QAIHGNlQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGT 719
Cdd:COG0411 175 LLDEPAAGLnPEETEELAEliRRLRDE-RGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
500-718 |
3.89e-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: 112.73 E-value: 3.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKylHRVIS 579
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRN 656
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKLrkVPKDEIDERVREVAELLQIEHLLD-------RKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 657 PPVLILDEATSALDAESEYLIQQAI---HGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQG 718
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELkrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
517-724 |
4.04e-28 |
|
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: 113.20 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGayDHKYLHRVISLVSQEPVLFAR-SITDN 595
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 596 ISYGL-------PTVPfEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 668
Cdd:cd03299 92 IAYGLkkrkvdkKEIE-RKVLEIAEMLG----IDHLLN-------RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 669 LDAESE----YLIQQAIHGNlqRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLL 724
Cdd:cd03299 160 LDVRTKeklrEELKKIRKEF--GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
502-723 |
4.25e-28 |
|
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: 113.43 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLQGGRVLLDGKPIGAYDHKYLHRV- 577
Cdd:cd03256 3 VENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTllrCLNGLV---EPTSGSVLIDGTDINKLKGKALRQLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 --ISLVSQEPVLFAR-SITDNISYG-LPTVP-----FEMVVEAA-QKANAhgfIMElQDGYSTETGEKGAQLSGGQKQRV 647
Cdd:cd03256 78 rqIGMIFQQFNLIERlSVLENVLSGrLGRRStwrslFGLFPKEEkQRALA---ALE-RVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 648 AMARALVRNPPVLILDEATSALDAES-----EYLIQQAIHGNLqrhTVLIIAHRLStVERAHL--IVVLDKGRVVQQGTH 720
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASsrqvmDLLKRINREEGI---TVIVSLHQVD-LAREYAdrIVGLKDGRIVFDGPP 229
|
...
gi 66932952 721 QQL 723
Cdd:cd03256 230 AEL 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
520-737 |
7.33e-28 |
|
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: 115.58 E-value: 7.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 520 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgaYD---------HKylhRVISLVSQEPVLFA- 589
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDsargiflppHR---RRIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 590 RSITDNISYGL-------PTVPFEMVVEAAQkanahgfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLIL 662
Cdd:COG4148 92 LSVRGNLLYGRkrapraeRRISFDEVVELLG-------IGHLLDRRP-------ATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 663 DEATSALDAES-----EYLIQqaihgnLQRHT---VLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 733
Cdd:COG4148 158 DEPLAALDLARkaeilPYLER------LRDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLA 231
|
....
gi 66932952 734 VQRQ 737
Cdd:COG4148 232 GGEE 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
500-744 |
1.07e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.29 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALVR 655
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEALE---LVGMQDFKEREP----ARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 656 NPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGlyaKL 733
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN---DL 234
|
250
....*....|.
gi 66932952 734 VQrqmLGLEHP 744
Cdd:PRK13650 235 LQ---LGLDIP 242
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
500-714 |
1.38e-27 |
|
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: 110.96 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQV-LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHK---YLH 575
Cdd:cd03292 1 IEFINVTKTY---PNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RVISLVSQE-PVLFARSITDNisyglptVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARA 652
Cdd:cd03292 78 RKIGVVFQDfRLLPDRNVYEN-------VAFALEVTGVPPREIRKRVPAALElvGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 653 LVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQRHTVLIIAHRLSTVER-AHLIVVLDKGRV 714
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
503-718 |
2.43e-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: 110.00 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAyDHKYLHRVISLVS 582
Cdd:cd03268 4 NDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 qEPVLF-ARSITDNISYglptvpfemvveaaqKANAHGF----IMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVR 655
Cdd:cd03268 80 -APGFYpNLTARENLRL---------------LARLLGIrkkrIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 656 NPPVLILDEATSALDAESEYLIQQAIHgNLQR--HTVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELIL-SLRDqgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
503-724 |
3.34e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.36 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVS 582
Cdd:COG4559 5 ENLSVRLGGR---TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 Q-----------EPVLFARsitdnISYGLPTVPFEMVVEAAqkanahgfiMELqdgysTETGEKGA----QLSGGQKQRV 647
Cdd:COG4559 82 QhsslafpftveEVVALGR-----APHGSSAAQDRQIVREA---------LAL-----VGLAHLAGrsyqTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 648 AMARAL------VRNPP-VLILDEATSALDaeseylI--QQAIHGNLQRHT-----VLIIAHRLS-TVERAHLIVVLDKG 712
Cdd:COG4559 143 QLARVLaqlwepVDGGPrWLFLDEPTSALD------LahQHAVLRLARQLArrgggVVAVLHDLNlAAQYADRILLLHQG 216
|
250
....*....|..
gi 66932952 713 RVVQQGTHQQLL 724
Cdd:COG4559 217 RLVAQGTPEEVL 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
503-726 |
8.79e-27 |
|
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: 111.68 E-value: 8.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQG---GRVLLDGKPIGAYDHKYLHRV- 577
Cdd:COG0444 5 RNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKIr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ---ISLVSQE------PVLfarsitdnisyglpTVpFEMVVEAaqkanahgfiMELQDGYSTETGEKGA----------- 637
Cdd:COG0444 85 greIQMIFQDpmtslnPVM--------------TV-GDQIAEP----------LRIHGGLSKAEARERAiellervglpd 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 638 ----------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQRH---TVLIIAHRLSTVE 701
Cdd:COG0444 140 perrldryphELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQILNllkDLQRElglAILFITHDLGVVA 215
|
250 260
....*....|....*....|....*.
gi 66932952 702 R-AHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:COG0444 216 EiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
500-718 |
1.09e-26 |
|
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: 108.43 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQVLQNVSFSLSPGkVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYlHRVIS 579
Cdd:cd03264 1 LQLENLTKRY---GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL-RRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISY-----GLP--TVPfEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMAR 651
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPskEVK-ARVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 652 ALVRNPPVLILDEATSALDAES-----EYLIQQAihgnlQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEErirfrNLLSELG-----EDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
503-726 |
1.11e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.90 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPhtqvlqnVSFSLS--PGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKpigayDHKYL---HRV 577
Cdd:PRK10771 5 TDITWLYHHLP-------MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEPVLFAR-SITDNISYGL-PTVPF-----EMVVEAAQKANAHGFIMELQdgystetgekgAQLSGGQKQRVAMA 650
Cdd:PRK10771 73 VSMLFQENNLFSHlTVAQNIGLGLnPGLKLnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 651 RALVRNPPVLILDEATSALD----AESEYLIQQAIHgnlQRH-TVLIIAHRLstvERAHLI----VVLDKGRVVQQGTHQ 721
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQ---ERQlTLLMVSHSL---EDAARIaprsLVVADGRIAWDGPTD 215
|
....*
gi 66932952 722 QLLAQ 726
Cdd:PRK10771 216 ELLSG 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
500-723 |
2.00e-26 |
|
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: 108.58 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPigAYDHKYLHRVIS 579
Cdd:cd03296 3 IEVRNVSKRF---GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED--ATDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISYGLPTVP-FEMVVEAAQKANAHGFIMELQ-DGYSTETGekgAQLSGGQKQRVAMARALVRN 656
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPrSERPPEAEIRAKVHELLKLVQlDWLADRYP---AQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 657 PPVLILDEATSALDAEseylIQQAIHGNLQR------HTVLIIAHRLS-TVERAHLIVVLDKGRVVQQGTHQQL 723
Cdd:cd03296 155 PKVLLLDEPFGALDAK----VRKELRRWLRRlhdelhVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
498-723 |
2.54e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 116.03 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 498 GRVDFENVTFTYRT-RPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHR 576
Cdd:PTZ00243 1307 GSLVFEGVQMRYREgLP--LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VISLVSQEPVLFARSITDNISYGLPTVPFEmVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRN 656
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 657 PPVLIL-DEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQL 723
Cdd:PTZ00243 1464 GSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
515-693 |
3.01e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.49 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 515 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITD 594
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 595 NISYglptvPFEMvveAAQKANAHGFIMELQD-GYSTETGEKG-AQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 672
Cdd:PRK10247 100 NLIF-----PWQI---RNQQPDPAIFLDDLERfALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180
....*....|....*....|.
gi 66932952 673 SEYLIQQAIHGNLQRHTVLII 693
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVL 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
510-739 |
6.11e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.85 E-value: 6.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 510 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD---HKYLHRVISLVSQEP- 585
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 586 --VLFARSITDNIsyGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTEtgeKGAQLSGGQKQRVAMARALVRNPPVLI 661
Cdd:PRK10419 100 saVNPRKTVREII--REPLRHLLSLDKAERLARASEMLraVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 662 LDEATSALDaeseyLIQQA----IHGNLQRHT---VLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 733
Cdd:PRK10419 175 LDEAVSNLD-----LVLQAgvirLLKKLQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTFSSPAGRV 249
|
....*.
gi 66932952 734 VQRQML 739
Cdd:PRK10419 250 LQNAVL 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
513-715 |
6.90e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.03 E-value: 6.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 513 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIG------AYDHKylhrvISLVSQEPV 586
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdAQAAG-----IAIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 LFA-RSITDNISYG-LPTVPF-----EMVVEAAQKANAHGFIMELqdgySTETGEkgaqLSGGQKQRVAMARALVRNPPV 659
Cdd:COG1129 90 LVPnLSVAENIFLGrEPRRGGlidwrAMRRRARELLARLGLDIDP----DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 660 LILDEATSAL-DAESEYLIqqAIHGNLQRH--TVLIIAHRLSTVER-AHLIVVLDKGRVV 715
Cdd:COG1129 162 LILDEPTASLtEREVERLF--RIIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLV 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
508-724 |
1.20e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.78 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 508 TYRtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVL 587
Cdd:PRK13548 9 SVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 588 -FARSITDNISYGL-----PTVPFEMVVEAAqkanahgfiMELQD--GYStetGEKGAQLSGGQKQRVAMARALVR---- 655
Cdd:PRK13548 88 sFPFTVEEVVAMGRaphglSRAEDDALVAAA---------LAQVDlaHLA---GRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 656 --NPPVLILDEATSALDaeseyLIQQaihgnlqrHTVLIIAHRLsTVER-----------------AHLIVVLDKGRVVQ 716
Cdd:PRK13548 156 dgPPRWLLLDEPTSALD-----LAHQ--------HHVLRLARQL-AHERglavivvlhdlnlaaryADRIVLLHQGRLVA 221
|
....*...
gi 66932952 717 QGTHQQLL 724
Cdd:PRK13548 222 DGTPAEVL 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
500-725 |
1.68e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVR 655
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 656 NPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
503-740 |
1.75e-25 |
|
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: 105.70 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLV 581
Cdd:cd03218 4 ENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPVLFAR-SITDNISYGLPTVPFEmvvEAAQKANAHGFIMELQdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 660
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLS---KKEREEKLEELLEEFH--ITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 661 ILDEATSALDAESEYLIQQAIHGNLQRHT-VLIIAHR----LSTVERAHLIVvldKGRVVQQGTHQQLLAQgglyaKLVQ 735
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNvretLSITDRAYIIY---EGKVLAEGTPEEIAAN-----ELVR 227
|
....*
gi 66932952 736 RQMLG 740
Cdd:cd03218 228 KVYLG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
514-723 |
1.76e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 514 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKpigayDHKYLH---RVISLVSQEPVLFaR 590
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-----DVSRLHardRKVGFVFQHYALF-R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SIT--DNISYGLPTVPfemvveAAQKANAHGF---IMELQDGYSTE--TGEKGAQLSGGQKQRVAMARALVRNPPVLILD 663
Cdd:PRK10851 88 HMTvfDNIAFGLTVLP------RRERPNAAAIkakVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 664 EATSALDAE-----SEYLIQqaIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQL 723
Cdd:PRK10851 162 EPFGALDAQvrkelRRWLRQ--LHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
510-726 |
2.03e-25 |
|
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: 111.31 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 510 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSC----VNILEnfyplQGGRVLLDGKPIGAYDHKYLHRV---ISLVS 582
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSRRALRPLrrrMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPvlFA-----RSITDNISYGLpTVPF---------EMVVEAAQKAnahGFIMELQDGYSTEtgekgaqLSGGQKQRVA 648
Cdd:COG4172 369 QDP--FGslsprMTVGQIIAEGL-RVHGpglsaaerrARVAEALEEV---GLDPAARHRYPHE-------FSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 649 MARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQ 721
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDV----SVQAQILDllrDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTE 511
|
....*
gi 66932952 722 QLLAQ 726
Cdd:COG4172 512 QVFDA 516
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
178-447 |
2.07e-25 |
|
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: 107.16 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 178 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRL 257
Cdd:cd18567 1 KRALLQILLLSLALELFAL---ASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 258 RNCLFRSLVSQETSFFdENR-TGDLISRLTSDTTMVSDLVSQNINIFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 336
Cdd:cd18567 78 TSNLFRHLLRLPLSYF-EKRhLGDIVSRFGSLDEIQQTLTTGFVEALL-DGLMAILTLVMMFLYSPKLALIVLAAVALYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 337 MVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTL 416
Cdd:cd18567 156 LLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLF 235
|
250 260 270
....*....|....*....|....*....|.
gi 66932952 417 LVVQVSILYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:cd18567 236 GLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
518-702 |
2.91e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.02 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP--LQGGRVLLDGKPIGA--YDHKYLHRVISLVSQEPVLFAR 590
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPgfRVEGKVTFHGKNLYApdVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SITDNISYGlPTV-----PFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 665
Cdd:PRK14243 106 SIYDNIAYG-ARIngykgDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 66932952 666 TSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVER 702
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAAR 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
521-729 |
3.70e-25 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 107.89 E-value: 3.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 521 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDG-------KPIGAYDHKylhRVISLVSQEPVLFAR-SI 592
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEK---RRIGYVFQEARLFPHlSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 TDNISYGL--PTVPFEMVVEAAqkanahgfIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 670
Cdd:TIGR02142 93 RGNLRYGMkrARPSERRISFER--------VIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 671 AESEYLIQQAIHgNLQRHT---VLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQGGL 729
Cdd:TIGR02142 164 DPRKYEILPYLE-RLHAEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
510-723 |
4.68e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 106.74 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 510 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYL---HRVISLVSQEPv 586
Cdd:COG4608 26 RTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 lFA-----RSITDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGA-QLSGGQKQRVAMARALVRNPP 658
Cdd:COG4608 105 -YAslnprMTVGDIIAEPL------RIHGLASKAERRERVAELLElvGLRPEHADRYPhEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 659 VLILDEATSALDAeSeylIQ-QAIhgN----LQR---HTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQL 723
Cdd:COG4608 178 LIVCDEPVSALDV-S---IQaQVL--NlledLQDelgLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
516-725 |
6.00e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 6.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 516 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLQG----GRVLLDG-KPIGAYDH--KYLHRVISLVSQEP 585
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ--PEAGtirvGDITIDTaRSLSQQKGliRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 586 VLFA-RSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 664
Cdd:PRK11264 95 NLFPhRTVLENIIEG----PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 665 ATSALDAESEYLIQQAIHGNLQ-RHTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
500-747 |
6.63e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY---PLQGGRVLLDGKPIGAYDHKYLHR 576
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VISLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDGystetgeKGAQLSGGQKQRVAMARA 652
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLADVGMLDYIDS-------EPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 653 LVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVERAHLIVVLDKGrvvqqgthqQLLAQGG- 728
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIR-KLKKKnnlTVISITHDIDEANMADQVLVLDDG---------KLLAQGSp 227
|
250 260
....*....|....*....|.
gi 66932952 729 --LYAKLVQRQMLGLEHPLDY 747
Cdd:PRK13640 228 veIFSKVEMLKEIGLDIPFVY 248
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
510-725 |
7.49e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.41 E-value: 7.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 510 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGgRVLLDGKPIGAYDHKYL---HRVISLVSQEP- 585
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 586 -VLFAR-SITDNISYGLPTvpFEMVVEAAQKANAHGFIMElQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLIL 662
Cdd:PRK15134 373 sSLNPRlNVLQIIEEGLRV--HQPTLSAAQREQQVIAVME-EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 663 DEATSALDAESEYLIQQAIHGNLQRHTV--LIIAHRLSTVeRA--HLIVVLDKGRVVQQGTHQQLLA 725
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVV-RAlcHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
502-723 |
8.61e-25 |
|
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: 103.92 E-value: 8.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfypLQGGRVLLDGKPIGAYDHKYLHRV- 577
Cdd:TIGR02315 4 VENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTllrCINRLVE---PSSGSILLEGTDITKLRGKKLRKLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 --ISLVSQEPVLFAR-SITDNISYG----LPTVP--FEMVVEAaQKANAhgfiMELQD--GYSTETGEKGAQLSGGQKQR 646
Cdd:TIGR02315 79 rrIGMIFQHYNLIERlTVLENVLHGrlgyKPTWRslLGRFSEE-DKERA----LSALErvGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 647 VAMARALVRNPPVLILDEATSALDAES-----EYLIQQAIHGNLqrhTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTH 720
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTskqvmDYLKRINKEDGI---TVIINLHQVDLAKKyADRIVGLKAGEIVFDGAP 230
|
...
gi 66932952 721 QQL 723
Cdd:TIGR02315 231 SEL 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
500-734 |
8.67e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.82 E-value: 8.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 652
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVR---MWDFRD-------KPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 653 LVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQRHTVLIIAHRLS-TVERAHLIVVLDKGRVVQQG-----THQQLLA 725
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVE 232
|
....*....
