|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
44-681 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 698.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 44 FDSVLDLWAACLYRSCLLLGATIGVAKNSAlgpRRLRASWL-VITLVCLFVGIYAMVKLLLFSEVRRPI--RDPWFWALF 120
Cdd:TIGR00958 35 EKGLYVLWLEGTLRLGVLWLGALGILLNKA---GGLLAAVKpLVAALCLATPSLSSLRALAFWEALDPAvrVALGLWSWF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 121 VWTYISLGASFLLWWLLSTvrPGTQALEPgaateaegfpgsgrpPPEQAS-GATLQKLLSYTKPDVAFLVAASFFLIVAA 199
Cdd:TIGR00958 112 VWSYGAALPAAALWAVLSS--AGASEKEA---------------EQGQSEtADLLFRLLGLSGRDWPWLISAFVFLTLSS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 200 LGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDE 279
Cdd:TIGR00958 175 LGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 280 NRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQN 359
Cdd:TIGR00958 255 NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 360 ALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQ 439
Cdd:TIGR00958 335 AVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 440 MTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHT 519
Cdd:TIGR00958 415 VSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDN 599
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVREN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 600 ISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 679
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
..
gi 339895787 680 LI 681
Cdd:TIGR00958 655 LL 656
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
191-479 |
0e+00 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 523.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 339895787 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
169-681 |
6.18e-170 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 498.54 E-value: 6.18e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 169 ASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGG 248
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 249 IFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQL 328
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 329 SLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAA 408
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 409 YMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPT 488
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 489 MVH-DGSLAPDHLEGRVDFENVTFTYrtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG 567
Cdd:COG1132 324 IPDpPGAVPLPPVRGEIEFENVSFSY--PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 568 KPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQ 647
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510
....*....|....*....|....*....|....
gi 339895787 648 KQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALI 515
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
191-479 |
1.11e-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: 384.59 E-value: 1.11e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 339895787 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
493-681 |
4.71e-128 |
|
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: 377.97 E-value: 4.71e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 493 GSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA 572
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 573 YDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVA 652
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180
....*....|....*....|....*....
gi 339895787 653 MARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQV 189
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
174-681 |
2.09e-120 |
|
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: 375.33 E-value: 2.09e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 174 LQKLLSYTKPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLI 253
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLAL---ATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 254 FARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 334 MGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV 413
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 414 WGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYefvlgdcmesVGSVYSGLMQGVG----------AAEKVFEFI 483
Cdd:COG2274 383 TLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNIL----------SGRFLAPVAQLIGllqrfqdakiALERLDDIL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 484 DRQPTMVHDGS-LAPDHLEGRVDFENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGR 562
Cdd:COG2274 453 DLPPEREEGRSkLSLPRLKGDIELENVSFRYPGDS-PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 563 VLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQ 642
Cdd:COG2274 532 ILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSN 611
|
490 500 510
....*....|....*....|....*....|....*....
gi 339895787 643 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII 650
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
173-681 |
2.66e-113 |
|
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: 352.48 E-value: 2.66e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 173 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQfstaVVIVCLLAIGSSFAAGIRGGIFTL 252
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSV----LWWVPLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 253 IFARLNIR----LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQL 328
Cdd:TIGR02203 77 LLSWVSNKvvrdIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 329 SLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAA 408
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 409 YMYYvwgSGLTLLVVQVS---ILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDr 485
Cdd:TIGR02203 237 GSIS---SPITQLIASLAlavVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 486 QPTMVHDGSLAPDHLEGRVDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL 565
Cdd:TIGR02203 313 SPPEKDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 566 DGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLS 644
Cdd:TIGR02203 392 DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLS 471
|
490 500 510
....*....|....*....|....*....|....*..
gi 339895787 645 GGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLV 508
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
191-479 |
5.55e-97 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 300.41 E-value: 5.55e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKL-NRKEAAAYMYYVWGSGLTLLvVQVSILY 429
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLkDRRDTVRAVYLLVRRVLQLG-VQVLMLY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 339895787 430 YGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18590 240 CGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
191-479 |
5.63e-93 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 289.85 E-value: 5.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYY 430
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 339895787 431 GGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
173-681 |
9.80e-90 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 291.15 E-value: 9.80e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 173 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDgiviqksmDQFSTA----VVIVCLLAIGSSFAAGIRGG 248
Cdd:PRK11176 12 TFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLD--------DGFGKAdrsvLKWMPLVVIGLMILRGITSF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 249 IFTLIFA------RLNIRLRncLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMF 322
Cdd:PRK11176 84 ISSYCISwvsgkvVMTMRRR--LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 323 SLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrKLQQVYKLN 402
Cdd:PRK11176 162 YYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK----RFDKVSNRM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 403 RKEAaayMYYVWGSGLTLLVVQ-------VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGA 475
Cdd:PRK11176 238 RQQG---MKMVSASSISDPIIQliaslalAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 476 AEKVFEFIDRQPTmVHDGSLAPDHLEGRVDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF 555
Cdd:PRK11176 315 CQTLFAILDLEQE-KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 556 YPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYST 634
Cdd:PRK11176 393 YDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDT 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 339895787 635 ETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK11176 473 VIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI 519
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
504-681 |
8.46e-89 |
|
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: 277.11 E-value: 8.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170
....*....|....*...
gi 339895787 664 LILDEATSALDAESEYLI 681
Cdd:cd03249 161 LLLDEATSALDAESEKLV 178
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
193-479 |
1.28e-86 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 273.19 E-value: 1.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 193 FFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQ 272
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 273 ETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKR 352
Cdd:cd18589 83 EIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 353 LSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGG 432
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 339895787 433 HLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18589 243 QLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
191-479 |
4.28e-80 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 256.41 E-value: 4.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQ------KSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNC 264
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHsgsggeEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 265 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYvwgSGLTLLVVQ 424
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGF---NGFMGAAAQ 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895787 425 VSI---LYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18780 238 LAIvlvLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
191-479 |
7.60e-77 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 247.81 E-value: 7.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 191 ASFFLIVAALGETFLPYYTGRAID------GIVIQKSMDQFSTAVVIVCLLAIGSsFAAGIRGGIFTLIFARLNIRLRNC 264
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDvaskesGDIEIFGLSLKTFALALLGVFVVGA-AANFGRVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 265 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQ 424
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 425 VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18573 240 LSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
175-681 |
3.10e-76 |
|
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: 254.68 E-value: 3.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 175 QKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIF 254
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 255 A-RLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTsdtTMVSDL-------VSQNINVFLrntVKVTgVVVFMFSLSW 326
Cdd:COG4988 86 AaRVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLT---EGVEALdgyfaryLPQLFLAAL---VPLL-ILVAVFPLDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 327 QLSLVTFMGFPII---MMvsnIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrklqQVYKLNR 403
Cdd:COG4988 159 LSGLILLVTAPLIplfMI---LVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAE-------RIAEASE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 404 KEAAAYMyyvwG-------SGLTL-LVVQVSI---LYYGGHLVISGQMT--SGNLIAFIIYEFVLGdcMESVGSVYSGLM 470
Cdd:COG4988 229 DFRKRTM----KvlrvaflSSAVLeFFASLSIalvAVYIGFRLLGGSLTlfAALFVLLLAPEFFLP--LRDLGSFYHARA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 471 QGVGAAEKVFEFIDRQPTMVHDGSL-APDHLEGRVDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV 549
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTApLPAAGPPSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 550 NILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQ 629
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALP 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 339895787 630 DGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI 512
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
159-678 |
2.33e-75 |
|
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: 253.59 E-value: 2.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 159 PGSGRPPPEQASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLA-- 236
Cdd:COG5265 6 AMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAyg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 237 ---IGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDL---ISRLTSDT-TMVSDLVSQNINVFLR 309
Cdd:COG5265 86 llrLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIERGTKGIeFLLRFLLFNILPTLLE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 310 nTVKVTGVVVFMFSlsWQLSLVTFmgfpiIMMVSNIYgkyYKRLSKEVQNALARASNTAEeTISAMK---------TVRS 380
Cdd:COG5265 166 -IALVAGILLVKYD--WWFALITL-----VTVVLYIA---FTVVVTEWRTKFRREMNEAD-SEANTRavdsllnyeTVKY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 381 FANEEEEAEVYLRKLQqvyklnRKEAAAYMyyVWGSGLTLLVVQ--------VSILYYGGHLVISGQMTSGNLI---AFI 449
Cdd:COG5265 234 FGNEAREARRYDEALA------RYERAAVK--SQTSLALLNFGQaliialglTAMMLMAAQGVVAGTMTVGDFVlvnAYL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 450 IYEFV-LGdcmeSVGSVYSGLMQGVGAAEKVFEFIDRQPTmVHDgslAPD--HL---EGRVDFENVTFTYRtrPHTQVLQ 523
Cdd:COG5265 306 IQLYIpLN----FLGFVYREIRQALADMERMFDLLDQPPE-VAD---APDapPLvvgGGEVRFENVSFGYD--PERPILK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYG 603
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 604 LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 678
Cdd:COG5265 456 RPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
504-681 |
8.69e-72 |
|
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: 232.51 E-value: 8.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170
....*....|....*...
gi 339895787 664 LILDEATSALDAESEYLI 681
Cdd:cd03251 160 LILDEATSALDTESERLV 177
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
260-678 |
8.34e-71 |
|
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: 240.44 E-value: 8.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDttmVSDLVsqniNVFLR-------NTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVAD---VDALD----NLYLRvllpllvALLVILAAVAFLAFFSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 333 FMGF-------PIIMMVSNiygkyyKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKE 405
Cdd:COG4987 162 ALGLllaglllPLLAARLG------RRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 406 AAAYMyyvWGSGLTLLVVQ---VSILYYGGHLVISGQMtSGNLIAFIIYeFVLGdCMESVGSVySGLMQGVG----AAEK 478
Cdd:COG4987 236 ARLSA---LAQALLQLAAGlavVAVLWLAAPLVAAGAL-SGPLLALLVL-AALA-LFEALAPL-PAAAQHLGrvraAARR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 479 VFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPL 558
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 559 EGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGE 638
Cdd:COG4987 388 QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 339895787 639 KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 678
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE 507
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
173-681 |
1.56e-70 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 240.39 E-value: 1.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 173 TLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMdqfstAVVIVCLLA---IGSSFAAGIRGGI 249
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNL-----PLGLVAGLAaayVGLQLLAAGLHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 250 FTLIFARLNI----RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLS 325
Cdd:PRK10790 85 QSLLFNRAAVgvvqQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 326 WQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrKLQQVyklNRKE 405
Cdd:PRK10790 165 WRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGE----RMGEA---SRSH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 406 AAAYMYYVWGSGLTL--LVVQVSILYYGGHLVI-----SGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEK 478
Cdd:PRK10790 238 YMARMQTLRLDGFLLrpLLSLFSALILCGLLMLfgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 479 VFEFID--RQPTMVHDGSLApdhlEGRVDFENVTFTYRT-RPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF 555
Cdd:PRK10790 318 VFELMDgpRQQYGNDDRPLQ----SGRIDIDNVSFAYRDdNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 556 YPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPtVPFEMVVEAAQKANAHGFIMELQDGYSTE 635
Cdd:PRK10790 391 YPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTP 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 339895787 636 TGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK10790 470 LGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI 515
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
502-681 |
7.62e-69 |
|
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: 224.41 E-value: 7.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 502 GRVDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 581
Cdd:cd03254 1 GEIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180
....*....|....*....|
gi 339895787 662 PVLILDEATSALDAESEYLI 681
Cdd:cd03254 159 KILILDEATSNIDTETEKLI 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
504-681 |
1.58e-66 |
|
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: 218.64 E-value: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170
....*....|....*...
gi 339895787 664 LILDEATSALDAESEYLI 681
Cdd:cd03253 159 LLLDEATSALDTHTEREI 176
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
181-681 |
2.52e-65 |
|
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: 224.86 E-value: 2.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 181 TKPDVAFLVAASFFLIVAALGETFLpyyTGRAIDGIVIQKS-MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNI 259
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWL---LARVVDGLISAGEpLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQ---LSLVTFMGF 336
Cdd:TIGR02857 78 QLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWIsglILLLTAPLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 337 PIIMMVSniyGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVyLRKLQQVYklnRKEAAAYMYYVWGS 416
Cdd:TIGR02857 158 PIFMILI---GWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA-IRRSSEEY---RERTMRVLRIAFLS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 417 GLTL-----LVVQVSILYYGGHLViSGQMT--SGNLIAFIIYEFVLGdcMESVGSVYSGLMQGVGAAEKVFEFIDRQPTM 489
Cdd:TIGR02857 231 SAVLelfatLSVALVAVYIGFRLL-AGDLDlaTGLFVLLLAPEFYLP--LRQLGAQYHARADGVAAAEALFAVLDAAPRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 490 VHDGSLAPDHLEGRVDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKP 569
Cdd:TIGR02857 308 LAGKAPVTAAPASSLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 570 ISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQ 649
Cdd:TIGR02857 386 LADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQ 465
|
490 500 510
....*....|....*....|....*....|..
gi 339895787 650 RVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
178-678 |
6.10e-65 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 225.23 E-value: 6.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 178 LSYTKPD---VAFLVAASFFLIVAALGEtflPYYTGRAIDgiVIQKSMDQFSTAVVIVCLlaigssfaagirgGIFTLIF 254
Cdd:PRK13657 11 LQYLGAEkrlGILLAVANVLLAAATFAE---PILFGRIID--AISGKGDIFPLLAAWAGF-------------GLFNIIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 255 A--------RLNIRLRNCL----FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVsqnINVFLRNTVKVTGVVVFM- 321
Cdd:PRK13657 73 GvlvarhadRLAHRRRLAVlteyFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLW---LEFMREHLATLVALVVLLp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 322 --FSLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQNAL--------ARASntaeETISAMKTVRSFANEEEEAEVy 391
Cdd:PRK13657 150 laLFMNWRLSLVLV----VLGIVYTLITTLVMRKTKDGQAAVeehyhdlfAHVS----DAIGNVSVVQSYNRIEAETQA- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 392 LRKLqqvykLNRKEAAAYMYYVW---GSGLTLL---VVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSV 465
Cdd:PRK13657 221 LRDI-----ADNLLAAQMPVLSWwalASVLNRAastITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 466 YSGLMQgvgAAEKVFEFIDRQPTM--VHDGSLAPD--HLEGRVDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPS 541
Cdd:PRK13657 296 INQVFM---AAPKLEEFFEVEDAVpdVRDPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 542 GSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANA 621
Cdd:PRK13657 371 GAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQA 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 339895787 622 HGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 678
Cdd:PRK13657 451 HDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
191-479 |
1.12e-64 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 215.43 E-value: 1.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFST-AVVIVCLLAIGSSFAAgIRGGIFTLIFARLNIRLRNCLFRSL 269
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQiALLLLGLFLLQAVFSF-FRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 270 VSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKY 349
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 350 YKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILY 429
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 339895787 430 YGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18576 240 YGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
504-681 |
1.33e-62 |
|
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: 208.11 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03252 1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170
....*....|....*...