gi 66932952 726 QGGLYAKLV 734
Cdd:PRK13647 233 QAGLRLPLV 241
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
184-447 |
9.91e-25 |
|
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: 105.34 E-value: 9.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKS---------------MDQFTTAVVVVCLLAIGSSLAAGIRGGIFTL 248
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEAsflplvpaslgpadpRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 249 VFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVT 328
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 329 FMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRkeAAAYMS- 407
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANW--RAIRLRa 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 66932952 408 -YVWGSGLTLLVVQVSILYYGGHLVISG------QMSSGNLIAFIIY 447
Cdd:cd18565 239 aFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFY 285
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
514-741 |
1.06e-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: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 514 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQEPVLFAR-S 591
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 592 ITDNISYGLPTVPFEMVVEAAQKanahgFIMEL---------QdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLIL 662
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRADLE-----RVYELfprlkerrrQ---------RAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 663 DEATSALDAeseyLIQQAIHGNLQR-----HTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGTHQQLLAQGGlyaklVQR 736
Cdd:COG0410 161 DEPSLGLAP----LIVEEIFEIIRRlnregVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLADPE-----VRE 231
|
....*
gi 66932952 737 QMLGL 741
Cdd:COG0410 232 AYLGV 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
461-734 |
1.31e-24 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 110.81 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 461 VYSGLMQGVGAAEKVFEFIDRQptmvhdgSLAPDHLEGR---------VDFENVTFTY-RTRPHTqvLQNVSFSLSPGKV 530
Cdd:TIGR00957 596 VISSIVQASVSLKRLRIFLSHE-------ELEPDSIERRtikpgegnsITVHNATFTWaRDLPPT--LNGITFSIPEGAL 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 531 TALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKpigaydhkylhrvISLVSQEPVLFARSITDNISYGLPTVP--FEMV 608
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKALNEkyYQQV 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 609 VEAAqkanahGFIMELQ---DGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE-SEYLIQQAI--H 682
Cdd:TIGR00957 734 LEAC------ALLPDLEilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgpE 807
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 66932952 683 GNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 734
Cdd:TIGR00957 808 GVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
503-718 |
2.41e-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: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYR-TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDG-----KPIGAydhkylHR 576
Cdd:cd03266 5 DALTKRFRdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEA------RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VISLVSQEPVLFAR-SITDNISY-----GLptvpfemvveaaQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVA 648
Cdd:cd03266 79 RLGFVSDSTGLYDRlTARENLEYfaglyGL------------KGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 649 MARALVRNPPVLILDEATSALDAESEYLIQQAI-HGNLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIrQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
503-735 |
2.65e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.83 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLQGGRVLLDGKpigaydhkylhrvISLV 581
Cdd:PLN03130 618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPVLFARSITDNISYGLPTVP--FEMVVEAAqkANAHGFIMeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 659
Cdd:PLN03130 685 PQVSWIFNATVRDNILFGSPFDPerYERAIDVT--ALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 660 LILDEATSALDAE-SEYLIQQAIHGNLQRHTVLIIA---HRLSTVERahlIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQ 735
Cdd:PLN03130 762 YIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTnqlHFLSQVDR---IILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
504-744 |
2.82e-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: 102.96 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 504 NVTFTYRT------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD---HKYL 574
Cdd:TIGR02769 7 DVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 575 HRVISLVSQE-PVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGfIMELQDGYSTETGEKGAQLSGGQKQRVAMARAL 653
Cdd:TIGR02769 87 RRDVQLVFQDsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAE-LLDMVGLRSEDADKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTV--LIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQGGLY 730
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFKHPA 245
|
250
....*....|....
gi 66932952 731 AKLVQRQMLGlEHP 744
Cdd:TIGR02769 246 GRNLQSAVLP-EHP 258
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
184-446 |
3.00e-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: 103.79 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALgetFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFR 263
Cdd:cd18568 7 ILLASLLLQLLGL---ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 343
Cdd:cd18568 84 HLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 344 KYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEE-----EAEvFLRKLQQVYklnRKEAAAYMSYVWGSGLTLLv 418
Cdd:cd18568 163 PKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPirwrwENK-FAKALNTRF---RGQKLSIVLQLISSLINHL- 237
|
250 260
....*....|....*....|....*...
gi 66932952 419 VQVSILYYGGHLVISGQMSSGNLIAFII 446
Cdd:cd18568 238 GTIAVLWYGAYLVISGQLTIGQLVAFNM 265
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
503-717 |
3.26e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.63 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTY-RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPI---GAydhkylHRvi 578
Cdd:COG4525 7 RHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpGA------DR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFA-RSITDNISYGLPtvpFEMVVEAAQKANAHGFI--MELQDgysteTGEKG-AQLSGGQKQRVAMARALV 654
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGLR---LRGVPKAERRARAEELLalVGLAD-----FARRRiWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 655 RNPPVLILDEATSALDAESEYLIQQAIHG--NLQRHTVLIIAHrlsTVERAHL----IVVLDK--GRVVQQ 717
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH---SVEEALFlatrLVVMSPgpGRIVER 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
507-732 |
7.06e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.01 E-value: 7.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 507 FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-------------ILENFY---PLQGGRVLLDGKPIGAYD 570
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigdKKNNHELITNPYSKKIKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 571 HKYLHRVISLVSQEP--VLFARSITDNISYGlPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGekgAQLSGGQKQRVA 648
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSYLERSP---FGLSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 649 MARALVRNPPVLILDEATSALDAESEYLIQQAI-HGNLQRHTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTD 266
|
....*.
gi 66932952 727 GGLYAK 732
Cdd:PRK13631 267 QHIINS 272
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
516-702 |
9.60e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.01 E-value: 9.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 516 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP--LQGGRVLLDGKPIGA--YDHKYLHRVISLVSQEPVLF 588
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 589 ARSITDNISYGL------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL 662
Cdd:PRK14239 99 PMSIYENVVYGLrlkgikDKQVLDEAVEKSLKGAS------IWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 66932952 663 DEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVER 702
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASR 212
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
231-458 |
1.07e-23 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 102.35 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 231 LAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKV 310
Cdd:cd18558 68 IGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 311 TGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRK 390
Cdd:cd18558 148 GTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQN 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 391 LQQVYKLNRKEAAAYMSYVWGSGLTLLVVQVSILYYGGHLVISGQMSSGNLI----AFIIYEFVLGDCMESV 458
Cdd:cd18558 228 LEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLtvffSVLIGAFSAGQQVPSI 299
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
252-762 |
1.90e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 106.98 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 252 RLNIRLRNCLFRSLVSQETSFFDENR----TGDLISRLTSDTTMVSdLVSQNINIFLRNTVKVTgvvVFMFSLSWQLSLV 327
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDANALQ-QIAEQLHGLWSAPFRII---VSMVLLYQQLGVA 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 328 TFMGFPIIMMV---SNIYGKYYKRLSKE-VQSALARASTTaEETISAMKTVRSFANEEEeaevFLRKLQQV----YKLNR 399
Cdd:PLN03232 443 SLFGSLILFLLiplQTLIVRKMRKLTKEgLQWTDKRVGII-NEILASMDTVKCYAWEKS----FESRIQGIrneeLSWFR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 400 KEA--AAYMSYVWGSgltlLVVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFE 477
Cdd:PLN03232 518 KAQllSAFNSFILNS----IPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEE 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 478 -FIDRQPTMVHDGSLAPDhlEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLQ 555
Cdd:PLN03232 594 lLLSEERILAQNPPLQPG--APAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAE 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 556 GGRVLLDGKpigaydhkylhrvISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGfiMELQDGYS-TETGE 634
Cdd:PLN03232 672 TSSVVIRGS-------------VAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTEIGE 736
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 635 KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE-SEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGR 713
Cdd:PLN03232 737 RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGM 816
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 66932952 714 VVQQGTHQQLLAQGGLYAKLVQRQmlgleHPLDYTASHKEPPSNTEHKA 762
Cdd:PLN03232 817 IKEEGTFAELSKSGSLFKKLMENA-----GKMDATQEVNTNDENILKLG 860
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
515-718 |
2.43e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.99 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 515 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILENFYPLQ--GGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFA 589
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 590 R-SITDNISYGLP--------TVPFEMVVEAAQKAnahgfimELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 660
Cdd:PRK14247 96 NlSIFENVALGLKlnrlvkskKELQERVRWALEKA-------QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 661 ILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
517-733 |
3.77e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.02 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDgkpigaydhkylhRVISLVSQEPVLFARSITDNI 596
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 597 SYGLPTVPFEM--VVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE- 672
Cdd:PTZ00243 742 LFFDEEDAARLadAVRVSQlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHv 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 673 SEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQlLAQGGLYAKL 733
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATL 877
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
501-726 |
6.02e-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: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 501 DFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLQGGRVLLDGKPIGAYDHKYLH 575
Cdd:COG4172 8 SVEDLSVAFGQGGGtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RV----ISLVSQEPV-----LFarSITDNISYGLptvpfeMVVEAAQKANAHGFIMELQDgystETGEKGA--------- 637
Cdd:COG4172 88 RIrgnrIAMIFQEPMtslnpLH--TIGKQIAEVL------RLHRGLSGAAARARALELLE----RVGIPDPerrldayph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 638 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQRHT---VLIIAHRLSTVER-AHLIVVLD 710
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQAQILDllkDLQRELgmaLLLITHDLGVVRRfADRVAVMR 231
|
250
....*....|....*.
gi 66932952 711 KGRVVQQGTHQQLLAQ 726
Cdd:COG4172 232 QGEIVEQGPTAELFAA 247
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
503-726 |
6.83e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.38 E-value: 6.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgAYDHKYLHRV---IS 579
Cdd:PRK13639 3 ETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVrktVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfiMElqdGYstetgEKGA--QLSGGQKQRVAMA 650
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGplnlgLSKEEVEKRVKEALKAVG----ME---GF-----ENKPphHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 651 RALVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
500-719 |
7.90e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.18 E-value: 7.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKpigayDHKYL---HR 576
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ-----DITHVpaeNR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VISLVSQEPVLFAR-SITDNISYGL--PTVPFE----MVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAM 649
Cdd:PRK09452 87 HVNTVFQSYALFPHmTVFENVAFGLrmQKTPAAeitpRVMEALRMVQLEEFA-----------QRKPHQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 650 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGnLQRH---TVLIIAH----RLSTVERahlIVVLDKGRVVQQGT 719
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKA-LQRKlgiTFVFVTHdqeeALTMSDR---IVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
500-725 |
8.87e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSScvnILENFYPL---QGGRVLLDGKPI----GAYD 570
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKST---LMQHFNALlkpSSGTITIAGYHItpetGNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 571 HKYLHRVISLVSQ--EPVLFARSITDNISYGLPTVPFEmvvEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRV 647
Cdd:PRK13641 80 LKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFS---EDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 648 AMARALVRNPPVLILDEATSALDAESEYLIQQaIHGNLQR--HTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGTHQQLL 724
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKagHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIF 233
|
.
gi 66932952 725 A 725
Cdd:PRK13641 234 S 234
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
181-444 |
1.10e-22 |
|
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: 99.12 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 181 VAFLVAASFFLIVAALgetFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNC 260
Cdd:cd18555 4 LISILLLSLLLQLLTL---LIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 261 LFRSLVSQETSFFDENRTGDLISRLTSdTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 340
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANS-NVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 341 IYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKeaAAYMSYVWGSGLTLL--V 418
Cdd:cd18555 160 LTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKK--KERLSNILNSISSSIqfI 237
|
250 260
....*....|....*....|....*.
gi 66932952 419 VQVSILYYGGHLVISGQMSSGNLIAF 444
Cdd:cd18555 238 APLLILWIGAYLVINGELTLGELIAF 263
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
500-724 |
1.19e-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: 97.85 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL--ENfYPLQGGRVLLDGKPIGAYDHKYLHRV 577
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgDL-PPTYGNDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEpvlFARSITDNIsyglpTVpFEMV-------------VEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQK 644
Cdd:COG1119 80 IGLVSPA---LQLRFPRDE-----TV-LDVVlsgffdsiglyrePTDEQRERARELLELL--GLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 645 QRVAMARALVRNPPVLILDEATSALDAES-EYLIQ--QAIHGNLQRHTVLiIAHRL----STVERAhliVVLDKGRVVQQ 717
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGArELLLAllDKLAAEGAPTLVL-VTHHVeeipPGITHV---LLLKDGRVVAA 224
|
....*..
gi 66932952 718 GTHQQLL 724
Cdd:COG1119 225 GPKEEVL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
518-715 |
1.26e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKP--IG----AYDHKylhrvISLVSQEPVLFAR- 590
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRsprdAIALG-----IGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SITDNISYGLPTVPFEMV--VEAAQKanahgfIMELQDGYstetG------EKGAQLSGGQKQRVAMARALVRNPPVLIL 662
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLdrKAARAR------IRELSERY----GldvdpdAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 663 DEATSAL-DAESEYLIqqAIHGNL--QRHTVLIIAHRLSTVER-AHLIVVLDKGRVV 715
Cdd:COG3845 166 DEPTAVLtPQEADELF--EILRRLaaEGKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
500-727 |
2.50e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.93 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGA-YDHKYLHR 576
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 V---ISLVSQ--EPVLFARSITDNISYGLPTvpFEMVVEAAqKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMA 650
Cdd:PRK13646 83 VrkrIGMVFQfpESQLFEDTVEREIIFGPKN--FKMNLDEV-KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 651 RALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQ---RHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLK-SLQtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 66932952 727 G 727
Cdd:PRK13646 237 K 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
503-672 |
2.57e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.63 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQ---GGRVLLDGKPIGAYdhKYLHRVIS 579
Cdd:COG4136 5 ENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISYGLP-TVPFE----MVVEAAQKANAHGFimelqdgystetGEKG-AQLSGGQKQRVAMARA 652
Cdd:COG4136 80 ILFQDDLLFPHlSVGENLAFALPpTIGRAqrraRVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRA 147
|
170 180
....*....|....*....|
gi 66932952 653 LVRNPPVLILDEATSALDAE 672
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAA 167
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
503-716 |
3.65e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPI---GAydhkylHRVIs 579
Cdd:PRK11248 5 SHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpGA------ERGV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfimelqdgystETGEKGA------QLSGGQKQRVAMAR 651
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLagVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 652 ALVRNPPVLILDEATSALDA----ESEYLIQQAIHGnlQRHTVLIIAHRL-STVERAHLIVVL--DKGRVVQ 716
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAftreQMQTLLLKLWQE--TGKQVLLITHDIeEAVFMATELVLLspGPGRVVE 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-725 |
4.87e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.70 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLQG----GRVLLDGKPIGAY-DHKYLHRVISLVSQEPVLFAR 590
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 670
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 671 AESEYLIQQAIHGNLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
513-712 |
5.83e-22 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 95.09 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 513 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV-NILENFYPLQG----GRVLLDGKPIGAYDHKYLHRViSLVSQEPVL 587
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRYSV-AYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 588 FARSITDNISYGLP--TVPFEMVVEAAqkaNAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 665
Cdd:cd03290 91 LNATVEENITFGSPfnKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 66932952 666 TSALDAE-SEYLIQQAIHGNLQ--RHTVLIIAHRLSTVERAHLIVVLDKG 712
Cdd:cd03290 168 FSALDIHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
500-718 |
1.21e-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: 93.88 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHkylHRvIS 579
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR---NR-IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLF-ARSITDNISY-----GLPTvpfemvvEAAQKANAHGF----IMELQDgystetgEKGAQLSGGQKQRVAM 649
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlaqlkGLKK-------EEARRRIDEWLerleLSEYAN-------KRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 650 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH--TVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIR-ELARAgkTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
506-726 |
1.22e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 95.29 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 506 TFTYRT----RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLV 581
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPvlfarsitdNISYGlPTVPFEMVVEAAQKANAH-----------------GFIMELQDGYSTEtgekgaqLSGGQK 644
Cdd:COG4167 93 FQDP---------NTSLN-PRLNIGQILEEPLRLNTDltaeereerifatlrlvGLLPEHANFYPHM-------LSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 645 QRVAMARALVRNPPVLILDEATSALDAEseyLIQQAIhgNL-----QRHTV--LIIAHRLSTVEraHL---IVVLDKGRV 714
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMS---VRSQII--NLmlelqEKLGIsyIYVSQHLGIVK--HIsdkVLVMHQGEV 228
|
250
....*....|..
gi 66932952 715 VQQGTHQQLLAQ 726
Cdd:COG4167 229 VEYGKTAEVFAN 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
502-695 |
1.30e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGkpiGAydhkylhrVISLV 581
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---GL--------RIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPVLFA-RSITDNISYGLPTV-------------PFEMVVEAAQKANAHGfIMELQDGYSTET--------------- 632
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELraleaeleeleakLAEPDEDLERLAELQE-EFEALGGWEAEAraeeilsglgfpeed 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 633 -GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES-----EYLIQqaihgnlQRHTVLIIAH 695
Cdd:COG0488 146 lDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN-------YPGTVLVVSH 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
503-725 |
1.65e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.33 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLV 581
Cdd:COG1137 7 ENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPVLFaRSIT--DNIsyglptvpfEMVVE------AAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARAL 653
Cdd:COG1137 84 PQEASIF-RKLTveDNI---------LAVLElrklskKEREERLEELLEEFGITHLRKS--KAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 654 VRNPPVLILDEATSALD--AESEylIQQAIHgNLQRH--TVLIIAHR----LSTVERAHLIvvlDKGRVVQQGTHQQLLA 725
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiAVAD--IQKIIR-HLKERgiGVLITDHNvretLGICDRAYII---SEGKVLAEGTPEEILN 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
503-716 |
2.24e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 93.65 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV---- 577
Cdd:COG4181 12 RGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLrarh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQE----PVLFARsitDNIsyglpTVPFEM--VVEAAQKANAhgfimELQD-GYSTETGEKGAQLSGGQKQRVAMA 650
Cdd:COG4181 92 VGFVFQSfqllPTLTAL---ENV-----MLPLELagRRDARARARA-----LLERvGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 651 RALVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQRHTVLIIA-HRLSTVERAHLIVVLDKGRVVQ 716
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFElNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
514-719 |
2.29e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 93.36 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 514 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQEPVLFAR-S 591
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 592 ITDNISYGLPTVPfemvveaAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 671
Cdd:TIGR03410 92 VEENLLTGLAALP-------RRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 66932952 672 ESEYLIQQAIhGNLQRH---TVLIIAHRLS-TVERAHLIVVLDKGRVVQQGT 719
Cdd:TIGR03410 165 SIIKDIGRVI-RRLRAEggmAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
509-726 |
2.96e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 509 YRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGaYDHK---YLHRVISLVSQEP 585
Cdd:PRK13636 13 YNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmKLRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 586 --VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLI 661
Cdd:PRK13636 92 dnQLFSASVYQDVSFGAVNlkLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 662 LDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTVE-RAHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
503-719 |
3.36e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.61 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVS 582
Cdd:COG4604 5 KNVSKRYGG---KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPVLFAR-SITDNISYG-------LPTVPFEMVVEAAqkanahgfI-----MELQDGYSTEtgekgaqLSGGQKQR--V 647
Cdd:COG4604 82 QENHINSRlTVRELVAFGrfpyskgRLTAEDREIIDEA--------IayldlEDLADRYLDE-------LSGGQRQRafI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 648 AMarALVRNPPVLILDEATSALDaeseylIQQA--IHGNLQRH------TVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:COG4604 147 AM--VLAQDTDYVLLDEPLNNLD------MKHSvqMMKLLRRLadelgkTVVIVLHDINFASCyADHIVAMKDGRVVAQG 218
|
.
gi 66932952 719 T 719
Cdd:COG4604 219 T 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
500-728 |
3.68e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.79 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGaYDHKylhRVIS 579
Cdd:COG4152 2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDR---RRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISY-----GLPtvpfemvvEAAQKANAHGFI--MELQDgYSTETGEKgaqLSGGQKQRVAMAR 651
Cdd:COG4152 75 YLPEERGLYPKmKVGEQLVYlarlkGLS--------KAEAKRRADEWLerLGLGD-RANKKVEE---LSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIhgnLQRH----TVLIIAHRLSTVERahL---IVVLDKGRVVQQGTHQQLL 724
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVI---RELAakgtTVIFSSHQMELVEE--LcdrIVIINKGRKVLSGSVDEIR 217
|
....