gi 339895787 664 LILDEATSALDAESEYLI 681
Cdd:cd03252 160 LIFDEATSALDYESEHAI 177
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
188-479 |
7.06e-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: 205.48 E-value: 7.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeAAAYMYYVWG-SGLTLLVVQVS 426
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR-AARLSALFSPlIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 339895787 427 ILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
193-681 |
1.64e-59 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 209.95 E-value: 1.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 193 FFLIVAALGETFLPYYTGRAIDGIviqkSMDQFSTAVVIVCL--LAIGSSFAAGIRGGIFTLIFA---RLNIRLRNCLFR 267
Cdd:PRK10789 2 ALLIIIAMLQLIPPKVVGIIVDGV----TEQHMTTGQILMWIgtMVLIAVVVYLLRYVWRVLLFGasyQLAVELREDFYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFS-LSWQLSLVTFMGFPIIMMVSNIY 346
Cdd:PRK10789 78 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 347 GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANE-------EEEAEVYLRKLQQVYKLN-RKEAAAYMyyvwGSGL 418
Cdd:PRK10789 158 GDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEdrqsalfAADAEDTGKKNMRVARIDaRFDPTIYI----AIGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 419 T-LLVVQvsilyYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPtMVHDGSLAP 497
Cdd:PRK10789 234 AnLLAIG-----GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAP-VVKDGSEPV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 498 DHLEGRVDFENVTFTYrtrPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 575
Cdd:PRK10789 308 PEGRGELDVNIRQFTY---PQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 576 KYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:PRK10789 385 DSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIAR 464
|
490 500
....*....|....*....|....*.
gi 339895787 656 ALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQI 490
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
188-479 |
4.02e-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: 200.73 E-value: 4.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDqfstAVVIVCLLAIGSSFAAGI--RGGIFTLIFARLNI--RLRN 263
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLE----ALLLVPLAIIGLFLLRGLasYLQTYLMAYVGQRVvrDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAymyyvwgSGLTLLVV 423
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARA-------RALSSPLM 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895787 424 QV-------SILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18552 230 ELlgaiaiaLVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
504-681 |
7.73e-59 |
|
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: 195.68 E-value: 7.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170
....*....|....*...
gi 339895787 664 LILDEATSALDAESEYLI 681
Cdd:cd03228 118 LILDEATSALDPETEALI 135
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
188-455 |
1.01e-55 |
|
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: 190.93 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIG--SSFAAGIRGGIFTLIFARLNIRLRNCL 265
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGlaQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 266 FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNI 345
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 346 YGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQV 425
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|
gi 339895787 426 SILYYGGHLVISGQMTSGNLIAFIIYEFVL 455
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQL 270
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
191-479 |
3.67e-54 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 187.31 E-value: 3.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 271 SQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYY 350
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 351 KRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYmyyvwgSGLTLLVVQ------ 424
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRAR------ALLTALVIFlvfgai 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 425 VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18575 235 VFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
188-479 |
3.05e-53 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 184.94 E-value: 3.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSI 427
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 339895787 428 LYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
421-678 |
3.92e-53 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 192.27 E-value: 3.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 421 LVVQVSILYYGGHLVISGQMTSGNLIAFIIyefVLGDCM---ESVGSVYSGLMQGVGAAEKVFEFIDRQPTmvHDGSLAP 497
Cdd:COG4618 250 LLLQSAVLGLGAYLVIQGEITPGAMIAASI---LMGRALapiEQAIGGWKQFVSARQAYRRLNELLAAVPA--EPERMPL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 498 DHLEGRVDFENVTFTY--RTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 575
Cdd:COG4618 325 PRPKGRLSVENLTVVPpgSKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 576 KYLHRVISLVSQEPVLFARSITDNISyGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:COG4618 402 EELGRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
250 260
....*....|....*....|...
gi 339895787 656 ALVRNPPVLILDEATSALDAESE 678
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGE 503
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
502-678 |
2.62e-52 |
|
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: 180.09 E-value: 2.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 502 GRVDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 581
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170
....*....|....*..
gi 339895787 662 PVLILDEATSALDAESE 678
Cdd:cd03245 160 PILLLDEPTSAMDMNSE 176
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
189-681 |
2.17e-51 |
|
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: 189.95 E-value: 2.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 189 VAASFFLIVAALGEtflpYYTGRAIDGIVIQKSMDQFStaVVIVCLLA--IGSSFAAGIRGGIFTLIFARLNIRLRNCLF 266
Cdd:TIGR01193 163 IAAIIVTLISIAGS----YYLQKIIDTYIPHKMMGTLG--IISIGLIIayIIQQILSYIQIFLLNVLGQRLSIDIILSYI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 267 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTgVVVFMFSLSWQLSLVTFMGFPIIMMVSNIY 346
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVI-VGLFLVRQNMLLFLLSLLSIPVYAVIIILF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 347 GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE-------EAEVYLRKlqqVYKLNRKEAAAYMYYVwgsgLT 419
Cdd:TIGR01193 316 KRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAEryskidsEFGDYLNK---SFKYQKADQGQQAIKA----VT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 420 LLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFE--FIDRQPTMVHDGSlAP 497
Cdd:TIGR01193 389 KLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEFINKKKRT-EL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 498 DHLEGRVDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY 577
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 578 LHRVISLVSQEPVLFARSITDNISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 656
Cdd:TIGR01193 546 LRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
490 500
....*....|....*....|....*
gi 339895787 657 LVRNPPVLILDEATSALDAESEYLI 681
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKI 650
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
226-678 |
9.37e-50 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 182.18 E-value: 9.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 226 STAVVIVCLLAIGSSFAAGI-RGGIFTLIFARLNiRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 304
Cdd:TIGR02868 53 SVAAVAVRAFGIGRAVFRYLeRLVGHDAALRSLG-ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 305 NVFLRNTVKVTGVVVFMFSLSWQLSLVT--------FMGFPIIMMVSNIYGKYYKRLSKEVQNALARA-SNTAEETIS-A 374
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALILaaglllagFVAPLVSLRAARAAEQALARLRGELAAQLTDAlDGAAELVASgA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 375 MKTVRSfanEEEEAEVYLRKLQQvyklNRKEAAAymyyvWGSGLTLLVVQVSI---LYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:TIGR02868 212 LPAALA---QVEEADRELTRAER----RAAAATA-----LGAALTLLAAGLAVlgaLWAGGPAVADGRLAPVTLAVLVLL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 452 EFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDrQPTMVHDGSLAPDHLEG----RVDFENVTFTYRTRPhtQVLQNVSF 527
Cdd:TIGR02868 280 PLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD-AAGPVAEGSAPAAGAVGlgkpTLELRDLSAGYPGAP--PVLDGVSL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 528 SLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTV 607
Cdd:TIGR02868 357 DLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDA 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339895787 608 PFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 678
Cdd:TIGR02868 437 TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
188-479 |
2.38e-49 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 174.16 E-value: 2.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMdqfSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSS---GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAaymYYVWGSGLTLLVVQVS- 426
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAK---IEALIGPLMGLAVQLAl 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 427 --ILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18551 235 lvVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
188-451 |
1.98e-47 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 169.13 E-value: 1.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQK-SMDQFSTAVVIVCLLAIGSsfaAGIR-GGIFTLIFARLNI--RLRN 263
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLI---GIFRfLWRYLIFGASRRIeyDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaayMYYVWG-------- 415
Cdd:cd18541 158 YRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR-----LARVDAlffpligl 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 339895787 416 -SGLTLLVVqvsiLYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18541 233 lIGLSFLIV----LWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
178-489 |
2.27e-46 |
|
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: 166.86 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 178 LSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVV---IVCLLAIGSSFAAGIRGGIFTLIF 254
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFwalMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 255 ARLNIRLRNCLFRSLVSQETSFFD--ENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMyy 412
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISG-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 413 vWGSGLT---LLVVQVSILYYGGHLVISGQMTSGNLiaFIIYEFVLGdCMESVGSVYSGL---MQGVGAAEKVFEFIDRQ 486
Cdd:cd18578 239 -LGFGLSqslTFFAYALAFWYGGRLVANGEYTFEQF--FIVFMALIF-GAQSAGQAFSFApdiAKAKAAAARIFRLLDRK 314
|
...