gi 66932952 725 AQGG 728
Cdd:COG4152 218 RQFG 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
497-704 |
4.03e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.96 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 497 EGRVDFENVTFTyrtRPHTQVL-QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLdgkPIGAydhkylh 575
Cdd:COG4178 360 DGALALEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---PAGA------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RVIsLVSQEPVLFARSITDNISYGLPTVPF--EMVVEAAQKANAHGFIMELQdgystETGEKGAQLSGGQKQRVAMARAL 653
Cdd:COG4178 427 RVL-FLPQRPYLPLGTLREALLYPATAEAFsdAELREALEAVGLGHLAERLD-----EEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRlSTVERAH 704
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAFH 550
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
517-726 |
4.18e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.56 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNI---LENfyPlQGGRVLLDGKPIGayDHKYLHRVISLVSQEPVLFAR-SI 592
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLvagLEK--P-TEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 TDNISYGLPT--VPFE----MVVEAAQKANAHGFimelQDGYSTetgekgaQLSGGQKQRVAMARALVRNPPVLILDEAT 666
Cdd:PRK11432 96 GENVGYGLKMlgVPKEerkqRVKEALELVDLAGF----EDRYVD-------QISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 667 SALDAESEYLIQQAIHgNLQRH---TVLIIAHRLS-TVERAHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:PRK11432 165 SNLDANLRRSMREKIR-ELQQQfniTSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
185-444 |
4.50e-21 |
|
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: 94.10 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 185 VAASFFLIVAALGetfLPYYTGRAIDSIVIQKSMDqfTTAVVVVCLLAIG--SSLAAGIRGGIFTLVFARLNIRLRNCLF 262
Cdd:cd18588 8 LLASLFLQLFALV---TPLFFQVIIDKVLVHRSLS--TLDVLAIGLLVVAlfEAVLSGLRTYLFSHTTNRIDAELGARLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 263 RSLVSQETSFFDENRTGDLISR----------LTSDT-TMVSDLVSqnINIFLrntvkvtgvvVFMFSLSWQLSLVTFMG 331
Cdd:cd18588 83 RHLLRLPLSYFESRQVGDTVARvrelesirqfLTGSAlTLVLDLVF--SVVFL----------AVMFYYSPTLTLIVLAS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 332 FPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEeeeaEVFLRKLQQvyKLNRKEAAAY---MSY 408
Cdd:cd18588 151 LPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVE----PQFQRRWEE--LLARYVKASFktaNLS 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 66932952 409 VWGSGLTLLVVQVS---ILYYGGHLVISGQMSSGNLIAF 444
Cdd:cd18588 225 NLASQIVQLIQKLTtlaILWFGAYLVMDGELTIGQLIAF 263
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
500-744 |
5.07e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.90 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDH-KYLHRV 577
Cdd:PRK13644 2 IRLENVSYSY---PDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAqkanahgfIMELQDGYSTETGEKgaQLSGGQKQRVAMA 650
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRA--------LAEIGLEKYRHRSPK--TLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 651 RALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQR--HTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGG 728
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIK-KLHEkgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
250
....*....|....*.
gi 66932952 729 LyaklvqrQMLGLEHP 744
Cdd:PRK13644 228 L-------QTLGLTPP 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
501-724 |
7.25e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 7.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 501 DFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQG------GRVLLDGKPIGAYDHKYL 574
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 575 HRVISLVSQEPVLFAR-SITDNISYGLPTVPFE-------MVVEAAQKAnahGFIMELQDGYSTetgeKGAQLSGGQKQR 646
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKekreikkIVEECLRKV---GLWKEVYDRLNS----PASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 647 VAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLL 724
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
502-704 |
7.69e-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: 89.91 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFtyRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVlldgkpigaydHKYLHRVISLV 581
Cdd:cd03223 3 LENLSL--ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPVLFARSITDNISYglptvPFEMVveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 661
Cdd:cd03223 70 PQRPYLPLGTLREQLIY-----PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 66932952 662 LDEATSALDAESEyliqQAIHGNLQRH--TVLIIAHRlSTVERAH 704
Cdd:cd03223 115 LDEATSALDEESE----DRLYQLLKELgiTVISVGHR-PSLWKFH 154
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
503-714 |
8.85e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.43 E-value: 8.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAydhkyLHRVISLVS 582
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPVLFA-RSITDNISYGLptvpfemvvEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLI 661
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGL---------KGQWRDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 662 LDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLS-TVERAHLIVVLDKGRV 714
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
500-719 |
9.98e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.52 E-value: 9.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKylHRVIS 579
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISYGLPT--VP----FEMVVEAAQkanahgfIMELQ---DgystetgEKGAQLSGGQKQRVAM 649
Cdd:PRK11650 80 MVFQNYALYPHmSVRENMAYGLKIrgMPkaeiEERVAEAAR-------ILELEpllD-------RKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 650 ARALVRNPPVLILDEATSALDA--------EseylIQQaihgnLQRhtvliiahRLST---------VER---AHLIVVL 709
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAklrvqmrlE----IQR-----LHR--------RLKTtslyvthdqVEAmtlADRVVVM 208
|
250
....*....|
gi 66932952 710 DKGRVVQQGT 719
Cdd:PRK11650 209 NGGVAEQIGT 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
517-694 |
1.01e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.09 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHK----YL-HRVislvSQEPVLfarS 591
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHRN----AMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 592 ITDNIS-----YGlptvPFEMVVEAAQKANAHGFIMELQDGYstetgekgaqLSGGQKQRVAMARALVRNPPVLILDEAT 666
Cdd:PRK13539 90 VAENLEfwaafLG----GEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 66932952 667 SALDAESEYLIQQAIHGNLQRHTVLIIA 694
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
503-719 |
2.80e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.65 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKY--LHRVI 578
Cdd:PRK13637 6 ENLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEP--VLFARSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQdGYSTET-GEKGA-QLSGGQKQRVAMARALV 654
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAFG----PINLGLSEEEIENRVKRAMNIV-GLDYEDyKDKSPfELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 655 RNPPVLILDEATSALD--AESEYLIQ-QAIHGNLQrHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGT 719
Cdd:PRK13637 161 MEPKILILDEPTAGLDpkGRDEILNKiKELHKEYN-MTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
503-702 |
3.36e-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: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENV--TFTYRTRPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSS---CvnILENFYPlQGGRVLL--DGKPI---GAYD 570
Cdd:COG4778 8 ENLskTFTLHLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTllkC--IYGNYLP-DSGSILVrhDGGWVdlaQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 571 HKYLH---RVISLVSQepvlFARSItdnisyglPTVP-FEMVVEAAqkanahgfimeLQDGYSTETG-EKGAQL------ 639
Cdd:COG4778 85 REILAlrrRTIGYVSQ----FLRVI--------PRVSaLDVVAEPL-----------LERGVDREEArARARELlarlnl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 640 ------------SGGQKQRVAMARALVRNPPVLILDEATSALDAESE----YLIQQAihgnLQRHTVLI-IAHRLSTVER 702
Cdd:COG4778 142 perlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEA----KARGTAIIgIFHDEEVREA 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
500-732 |
6.69e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.63 E-value: 6.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:PRK13652 4 IETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 652
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpinlgLDEETVAHRVSSALHMLG---LEELRD-------RVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 653 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGTHQQLLAQGGL 729
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
...
gi 66932952 730 YAK 732
Cdd:PRK13652 232 LAR 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
510-730 |
7.23e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.34 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 510 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP---LQGGRVLLDGKPIGAydhKYLHRVISLVSQepv 586
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA---KEMRAISAYVQQ--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 lfarsitDNISYGLPTVPFEMVVEAAQKANAHGFI-------------MELQDGYSTETGEKGAQ--LSGGQKQRVAMAR 651
Cdd:TIGR00955 107 -------DDLFIPTLTVREHLMFQAHLRMPRRVTKkekrervdevlqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQR-HTVLIIAHRLST--VERAHLIVVLDKGRVVQQGTHQQL---LA 725
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAvpfFS 259
|
....*
gi 66932952 726 QGGLY 730
Cdd:TIGR00955 260 DLGHP 264
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
178-446 |
7.41e-20 |
|
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: 90.73 E-value: 7.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 178 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRL 257
Cdd:cd18782 1 RRALIEVLALSFVVQLLGL---ANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 258 RNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 337
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 338 VSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEE----EEAEVFLRKLQQVYKLNRkeaaayMSYVWGSG 413
Cdd:cd18782 157 LTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELkarwRWQNRYARSLGEGFKLTV------LGTTSGSL 230
|
250 260 270
....*....|....*....|....*....|....*
gi 66932952 414 LTLL--VVQVSILYYGGHLVISGQMSSGNLIAFII 446
Cdd:cd18782 231 SQFLnkLSSLLVLWVGAYLVLRGELTLGQLIAFRI 265
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
517-694 |
1.02e-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: 87.93 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNI 596
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 597 SYGLPTVPFEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 676
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNGF-----------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170
....*....|....*...
gi 66932952 677 IQQAIHGNLQRHTVLIIA 694
Cdd:cd03231 164 FAEAMAGHCARGGMVVLT 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
512-726 |
1.91e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.02 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 512 RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDH---KYLHRVISLVSQ--- 583
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQnpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 584 --------------EPVLfarsITDNISyglptvpfemVVEAAQKANAhgfiMELQDGYSTE-TGEKGAQLSGGQKQRVA 648
Cdd:PRK11308 103 gslnprkkvgqileEPLL----INTSLS----------AAERREKALA----MMAKVGLRPEhYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 649 MARALVRNPPVLILDEATSALDAEseylIQQAIHG---NLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQ 721
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVS----VQAQVLNlmmDLQQElglSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKE 240
|
....*
gi 66932952 722 QLLAQ 726
Cdd:PRK11308 241 QIFNN 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
517-718 |
2.20e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV-ISLVSQEPVLFAR-SITD 594
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 595 NISYGLPTVPfemvvEAAQKANAhgFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD-AES 673
Cdd:PRK15439 106 NILFGLPKRQ-----ASMQKMKQ--LLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 66932952 674 EYLIQQAIHGNLQRHTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQG 718
Cdd:PRK15439 177 ERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
517-723 |
2.32e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.66 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgAYDHKYLhRVISLVSQEPVLFAR-SITDN 595
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQ-RPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 596 ISYGLPTVPFEMVvEAAQKANAHGFIMELQDGysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 675
Cdd:PRK11607 112 IAFGLKQDKLPKA-EIASRVNEMLGLVHMQEF----AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 66932952 676 LIQQAIHGNLQR--HTVLIIAH-RLSTVERAHLIVVLDKGRVVQQGTHQQL 723
Cdd:PRK11607 187 RMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
500-724 |
2.45e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAydHKYLHRV-I 578
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARArI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQ----EPVLFARsitDNI-----SYGLPTVPFEMVV----EAAQ---KANAhgfimelqdgystetgeKGAQLSGG 642
Cdd:PRK13536 117 GVVPQfdnlDLEFTVR---ENLlvfgrYFGMSTREIEAVIpsllEFARlesKADA-----------------RVSDLSGG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 643 QKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQR-HTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTH 720
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRP 256
|
....
gi 66932952 721 QQLL 724
Cdd:PRK13536 257 HALI 260
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
500-725 |
3.20e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.09 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 L-----------VSQEPVLFARSitdnisYGLPT------VPfeMVVEAA---QKANAhgfimelqdgystetgeKGAQL 639
Cdd:PRK13537 85 VpqfdnldpdftVRENLLVFGRY------FGLSAaaaralVP--PLLEFAkleNKADA-----------------KVGEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 640 SGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQR-HTVLIIAHRLSTVER-AHLIVVLDKGRVVQQ 717
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAE 219
|
....*...
gi 66932952 718 GTHQQLLA 725
Cdd:PRK13537 220 GAPHALIE 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
518-724 |
3.95e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.48 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV----ISLVSQEPVLFAR-SI 592
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 TDNISYG--LPTVPFEMVVEAAQKANAHGFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALD 670
Cdd:PRK10070 124 LDNTAFGmeLAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 671 A------ESEYLIQQAIHgnlqRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLL 724
Cdd:PRK10070 197 PlirtemQDELVKLQAKH----QRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
500-720 |
4.37e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 87.38 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDG------KPIGAYDHKY 573
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 574 LHRVISLVSQEPVLFA-RSITDNISYGlPTVPFEMVVEAAQ-KANAHGFIMELQDgystETGEKGAQLSGGQKQRVAMAR 651
Cdd:COG4161 80 LRQKVGMVFQQYNLWPhLTVMENLIEA-PCKVLGLSKEQAReKAMKLLARLRLTD----KADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH--TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTH 720
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIR-ELSQTgiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
503-721 |
4.85e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILEnfYPLQG-----GRVLLDGKPIGAYDHKYL 574
Cdd:PRK11124 6 NGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLrvlNLLE--MPRSGtlniaGNHFDFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 575 HRVISLVSQEPVLFAR-SITDNisygLPTVPfeMVVEAAQKANAHGFIMELQDGYS-TETGEK-GAQLSGGQKQRVAMAR 651
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHlTVQQN----LIEAP--CRVLGLSKDQALARAEKLLERLRlKPYADRfPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH-TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQ 721
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
514-719 |
4.85e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.79 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 514 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPI----GAYDHKYLHRVISLVSQepvlFA 589
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRNQKLGFIYQ----FH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 590 RSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 669
Cdd:PRK11629 97 HLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 66932952 670 DAESEYLIQQAIhGNLQRH---TVLIIAHRLSTVERAHLIVVLDKGRVVQQGT 719
Cdd:PRK11629 177 DARNADSIFQLL-GELNRLqgtAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
503-745 |
4.92e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.26 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLV 581
Cdd:PRK10895 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPVLFAR-SITDNIsygLPTVPFEMVVEAAQKANAHGFIME------LQDGYstetgekGAQLSGGQKQRVAMARALV 654
Cdd:PRK10895 84 PQEASIFRRlSVYDNL---MAVLQIRDDLSAEQREDRANELMEefhiehLRDSM-------GQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 655 RNPPVLILDEATSALDAESEYLIQQAI-HGNLQRHTVLIIAHR----LSTVERAHLIvvlDKGRVVQQGTHQQLLAQggl 729
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIeHLRDSGLGVLITDHNvretLAVCERAYIV---SQGHLIAHGTPTEILQD--- 227
|
250
....*....|....*.
gi 66932952 730 yaKLVQRQMLGLEHPL 745
Cdd:PRK10895 228 --EHVKRVYLGEDFRL 241
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
512-694 |
5.16e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 85.87 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 512 RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYlHRVISLVSQEPVLFAR- 590
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SITDNISYGLPTVPFE--MVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 668
Cdd:TIGR01189 89 SALENLHFWAAIHGGAqrTIEDALAAVGLTGF-----------EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 66932952 669 LDAESEYLIQQAIHGNLQRHTVLIIA 694
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLT 183
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
500-723 |
5.45e-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: 86.27 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgAYDHKYLHRVIS 579
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLfARSIT--DNIS-----YGLPTvpfemvVEAAQKanahgfIMELQDGYstETGEKGAQL----SGGQKQRVA 648
Cdd:cd03265 77 IVFQDLSV-DDELTgwENLYiharlYGVPG------AERRER------IDELLDFV--GLLEAADRLvktySGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 649 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQL 723
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
500-719 |
8.57e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.11 E-value: 8.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAY----DHKY 573
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 574 LHRVISLVSQ--EPVLFARSITDNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMA 650
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQN--FGVSQEEAEALAREKLALV---GISESLFEKNPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 651 RALVRNPPVLILDEATSALDA----ESEYLIQQAIHGNLqrhTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGT 719
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPkgrkELMTLFKKLHQSGM---TIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
503-744 |
8.63e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.77 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHR-VISLV 581
Cdd:PRK10575 15 RNVSFRV---PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPVLFARSITDNISYGlpTVPF------------EMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAM 649
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIG--RYPWhgalgrfgaadrEKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 650 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTVER--AHLiVVLDKGRVVQQGTHQQLLa 725
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARycDYL-VALRGGEMIAQGTPAELM- 236
|
250
....*....|....*....
gi 66932952 726 QGGLYAKLVQRQMLGLEHP 744
Cdd:PRK10575 237 RGETLEQIYGIPMGILPHP 255
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
184-446 |
1.00e-18 |
|
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: 87.25 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGetfLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFR 263
Cdd:cd18566 7 VLLASLFINILALA---TPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLrntvKVTGVVVF---MFSLSWQLSLVTFMGFPIIMMVSN 340
Cdd:cd18566 84 HLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALL----DLPFVLIFlglIWYLGGKLVLVPLVLLGLFVLVAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 341 IYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEeeeaEVFLRKLQQVYK---LNRKEAAAYMSYVWGSGLTL- 416
Cdd:cd18566 160 LLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAME----PQMLRRYERLQAnaaYAGFKVAKINAVAQTLGQLFs 235
|
250 260 270
....*....|....*....|....*....|
gi 66932952 417 LVVQVSILYYGGHLVISGQMSSGNLIAFII 446
Cdd:cd18566 236 QVSMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
226-664 |
1.68e-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: 89.47 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 226 VVVCLLAIGSSLAAGIRggiFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSqNINIFLR 305
Cdd:COG4615 55 AGLLVLLLLSRLASQLL---LTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 306 NTVKVTGVVVFMFSLSWQLSLVTFmgfpiIMMVSNIYGkyYKRLSKEVQSALARASTTAEETISAMKTVRSFANE----E 381
Cdd:COG4615 131 SVALVLGCLAYLAWLSPPLFLLTL-----VLLGLGVAG--YRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKElklnR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 382 EEAEVFLRKL-----QQVYKLNRKEAAAYMSYV-WGSgLTLLVVQVSILYYGGHLV-ISGQMSSGnlIAFIIYeFVLGDc 454
Cdd:COG4615 204 RRRRAFFDEDlqptaERYRDLRIRADTIFALANnWGN-LLFFALIGLILFLLPALGwADPAVLSG--FVLVLL-FLRGP- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 455 MESVGSVYSGLMQGVGAAEKVFEF---IDRQPTMVHDGSLAPDHLE-GRVDFENVTFTYRTRPHTQ--VLQNVSFSLSPG 528
Cdd:COG4615 279 LSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDEgfTLGPIDLTIRRG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 529 KVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGA--YDHkYLHRvISLVSQEPVLFARsitdniSYGLPTVPfe 606
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREA-YRQL-FSAVFSDFHLFDR------LLGLDGEA-- 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 607 mvveAAQKANAHGFIMELQ------DGYSTETgekgaQLSGGQKQRVAMARALVRNPPVLILDE 664
Cdd:COG4615 429 ----DPARARELLERLELDhkvsveDGRFSTT-----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
506-725 |
3.57e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.23 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 506 TFTYRT----RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLV 581
Cdd:PRK15112 13 TFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 SQEPvlfARSITDNISYG-LPTVPFEMVVEAAQKANAHGFIMEL-QDGYSTE-TGEKGAQLSGGQKQRVAMARALVRNPP 658
Cdd:PRK15112 93 FQDP---STSLNPRQRISqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 659 VLILDEATSALDAEseyLIQQAIHGNLQRHTVLIIAHRLSTverAHL---------IVVLDKGRVVQQGTHQQLLA 725
Cdd:PRK15112 170 VIIADEALASLDMS---MRSQLINLMLELQEKQGISYIYVT---QHLgmmkhisdqVLVMHQGEVVERGSTADVLA 239
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
499-718 |
4.77e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.37 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 499 RVDFENVTFTyrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKS-SCVNILENFYP---LQGGRVLLDGKPIGAYDHKyl 574
Cdd:PRK10418 4 QIELRNIALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVAPCALR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 575 HRVISLVSQEPvlfaRSITDNI----SYGLPTVpfemvvEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQ 645
Cdd:PRK10418 78 GRKIATIMQNP----RSAFNPLhtmhTHARETC------LALGKPADDATLTAALEAVGLENAARVLKLypfemSGGMLQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 646 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHT--VLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
518-713 |
7.74e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.29 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlQG---GRVLLDGKPIGAYDHKYLHRV-ISLVSQEPVLFAR-SI 592
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP-HGtyeGEIIFEGEELQASNIRDTERAgIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 TDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALdAE 672
Cdd:PRK13549 100 LENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPAT--PVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 66932952 673 SEYLIQQAIHGNLQRHTV--LIIAHRLSTVER-AHLIVVLDKGR 713
Cdd:PRK13549 177 SETAVLLDIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
498-733 |
8.24e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 8.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 498 GRVDFENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGA-----YD 570
Cdd:PRK13645 5 KDIILDNVSYTYakKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 571 HKYLHRVISLVSQEP--VLFARSITDNISYGlptvPFEMvveAAQKANAHGFIMELQDGYS--TETGEKGA-QLSGGQKQ 645
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFG----PVNL---GENKQEAYKKVPELLKLVQlpEDYVKRSPfELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 646 RVAMARALVRNPPVLILDEATSALD--AESEYL-IQQAIHGNlQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQ 721
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDpkGEEDFInLFERLNKE-YKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPF 236
|
250
....*....|..