gi 339895787 487 PTM 489
Cdd:cd18578 315 PEI 317
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
188-451 |
3.55e-45 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 162.94 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDqfSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARL--NI--RLRN 263
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGD--LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLgqRIiyDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18544 79 DLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEaaAYMYYVWGSGLTLL-- 421
Cdd:cd18544 159 YLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKS--IKLFALFRPLVELLss 236
|
250 260 270
....*....|....*....|....*....|
gi 339895787 422 VVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18544 237 LALALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
421-678 |
4.00e-45 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 169.45 E-value: 4.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 421 LVVQVSILYYGGHLVISGQMTSGNLIA-FIIYEFVLGDCMESVGsVYSGLMQGVGAAEKVFEFIDRQPtmvhdgsLAPDH 499
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAgSILVGRALAPIDGAIG-GWKQFSGARQAYKRLNELLANYP-------SRDPA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 500 L-----EGRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD 574
Cdd:TIGR01842 308 MplpepEGHLSVENVTIVP-PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 575 HKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMA 654
Cdd:TIGR01842 387 RETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALA 466
|
250 260
....*....|....*....|....
gi 339895787 655 RALVRNPPVLILDEATSALDAESE 678
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGE 490
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
188-479 |
2.09e-44 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 161.10 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIV----IQKSMDQFSTAVVIVCL----LAIGSSFAAGIRGGIFTLIFARLNI 259
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsGESSPDEFLDDVNKYALyfvyLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 339
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 340 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMyyvWGSGLT 419
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSG---LGLGLL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895787 420 LLVVQVSI---LYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18577 238 FFIIFAMYalaFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
188-681 |
1.56e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 169.05 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFflIVAALGETFLPYYTgrAIDGiVIQKSMDQFSTA-VVIVCLLAIG---------SSFAAGIrggIFTLIFARL 257
Cdd:PTZ00265 61 LLGVSF--VCATISGGTLPFFV--SVFG-VIMKNMNLGENVnDIIFSLVLIGifqfilsfiSSFCMDV---VTTKILKTL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 258 NIRLrnclFRSLVSQETSFFDENRTgdliSRLTSDTTMVSDLVSQNINV----FLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:PTZ00265 133 KLEF----LKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIGTkfitIFTYASAFLGLYIWSLFKNARLTLCIT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 334 MGFPIIMMVSNIYGKYYKrLSKevQNALARASNTA---EETISAMKTVRSFANEEEEAEVY--LRKLQQVY--KLNRKEA 406
Cdd:PTZ00265 205 CVFPLIYICGVICNKKVK-INK--KTSLLYNNNTMsiiEEALVGIRTVVSYCGEKTILKKFnlSEKLYSKYilKANFMES 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 407 -----------AAYMYYVWgSGLTLLVVQVSILY----YGGHLVISgqMTSGNLIAFIIYEFVLGDCMEsvgsvysgLMQ 471
Cdd:PTZ00265 282 lhigmingfilASYAFGFW-YGTRIIISDLSNQQpnndFHGGSVIS--ILLGVLISMFMLTIILPNITE--------YMK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 472 GVGAAEKVFEFIDRQPTMVH--DGSLAPDhlEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV 549
Cdd:PTZ00265 351 SLEATNSLYEIINRKPLVENndDGKKLKD--IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 550 NILENFY-PLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGL------------------------ 604
Cdd:PTZ00265 429 KLIERLYdPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenk 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 605 ---------------------------------PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRV 651
Cdd:PTZ00265 509 nkrnscrakcagdlndmsnttdsneliemrknyQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRI 588
|
570 580 590
....*....|....*....|....*....|
gi 339895787 652 AMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PTZ00265 589 SIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
175-681 |
2.55e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 168.67 E-value: 2.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 175 QKLLSYTKpDVAF-----LVAASFFLIVAALgetfLPYYTGRAIDGIVIQKSMDQFStavVIVCLLAIGSSFAAGIRGGI 249
Cdd:PTZ00265 818 REIFSYKK-DVTIialsiLVAGGLYPVFALL----YAKYVSTLFDFANLEANSNKYS---LYILVIAIAMFISETLKNYY 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 250 FTLIFARLNIRLRNCLFRSLVSQETSFFDE--NRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK--VTGVVVFMFSlS 325
Cdd:PTZ00265 890 NNVIGEKVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLflVSMVMSFYFC-P 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 326 WQLSLVTFMGFpIIMMVSNIYGKYYKrlSKEVQNALARASNTA-----------------EETISAMKTVRSFANEE--- 385
Cdd:PTZ00265 969 IVAAVLTGTYF-IFMRVFAIRARLTA--NKDVEKKEINQPGTVfaynsddeifkdpsfliQEAFYNMNTVIIYGLEDyfc 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 386 ---EEAEVYLRKLQQvyklnRKEAAAYMyyVWG-SGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIiYEFVLgdcmes 461
Cdd:PTZ00265 1046 nliEKAIDYSNKGQK-----RKTLVNSM--LWGfSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSL-FTFLF------ 1111
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 462 VGSVYSGLMQGVGAAEKV-FEFIDRQPTMVH--------DGSLA---PDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSL 529
Cdd:PTZ00265 1112 TGSYAGKLMSLKGDSENAkLSFEKYYPLIIRksnidvrdNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSC 1191
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 530 SPGKVTALVGPSGSGKSSCVNILENFYPLE-------------------------------------------------- 559
Cdd:PTZ00265 1192 DSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedst 1271
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 560 ----GGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTE 635
Cdd:PTZ00265 1272 vfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTN 1351
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 339895787 636 TGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
256-450 |
5.39e-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: 156.94 E-value: 5.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 256 RLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDttmVSDLVS---QNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSsfkQCVSQGLRSVTQTVGCVVSLYLISPKLTLLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYY 412
Cdd:cd18574 149 LVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIF 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895787 413 VWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18574 229 QGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
139-674 |
1.40e-42 |
|
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: 163.97 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 139 TVRPGTQALEPGAATEAEGFPgsgRPPPEQASGAT--LQKLLSYTKPDVAFLVAASffLIVAALGeTFLPYYTGRAIDGI 216
Cdd:TIGR03797 93 TRRRVDAAMAATLAPEAYMFY---RPLPDKALGLRdlLRFALRGARRDLLAILAMG--LLGTLLG-MLVPIATGILIGTA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 217 VIQKSMDQfstaVVIVCLLAIGSSFAAGIrggiFTLIFARLNIRLRN--------CLFRSLVSQETSFFDENRTGDLISR 288
Cdd:TIGR03797 167 IPDADRSL----LVQIALALLAAAVGAAA----FQLAQSLAVLRLETrmdaslqaAVWDRLLRLPVSFFRQYSTGDLASR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 289 LTSDTTMVSDLVSQNINVFLRNTVKVTGVVVfMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTA 368
Cdd:TIGR03797 239 AMGISQIRRILSGSTLTTLLSGIFALLNLGL-MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 369 EETIS-------AMKTVRSFAneeEEAEVYLRKLQQVYKLNRkeaaaymyyvWGSGLT-----LLVVQVSILYYgghLVI 436
Cdd:TIGR03797 318 VQLINgisklrvAGAENRAFA---RWAKLFSRQRKLELSAQR----------IENLLTvfnavLPVLTSAALFA---AAI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 437 SGQMTSG-NLIAFIIYEFVLGDCMESVGSVySGLMQGVGAAEKVFEFID---RQPTMVHDGSLAPDHLEGRVDFENVTFT 512
Cdd:TIGR03797 382 SLLGGAGlSLGSFLAFNTAFGSFSGAVTQL-SNTLISILAVIPLWERAKpilEALPEVDEAKTDPGKLSGAIEVDRVTFR 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 513 YRtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLF 592
Cdd:TIGR03797 461 YR-PDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLM 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 593 ARSITDNISYGLPTVPfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:TIGR03797 540 SGSIFENIAGGAPLTL-DEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSA 618
|
..
gi 339895787 673 LD 674
Cdd:TIGR03797 619 LD 620
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
502-681 |
2.31e-42 |
|
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: 152.65 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 502 GRVDFENVTFTYRtrPHTQ-VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR 580
Cdd:cd03244 1 GDIEFKNVSLRYR--PNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VISLVSQEPVLFARSITDNISyglptvPF-----EMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PFgeysdEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180
....*....|....*....|....*.
gi 339895787 656 ALVRNPPVLILDEATSALDAESEYLI 681
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALI 178
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
188-451 |
6.59e-42 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 153.78 E-value: 6.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeAAAYMYYVWGS-GLTLLVVQVS 426
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMR-AVRLNALFWPLvELISALGTAL 240
|
250 260
....*....|....*....|....*
gi 339895787 427 ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGY 265
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
471-681 |
6.92e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 160.78 E-value: 6.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 471 QGVGAAEKVFEFIDRQPTMVHDGSlAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 550
Cdd:PRK11174 316 QAVGAAESLVTFLETPLAHPQQGE-KELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 551 ILENFYPLEGgRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQD 630
Cdd:PRK11174 395 ALLGFLPYQG-SLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQ 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 339895787 631 GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
189-451 |
4.52e-41 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 151.51 E-value: 4.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 189 VAASFFLIVAAlgeTFL----PYYTGRAIDGIVIQKSMDQFSTAVVIVCL----LAIGSSFAAGIRGGIFTLIFARLNIR 260
Cdd:cd18563 1 LILGFLLMLLG---TALglvpPYLTKILIDDVLIQLGPGGNTSLLLLLVLglagAYVLSALLGILRGRLLARLGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 261 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaAAYMYYVWGSGLTL 420
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR--AEKLWATFFPLLTF 235
|
250 260 270
....*....|....*....|....*....|...
gi 339895787 421 LVV--QVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18563 236 LTSlgTLIVWYFGGRQVLSGTMTLGTLVAFLSY 268
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
506-677 |
3.19e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 3.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRViSL 584
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQV-AY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 585 VSQEPVLFARSITDNISYglptvPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPV 663
Cdd:COG4619 79 VPQEPALWGGTVRDNLPF-----PFQLRERKFDRERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLLQPDV 151
|
170
....*....|....
gi 339895787 664 LILDEATSALDAES 677
Cdd:COG4619 152 LLLDEPTSALDPEN 165
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
522-671 |
4.00e-40 |
|
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: 143.94 E-value: 4.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFAR-SITDNI 600
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895787 601 SYGLptvPFEMVVEAAQKANAHGFI--MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 671
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
416-681 |
6.38e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 154.98 E-value: 6.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 416 SGLTLLVvqvsILYYGGHLViSGQMTSGNLIAFIIyeFVLGDCMES---VGSVYSGLMQGVGAAEKVFEFIDRQPTMVHD 492
Cdd:PRK11160 255 NGLTVVL----MLWLAAGGV-GGNAQPGALIALFV--FAALAAFEAlmpVAGAFQHLGQVIASARRINEITEQKPEVTFP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 493 GSLAPDHLEGRVDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA 572
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 573 YDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFImELQDGYSTETGEKGAQLSGGQKQRVA 652
Cdd:PRK11160 407 YSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLG 485
|
250 260
....*....|....*....|....*....
gi 339895787 653 MARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQI 514
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
504-675 |
2.01e-39 |
|
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: 144.54 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkyLHRVI 582
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEPVLFA-RSITDNISYGLptvpfEM--VVEAAQKANAHGFImelqdgysTETGEKGA------QLSGGQKQRVAM 653
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL-----ELqgVPKAEARERAEELL--------ELVGLSGFenayphQLSGGMRQRVAL 142
|
170 180
....*....|....*....|..
gi 339895787 654 ARALVRNPPVLILDEATSALDA 675
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDA 164
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
188-479 |
6.46e-39 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 145.62 E-value: 6.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIV------IQKSMDQFSTAVVIVCLLAIGSSfaagirggIFTLIFARLNI-- 259
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIeglgggGGVDFSGLLRILLLLLGLYLLSA--------LFSYLQNRLMArv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 260 ------RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTF 333
Cdd:cd18547 73 sqrtvyDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 334 MGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaAYMYyv 413
Cdd:cd18547 153 VTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK---AQFY-- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895787 414 wgSGLTL-------LVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18547 228 --SGLLMpimnfinNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
501-675 |
1.57e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 143.31 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 501 EGRVDFENVTFTYRTRP-HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylh 579
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 rvISLVSQEPVLFA-RSITDNISYGLptvpfEMVVEAAQKANAHgfIMELQDgystETGEKGA------QLSGGQKQRVA 652
Cdd:COG1116 82 --RGVVFQEPALLPwLTVLDNVALGL-----ELRGVPKAERRER--ARELLE----LVGLAGFedayphQLSGGMRQRVA 148
|
170 180
....*....|....*....|...
gi 339895787 653 MARALVRNPPVLILDEATSALDA 675
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDA 171
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
507-674 |
3.46e-37 |
|
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: 139.41 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 586
Cdd:COG1120 5 ENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPVL-FARSITDNISYG-LPTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMAR 655
Cdd:COG1120 82 QEPPApFGLTVRELVALGrYPHLGLfgrpsaedrEAVEEALERTG----LEHLADRPVDE-------LSGGERQRVLIAR 150
|
170
....*....|....*....
gi 339895787 656 ALVRNPPVLILDEATSALD 674
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLD 169
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
506-677 |
4.12e-36 |
|
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: 134.90 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:cd03225 2 LKNLSFSYPDGA-RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEP--VLFARSITDNISYGLP--TVPFEMVVEAAQKANAHGFIMELQDgYSTETgekgaqLSGGQKQRVAMARALVRNP 661
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALELVGLEGLRD-RSPFT------LSGGQKQRVAIAGVLAMDP 153
|
170
....*....|....*.
gi 339895787 662 PVLILDEATSALDAES 677
Cdd:cd03225 154 DILLLDEPTAGLDPAG 169
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
504-677 |
5.75e-36 |
|
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: 135.00 E-value: 5.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLE--GGRVLLDGKPISAYDHK-- 576
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPGApdEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 577 YLHRVISLVSQEPVLFARSITDNISYGLP-------TVPFEMVVEAAQKANAHGFIMELQDGYStetgekgaqLSGGQKQ 649
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180
....*....|....*....|....*...