gi 66932952 722 QLLAQGGLYAKL 733
Cdd:PRK13645 237 EIFSNQELLTKI 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
500-719 |
9.14e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRP--HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLQGGRVLLDGKPIGAYDHKYLHR 576
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 V---ISLVSQEP--VLFARSITDNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMA 650
Cdd:PRK13643 82 VrkkVGVVFQFPesQLFEETVLKDVAFGPQN--FGIPKEKAEKIAAEKLEMV---GLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 651 RALVRNPPVLILDEATSALDAESEYLIQ---QAIHGNLQrhTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGT 719
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQSGQ--TVVLVTHLMDDVaDYADYVYLLEKGHIISCGT 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
500-761 |
1.14e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV-I 578
Cdd:PRK09700 6 ISMAGIGKSF---GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQE-PVLFARSITDNISYG-LPT-----VPF----EMVVEAAqkanahgfIMELQDGYSTETGEKGAQLSGGQKQRV 647
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGrHLTkkvcgVNIidwrEMRVRAA--------MMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 648 AMARALVRNPPVLILDEATSAL-DAESEYLIqqAIHGNLQRH--TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQL 723
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRKEgtAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 66932952 724 LAQGglyaklVQRQMLGLEHPLDYTAsHKEPPSNTEHK 761
Cdd:PRK09700 233 SNDD------IVRLMVGRELQNRFNA-MKENVSNLAHE 263
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
228-743 |
1.29e-17 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 88.04 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 228 VCLLAIGSSLAagIRGGIFTLvfARLNIRLRNCLFrSLVSQET-----SFFDENRTGDLISrltsdttmvsdLVSQNINI 302
Cdd:TIGR01271 128 LCLLFIVRTLL--LHPAIFGL--HHLGMQMRIALF-SLIYKKTlklssRVLDKISTGQLVS-----------LLSNNLNK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 303 F-----LRNTVKVTGV-VVFMFSLSWQL---SLVTFMGFPIIMMV-----SNIYGKYYKRLSKEVQSALARASttaeETI 368
Cdd:TIGR01271 192 FdeglaLAHFVWIAPLqVILLMGLIWELlevNGFCGLGFLILLALfqaclGQKMMPYRDKRAGKISERLAITS----EII 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 369 SAMKTVRSFAnEEEEAEVFLRKLQQV-YKLNRKeaAAYMSYVWGSGL---TLLVVQVSILYYGghlvISGQMSSGNLIAF 444
Cdd:TIGR01271 268 ENIQSVKAYC-WEEAMEKIIKNIRQDeLKLTRK--IAYLRYFYSSAFffsGFFVVFLSVVPYA----LIKGIILRRIFTT 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 445 IIYEFVLgdcMESVGSVYSGLMQ----GVGAAEKVFEFIDRQPTMVHDGSLAPDHLEgrvdFENVT-------------- 506
Cdd:TIGR01271 341 ISYCIVL---RMTVTRQFPGAIQtwydSLGAITKIQDFLCKEEYKTLEYNLTTTEVE----MVNVTaswdegigelfeki 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 507 -----------------FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLQGgRVLLDGKpiga 568
Cdd:TIGR01271 414 kqnnkarkqpngddglfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEG-KIKHSGR---- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 569 ydhkylhrvISLVSQEPVLFARSITDNISYGLPTVPFEM--VVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQR 646
Cdd:TIGR01271 489 ---------ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYtsVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRAR 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 647 VAMARALVRNPPVLILDEATSALDAESEYLI-QQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:TIGR01271 557 ISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQA 636
|
570
....*....|....*...
gi 66932952 726 QGGLYAKlvqrQMLGLEH 743
Cdd:TIGR01271 637 KRPDFSS----LLLGLEA 650
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
502-712 |
1.31e-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: 81.52 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN--FYPLQGGRVLLDGKPIGaydhKYLHRVI 578
Cdd:cd03232 6 WKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD----KNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFarsitdnisyglptvPFEMVVEAAQ-KANAHGfimelqdgystetgekgaqLSGGQKQRVAMARALVRNP 657
Cdd:cd03232 82 GYVEQQDVHS---------------PNLTVREALRfSALLRG-------------------LSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 658 PVLILDEATSALDAESEYLIQQAIHgNLQRH--TVLIIAHRLSTV--ERAHLIVVLDKG 712
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLK-KLADSgqAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
510-718 |
1.43e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 510 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPI---GAYDHKYLHRVISLVSQEPV 586
Cdd:PRK10261 332 RVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 --LFAR-SITDNISYGLpTVPFEMVVEAAQKANAH-----GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPP 658
Cdd:PRK10261 412 asLDPRqTVGDSIMEPL-RVHGLLPGKAAAARVAWllervGLLPEHAWRYPHE-------FSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 659 VLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLL-DLQRDfgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
518-695 |
1.68e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 82.51 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgayDHKYLHRVIslVSQEPVLFA-RSITDNI 596
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGPDRMV--VFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 597 SYGLPTVPFEMVVEAAQKANAHGFIMElqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 676
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALV---GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|.
gi 66932952 677 IQQAIHGNLQRH--TVLIIAH 695
Cdd:TIGR01184 153 LQEELMQIWEEHrvTVLMVTH 173
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
518-724 |
1.90e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.58 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGgRVLLDGKPIGAYDHKYLHRVIS-LVSQEPVLFARSITDNI 596
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQG-EILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 597 SYGLPTVPFEMVVEA--AQKANAhgfiMELQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NPP--VLILDEATS 667
Cdd:COG4138 91 ALHQPAGASSEAVEQllAQLAEA----LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 668 ALDaeseyLIQQAIHGNLQRH------TVLIIAHRLS-TVERAHLIVVLDKGRVVQQGTHQQLL 724
Cdd:COG4138 163 SLD-----VAQQAALDRLLRElcqqgiTVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
516-718 |
3.29e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 81.16 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 516 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN---FYPLQGGRVLLDGKPIGAYDHKYlhrVISLVSQEPVlFARSI 592
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQK---CVAYVRQDDI-LLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 T--DNISYglpTVPFEMVVEA--AQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 668
Cdd:cd03234 97 TvrETLTY---TAILRLPRKSsdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 669 LDAESEYLI----QQAIHGNlqrHTVLIIAH--RLSTVERAHLIVVLDKGRVVQQG 718
Cdd:cd03234 174 LDSFTALNLvstlSQLARRN---RIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
257-447 |
3.51e-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: 82.85 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 257 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 336
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 337 MVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEaAAYMSYVWGSGLTL 416
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKH-TRWNAKTFSAVNTI 239
|
170 180 190
....*....|....*....|....*....|..
gi 66932952 417 L-VVQVSILYYGGHLVISGQMSSGNLIAFIIY 447
Cdd:cd18554 240 TdLAPLLVIGFAAYLVIEGNLTVGTLVAFVGY 271
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
502-727 |
4.09e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 82.38 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGA----YDHKYLH 575
Cdd:PRK13634 5 FQKVEHRYqyKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RVISLVSQ--EPVLFARSITDNISYGlPT---VPFEmvvEAAQKANAhgfIMELQdGYSTETGEKGA-QLSGGQKQRVAM 649
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFG-PMnfgVSEE---DAKQKARE---MIELV-GLPEELLARSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 650 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFY-KLHKEkglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
..
gi 66932952 726 QG 727
Cdd:PRK13634 236 DP 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
518-742 |
4.29e-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: 84.88 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP--LQGGRVLLDGKPIGAYDHKYLHRV-ISLVSQEPVLFAR-SIT 593
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 594 DNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGaQLSGGQKQRVAMARALVRNPPVLILDEATSAL-DA 671
Cdd:TIGR02633 97 ENIFLGNEiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEK 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 672 ESEYLIQqaIHGNLQRHTV--LIIAHRLSTVErahliVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLGLE 742
Cdd:TIGR02633 176 ETEILLD--IIRDLKAHGVacVYISHKLNEVK-----AVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGRE 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
500-715 |
5.39e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHK---YLHR 576
Cdd:PRK10908 2 IRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VISLVSQEP-VLFARSITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARAL 653
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVA--IP-----LIIAGASGDDIRRRVSAALDkvGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 654 VRNPPVLILDEATSALD-AESEYLIQQAIHGNLQRHTVLIIAHRLSTVE-RAHLIVVLDKGRVV 715
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDdALSEGILRLFEEFNRVGVTVLMATHDIGLISrRSYRMLTLSDGHLH 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
500-718 |
6.13e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.16 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGayDHKYLHRVIS 579
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISYGLPTVPFEMVvEAAQKANAHGFImeLQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPP 658
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGLKLAGAKKE-EINQRVNQVAEV--LQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 659 VLILDEATSALDAESEylIQQAI-----HGNLQRhTVLIIAHrlSTVER---AHLIVVLDKGRVVQQG 718
Cdd:PRK11000 154 VFLLDEPLSNLDAALR--VQMRIeisrlHKRLGR-TMIYVTH--DQVEAmtlADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
184-391 |
1.40e-16 |
|
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: 81.01 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFR 263
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVtfmgFPIIMMVSNIYG 343
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV----LPPLLVVYYLLQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 66932952 344 KYYKRLSKEVQ--SALARAS--TTAEETISAMKTVRSFANEEEEAEVFLRKL 391
Cdd:cd18580 157 RYYLRTSRQLRrlESESRSPlySHFSETLSGLSTIRAFGWQERFIEENLRLL 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
502-726 |
1.57e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 502 FENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPigaydHKY------LH 575
Cdd:PRK11288 7 FDGIGKTF---PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaaLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RVISLVSQE----PVLfarSITDNISYG-LPTvPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMA 650
Cdd:PRK11288 79 AGVAIIYQElhlvPEM---TVAENLYLGqLPH-KGGIVNRRLLNYEAREQLEHLGVDIDPDT--PLKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 651 RALVRNPPVLILDEATSALDA-ESEYLIqqAIHGNL--QRHTVLIIAHRLSTVER-AHLIVVLDKGRVV------QQGTH 720
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSArEIEQLF--RVIRELraEGRVILYVSHRMEEIFAlCDAITVFKDGRYVatfddmAQVDR 230
|
....*.
gi 66932952 721 QQLLAQ 726
Cdd:PRK11288 231 DQLVQA 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
501-726 |
2.01e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 501 DFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILEN---FYPlqGGRVLLDGKPIGAYDHK 572
Cdd:PRK15134 7 AIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYP--SGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 573 YLHRV----ISLVSQEPVlfarsITDNISYGLPTVPFEMVV--EAAQKANAHGFIMELQDgystETGEKGA--------- 637
Cdd:PRK15134 85 TLRGVrgnkIAMIFQEPM-----VSLNPLHTLEKQLYEVLSlhRGMRREAARGEILNCLD----RVGIRQAakrltdyph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 638 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGR 713
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLR-ELQQElnmGLLFITHNLSIVRKlADRVAVMQNGR 234
|
250
....*....|...
gi 66932952 714 VVQQGTHQQLLAQ 726
Cdd:PRK15134 235 CVEQNRAATLFSA 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
235-755 |
3.56e-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: 83.42 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 235 SSLAAG-IRGGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGV 313
Cdd:TIGR01271 937 SVLALGfFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGA 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 314 VvFMFSLSWQLSLVTFMGFPIIMMVSNIY----GKYYKRLSKEVQSALARASTTaeeTISAMKTVRSFANEEEEAEVFLR 389
Cdd:TIGR01271 1017 I-FVVSVLQPYIFIAAIPVAVIFIMLRAYflrtSQQLKQLESEARSPIFSHLIT---SLKGLWTIRAFGRQSYFETLFHK 1092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 390 KLQqvykLNRKEAAAYMSYV-WGSG-----LTLLVVQVSILYYGGHLVISGQMSsgnlIAFIIYEFVLGDCMESVGSVYS 463
Cdd:TIGR01271 1093 ALN----LHTANWFLYLSTLrWFQMridiiFVFFFIAVTFIAIGTNQDGEGEVG----IILTLAMNILSTLQWAVNSSID 1164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 464 --GLMQGVgaaEKVFEFIDRQP----------------TMVHDGSLAPDHL--EGRVDFENVTFTYrTRPHTQVLQNVSF 523
Cdd:TIGR01271 1165 vdGLMRSV---SRVFKFIDLPQeeprpsggggkyqlstVLVIENPHAQKCWpsGGQMDVQGLTAKY-TEAGRAVLQDLSF 1240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 524 SLSPGKVTALVGPSGSGKSSCVNILENFYPLQGgRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISyglptv 603
Cdd:TIGR01271 1241 SVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-EIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD------ 1313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 604 PFEM-----VVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQ 678
Cdd:TIGR01271 1314 PYEQwsdeeIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 679 QAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLGLEHPLDYTASHKEPP 755
Cdd:TIGR01271 1394 KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRLKLFPLHRRNSSKRKP 1470
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
509-709 |
6.23e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.89 E-value: 6.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 509 YRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGkpigaydhkylHRVISLVSQ---EP 585
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 586 VLFARSITDNISYGL---------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRN 656
Cdd:NF040873 68 DSLPLTVRDLVAMGRwarrglwrrLTRDDRAAVDDALER------VGLADLAGRQLGE----LSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 657 PPVLILDEATSALDAESEYLIQQAIhgnLQRH----TVLIIAHRLSTVERAHLIVVL 709
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALL---AEEHargaTVVVVTHDLELVRRADPCVLL 191
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
500-695 |
7.75e-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: 75.18 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVlldgkpigaydhkylhrvis 579
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 lvsqepvlfARSITDNISYglptvpFEmvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPV 659
Cdd:cd03221 58 ---------TWGSTVKIGY------FE-------------------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*....
gi 66932952 660 LILDEATSALDAES-EYLIQQaihgnLQRH--TVLIIAH 695
Cdd:cd03221 92 LLLDEPTNHLDLESiEALEEA-----LKEYpgTVILVSH 125
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
182-391 |
1.49e-15 |
|
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: 77.96 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 182 AFLVAASFFLIVAA--LGETFLPYYTGRAIDSIViQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRN 259
Cdd:cd18605 1 LILILLSLILMQASrnLIDFWLSYWVSHSNNSFF-NFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 260 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTG-VVVFMFSLSWQLSLVtfmgFPIIMMV 338
Cdd:cd18605 80 KLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGyLVVICYQLPWLLLLL----LPLAFIY 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 339 SNIYgKYYKRLSKEvqsaLARASTTAE--------ETISAMKTVRSFANEEEEAEVFLRKL 391
Cdd:cd18605 156 YRIQ-RYYRATSRE----LKRLNSVNLsplythfsETLKGLVTIRAFRKQERFLKEYLEKL 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
499-736 |
1.52e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 499 RVDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVI 578
Cdd:PRK10253 7 RLRGEQLTLGYGKY---TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFAR-SITDNISYG-LPTVPF--------EMVVEAAQKANAhgfIMELQDgYSTETgekgaqLSGGQKQRVA 648
Cdd:PRK10253 84 GLLAQNATTPGDiTVQELVARGrYPHQPLftrwrkedEEAVTKAMQATG---ITHLAD-QSVDT------LSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 649 MARALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQR---HTVLIIAHRLSTVER--AHLIVVLDkGRVVQQGTHQQL 723
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELL-SELNRekgYTLAAVLHDLNQACRyaSHLIALRE-GKIVAQGAPKEI 231
|
250
....*....|...