gi 339895787 650 RVAMARALVRNPPVLILDEATSALDAES 677
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPIS 176
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
188-479 |
5.88e-36 |
|
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: 137.23 E-value: 5.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQnINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaAAYMYYVWGSGLTLL--VVQV 425
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLR--AARLRARFWPLLEALpeLGLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 339895787 426 SILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18543 238 AVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
504-677 |
8.33e-36 |
|
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: 134.77 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPV--LFARSITDNISYGlPT---VPFEMVVEAAQKA-NAHGfIMELQDgYSTetgekgAQLSGGQKQRVAMARAL 657
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFG-PEnlgLPREEIRERVEEAlELVG-LEHLAD-RPP------HELSGGQKQRVAIAGVL 149
|
170 180
....*....|....*....|
gi 339895787 658 VRNPPVLILDEATSALDAES 677
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRG 169
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
504-677 |
6.03e-35 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 131.87 E-value: 6.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVI 582
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpER---RNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEPVLFA-RSITDNISYGLPtvpfEMVVEAAQKANAHGFIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:cd03259 75 GMVFQDYALFPhLTVAENIAFGLK----LRGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170
....*....|....*.
gi 339895787 662 PVLILDEATSALDAES 677
Cdd:cd03259 150 SLLLLDEPLSALDAKL 165
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
189-451 |
9.51e-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: 133.76 E-value: 9.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 189 VAASFFLIVA-ALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18550 1 LALVLLLILLsALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 348 KYYKRLSKEVQNALARASNTAEET--ISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQV 425
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260
....*....|....*....|....*.
gi 339895787 426 SILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTAL 266
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
446-675 |
1.58e-34 |
|
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: 138.11 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 446 IAFIIYEFVLGDCMESVGSV---YSGLMQGVGAAEKVFEFIDR---QPTMVHDGSLAPDHLEGR---VDFENVTFTYRTR 516
Cdd:COG1123 194 TTVLLITHDLGVVAEIADRVvvmDDGRIVEDGPPEEILAAPQAlaaVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 517 P--HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH---KYLHRVISLVSQEPV- 590
Cdd:COG1123 274 GkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYs 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 591 -LFAR-SITDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:COG1123 354 sLNPRmTVGDIIAEPL------RLHGLLSRAERRERVAELLErvGLPPDLADRyPHELSGGQRQRVAIARALALEPKLLI 427
|
250
....*....|
gi 339895787 666 LDEATSALDA 675
Cdd:COG1123 428 LDEPTSALDV 437
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
504-675 |
3.98e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 133.68 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS---AYdhkylHR 580
Cdd:COG3842 6 LELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPE-----KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VISLVSQEPVLFA-RSITDNISYGLptvpfEM--VVEAAQKANAHGFI--MELqDGYStetGEKGAQLSGGQKQRVAMAR 655
Cdd:COG3842 78 NVGMVFQDYALFPhLTVAENVAFGL-----RMrgVPKAEIRARVAELLelVGL-EGLA---DRYPHQLSGGQQQRVALAR 148
|
170 180
....*....|....*....|
gi 339895787 656 ALVRNPPVLILDEATSALDA 675
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDA 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
507-681 |
5.13e-34 |
|
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: 127.72 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTY--RTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISL 584
Cdd:cd03246 4 ENVSFRYpgAEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 585 VSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVL 664
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170
....*....|....*..
gi 339895787 665 ILDEATSALDAESEYLI 681
Cdd:cd03246 119 VLDEPNSHLDVEGERAL 135
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
504-677 |
6.79e-34 |
|
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: 129.15 E-value: 6.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK----YL 578
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 579 HRVISLVSQEPVLFAR-SITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVE--LP-----LLLAGVPKKERRERAEELLErvGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180
....*....|....*....|..
gi 339895787 656 ALVRNPPVLILDEATSALDAES 677
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSET 175
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
188-451 |
1.18e-33 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 131.09 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQK---------------SMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTL 252
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKplpgllglapllgpdPLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 253 IFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYY 412
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 339895787 413 VWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
195-451 |
2.68e-33 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 129.49 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 195 LIVAALgETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQET 274
Cdd:cd18549 12 VLIAAL-DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 275 SFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLS 354
Cdd:cd18549 91 SFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 355 KEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQvYKLNRKEAAAYM-YYVWGSGLTLLVVQVSILYYGGH 433
Cdd:cd18549 171 RRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR-FLESKKKAYKAMaYFFSGMNFFTNLLNLVVLVAGGY 249
|
250
....*....|....*...
gi 339895787 434 LVISGQMTSGNLIAFIIY 451
Cdd:cd18549 250 FIIKGEITLGDLVAFLLY 267
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
504-677 |
3.48e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.49 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvIS 583
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNIS-----YGLPTVPFEMVVEAAQKAnahgfiMELQDgystETGEKGAQLSGGQKQRVAMARAL 657
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEARERIDELLEL------FGLTD----AADRKVGTLSGGMKQRLGLALAL 146
|
170 180
....*....|....*....|
gi 339895787 658 VRNPPVLILDEATSALDAES 677
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEA 166
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
219-681 |
7.61e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 136.26 E-value: 7.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 219 QKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMV 296
Cdd:PLN03232 941 QSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAakRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDI 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 297 SDLVSQNINVFLRNTVKVTGVVVFMFSLSwQLSLVTFMgfPIIMMVSNIYgKYYKRLSKEVQ--NALARASNTAE--ETI 372
Cdd:PLN03232 1021 DRNVANLMNMFMNQLWQLLSTFALIGTVS-TISLWAIM--PLLILFYAAY-LYYQSTSREVRrlDSVTRSPIYAQfgEAL 1096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 373 SAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV-----WGSGLTLLVVQVSILYYG---GHLVISGQMtsGN 444
Cdd:PLN03232 1097 NGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTirletLGGVMIWLTATFAVLRNGnaeNQAGFASTM--GL 1174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 445 LIAFIIyefvlgdcmeSVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLE-----------GRVDFENVTFTY 513
Cdd:PLN03232 1175 LLSYTL----------NITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIEnnrpvsgwpsrGSIKFEDVHLRY 1244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 514 RTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFA 593
Cdd:PLN03232 1245 RPG-LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 594 RSITDNISyglptvPFEM-----VVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:PLN03232 1324 GTVRFNID------PFSEhndadLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
490
....*....|...
gi 339895787 669 ATSALDAESEYLI 681
Cdd:PLN03232 1398 ATASVDVRTDSLI 1410
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
504-676 |
8.70e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 126.65 E-value: 8.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAyDHKYLHR 580
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLE---EPDSGTITVDGEDLTD-SKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 V---ISLVSQEPVLFA-RSITDNISYGLptvpfeMVV------EAAQKAnahgfiMEL---------QDGYStetgekgA 641
Cdd:COG1126 75 LrrkVGMVFQQFNLFPhLTVLENVTLAP------IKVkkmskaEAEERA------MELlervgladkADAYP-------A 135
|
170 180 190
....*....|....*....|....*....|....*
gi 339895787 642 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
507-675 |
1.16e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 126.46 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:COG1124 5 RNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEP--VLFAR-SITDNIS-----YGLPTVPfEMVVEAAQKanahgfiMELQDGYSTetgEKGAQLSGGQKQRVAMARAL 657
Cdd:COG1124 85 FQDPyaSLHPRhTVDRILAeplriHGLPDRE-ERIAELLEQ-------VGLPPSFLD---RYPHQLSGGQRQRVAIARAL 153
|
170
....*....|....*...
gi 339895787 658 VRNPPVLILDEATSALDA 675
Cdd:COG1124 154 ILEPELLLLDEPTSALDV 171
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
507-674 |
1.17e-32 |
|
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: 124.08 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 586
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QepvlfarsitdnisyglptvpfemVVEAAQKAN-AHGFIMElqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 665
Cdd:cd03214 80 Q------------------------ALELLGLAHlADRPFNE---------------LSGGERQRVLLARALAQEPPILL 120
|
....*....