gi 66932952 724 LAqgglyAKLVQR 736
Cdd:PRK10253 232 VT-----AELIER 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
515-715 |
3.62e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 515 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV----ISLVSQEPVLFAR 590
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 -SITDNISygLPTVpFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 669
Cdd:PRK10535 101 lTAAQNVE--VPAV-YAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 66932952 670 DAESEYLIQQAIHGNLQR-HTVLIIAHRLSTVERAHLIVVLDKGRVV 715
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
520-723 |
3.66e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.18 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 520 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPI-GAYDHKY-------------LHRVISLVsqEP 585
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeGLPGHQIarmgvvrtfqhvrLFREMTVI--EN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 586 VLFA--RSITDNISYGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTETGekgaQLSGGQKQRVAMARALVRNPPVLI 661
Cdd:PRK11300 101 LLVAqhQQLKTGLFSGLLKTPAFRRAESEALDRAATWLerVGLLEHANRQAG----NLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 662 LDEATSALDAESEYLIQQAIhGNLQRH---TVLIIAHRLSTV----ERahlIVVLDKGRVVQQGTHQQL 723
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELI-AELRNEhnvTVLLIEHDMKLVmgisDR---IYVVNQGTPLANGTPEEI 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
510-723 |
4.33e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.82 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 510 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----------ENFYPLQGGRVLLDGKPigAYDHKYLHRVIS 579
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRL--ARDIRKSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFAR-SITDNISYG-LPTVPFEMVV----EAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARAL 653
Cdd:PRK09984 90 YIFQQFNLVNRlSVLENVLIGaLGSTPFWRTCfswfTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQL 723
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
504-726 |
6.05e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.39 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 504 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLQGGRVL----------LDGKpIGAYD 570
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK--PSEGSIVVngqtinlvrdKDGQ-LKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 571 HKYLHRV---ISLVSQEPVLFAR-SITDNISYGLPTVPFEMVVEAAQKA----NAHGFIMELQDGYStetgekgAQLSGG 642
Cdd:PRK10619 84 KNQLRLLrtrLTMVFQHFNLWSHmTVLENVMEAPIQVLGLSKQEARERAvkylAKVGIDERAQGKYP-------VHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 643 QKQRVAMARALVRNPPVLILDEATSALDAE--SEYL-IQQAIHGnlQRHTVLIIAHRLSTVER--AHLIvVLDKGRVVQQ 717
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPElvGEVLrIMQQLAE--EGKTMVVVTHEMGFARHvsSHVI-FLHQGKIEEE 233
|
....*....
gi 66932952 718 GTHQQLLAQ 726
Cdd:PRK10619 234 GAPEQLFGN 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
517-714 |
6.94e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 73.24 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV-ISLVSQEP----VLFARS 591
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 592 ITDNISYGlptvpfemvveaaqkanahgfimelqdgystetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 671
Cdd:cd03215 95 VAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 66932952 672 ESeyliQQAIHGNLQR-----HTVLIIAHRLSTVER-AHLIVVLDKGRV 714
Cdd:cd03215 138 GA----KAEIYRLIREladagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
511-731 |
7.82e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.19 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 511 TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPvlfar 590
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 sitdnisyglpTVPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ------------------LSGGQKQRVAMARA 652
Cdd:PRK09536 87 -----------SLSFEFDVRQVVEMGRTPHRSRF--DTWTETDRAAVEramertgvaqfadrpvtsLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 653 LVRNPPVLILDEATSALDaeseylIQQAIHG-NLQR------HTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLL 724
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD------INHQVRTlELVRrlvddgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
....*..
gi 66932952 725 AQGGLYA 731
Cdd:PRK09536 228 TADTLRA 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
516-736 |
9.72e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.72 E-value: 9.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 516 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQEPV------ 586
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSpDERARAGIFLAFQYPVeipgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 --LFARSITDNISYGLPTVPfEMVVEAAQKANAHGFIMELQDGYSTETgekgaqLSGGQKQRVAMARALVRNPPVLILDE 664
Cdd:COG0396 94 vsNFLRTALNARRGEELSAR-EFLKLLKEKMKELGLDEDFLDRYVNEG------FSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 665 ATSALDAE-----SEYLiqQAIHGnlQRHTVLIIAH--RLSTVERAHLIVVLDKGRVVQQGTH---QQLLAQGglYAKLV 734
Cdd:COG0396 167 TDSGLDIDalrivAEGV--NKLRS--PDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKelaLELEEEG--YDWLK 240
|
..
gi 66932952 735 QR 736
Cdd:COG0396 241 EE 242
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
498-726 |
1.06e-14 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 75.28 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 498 GRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGgRVLLDGKPIGAYDHKYLHRV 577
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 ISLVSQEPVLFARSITDNIS-YGLPTVpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRN 656
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 657 PPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
180-444 |
1.37e-14 |
|
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: 75.25 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 180 DVAFlvaASFFLIVAALgetFLPYYTGRAIDSIVIQKSMDQFTT-AVVVVCLLAIGSSLAAgIRGGIFTLVFARLNIRLR 258
Cdd:cd18783 6 DVAI---ASLILHVLAL---APPIFFQIVIDKVLVHQSYSTLYVlTIGVVIALLFEGILGY-LRRYLLLVATTRIDARLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 259 NCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNiniFLRNTVKVTGVVVF---MFSLSWQLSLVTFMGFPII 335
Cdd:cd18783 79 LRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQ---LFGTLLDATSLLVFlpvLFFYSPTLALVVLAFSALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 336 MMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRkeAAAYMSyVWGSGLT 415
Cdd:cd18783 155 ALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARF--AVGRLS-NWPQTLT 231
|
250 260 270
....*....|....*....|....*....|..
gi 66932952 416 LL---VVQVSILYYGGHLVISGQMSSGNLIAF 444
Cdd:cd18783 232 GPlekLMTVGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
503-718 |
2.05e-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: 73.52 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRT----------------RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGK 564
Cdd:cd03267 4 SNLSKSYRVyskepgligslkslfkRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 565 PIGAYDHKYLHRVISLVSQE-------PVLFARSITDNIsYGLPTVPFemvveaaqKANAHGF--IMELQDGYSTETgek 635
Cdd:cd03267 84 VPWKRRKKFLRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-YDLPPARF--------KKRLDELseLLDLEELLDTPV--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 636 gAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESeyliQQAIHGNLQRH------TVLIIAHRLSTVER-AHLIVV 708
Cdd:cd03267 152 -RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA----QENIRNFLKEYnrergtTVLLTSHYMKDIEAlARRVLV 226
|
250
....*....|
gi 66932952 709 LDKGRVVQQG 718
Cdd:cd03267 227 IDKGRLLYDG 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
512-719 |
2.14e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.09 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 512 RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQG--------GRVLLDGKPIGAYDHKYLHRVISLVSQ 583
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 584 --EPVlFARSITDNISYGLptvpFEMVVEAAQKANAHGFI----MELQDGySTETGEKGAQLSGGQKQRVAMARAL---- 653
Cdd:PRK13547 91 aaQPA-FAFSAREIVLLGR----YPHARRAGALTHRDGEIawqaLALAGA-TALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 654 -----VRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVER-AHLIVVLDKGRVVQQGT 719
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVR-RLARDwnlGVLAIVHDPNLAARhADRIAMLADGAIVAHGA 238
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
507-745 |
2.91e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 507 FTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGaYDHK---YLHRVISLVSQ 583
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRgllALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 584 EP--VLFARSITDNISYGLPT--VPFEMVV----EAAQKANAHGFIME-LQdgystetgekgaQLSGGQKQRVAMARALV 654
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRNlgVPEAEITrrvdEALTLVDAQHFRHQpIQ------------CLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 655 RNPPVLILDEATSALD----AESEYLIQQAIHgnlQRHTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGTHQQLLAQGGL 729
Cdd:PRK13638 153 LQARYLLLDEPTAGLDpagrTQMIAIIRRIVA---QGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
250
....*....|....*...
gi 66932952 730 Y--AKLVQRQMLGLEHPL 745
Cdd:PRK13638 230 MeqAGLTQPWLVKLHTQL 247
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
500-726 |
4.16e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTQ---VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGkpIGAYDHKYLHR 576
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 VIS---LVSQEP--VLFARSITDNISYG---LPTVPFEM---VVEAAQKANAHGFimelqdgystetgEKGAQ--LSGGQ 643
Cdd:PRK13633 83 IRNkagMVFQNPdnQIVATIVEEDVAFGpenLGIPPEEIrerVDESLKKVGMYEY-------------RRHAPhlLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 644 KQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQ 721
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 66932952 722 QLLAQ 726
Cdd:PRK13633 230 EIFKE 234
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
148-698 |
4.79e-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: 75.94 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 148 EPGNEGFHGEGGAPAEQAS--GATLQKLLSYTK---PDV-----AFLVAASFFLIVAALGETFLPYYTGRaIDSIVIQKS 217
Cdd:TIGR00954 52 ELTIVGKHSTIEGAKKKAHvnGVFLGKLDFLLKiliPRVfcketGLLILIAFLLVSRTYLSVYVATLDGQ-IESSIVRRS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 218 MDQFTTAVVVVCLLAIGSSLA-AGIRggiFTLVFARLNIRLRncLFRSLVSQETSFFDENRTGDLISRLTSdttmVSDLV 296
Cdd:TIGR00954 131 PRNFAWILFKWFLIAPPASFInSAIK---YLLKELKLRFRVR--LTRYLYSKYLSGFTFYKVSNLDSRIQN----PDQLL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 297 SQNINIFLRNTVKVTG--------VVVFMFSLswqLSLVTFMG----FPIIMMVSNIYGKYYKRLSKevqsaLARASTTA 364
Cdd:TIGR00954 202 TQDVEKFCDSVVELYSnltkpildVILYSFKL---LTALGSVGpaglFAYLFATGVVLTKLRPPIGK-----LTVEEQAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 365 EETISAMKTvRSFANEEEEA-----EVFLRKLQQ-----VYKLNR--KEAAAY-------MSYVWgSGLTLLVVQVSILY 425
Cdd:TIGR00954 274 EGEYRYVHS-RLIMNSEEIAfyqgnKVEKETVMSsfyrlVEHLNLiiKFRFSYgfldnivAKYTW-SAVGLVAVSIPIFD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 426 yGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVG---SVYSGLMQGVGAAEKVFEFI---------DRQPTMVHD----- 488
Cdd:TIGR00954 352 -KTHPAFLEMSEEELMQEFYNNGRLLLKAADALGrlmLAGRDMTRLAGFTARVDTLLqvlddvksgNFKRPRVEEiesgr 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 489 -GSLAPDHLEGR---------VDFENVTFTyrtRPHTQVL-QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGG 557
Cdd:TIGR00954 431 eGGRNSNLVPGRgiveyqdngIKFENIPLV---TPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 558 RVLLDGKpiGAydhkylhrvISLVSQEPVLFARSITDNISYglPTVPFEMVVEAAQKANAHGFIMELQDGY--STETGEK 635
Cdd:TIGR00954 508 RLTKPAK--GK---------LFYVPQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDKDLEQILDNVQLTHilEREGGWS 574
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 636 GAQ-----LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEyliqQAIHGNLQRH--TVLIIAHRLS 698
Cdd:TIGR00954 575 AVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREFgiTLFSVSHRKS 640
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
500-725 |
1.27e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.07 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLQGGRVL----------------L 561
Cdd:TIGR03269 1 IEVKNLTKKFDGK---EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 562 DGKPIGAYDHKYLHRVISLVSQEPVLFARsITDNIS---------YGLPTVpFEMVVEAAQKAnahgfimelqdGYSTET 632
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFWNLSDKLRRR-IRKRIAimlqrtfalYGDDTV-LDNVLEALEEI-----------GYEGKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 633 GEKGA------------------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRH--TVLI 692
Cdd:TIGR03269 145 AVGRAvdliemvqlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVL 224
|
250 260 270
....*....|....*....|....*....|....
gi 66932952 693 IAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:TIGR03269 225 TSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
503-739 |
1.41e-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: 74.09 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQ-GGRVLLDGKPIGAYD-HKYLHRVISL 580
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 581 VSQE-------PVLfarSITDNISYG-LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 652
Cdd:TIGR02633 341 VPEDrkrhgivPIL---GVGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKM 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 653 LVRNPPVLILDEATSALDAESEYLIQQAIhGNLQRHTVLIIahrLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGlyak 732
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEIYKLI-NQLAQEGVAII---VVSSELAEVLGLSDRVLVIGEGKLKGDFVNHA---- 489
|
....*..
gi 66932952 733 LVQRQML 739
Cdd:TIGR02633 490 LTQEQVL 496
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
516-718 |
1.62e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 516 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQG-----GRVLLDGKPIGAYDHKYLH--RVISLVSQEPVLF 588
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEvrREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 589 AR-SITDNISYGL-------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 660
Cdd:PRK14267 98 PHlTIYDNVAIGVklnglvkSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 661 ILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
500-715 |
1.62e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVlldgkpigaydhKYLHRV-I 578
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------------KLGETVkI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLF--ARSITDNISYGLPTvpfemvveaAQKANAHGFimeLQD-GYSTETGEKG-AQLSGGQKQRVAMARALV 654
Cdd:COG0488 381 GYFDQHQEELdpDKTVLDELRDGAPG---------GTEQEVRGY---LGRfLFSGDDAFKPvGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 655 RNPPVLILDEATSALDAESEYLIQQAihgnLQRH--TVLIIAH-R--LSTVerAHLIVVLDKGRVV 715
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEA----LDDFpgTVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
504-726 |
1.90e-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: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 504 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKpigaydhkylhrvISLVSQ 583
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 584 EPVLFARSITDNISYGLP--TVPFEMVVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLI 661
Cdd:cd03291 106 FSWIMPGTIKENIIFGVSydEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 662 LDEATSALDAESEYLI-QQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQ 726
Cdd:cd03291 183 LDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
521-723 |
2.03e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.05 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 521 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV---ISLVSQEPV--LFAR-SITD 594
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLasLNPRmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 595 NISYGL----PTVPFEMVVEAAQKANAH-GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSAL 669
Cdd:PRK15079 120 IIAEPLrtyhPKLSRQEVKDRVKAMMLKvGLLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 670 D----AESEYLIQQaihgnLQRH---TVLIIAHRLSTVEraHL---IVVLDKGRVVQQGTHQQL 723
Cdd:PRK15079 193 DvsiqAQVVNLLQQ-----LQREmglSLIFIAHDLAVVK--HIsdrVLVMYLGHAVELGTYDEV 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
503-724 |
2.03e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.11 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKpigaydHKYLHRVISLVS 582
Cdd:PRK11701 10 RGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------DGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPVLFARS----ITDNISYGLptvpfEMVVEA---------AQKANAHGFI----------MELQdgySTETGEKGAQL 639
Cdd:PRK11701 81 AERRRLLRTewgfVHQHPRDGL-----RMQVSAggnigerlmAVGARHYGDIratagdwlerVEID---AARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 640 SGGQKQRVAMARALVRNPPVLILDEATSALDAESeyliqQAIHGNLQRH-------TVLIIAHRLStVER--AHLIVVLD 710
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGlvrelglAVVIVTHDLA-VARllAHRLLVMK 226
|
250
....*....|....
gi 66932952 711 KGRVVQQGTHQQLL 724
Cdd:PRK11701 227 QGRVVESGLTDQVL 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
519-733 |
2.50e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 519 QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVI----------SLVSQEPVLF 588
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpgiktELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 589 ARSITDNISYglptvpfEMVVEAAQKANAHGFiMELqdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 668
Cdd:PRK13538 98 YQRLHGPGDD-------EALWEALAQVGLAGF-EDV----------PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 669 LDAESEYLIQQaihgnlqrhtvLIIAHrlstverahlivvLDKGRVVQQGTHQQLLAQGGLYAKL 733
Cdd:PRK13538 160 IDKQGVARLEA-----------LLAQH-------------AEQGGMVILTTHQDLPVASDKVRKL 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
504-723 |
3.61e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 504 NVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILenFYPLQGG--RVLLDGKPIGAYDH----- 571
Cdd:PRK13651 7 NIVKIFnkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNAL--LLPDTGTieWIFKDEKNKKKTKEkekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 572 ----------------KYLHRVISLVSQ--EPVLFARSITDNISYGlptvPFEMVV---EAAQKANAHGFIMELQDGYSt 630
Cdd:PRK13651 85 eklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVskeEAKKRAAKYIELVGLDESYL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 631 etgEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQRHTVLIIAHRLSTV-ERAHLIV 707
Cdd:PRK13651 160 ---QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVlEWTKRTI 236
|
250
....*....|....*..
gi 66932952 708 VLDKGRVVQQG-THQQL 723
Cdd:PRK13651 237 FFKDGKIIKDGdTYDIL 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
504-715 |
3.70e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.11 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 504 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAY-DHKYlHRVISLVS 582
Cdd:COG1101 8 SKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEYKR-AKYIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPVLfarsitdnisyGlpTVPfEMVVE-----AAQKANAHGFI-------------------MELQDGYSTETGekgaQ 638
Cdd:COG1101 87 QDPMM-----------G--TAP-SMTIEenlalAYRRGKRRGLRrgltkkrrelfrellatlgLGLENRLDTKVG----L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 639 LSGGQKQRVAMARALVRNPPVLILDEATSALD---AE-----SEYLIQQaihGNLqrhTVLIIAHRLS-TVERAHLIVVL 709
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAAlvlelTEKIVEE---NNL---TTLMVTHNMEqALDYGNRLIMM 222
|
....*.
gi 66932952 710 DKGRVV 715
Cdd:COG1101 223 HEGRII 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
520-726 |
3.98e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.53 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 520 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRV-------LLDGKPIGAYDHKYLHRVISLVSQEPVLFA-RS 591
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 592 ITDNI--SYGLpTVPFEM-VVEAAQKANAHGFimelQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLILDEATS 667
Cdd:TIGR03269 382 VLDNLteAIGL-ELPDELaRMKAVITLKMVGF----DEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 668 ALDAESEYLIQQAIHGNLQR--HTVLIIAHRLSTV----ERAHLivvLDKGRVVQQGTHQQLLAQ 726
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVldvcDRAAL---MRDGKIVKIGDPEEIVEE 518
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
517-725 |
4.20e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDH----KYLHRVISLVSQE----PVLF 588
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaKLRAKHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 589 ARsitDNISygLPTVpfeMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATsa 668
Cdd:PRK10584 105 AL---ENVE--LPAL---LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT-- 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 669 ldaeseyliqqaihGNLQRHTVLIIAHRLSTVERAH---LIVVldkgrvvqqgTHQQLLA 725
Cdd:PRK10584 175 --------------GNLDRQTGDKIADLLFSLNREHgttLILV----------THDLQLA 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
517-715 |
1.29e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIG------AYDHKylhrvISLVS----QEPV 586
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAG-----IAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 LFARSITDNISygLPTVP----FEMVVEAAQKANAHGFIMELQ---DGYSTETGekgaQLSGGQKQRVAMARALVRNPPV 659
Cdd:COG1129 342 VLDLSIRENIT--LASLDrlsrGGLLDRRRERALAEEYIKRLRiktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 660 LILDEATSALDAESEYLIQQAIHGNLQR-HTVLII----------AHRlstverahlIVVLDKGRVV 715
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVIsselpellglSDR---------ILVMREGRIV 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
513-697 |
1.69e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 513 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV-ISLVSQEPVLFAR- 590
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SITDNISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 669
Cdd:PRK10762 95 TIAENIFLGReFVNRFGRIDWKKMYAEADKLLARLNLRFSSDK--LVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180
....*....|....*....|....*....
gi 66932952 670 -DAESEYLIQQAIHGNLQRHTVLIIAHRL 697
Cdd:PRK10762 173 tDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
516-718 |
1.77e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 66.78 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 516 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQEPVLFarsi 592
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPpEERARLGIFLAFQYPPEI---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 tdnisyglPTVPFEMvveaaqkanahgFIMELQDGystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 672
Cdd:cd03217 90 --------PGVKNAD------------FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 66932952 673 SEYLIQQAIHGNLQRHT-VLIIAH--RLSTVERAHLIVVLDKGRVVQQG 718
Cdd:cd03217 139 ALRLVAEVINKLREEGKsVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
500-700 |
1.86e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGK-PIGaydhkYLHRVI 578
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIG-----YVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFARSITDNisyglPTVPFEMVVEAAQKANA-HGFIMELQdgystetgekgaQLSGGQKQRVAMARALVRNP 657
Cdd:PRK09544 77 YLDTTLPLTVNRFLRLR-----PGTKKEDILPALKRVQAgHLIDAPMQ------------KLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 66932952 658 PVLILDEATSALDAESEYLIQQAIhgNLQRHT----VLIIAHRLSTV 700
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLI--DQLRREldcaVLMVSHDLHLV 184
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
500-718 |
4.16e-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: 65.75 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYR-TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQG---GRVLLDGKPIGAYDHKYlH 575
Cdd:cd03233 4 LSWRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RVISLVSQEPVLFarsitdnisyglPTVPFEMVVEAAQKANAHGFImelqdgystetgeKGaqLSGGQKQRVAMARALVR 655
Cdd:cd03233 83 GEIIYVSEEDVHF------------PTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 656 NPPVLILDEATSALDAESEYLIQQAIH--GNLQRHTVLIIAHRLS--TVERAHLIVVLDKGRVVQQG 718
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRtmADVLKTTTFVSLYQASdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
184-445 |
4.24e-12 |
|
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: 67.57 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGetfLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFR 263
Cdd:cd18779 7 ILLASLLLQLLGLA---LPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 264 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLrNTVKVTGVVVFMFSLSWQLSLVTfMGFPII----MMVS 339
Cdd:cd18779 84 HLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALL-DGTLVLGYLALLFAQSPLLGLVV-LGLAALqvalLLAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 340 NiygKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVykLNRKEAAAYMSYVWGSGLTLL-- 417
Cdd:cd18779 162 R---RRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQ--LNASLRRGRLDALVDALLATLrl 236
|
250 260
....*....|....*....|....*...
gi 66932952 418 VVQVSILYYGGHLVISGQMSSGNLIAFI 445
Cdd:cd18779 237 AAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
503-718 |
4.86e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 503 ENVTFTYRTrPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLhrvISLVS 582
Cdd:PRK15056 10 NDVTVTWRN-GHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QE-------PVLfarsITDNISYG---------LPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQR 646
Cdd:PRK15056 85 QSeevdwsfPVL----VEDVVMMGryghmgwlrRAKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 647 VAMARALVRNPPVLILDEATSALDAESEYLIqQAIHGNLQRH--TVLIIAHRLSTVERAHLIVVLDKGRVVQQG 718
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARI-ISLLRELRDEgkTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
500-723 |
4.90e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.10 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV-- 577
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 -ISLVSQEPVLFAR-SITDNISY------GLPTVPFEMVVeaaqkanahgfIMELQdgystETGEKGA------QLSGGQ 643
Cdd:PRK11831 85 rMSMLFQSGALFTDmNVFDNVAYplrehtQLPAPLLHSTV-----------MMKLE-----AVGLRGAaklmpsELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 644 KQRVAMARALVRNPPVLILDEATSALDAESE----YLIQQAIHGnlQRHTVLIIAHR----LSTVERAHliVVLDKgRVV 715
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMgvlvKLISELNSA--LGVTCVVVSHDvpevLSIADHAY--IVADK-KIV 223
|
....*...
gi 66932952 716 QQGTHQQL 723
Cdd:PRK11831 224 AHGSAQAL 231
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
181-469 |
9.04e-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: 66.37 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 181 VAFLVAASFFLIVAalgetflPYYTGRAIDSIVIQKSMDQFTTAVVVVC--LLAIGSSLAAGIRGGIFTLVFARLNIRLR 258
Cdd:cd18582 2 LLLLVLAKLLNVAV-------PFLLKYAVDALSAPASALLAVPLLLLLAygLARILSSLFNELRDALFARVSQRAVRRLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 259 NCLFRSLVSQETSFFDENRTGDL---ISRLTSDTTMVSDLVSQNInifLRNTVKVTGVVVFMFSL-SWQLSLVTFMGFPI 334
Cdd:cd18582 75 LRVFRHLHSLSLRFHLSRKTGALsraIERGTRGIEFLLRFLLFNI---LPTILELLLVCGILWYLyGWSYALITLVTVAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 335 IMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGL 414
Cdd:cd18582 152 YVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQAL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 415 TLLVVQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 469
Cdd:cd18582 232 IISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
501-726 |
9.33e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.85 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 501 DFENVTFTYRTrPH--TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLQGGRVLLDGKPI----GAYD 570
Cdd:COG4170 5 DIRNLTIEIDT-PQgrVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLlklsPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 571 HKYLHRVISLVSQEPVLF---ARSITDNISYGLPTVPFE---MVVEAAQKANA-----------HGFIMelqDGYSTEtg 633
Cdd:COG4170 84 RKIIGREIAMIFQEPSSCldpSAKIGDQLIEAIPSWTFKgkwWQRFKWRKKRAiellhrvgikdHKDIM---NSYPHE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 634 ekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESeyliQQAIHGNLQR------HTVLIIAHRLSTVER-AHLI 706
Cdd:COG4170 159 -----LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTT----QAQIFRLLARlnqlqgTSILLISHDLESISQwADTI 229
|
250 260
....*....|....*....|
gi 66932952 707 VVLDKGRVVQQGTHQQLLAQ 726
Cdd:COG4170 230 TVLYCGQTVESGPTEQILKS 249
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
527-711 |
9.80e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.55 E-value: 9.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 527 PGKVTALVGPSGSGKSSCVNILENFYPLQGGRVL-LDGKPIGAYDHKYLHRVIslvsqepvlfarsitdnisyglptvpf 605
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 606 emvveaaqkanahgfimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNL 685
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180 190
....*....|....*....|....*....|...
gi 66932952 686 QRH-------TVLIIAHRLSTVERAHLIVVLDK 711
Cdd:smart00382 108 LLLlkseknlTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
521-729 |
1.50e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 521 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlQGGRVLLDGKPIGAYDHKYLHRVIS-LVSQEPVLF--------ARS 591
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFampvfqylTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 592 ITDNISYGLPTVPFEMVVEAAQkanahgfimeLQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NP--PVLILDE 664
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 665 ATSALDaeseyLIQQAIHGNLQRH------TVLIIAHRLS-TVERAHLIVVLDKGRVVQQGTHQQLLAQGGL 729
Cdd:PRK03695 160 PMNSLD-----VAQQAALDRLLSElcqqgiAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
517-725 |
2.05e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 517 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENfyPLQG----GRVLLDGKPIGaydhKYLHRVISLVSQEPVLFAR-S 591
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQGnnftGTILANNRKPT----KQILKRTGFVTQDDILYPHlT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 592 ITDNISY-GLPTVPFEMVVEAAQKAnAHGFIMEL--QDGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATS 667
Cdd:PLN03211 157 VRETLVFcSLLRLPKSLTKQEKILV-AESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 668 ALDAESEYLIQQAIHGNLQR-HTVLIIAHRLST--VERAHLIVVLDKGRVVQQGTHQQLLA 725
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKgKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
495-693 |
2.09e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 495 HLEGRVDFE--NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlqG---GRVLLDGKPIG-- 567
Cdd:PRK13549 253 HTIGEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKir 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 568 ----AYDHKylhrvISLVSQE-------PVLfarSITDNISYG-LPTVPFEMVV-EAAQKANAHGFIMELQdgYSTETGE 634
Cdd:PRK13549 331 npqqAIAQG-----IAMVPEDrkrdgivPVM---GVGKNITLAaLDRFTGGSRIdDAAELKTILESIQRLK--VKTASPE 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 635 -KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLII 693
Cdd:PRK13549 401 lAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
530-718 |
2.22e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.05 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 530 VTALVGPSGSGKSSCVNILENF-YPLQG-----GRVLLD-GKPIGAYDHKylhRVISLVSQEPVLFAR-SITDNISYGLp 601
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLtRPQKGrivlnGRVLFDaEKGICLPPEK---RRIGYVFQDARLFPHyKVRGNLRYGM- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 602 tvpfemvveaAQKANAHgF--------IMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 673
Cdd:PRK11144 102 ----------AKSMVAQ-FdkivallgIEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 66932952 674 E-----YLIQQAIHGNLqrhTVLIIAHRLSTVER-AHLIVVLDKGRVVQQG 718
Cdd:PRK11144 164 KrellpYLERLAREINI---PILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
513-713 |
2.42e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 513 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF-YPLQGGRVLLDGKPIGaydhkYLhrvislvSQEPVL-FAR 590
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFNGEARPQPGIKVG-----YL-------PQEPQLdPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SITDNI-------------------SYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GE-KGA 637
Cdd:TIGR03719 84 TVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAAEQAELQE---IIDAADAWDLDSqleiamdalrcppWDaDVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 638 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAihgnLQRH--TVLIIAH-R--LSTVerAHLIVVLDKG 712
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH----LQEYpgTVVAVTHdRyfLDNV--AGWILELDRG 234
|
.
gi 66932952 713 R 713
Cdd:TIGR03719 235 R 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
504-723 |
3.02e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 504 NVTFtYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGK----------PIGAYDHKY 573
Cdd:PRK10261 19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 574 LHRV----ISLVSQEPVL-----------FARSItdNISYGLPTvpfEMVVEAAQKANAHGFIMELQdgysTETGEKGAQ 638
Cdd:PRK10261 98 MRHVrgadMAMIFQEPMTslnpvftvgeqIAESI--RLHQGASR---EEAMVEAKRMLDQVRIPEAQ----TILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 639 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRHT---VLIIAHRLSTV-ERAHLIVVLDKGRV 714
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMsmgVIFITHDMGVVaEIADRVLVMYQGEA 247
|
....*....
gi 66932952 715 VQQGTHQQL 723
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
518-719 |
6.62e-11 |
|
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: 63.40 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNilENFYPLQGGRVLLDGKPIGAYD----HKYLHRVIsLVSQEPV------- 586
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNHDriegLEHIDKVI-VIDQSPIgrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 -------------LF------AR--SITDNISYGLPTVP--FEMVVEAAQK-----ANAHGFIMELQD---GYSTeTGEK 635
Cdd:cd03271 88 patytgvfdeireLFcevckgKRynRETLEVRYKGKSIAdvLDMTVEEALEffeniPKIARKLQTLCDvglGYIK-LGQP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 636 GAQLSGGQKQRVAMARALVR---NPPVLILDEATSALDAESeylIQQAIHGnLQR-----HTVLIIAHRLSTVERAHLIV 707
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHD---VKKLLEV-LQRlvdkgNTVVVIEHNLDVIKCADWII 242
|
250
....*....|....*...
gi 66932952 708 VL-----DK-GRVVQQGT 719
Cdd:cd03271 243 DLgpeggDGgGQVVASGT 260
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
500-719 |
8.76e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.99 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPHTQVlQNVSFSLSPGKVTALVGPSGSGKS-SCVNILENF-YPlqgGRVL-----LDGKPIGAYDHK 572
Cdd:PRK11022 6 VDKLSVHFGDESAPFRAV-DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIdYP---GRVMaekleFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 573 YLHRVI----SLVSQEPVlfarsITDNISYglpTVPFEM-----VVEAAQKANAHGFIMEL--QDGYSTETGEKGA---Q 638
Cdd:PRK11022 82 ERRNLVgaevAMIFQDPM-----TSLNPCY---TVGFQImeaikVHQGGNKKTRRQRAIDLlnQVGIPDPASRLDVyphQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 639 LSGGQKQRVAMARALVRNPPVLILDEATSALDAEseylIQQAIHG---NLQRH---TVLIIAHRLSTV-ERAHLIVVLDK 711
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT----IQAQIIElllELQQKenmALVLITHDLALVaEAAHKIIVMYA 229
|
....*...
gi 66932952 712 GRVVQQGT 719
Cdd:PRK11022 230 GQVVETGK 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
518-716 |
1.47e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.43 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlQG---GRVLLDGKPIGAYD-HKYLHRVISLVSQE----PVLfa 589
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEVCRFKDiRDSEALGIVIIHQElaliPYL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 590 rSITDNISYGLPTVPF------EMVVEAAQKANAHGfimeLQDGYSTETGEKGAqlsgGQKQRVAMARALVRNPPVLILD 663
Cdd:NF040905 94 -SIAENIFLGNERAKRgvidwnETNRRARELLAKVG----LDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 664 EATSAL-DAESEYLIQQAIHGNLQRHTVLIIAHRLSTVER-AHLIVVLDKGRVVQ 716
Cdd:NF040905 165 EPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
500-719 |
1.53e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.02 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRT-------------------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVL 560
Cdd:COG1134 5 IEVENVSKSYRLyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 561 LDGkpigaydhkylhRVISLVSqepvL---FARSIT--DNIS-----YGLPTVP----FEMVVEAAqkanahgfimELQD 626
Cdd:COG1134 85 VNG------------RVSALLE----LgagFHPELTgrENIYlngrlLGLSRKEidekFDEIVEFA----------ELGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 627 -------GYSTetgekgaqlsgGQKQRVAMARALVRNPPVLILDEATSALDAE----SEYLIQQAIHgnlQRHTVLIIAH 695
Cdd:COG1134 139 fidqpvkTYSS-----------GMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSH 204
|
250 260
....*....|....*....|....*
gi 66932952 696 RLSTVER-AHLIVVLDKGRVVQQGT 719
Cdd:COG1134 205 SMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
518-715 |
1.80e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfyplqGGRVLLD-GKPIGAYDhkylhRVISLVSQEPvlfARSITDN- 595
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQD-----LIVARLQQDP---PRNVEGTv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 596 --------------------ISYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GEKGAQLSGG 642
Cdd:PRK11147 84 ydfvaegieeqaeylkryhdISHLVETDPSEKNLNELAKLQE---QLDHHNLWQLENrinevlaqlgldpDAALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 643 QKQRVAMARALVRNPPVLILDEATSALDAES-EYLiqqaiHGNLQ--RHTVLIIAHRLSTVER-AHLIVVLDKGRVV 715
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL-----EGFLKtfQGSIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
514-716 |
1.96e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 514 HTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLQGGRVLLDGKpigaydhkylhrvislVSQEpvlfaR 590
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTllrLLAGALKGTPVAGCVDVPDNQ----------------FGRE-----A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SITDNIsygLPTVPFEMVVEAAqkaNAHGfimeLQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 670
Cdd:COG2401 101 SLIDAI---GRKGDFKDAVELL---NAVG----LSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 66932952 671 AESEYLIQQAIHGNLQRH--TVLIIAHRlSTVERA---HLIVVLDKGRVVQ 716
Cdd:COG2401 169 RQTAKRVARNLQKLARRAgiTLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
512-734 |
2.12e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.80 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 512 RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN-FYPlQGGRVLLDGkpigaYD-----HKYLHRvISLV-- 581
Cdd:COG4586 30 REYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLG-----YVpfkrrKEFARR-IGVVfg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 582 --SQ----EPVL--FA--RSItdnisYGLPTVPF----EMVVEaaqkanahgfIMELQDGYSTETgekgAQLSGGQKQRV 647
Cdd:COG4586 103 qrSQlwwdLPAIdsFRllKAI-----YRIPDAEYkkrlDELVE----------LLDLGELLDTPV----RQLSLGQRMRC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 648 AMARALVRNPPVLILDEATSALDAESeyliQQAIHGNL----QRH--TVLIIAHRLSTVERahL---IVVLDKGRVVQQG 718
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVS----KEAIREFLkeynRERgtTILLTSHDMDDIEA--LcdrVIVIDHGRIIYDG 237
|
250
....*....|....*.
gi 66932952 719 THQQLLAQGGLYAKLV 734
Cdd:COG4586 238 SLEELKERFGPYKTIV 253
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
513-713 |
2.30e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 513 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFyplQGGRVLLDGKPIGaydhkYLhrvislvSQEPVL- 587
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdKEF---EGEARPAPGIKVG-----YL-------PQEPQLd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 588 FARSITDNISYGLPTVpfemvVEAAQKANAHGFIMELQDGYSTETGEKGAQ----------------------------- 638
Cdd:PRK11819 83 PEKTVRENVEEGVAEV-----KAALDRFNEIYAAYAEPDADFDALAAEQGElqeiidaadawdldsqleiamdalrcppw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 639 ------LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQaiHgnLQRH--TVLIIAH-R--LSTVerAHLIV 707
Cdd:PRK11819 158 dakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ--F--LHDYpgTVVAVTHdRyfLDNV--AGWIL 231
|
....*.
gi 66932952 708 VLDKGR 713
Cdd:PRK11819 232 ELDRGR 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
513-676 |
2.39e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 513 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKY-LHRVISLVSQE-PVLFAR 590
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 SITDNISYG-LPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 669
Cdd:PRK10982 89 SVMDNMWLGrYPTKGM-FVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
....*...
gi 66932952 670 -DAESEYL 676
Cdd:PRK10982 166 tEKEVNHL 173
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
518-712 |
3.24e-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: 59.64 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNilENFYPlQGGRVLLDGKPigAYDHKYLHRVISLvsqepvlfaRSITDNis 597
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA-SGKARLISFLP--KFSRNKLIFIDQL---------QFLIDV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 598 yGLptvpfemvveaaqkanahgfimelqdGYSTeTGEKGAQLSGGQKQRVAMARALVRNPP--VLILDEATSALDAESEY 675
Cdd:cd03238 75 -GL--------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 66932952 676 LIQQAIHGNL-QRHTVLIIAHRLSTVERAHLIVVLDKG 712
Cdd:cd03238 127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
499-664 |
3.68e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 499 RVDFENVTFTYrtrphtqvlQNVSFSLSP-------GKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDH 571
Cdd:PRK10522 322 TLELRNVTFAY---------QDNGFSVGPinltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 572 KYLHRVISLVSQEPVLFARSITDNisyglptvPFEMVVEAAQKANAH---GFIMELQDGYSTETgekgaQLSGGQKQRVA 648
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFDQLLGPE--------GKPANPALVEKWLERlkmAHKLELEDGRISNL-----KLSKGQKKRLA 459
|
170
....*....|....*.