gi 339895787 666 LDEATSALD 674
Cdd:cd03214 121 LDEPTSHLD 129
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
188-479 |
2.26e-32 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 126.83 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMdqfsTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIR----LRN 263
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDL----GVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERllydLRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18546 77 RVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 344 NIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYlRKLQQVYKLNRKEAAAYMyYVWGSGLTLL-- 421
Cdd:cd18546 157 RWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF-AELSDDYRDARLRAQRLV-AIYFPGVELLgn 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895787 422 VVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18546 235 LATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
504-681 |
2.47e-32 |
|
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: 124.93 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRP-HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYLH 579
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 RVISLVSQEPVL---FARSITDNISYGLptVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 656
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIAEPL--RIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180
....*....|....*....|....*
gi 339895787 657 LVRNPPVLILDEATSALDAESEYLI 681
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQI 184
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
506-681 |
3.63e-32 |
|
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: 121.97 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SqepvlfarsitdnisyglptvpfemvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:cd00267 79 P-------------------------------------------------------QLSGGQRQRVALARALLLNPDLLL 103
|
170
....*....|....*.
gi 339895787 666 LDEATSALDAESEYLI 681
Cdd:cd00267 104 LDEPTSGLDPASRERL 119
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
504-676 |
3.94e-32 |
|
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: 123.35 E-value: 3.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgrvlldgkpisaydHKYLHR 580
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSG--------------SVSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VISLVSQEPVLFARSITDNISYGLPTVP--FEMVVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARAL 657
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPFDEerYEKVIKACAlEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170
....*....|....*....
gi 339895787 658 VRNPPVLILDEATSALDAE 676
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAH 161
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
504-677 |
4.14e-32 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 124.23 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfYPLEGgRVLLDGKPISAYDHKYL- 578
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLE--RPTSG-SVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 579 --HRVISLVSQEPVLF-ARSITDNISYglptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAM 653
Cdd:cd03258 79 kaRRRIGMIFQHFNLLsSRTVFENVAL-----PLE--IAGVPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180
....*....|....*....|....
gi 339895787 654 ARALVRNPPVLILDEATSALDAES 677
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPET 175
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
506-674 |
4.17e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.48 E-value: 4.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRTRPhtqvlQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVISL 584
Cdd:COG3840 4 LDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAE---RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 585 VSQEPVLFAR-SITDNISYGL-----PTVP-FEMVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAMARAL 657
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGLrpglkLTAEqRAQVEQALERVGLAGLL-----------DRLPGQLSGGQRQRVALARCL 144
|
170
....*....|....*..
gi 339895787 658 VRNPPVLILDEATSALD 674
Cdd:COG3840 145 VRKRPILLLDEPFSALD 161
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
188-451 |
5.62e-32 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 125.59 E-value: 5.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSsFAAGIRGGIF-TLIFARLNIRLRNCLF 266
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLG-LIAGILAGYFaAKASQGFGRDLRKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 267 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIY 346
Cdd:cd18548 80 EKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 347 GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaAYMYYVWGSGLTLLVVQVS 426
Cdd:cd18548 160 MKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLK---AGRLMALLNPLMMLIMNLA 236
|
250 260
....*....|....*....|....*...
gi 339895787 427 ---ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18548 237 ivaILWFGGHLINAGSLQVGDLVAFINY 264
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
504-676 |
1.31e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 125.96 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEGgRVLLDGKPISAYDHKYLH 579
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER--PTSG-SVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 RV---ISLVSQEPVLF-ARSITDNISYglptvPFEMV----VEAAQKANahgfimELQD--GYStetgEKG----AQLSG 645
Cdd:COG1135 79 AArrkIGMIFQHFNLLsSRTVAENVAL-----PLEIAgvpkAEIRKRVA------ELLElvGLS----DKAdaypSQLSG 143
|
170 180 190
....*....|....*....|....*....|.
gi 339895787 646 GQKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
504-677 |
1.53e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.46 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfypleG-------GRVLLDGKPISAYDH 575
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL-------GgldrptsGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 576 KYLHRV----ISLVSQEPVLFAR-SITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQK 648
Cdd:COG1136 78 RELARLrrrhIGFVFQFFNLLPElTALENVA--LP-----LLLAGVSRKERRERARELLErvGLGDRLDHRPSQLSGGQQ 150
|
170 180
....*....|....*....|....*....
gi 339895787 649 QRVAMARALVRNPPVLILDEATSALDAES 677
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKT 179
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
504-677 |
3.17e-31 |
|
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: 119.98 E-value: 3.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD--HKYLHRV 581
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ISLVSQEPVLFAR-SITDNISYGlptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRN 660
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170
....*....|....*..
gi 339895787 661 PPVLILDEATSALDAES 677
Cdd:cd03229 119 PDVLLLDEPTSALDPIT 135
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
520-676 |
5.54e-31 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 120.71 E-value: 5.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 520 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFyplEGGRVLLDGKPISAyDHKYLHRV---ISLVSQEPVLFA 593
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEEP---DSGTIIIDGLKLTD-DKKNINELrqkVGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 594 -RSITDNISYGLPTVPFEMVVEAAQKAnahgfiMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:cd03262 90 hLTVLENITLAPIKVKGMSKAEAEERA------LELLEkvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
....*.
gi 339895787 671 SALDAE 676
Cdd:cd03262 164 SALDPE 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
234-681 |
1.24e-30 |
|
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: 129.30 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 234 LLAIGSSFAAGIrGGIFTlifARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 313
Cdd:TIGR00957 1020 FAVFGYSMAVSI-GGIQA---SR---VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFN 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 314 VTGVVVFMFsLSWQLSLVTFMGFPII-MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFaNEEEEAEVyl 392
Cdd:TIGR00957 1093 VIGALIVIL-LATPIAAVIIPPLGLLyFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIH-- 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 393 rklQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVS---ILYYGGHLVISGQMTSGNLIAFII-YEFVLGDCMESVGSVYSG 468
Cdd:TIGR00957 1169 ---QSDLKVDENQKAYYPSIVANRWLAVRLECVGnciVLFAALFAVISRHSLSAGLVGLSVsYSLQVTFYLNWLVRMSSE 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 469 LMQGVGAAEKVFEF--IDRQPTMVHDGSLAPDHL--EGRVDFENvtFTYRTRPHTQ-VLQNVSFSLSPGKVTALVGPSGS 543
Cdd:TIGR00957 1246 METNIVAVERLKEYseTEKEAPWQIQETAPPSGWppRGRVEFRN--YCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGA 1323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 544 GKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPF-----EMVVEAAQK 618
Cdd:TIGR00957 1324 GKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD------PFsqysdEEVWWALEL 1397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895787 619 ANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:TIGR00957 1398 AHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
187-479 |
1.53e-30 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 121.82 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 187 FLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVI-VCLLAIgssFAAGIRGGIFT--LIFARLNIRLRN 263
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLyLGLILI---QALSVFLFIRLagKIEMGVSYDLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 264 CLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVS 343
Cdd:cd18540 80 KAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 344 NIygkYYKRLSKevQNALARASN---TA--EETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaAAYMyyvwgSGL 418
Cdd:cd18540 160 IY---FQKKILK--AYRKVRKINsriTGafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVR--AARL-----SAL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895787 419 TLLVVQV-------SILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18540 228 FLPIVLFlgsiataLVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
506-681 |
2.20e-30 |
|
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: 117.80 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYrtrPH--TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDhKYLHRVIS 583
Cdd:cd03247 3 INNVSFSY---PEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170
....*....|....*...