gi 66932952 649 MARALVRNPPVLILDE 664
Cdd:PRK10522 460 LLLALAEERDILLLDE 475
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
500-725 |
5.06e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHR-VI 578
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMReAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SLVSQEPVLFAR-SITDNISYGlptvpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 657
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMG------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 658 PVLILDEATSALdaeSEYLIQQaIHGNLQR-----HTVLIIAHR----LSTVERAHlivVLDKGRVVQQGTHQQLLA 725
Cdd:PRK11614 157 RLLLLDEPSLGL---APIIIQQ-IFDTIEQlreqgMTIFLVEQNanqaLKLADRGY---VLENGHVVLEDTGDALLA 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
515-755 |
1.29e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 515 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRvisLVSQEpvlFARSITD 594
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDE---WQRNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 595 NIS-----YGLPTVpfEMVVEAAqKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 669
Cdd:PRK10938 90 MLSpgeddTGRTTA--EIIQDEV-KDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 670 DAESEYLIQQAIHG-NLQRHTVLIIAHRLSTV-ERAHLIVVLDKGRVVQQGTHQQLLAQgGLYAKLVQRQMLG---LEHP 744
Cdd:PRK10938 167 DVASRQQLAELLASlHQSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ-ALVAQLAHSEQLEgvqLPEP 245
|
250
....*....|.
gi 66932952 745 LDYTASHKEPP 755
Cdd:PRK10938 246 DEPSARHALPA 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
500-718 |
2.23e-09 |
|
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: 58.31 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRT-------------------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVL 560
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 561 LDGKPIGaydhkylhrVISL-VSQEPVLFARsitDNIS-----YGLPTvpfemvVEAAQKANahgFIMELqdgysTETGE 634
Cdd:cd03220 81 VRGRVSS---------LLGLgGGFNPELTGR---ENIYlngrlLGLSR------KEIDEKID---EIIEF-----SELGD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 635 KGAQ----LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIA-HRLSTVER-AHLIVV 708
Cdd:cd03220 135 FIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALV 214
|
250
....*....|
gi 66932952 709 LDKGRVVQQG 718
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
512-736 |
3.83e-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: 60.41 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 512 RPHTQVLqNVSFSLSpgKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAyDHKYLHRVISLVSQEPVLFARS 591
Cdd:TIGR01257 943 RPAVDRL-NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 592 itdnisyglpTVPFEMVVEAAQKANAH---GFIME--LQD-GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 665
Cdd:TIGR01257 1019 ----------TVAEHILFYAQLKGRSWeeaQLEMEamLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 666 TSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVE-RAHLIVVLDKGRVVQQGTHQQL--LAQGGLYAKLVQR 736
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLknCFGTGFYLTLVRK 1162
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
515-719 |
6.00e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 515 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQEPVL---- 587
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEipgv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 588 ----FARSI--TDNISYGLPTV-PFEMVVEAAQKANahgfIMELQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPPVL 660
Cdd:CHL00131 100 snadFLRLAynSKRKFQGLPELdPLEFLEIINEKLK----LVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 661 ILDEATSALDAESEYLIQQAIHgNL--QRHTVLIIAH--RLSTVERAHLIVVLDKGRVVQQGT 719
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGIN-KLmtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
520-681 |
1.32e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 520 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQEP----VLFARSITD 594
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 595 NISY-GLPTVPFEMVV--EAAQKANAHGFImelqDGYSTETGEKGAQ---LSGGQKQRVAMARALVRNPPVLILDEATSA 668
Cdd:PRK10762 350 NMSLtALRYFSRAGGSlkHADEQQAVSDFI----RLFNIKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170
....*....|...
gi 66932952 669 LDAESEYLIQQAI 681
Cdd:PRK10762 426 VDVGAKKEIYQLI 438
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
178-443 |
1.71e-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: 56.46 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 178 KPDVAFLVAASFFLIVAALGetfLPYYTGRAIDSIVIQKSMD--QFTTAVVVVCLLAIGssLAAGIRGGIFTLVFARLNI 255
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALA---PPIFMLQVYDRVLPSGSLStlLGLTLGMVVLLAFDG--LLRQVRSRILQRVGLRLDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 256 RLRNCLFRSLVSQETsffdENRTGDLISRLTSDTTMVSDLVSQN--INIFLRNTVKVTGVVVFMFSlSWqLSLVTFMGFP 333
Cdd:cd18586 76 ELGRRVFRAVLELPL----ESRPSGYWQQLLRDLDTLRNFLTGPslFAFFDLPWAPLFLAVIFLIH-PP-LGWVALVGAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 334 IIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRK---EAAAYMSyvW 410
Cdd:cd18586 150 VLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRasdLAGAISA--I 227
|
250 260 270
....*....|....*....|....*....|...
gi 66932952 411 GSGLTlLVVQVSILYYGGHLVISGQMSSGNLIA 443
Cdd:cd18586 228 GKTLR-MALQSLILGVGAYLVIDGELTIGALIA 259
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
504-726 |
4.11e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.89 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 504 NVTFTYRTRPHTQVlQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQG---GRVLLDGKPIGAYDHKYLHRV--- 577
Cdd:PRK09473 19 RVTFSTPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNKLrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 578 -ISLVSQEPVlfaRSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQRVAMAR 651
Cdd:PRK09473 98 qISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphefSGGMRQRVMIAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 652 ALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRLSTVerAHL---IVVLDKGRVVQQGTHQQLLA 725
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLLN-ELKREfntAIIMITHDLGVV--AGIcdkVLVMYAGRTMEYGNARDVFY 251
|
.
gi 66932952 726 Q 726
Cdd:PRK09473 252 Q 252
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
491-695 |
4.33e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 491 LAPDhlEGRVDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlQG--------GRVLLD 562
Cdd:PRK10938 254 LPAN--EPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-QGysndltlfGRRRGS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 563 GKPIgaYDHKylhRVISLVSQEPVLFAR---SITDNI------SYGLptvpFEMVVEAAQKanahgFIMELQD--GYSTE 631
Cdd:PRK10938 328 GETI--WDIK---KHIGYVSSSLHLDYRvstSVRNVIlsgffdSIGI----YQAVSDRQQK-----LAQQWLDilGIDKR 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 632 TGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAI-----HGNLQrhtVLIIAH 695
Cdd:PRK10938 394 TADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdvlisEGETQ---LLFVSH 460
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
520-714 |
6.84e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 520 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHK-YLHRVISLVS---QEPVLFARS-ITD 594
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYLPedrQSSGLYLDApLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 595 NI-SYGLPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALDAE 672
Cdd:PRK15439 361 NVcALTHNRRGF-WIKPARENAVLERYRRAL--NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 66932952 673 SEYLIQQAIHGNLQRHT-VLIIAHRLSTVER-AHLIVVLDKGRV 714
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
522-710 |
7.12e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 522 SFSL------SPGKVTALVGPSGSGKSSCVNILENFYPLQGGRvlLDGKP-----IGAYD----HKYLHRVIS------- 579
Cdd:cd03236 14 SFKLhrlpvpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRgselQNYFTKLLEgdvkviv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 ---LVSQEPVLFARSITDNISYGLPTVPFEMVVEAaqkanahgfiMELQDGYSTETgekgAQLSGGQKQRVAMARALVRN 656
Cdd:cd03236 92 kpqYVDLIPKAVKGKVGELLKKKDERGKLDELVDQ----------LELRHVLDRNI----DQLSGGELQRVAIAAALARD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 657 PPVLILDEATSALDAEseyliqqaihgnlQRHTVLIIAHRLSTVERAHLIV-----VLD 710
Cdd:cd03236 158 ADFYFFDEPSSYLDIK-------------QRLNAARLIRELAEDDNYVLVVehdlaVLD 203
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
230-418 |
7.35e-08 |
|
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: 54.79 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 230 LLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVK 309
Cdd:cd18606 43 GLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 310 VTGVVVfmfslswqLSLVTF----MGFPIIMMVSNIYGKYYKRLSKEVQ--SALARASTTAE--ETISAMKTVRSFANEe 381
Cdd:cd18606 123 IIGTFI--------LIIIYLpwfaIALPPLLVLYYFIANYYRASSRELKrlESILRSFVYANfsESLSGLSTIRAYGAQ- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 66932952 382 eeaEVFLRKLQqvYKLNRKEAAAYMSYV---W--------GSGLTLLV 418
Cdd:cd18606 194 ---DRFIKKNE--KLIDNMNRAYFLTIAnqrWlairldllGSLLVLIV 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
509-724 |
1.51e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 509 YRTRPHTQVL------------QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLH 575
Cdd:PRK11288 248 YRPRPLGEVRlrldglkgpglrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RVISLV----SQEPVLFARSITDN--ISYGLPTVPFEMVVEAAQKA-NAHGFIMELQdgYSTETGE-KGAQLSGGQKQRV 647
Cdd:PRK11288 328 AGIMLCpedrKAEGIIPVHSVADNinISARRHHLRAGCLINNRWEAeNADRFIRSLN--IKTPSREqLIMNLSGGNQQKA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 648 AMARALVRNPPVLILDEATSALD--AESEylIQQAIHGNLQRH-TVLIIAHRLSTV----ERahlIVVLDKGRVV----- 715
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDvgAKHE--IYNVIYELAAQGvAVLFVSSDLPEVlgvaDR---IVVMREGRIAgelar 480
|
....*....
gi 66932952 716 QQGTHQQLL 724
Cdd:PRK11288 481 EQATERQAL 489
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
460-724 |
1.59e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 460 SVYSGLMQGVGAAEKVF-----EFIDRQPTMVHdgslAPDHLEGRVDFE--NVTFTYRTRphtqvLQNVSFSLSPGKVTA 532
Cdd:PRK09700 223 SVCSGMVSDVSNDDIVRlmvgrELQNRFNAMKE----NVSNLAHETVFEvrNVTSRDRKK-----VRDISFSVCRGEILG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 533 LVGPSGSGKSSCVNILENFYPLQGGRVLLDGK---PIGAYDHkyLHRVISLVSQ---EPVLFAR-SITDN--ISYGLPTV 603
Cdd:PRK09700 294 FAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDA--VKKGMAYITEsrrDNGFFPNfSIAQNmaISRSLKDG 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 604 PFEMVV------EAAQKANAHGFIMELQdgySTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD--AESE- 674
Cdd:PRK09700 372 GYKGAMglfhevDEQRTAENQRELLALK---CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAEi 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 66932952 675 YLIQQAIHGnlQRHTVLIIAHRLStveraHLIVVLDKGRVVQQGTHQQLL 724
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 ... |
187-469 |
1.62e-07 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 53.77 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIVIQKSMD--QFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFARLNIRLRNCLFRS 264
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDleSAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 265 LVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQniniFLRNTVK-----VTGVVVFMFSLSWQLSLVTFMGFpIIMMVS 339
Cdd:cd18560 81 LHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSY----LVFYLVPtllelIVVSVVFAFHFGAWLALIVFLSV-LLYGVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 340 NIYG-KYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLV 418
Cdd:cd18560 156 TIKVtEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 66932952 419 VQVSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 469
Cdd:cd18560 236 GLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
623-728 |
1.62e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 623 ELQDGYS-TET-GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQR-HTVLIIAHRLST 699
Cdd:NF000106 127 ELLERFSlTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEE 206
|
90 100 110
....*....|....*....|....*....|
gi 66932952 700 VER-AHLIVVLDKGRVVQQGTHQQLLAQGG 728
Cdd:NF000106 207 AEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
514-700 |
1.89e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 514 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILE---NFYPLQGGRVLLDGKP--------IGAYDHKYLHRVISLVS 582
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPldssfqrsIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 583 QEPVLFAR-------SITDNISYglptvpfemvVEAAQKanahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVR 655
Cdd:TIGR00956 855 ESLRFSAYlrqpksvSKSEKMEY----------VEEVIK------LLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVA 918
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 66932952 656 NPPVLI-LDEATSALDAESEYLIQQAIHgNLQRH--TVLIIAHRLSTV 700
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSICKLMR-KLADHgqAILCTIHQPSAI 965
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
500-718 |
2.13e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGK-PIGAYDHkylHRVI 578
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQ---HHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 SL-VSQEPVLFarsitdnISYGLPTVPfemvveaAQKANAH----GFI--MELQDGYStetgekgaqLSGGQKQRVAMAR 651
Cdd:PLN03073 584 GLdLSSNPLLY-------MMRCFPGVP-------EQKLRAHlgsfGVTgnLALQPMYT---------LSGGQKSRVAFAK 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66932952 652 ALVRNPPVLILDEATSALDAES-EYLIQQAIhgnLQRHTVLIIAHrlstveRAHLIV-VLDKGRVVQQG 718
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAvEALIQGLV---LFQGGVLMVSH------DEHLISgSVDELWVVSEG 700
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
500-703 |
4.04e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.10 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVIS 579
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 580 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYstetgekgaqLSGGQKQRVAMARALVRNPPV 659
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 66932952 660 LILDEATSALDAESEYLIQQAIHGN-LQRHTVLIIAHRLSTVERA 703
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHrAKGGAVLLTSHQDLPLNKA 193
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
524-703 |
6.35e-07 |
|
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: 49.67 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 524 SLSPGKVTALVGPSGSGKSscvNILenfyplqggrvlldgkpigaydhkylhRVISLVsqepVLFARSITDNISYGLPTV 603
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKS---TIL---------------------------DAIGLA----LGGAQSATRRRSGVKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 604 PfemvvEAAQKANAHGFIMelqdgystetgekgaQLSGGQKQRVAMARAL----VRNPPVLILDEATSALDAESEYLIQQ 679
Cdd:cd03227 63 I-----VAAVSAELIFTRL---------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180
....*....|....*....|....*
gi 66932952 680 AIHGNLQRH-TVLIIAHRLSTVERA 703
Cdd:cd03227 123 AILEHLVKGaQVIVITHLPELAELA 147
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
224-391 |
6.73e-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: 51.84 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 224 AVVVVCLLAIGSSLAAGIRGgiftlvfARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIF 303
Cdd:cd18602 62 GAVILSLVTNLAGELAGLRA-------AR---RLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 304 LRNTVKV-TGVVVFMFSLSWQLslvtFMGFPIImMVSNIYGKYYKRLSKEVQ----SALARASTTAEETISAMKTVRSFA 378
Cdd:cd18602 132 LRFLLLClSAIIVNAIVTPYFL----IALIPII-IVYYFLQKFYRASSRELQrldnITKSPVFSHFSETLGGLTTIRAFR 206
|
170
....*....|...
gi 66932952 379 NEEEEAEVFLRKL 391
Cdd:cd18602 207 QQARFTQQMLELI 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
511-686 |
7.14e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 511 TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKylhRVISLVSQEPVLFAR 590
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 -SITDNISY--GLPTVpfemvvEAAQKANAHGFIMELQDGYSTETgekgAQLSGGQKQRVAMARALVRNPPVLILDEATS 667
Cdd:PRK13543 97 lSTLENLHFlcGLHGR------RAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170
....*....|....*....
gi 66932952 668 ALDAESEYLIQQAIHGNLQ 686
Cdd:PRK13543 167 NLDLEGITLVNRMISAHLR 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
518-681 |
7.16e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQE----------PV 586
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyaylDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 LFARSITDNISYglpTVPFEMVVEAAQKANAHGFI--MELQD-GYSTETGekgaQLSGGQKQRVAMARALVRNPPVLILD 663
Cdd:PRK10982 344 GFNSLISNIRNY---KNKVGLLDNSRMKSDTQWVIdsMRVKTpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170
....*....|....*...
gi 66932952 664 EATSALDAESEYLIQQAI 681
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLI 434
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
518-723 |
8.36e-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: 52.71 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 518 LQNVSFSLSPGKVTALVGPSGSGKSSCVN-----ILENFYpLQGGRVLLDGKPIGAYDHkyLHRVISlVSQEPV------ 586
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypALANRL-NGAKTVPGRYTSIEGLEH--LDKVIH-IDQSPIgrtprs 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 --------------LFARS--------------------------------ITDNIsygLPT--VP-------------- 604
Cdd:TIGR00630 700 npatytgvfdeireLFAETpeakvrgytpgrfsfnvkggrceacqgdgvikIEMHF---LPDvyVPcevckgkrynretl 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 605 ------------FEMVVEAAQK-----ANAHGFIMELQD---GYSTeTGEKGAQLSGGQKQRVAMARALVR---NPPVLI 661
Cdd:TIGR00630 777 evkykgkniadvLDMTVEEAYEffeavPSISRKLQTLCDvglGYIR-LGQPATTLSGGEAQRIKLAKELSKrstGRTLYI 855
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 662 LDEATSALDAES----EYLIQQAIHgnlQRHTVLIIAHRLSTVERAHLIVVL-----DK-GRVVQQGTHQQL 723
Cdd:TIGR00630 856 LDEPTTGLHFDDikklLEVLQRLVD---KGNTVVVIEHNLDVIKTADYIIDLgpeggDGgGTVVASGTPEEV 924
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
508-715 |
9.45e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 508 TYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQEP- 585
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 586 ----VLfARSITDNI----SYGLPTVPFEMVVEAAQKANAHGFIMELQ---DGYSTETGekgaQLSGGQKQRVAMARALV 654
Cdd:COG3845 344 grglVP-DMSVAENLilgrYRRPPFSRGGFLDRKAIRAFAEELIEEFDvrtPGPDTPAR----SLSGGNQQKVILARELS 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66932952 655 RNPPVLILDEATSALDAESeyliQQAIHGNL-----QRHTVLIIAHRLSTV-ERAHLIVVLDKGRVV 715
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGA----IEFIHQRLlelrdAGAAVLLISEDLDEIlALSDRIAVMYEGRIV 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
524-695 |
1.20e-06 |
|
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: 50.48 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 524 SLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgAYDHKYLHRVISLVSQEpvlFARSITDnisyGLPTV 603
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYEGTVRD---LLSSITK----DFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 604 PFeMVVEAAQKanahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG 683
Cdd:cd03237 93 PY-FKTEIAKP-------LQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170
....*....|....
gi 66932952 684 NLQRH--TVLIIAH 695
Cdd:cd03237 161 FAENNekTAFVVEH 174
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
178-444 |
1.55e-06 |
|
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: 50.55 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 178 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDSIVIQKSMDQFTtavvvvcLLAIGSSLAAGIRGGIFTL---VFARLN 254
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGL---VIPVFSRIFIDDILVGGLPDWLR-------PLLLGMALTALLQGLLTWLqqyYLLRLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 255 IRLrnclfrSLVSQET----------SFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLrNTVKVTGVVVFMFSLSWQL 324
Cdd:cd18569 71 TKL------ALSSSSRffwhvlrlpvEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVL-NLVMAVFYALLMLQYDVPL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 325 SLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEeaevFLRKL--QQVYKLNRKEA 402
Cdd:cd18569 144 TLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESD----FFSRWagYQAKVLNAQQE 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 66932952 403 AAYMSYVWGSGLTLL--VVQVSILYYGGHLVISGQMSSGNLIAF 444
Cdd:cd18569 220 LGRTNQLLGALPTLLsaLTNAAILGLGGLLVMDGALTIGMLVAF 263
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
501-695 |
1.78e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 501 DFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNI-LENFYPlQGGRVLLDGKPIGAY-DHkylHRVI 578
Cdd:PRK11147 321 EMENVNYQI---DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHCGTKLEVAYfDQ---HRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 slvsQEPvlfARSITDNISYGLPTVpfeMVveAAQKANAHGFimeLQD----GYSTETGEKGaqLSGGQKQRVAMARALV 654
Cdd:PRK11147 394 ----LDP---EKTVMDNLAEGKQEV---MV--NGRPRHVLGY---LQDflfhPKRAMTPVKA--LSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 66932952 655 RNPPVLILDEATSALDAESEYLIQQAIHGnlQRHTVLIIAH 695
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDS--YQGTVLLVSH 495
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
522-670 |
2.06e-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: 51.32 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 522 SFSL------SPGKVTALVGPSGSGKSSCVNILenfyplqGGRVlldgKP-IGAYDHKylhrvislVSQEPVL--FARSI 592
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKIL-------SGEL----KPnLGDYDEE--------PSWDEVLkrFRGTE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 593 TDNisYglptvpFEMVVE----AAQKANAHGFIMELQDGYSTE----TGEKGA-------------------QLSGGQKQ 645
Cdd:COG1245 148 LQD--Y------FKKLANgeikVAHKPQYVDLIPKVFKGTVREllekVDERGKldelaeklglenildrdisELSGGELQ 219
|
170 180
....*....|....*....|....*
gi 66932952 646 RVAMARALVRNPPVLILDEATSALD 670
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
525-697 |
2.36e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 525 LSPGKVTALVGPSGSGKSSCVNILenfyplqGGRVlldgKP-IGAYDHKylhrvislVSQEPVL--FARSITDNisYglp 601
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGEL----IPnLGDYEEE--------PSWDEVLkrFRGTELQN--Y--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 602 tvpFEMVVE----AAQKANAHGFIMELQDGYSTE----TGEKGA-------------------QLSGGQKQRVAMARALV 654
Cdd:PRK13409 152 ---FKKLYNgeikVVHKPQYVDLIPKVFKGKVREllkkVDERGKldevverlglenildrdisELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 66932952 655 RNPPVLILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRL 697
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
515-737 |
5.05e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 515 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL--ENFYPLQGGRVLLDGKPIGAYD-HKYLHRVISLVSQEPV----- 586
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 587 ---LFARSITDNI-SY----GLPTVPFEMVVEAAQKanahgfIMELQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPP 658
Cdd:PRK09580 94 snqFFLQTALNAVrSYrgqePLDRFDFQDLMEEKIA------LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 659 VLILDEATSALDAESEYLIQQAIHgNLQ--RHTVLIIAH--RLSTVERAHLIVVLDKGRVVQQGTH---QQLLAQGglYA 731
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVN-SLRdgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQG--YG 242
|
....*.
gi 66932952 732 KLVQRQ 737
Cdd:PRK09580 243 WLTEQQ 248
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
256-475 |
5.70e-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: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 256 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 335
Cdd:cd18561 70 HLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 336 MMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAayMSyVWGSGLT 415
Cdd:cd18561 150 PLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLA--VS-LLSSGIM 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 416 LLVVQVSI---LYYGGHLVISGQMSSGNLIAFIiyeFVLGDC---MESVGSVYSGLMQGVGAAEKV 475
Cdd:cd18561 227 GLATALGTalaLGVGALRVLGGQLTLSSLLLIL---FLSREFfrpLRDLGAYWHAGYQGISAADSI 289
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
314-446 |
9.25e-06 |
|
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: 48.20 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 314 VVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEeeeaevflRKLQQ 393
Cdd:cd18587 132 LAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAE--------GRMQR 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932952 394 VYKlnrkEAAAYMSYV---------WGSGLTLLVVQ---VSILYYGGHLVISGQMSSGNLIAFII 446
Cdd:cd18587 204 RWE----EAVAALARSslksrllssSATNFAQFVQQlvtVAIVIVGVYLISDGELTMGGLIACVI 264
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
520-728 |
1.02e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 520 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRV------ISL-----VSQEPVLF 588
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVgymsqaFSLygeltVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 589 ARSitdnisYGLP--TVPfEMVVEAAQKanahgFimELQDgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 666
Cdd:NF033858 364 ARL------FHLPaaEIA-ARVAEMLER-----F--DLAD----VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 667 S-----ALDAESEYLIQqaihgnLQRH---TVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGG 728
Cdd:NF033858 426 SgvdpvARDMFWRLLIE------LSREdgvTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
500-725 |
2.07e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLQGGRVLLDGKPIGAYDHKYL 574
Cdd:PRK15093 4 LDIRNLTIEFKTSDGwVKAVDRVSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 575 HRVI----SLVSQEP---VLFARSITDNISYGLP----------------TVPFEMVVEAAQKAnaHGFIMElqdGYSTE 631
Cdd:PRK15093 84 RKLVghnvSMIFQEPqscLDPSERVGRQLMQNIPgwtykgrwwqrfgwrkRRAIELLHRVGIKD--HKDAMR---SFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 632 tgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESeyliQQAIHGNLQR------HTVLIIAHRLSTVER-AH 704
Cdd:PRK15093 159 -------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTT----QAQIFRLLTRlnqnnnTTILLISHDLQMLSQwAD 227
|
250 260
....*....|....*....|.
gi 66932952 705 LIVVLDKGRVVQQGTHQQLLA 725
Cdd:PRK15093 228 KINVLYCGQTVETAPSKELVT 248
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
224-408 |
4.08e-05 |
|
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: 46.40 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 224 AVVVVCLLAIgsslaagIRGGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIF 303
Cdd:cd18599 67 SILVILLLSL-------IRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 304 LRNTVKVTGVVVF-MFSLSWQLSLVTFMG--FPIIMMVSNIYGKYYKRLSKEVQSALArASTTAeeTISAMKTVRSFANE 380
Cdd:cd18599 140 LQNVLLVVFSLIIiAIVFPWFLIALIPLAiiFVFLSKIFRRAIRELKRLENISRSPLF-SHLTA--TIQGLSTIHAFNKE 216
|
170 180
....*....|....*....|....*...
gi 66932952 381 EEeaevFLRKLQQVykLNRKEAAAYMSY 408
Cdd:cd18599 217 KE----FLSKFKKL--LDQNSSAFFLFN 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
507-718 |
5.33e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 507 FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFYPLQGGRVLLDGKPIGAYDHKYLHRVI---- 578
Cdd:TIGR00956 66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVynae 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 579 ------SLVSQEPVLF-ARSITDNISYGLPTvpfeMVVEAAQKANAHGFIMELQDGYSTETGE---KGaqLSGGQKQRVA 648
Cdd:TIGR00956 146 tdvhfpHLTVGETLDFaARCKTPQNRPDGVS----REEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVS 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 649 MARALVRNPPVLILDEATSALDAESEYLIQQAIH--GNLQRHTVLIIAHRLS--TVERAHLIVVLDKGRVVQQG 718
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKtsANILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
516-690 |
6.00e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 516 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEnfyplqggrvlldGKPIGAYDHKYLHrvISLVSQEPVLFAR----- 590
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA-------------GRKTGGYIEGDIR--ISGFPKKQETFARisgyc 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 591 ----------SITDNISY-GLPTVPFEmvVEAAQKANAHGFIMEL------QDGYSTETGEKGaqLSGGQKQRVAMARAL 653
Cdd:PLN03140 959 eqndihspqvTVRESLIYsAFLRLPKE--VSKEEKMMFVDEVMELveldnlKDAIVGLPGVTG--LSTEQRKRLTIAVEL 1034
|
170 180 190
....*....|....*....|....*....|....*..
gi 66932952 654 VRNPPVLILDEATSALDAESEYLIQQAIhgnlqRHTV 690
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLDARAAAIVMRTV-----RNTV 1066
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
225-409 |
6.93e-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: 45.54 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 225 VVVVCLLAIGSSLAAGIRggifTLVFARLNIRLRNCLFRSLVSQ----ETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 300
Cdd:cd18604 46 LGIYALISLLSVLLGTLR----YLLFFFGSLRASRKLHERLLHSvlraPLRWLDTTPVGRILNRFSKDIETIDSELADSL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 301 NIFLRNTVKVTGVVVFMFSLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQsalaRASTTA--------EETISAMK 372
Cdd:cd18604 122 SSLLESTLSLLVILIAIVVVSPAFLLPAV----VLAALYVYIGRLYLRASRELK----RLESVArspilshfGETLAGLV 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 66932952 373 TVRSFANEeeeaEVFLRKLQQvyKLNRKEAAAYMSYV 409
Cdd:cd18604 194 TIRAFGAE----ERFIEEMLR--RIDRYSRAFRYLWN 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
522-695 |
1.09e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 522 SFSLS-------PGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKpIgAYDHKYlhrvISLVSQEPV-LFARSIT 593
Cdd:PRK13409 352 DFSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-I-SYKPQY----IKPDYDGTVeDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 594 DNISyglpTVPFEmvVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 673
Cdd:PRK13409 426 DDLG----SSYYK--SEIIKPLQ----LERLLDKNVKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180
....*....|....*....|....*....
gi 66932952 674 EYLIQQAIhgnlqRH-------TVLIIAH 695
Cdd:PRK13409 489 RLAVAKAI-----RRiaeereaTALVVDH 512
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
500-672 |
1.13e-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: 45.70 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 500 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL---ENfyPLQGGRVLLDGKPIGAYDHkylhr 576
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMItgqEQ--PDSGTIEIGETVKLAYVDQ----- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 vislvSQEPVLFARSITDNISYGLPTVpfeMV--VEAAQKANAHGFIMELQDgysteTGEKGAQLSGGQKQRVAMARALV 654
Cdd:TIGR03719 393 -----SRDALDPNKTVWEEISGGLDII---KLgkREIPSRAYVGRFNFKGSD-----QQKKVGQLSGGERNRVHLAKTLK 459
|
170
....*....|....*...
gi 66932952 655 RNPPVLILDEATSALDAE 672
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVE 477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
504-695 |
1.36e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 504 NVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLD-GKPIG-------AYDHkylH 575
Cdd:PRK15064 6 NITMQFGAKP---LFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGklrqdqfAFEE---F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 576 RVISLV--SQEPVLFARSITDNIsYGLPtvpfEMVVEAAQKAnahgfiMELQ------DGYSTET--GE--KGA------ 637
Cdd:PRK15064 80 TVLDTVimGHTELWEVKQERDRI-YALP----EMSEEDGMKV------ADLEvkfaemDGYTAEAraGEllLGVgipeeq 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66932952 638 ------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhgNLQRHTVLIIAH 695
Cdd:PRK15064 149 hyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL--NERNSTMIIISH 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
527-728 |
1.43e-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: 45.77 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 527 PGKVTALVGPSGSGKSSCVNILENFYPLQGGRVLLDGKPIgAYDHKYLHRVISLVSQ------------EPVLFARsitd 594
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQfdaiddlltgreHLYLYAR---- 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 595 nisygLPTVPFEMVVEAAQKAnahgfIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 674
Cdd:TIGR01257 2039 -----LRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 66932952 675 YLIQQAIHGNLQR-HTVLIIAHRLSTVER-AHLIVVLDKGRVVQQGTHQQLLAQGG 728
Cdd:TIGR01257 2107 RMLWNTIVSIIREgRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
241-381 |
1.55e-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: 44.62 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 241 IRGGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSL 320
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 321 S-WqlslvTFMGFPIIMMVSNIYGKYYKRLSKEVQ--SALARA------STtaeeTISAMKTVRSFANEE 381
Cdd:cd18601 158 NpW-----VLIPVIPLVILFLFLRRYYLKTSREVKriEGTTRSpvfshlSS----TLQGLWTIRAYSAQE 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
513-677 |
2.29e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 513 PHTQVLQNVSFSLSPGKVTALVGPSGSG----------KSSCVNIlenfyplqGGRVLLDGKPI------GAYDHKylhr 576
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGrtelamsvfgRSYGRNI--------SGTVFKDGKEVdvstvsDAIDAG---- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 577 vISLVSQepvlfarsitDNISYGL---PTVPFEMVVEAAQKANAHGFI---MELQ--DGY-------STETGEKGAQLSG 641
Cdd:NF040905 339 -LAYVTE----------DRKGYGLnliDDIKRNITLANLGKVSRRGVIdenEEIKvaEEYrkkmnikTPSVFQKVGNLSG 407
|
170 180 190
....*....|....*....|....*....|....*.
gi 66932952 642 GQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 677
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 ... |
639-697 |
2.72e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 2.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66932952 639 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQRH---TVLIIAHRL 697
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR-RLSEEgkkTALVVEHDL 132
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
639-695 |
3.08e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.00 E-value: 3.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66932952 639 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhgnlQRH------TVLIIAH 695
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI----RRFaenrgkTAMVVDH 514
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
639-709 |
3.09e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 3.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66932952 639 LSGGQKQRVAMARAL---VRNPPVLILDEATSALDAESeylIQQAIHGNL----QRHTVLIIAHRLSTVERAHLIVVL 709
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHD---IKALIYVLQslthQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
639-725 |
3.14e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 639 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI----QQAIHgnLQRHTVLI--IAHRLSTVERAHLIVVLDKG 712
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIvkclQQIVH--LTEATVLMslLQPAPETFDLFDDIILLSEG 414
|
90
....*....|...
gi 66932952 713 RVVQQGTHQQLLA 725
Cdd:PLN03140 415 QIVYQGPRDHILE 427
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
187-422 |
6.03e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)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. ABC transporters typically consist 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: 350023 [Multi-domain] Cd Length: 289 Bit Score: 42.47 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 187 ASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDqFTTAVVVVCLLAIGSSLAAGIRGGIFTLVFaRLNIRLRNCL----F 262
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEP-LSEGYLLALALFLVSLLQSLLLHQYFFLSF-RLGMRVRSALssliY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 263 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVsQNINIFLRNTVKVTGVVVFMFslsWQLSLVTFMGF-------PII 335
Cdd:cd18579 80 RKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLY---RLLGWAALAGLgvlllliPLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 336 MMVSNIYGKYYKRLSKEVQsalARASTTAeETISAMKTVRSFANEeeeaEVFLRKLQqvyKLNRKEAAAYMSYVWGSGLT 415
Cdd:cd18579 156 AFLAKLISKLRKKLMKATD---ERVKLTN-EILSGIKVIKLYAWE----KPFLKRIE---ELRKKELKALRKFGYLRALN 224
|
....*..
gi 66932952 416 LLVVQVS 422
Cdd:cd18579 225 SFLFFST 231
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
277-446 |
9.64e-04 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 41.70 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 277 RTGDLISRLTSDttmvsdlVSQNINIFLR-------NTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMV-SNIYGKYYKR 348
Cdd:cd18585 90 RSGDLLNRIVAD-------IDTLDNLYLRvlsppvvALLVILATILFLAFFSPALALILLAGLLLAGVViPLLFYRLGKK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 349 LSKEVQSALARASTTAEETISAMKTVRSFANEEeeaevflRKLQQVYKLNRK--EAAAYMSYV--WGSGLTLLVVQVS-- 422
Cdd:cd18585 163 IGQQLVQLRAELRTELVDGLQGMAELLIFGALE-------RQRQQLEQLSDAliKEQRRLARLsgLSQALMILLSGLTvw 235
|
170 180
....*....|....*....|....*
gi 66932952 423 -ILYYGGHLVISGQMsSGNLIAFII 446
Cdd:cd18585 236 lVLWLGAPLVQNGAL-DGALLAMLV 259
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
183-469 |
1.46e-03 |
|
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: 41.47 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 183 FLVAASFFLIVAALGETFLPYYTGRAIDSIV--IQKSMDQ-FTTAVVVVCLLAIGSSLAAgIRGGIFTLVFARLNIRLRN 259
Cdd:cd18556 3 LFFSILFISLLSSILISISPVILAKITDLLTssSSDSYNYiVVLAALYVITISATKLLGF-LSLYLQSSLRVELIISISS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 260 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 339
Cdd:cd18556 82 SYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFLLYAVLFVIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 340 NiyGKYYKRLSK---EVQSALARASTTAEETISAMKTVRSFANeeeeAEVFLRKLQQVYKLNRKEAAAYmsyvWGSGLTL 416
Cdd:cd18556 162 N--TIFTKKIVSlrnDLMDAGRKSYSLLTDSVKNIVAAKQNNA----FDFLFKRYEATLTNDRNSQKRY----WKLTFKM 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66932952 417 LVVQV--------SILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 469
Cdd:cd18556 232 LILNSllnvilfgLSFFYSLYGVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
638-670 |
2.53e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 2.53e-03
10 20 30
....*....|....*....|....*....|...
gi 66932952 638 QLSGGQKQRVAMARALVRNPPVLILDEATSALD 670
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
233-426 |
2.91e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) 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: 350040 [Multi-domain] Cd Length: 309 Bit Score: 40.56 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 233 IGSSLAAGIRGGIFTLVFAR-LNIRLRNCLFRSLVSQETSFFDE------NRTGDLISRLTSDTTMVSDLVSqNINIFLR 305
Cdd:cd18596 62 IGRRLSVRLRAILTQLIFEKaLRRRDKSGSSKSSESKKKDKEEDedekssASVGKINNLMSVDANRISEFAA-FLHLLVS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 306 NTVKVTGVVVFMFSLSWQLSLV----TFMGFPIIMMVSNIYGKYYKRLSKevqSALARASTTAeETISAMKTVRSFANEE 381
Cdd:cd18596 141 APLQIVIAIVFLYRLLGWSALVglavMVLLLPLNGYLAKRYSRAQKELMK---ARDARVQLVT-EVLQGIRMIKFFAWER 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 66932952 382 E---------EAEvfLRKLQQVYKLNrkeaaAYMSYVWgSGLTLLVVQVSILYY 426
Cdd:cd18596 217 KweerilearEEE--LKWLRKRFLLD-----LLLSLLW-FLIPILVTVVTFATY 262
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
638-673 |
5.47e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.74 E-value: 5.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66932952 638 QLSGGQKQ------RVAMARALVRNPPVLILDEATSALDAES 673
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
184-445 |
7.76e-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: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 184 LVAASFFLIVAALGEtflPYYTGRAIDSIVIQKSmdqfttavvVVCLLAIGSSL-AAGIRGGIFTLVFA-RLNIRLRNCL 261
Cdd:cd18562 4 LALANVALAGVQFAE---PVLFGRVVDALSSGGD---------AFPLLALWAALgLFSILAGVLVALLAdRLAHRRRLAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 262 ----FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 337
Cdd:cd18562 72 masyFEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932952 338 VSNIYGKYYKRLSKEVQSALARASTTAEETISAMKTVRSFANEEEEAEVFLRKLQQVyklnrkEAAAYMSYVWGSGLTLL 417
Cdd:cd18562 152 LNRLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRL------LAAQYPVLNWWALASVL 225
|
250 260 270
....*....|....*....|....*....|....
gi 66932952 418 ------VVQVSILYYGGHLVISGQMSSGNLIAFI 445
Cdd:cd18562 226 traastLTMVAIFALGAWLVQRGELTVGEIVSFV 259
|
|
| |