gi 339895787 664 LILDEATSALDAESEYLI 681
Cdd:cd03247 120 VLLDEPTVGLDPITERQL 137
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
188-479 |
2.37e-30 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 121.10 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAID-GIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGgIFTLIFA-RLNIRLRNCL 265
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDlVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRI-YLNHVAEqKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 266 FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNI 345
Cdd:cd18778 80 YDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 346 YGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLN---RKEAAAY---MYYVWGSGlT 419
Cdd:cd18778 160 YSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQlraMKLWAIFhplMEFLTSLG-T 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 420 LLVvqvsiLYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18778 239 VLV-----LGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
494-674 |
3.30e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.76 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 494 SLAPDHLEGRVDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP---LEgGRVLLDG 567
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPgarVE-GEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 568 KPIsaYDHKY----LHRVISLVSQEPVLFARSITDNISYGL-------PTVPFEMVVEAAQKANahgfimeLQDgystET 636
Cdd:COG1117 78 EDI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiksKSELDEIVEESLRKAA-------LWD----EV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 339895787 637 ----GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:COG1117 145 kdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
507-677 |
5.03e-30 |
|
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: 118.81 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvISLVS 586
Cdd:COG4555 5 ENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPVLFAR-SITDNISY-----GLPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRN 660
Cdd:COG4555 81 DERGLYDRlTVRENIRYfaelyGLFDEELKKRIEELIEL------LGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170
....*....|....*..
gi 339895787 661 PPVLILDEATSALDAES 677
Cdd:COG4555 151 PKVLLLDEPTNGLDVMA 167
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
504-675 |
2.54e-29 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 116.57 E-value: 2.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVI 582
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPpHK---RPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEPVLFAR-SITDNISYGLPTvpfEMVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRN 660
Cdd:cd03300 75 NTVFQNYALFPHlTVFENIAFGLRL---KKLPKAEIKERVAEALDLVQlEGYA---NRKPSQLSGGQQQRVAIARALVNE 148
|
170
....*....|....*
gi 339895787 661 PPVLILDEATSALDA 675
Cdd:cd03300 149 PKVLLLDEPLGALDL 163
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
497-681 |
2.86e-29 |
|
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: 115.59 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 497 PDHleGRVDFENVTFTYRtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 575
Cdd:cd03369 2 PEH--GEIEVENLSVRYA--PDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 576 KYLHRVISLVSQEPVLFARSITDNISyglptvPFEMVVEAAqkanahgfIMElqdgySTETGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSNLD------PFDEYSDEE--------IYG-----ALRVSEGGLNLSQGQRQLLCLAR 138
|
170 180
....*....|....*....|....*.
gi 339895787 656 ALVRNPPVLILDEATSALDAESEYLI 681
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALI 164
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
507-677 |
2.88e-29 |
|
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: 114.42 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvISLVS 586
Cdd:cd03230 4 RNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPVLfarsitdnisyglptvpfemvveaaqkanahgfimelqdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:cd03230 80 EEPSL----------------------------------------YENLTVRENLKLSGGMKQRLALAQALLHDPELLIL 119
|
170
....*....|.
gi 339895787 667 DEATSALDAES 677
Cdd:cd03230 120 DEPTSGLDPES 130
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
182-449 |
4.89e-29 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 117.16 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRL 261
Cdd:cd18570 1 KKLLILILLLSLLITLLGI---AGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 262 RNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQN-INVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18570 78 ILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFL-DLLMVIISGIILFFYNWKLFLITLLIIPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTL 420
Cdd:cd18570 156 LIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLIS 235
|
250 260
....*....|....*....|....*....
gi 339895787 421 LVVQVSILYYGGHLVISGQMTSGNLIAFI 449
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFN 264
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
504-681 |
9.28e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.19 E-value: 9.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhrvIS 583
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEpVLFARS--IT--DNISYGL-PTVPF---------EMVVEAAQKANAHGF----ImelqdgystetgekgAQLSG 645
Cdd:COG1121 79 YVPQR-AEVDWDfpITvrDVVLMGRyGRRGLfrrpsradrEAVDEALERVGLEDLadrpI---------------GELSG 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 339895787 646 GQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAL 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
504-675 |
9.72e-29 |
|
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: 120.78 E-value: 9.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG---GRVLLDGKPISAYDHKYLHR 580
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VISLVSQEP--VLFARSITDNISYGL--PTVPFEMVVEAAQKANAHGFIMELQDGYStetgekgAQLSGGQKQRVAMARA 656
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALenLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170
....*....|....*....
gi 339895787 657 LVRNPPVLILDEATSALDA 675
Cdd:COG1123 157 LALDPDLLIADEPTTALDV 175
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
507-677 |
1.04e-28 |
|
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: 113.89 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhKYLHRVISLVS 586
Cdd:cd03226 3 ENISFSYK--KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEP--VLFARSITDNISYGLPTVPfemvvEAAQKANAhgfIMELQDGYSTEtgEKGAQ-LSGGQKQRVAMARALVRNPPV 663
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELD-----AGNEQAET---VLKDLDLYALK--ERHPLsLSGGQKQRLAIAAALLSGKDL 147
|
170
....*....|....
gi 339895787 664 LILDEATSALDAES 677
Cdd:cd03226 148 LIFDEPTSGLDYKN 161
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
504-676 |
2.20e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.03 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGkpISAYDHKYLHR 580
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLE---EITSGDLIVDG--LKVNDPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VI----SLVSQEPVLFAR-SITDNISYGlptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAM 653
Cdd:PRK09493 74 LIrqeaGMVFQQFYLFPHlTALENVMFG----PLR--VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAI 147
|
170 180
....*....|....*....|...
gi 339895787 654 ARALVRNPPVLILDEATSALDAE 676
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPE 170
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
502-675 |
2.35e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 116.71 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 502 GRVDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRV 581
Cdd:COG3839 2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ISLVSQEPVLF-ARSITDNISYGLptvpfEM-----------VVEAAQkanahgfIMELQDgYStetGEKGAQLSGGQKQ 649
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPL-----KLrkvpkaeidrrVREAAE-------LLGLED-LL---DRKPKQLSGGQRQ 140
|
170 180
....*....|....*....|....*.
gi 339895787 650 RVAMARALVRNPPVLILDEATSALDA 675
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDA 166
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
503-677 |
3.01e-28 |
|
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: 112.57 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 503 RVDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVI 582
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEPVLFAR-SITDNIS-----YGLPtVPFEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 656
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEAVG----LAGLAD-------LPVRQLSAGQKRRVALARL 145
|
170 180
....*....|....*....|.
gi 339895787 657 LVRNPPVLILDEATSALDAES 677
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAG 166
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
507-675 |
4.91e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 115.63 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfYPLE---GGRVLLDGKPISAyDHKYLHRVIS 583
Cdd:COG1118 6 RNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AGLEtpdSGRIVLNGRDLFT-NLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFaR--SITDNISYGLPTVPfemVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRN 660
Cdd:COG1118 79 FVFQHYALF-PhmTVAENIAFGLRVRP---PSKAEIRARVEELLELVQlEGLA---DRYPSQLSGGQRQRVALARALAVE 151
|
170
....*....|....*
gi 339895787 661 PPVLILDEATSALDA 675
Cdd:COG1118 152 PEVLLLDEPFGALDA 166
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
504-677 |
1.23e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 111.30 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLHR 580
Cdd:COG2884 2 IRFENVSKRYPGGR--EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VISLVSQE-PVLFARSITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARAL 657
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVA--LP-----LRVTGKSRKEIRRRVREVLDlvGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180
....*....|....*....|
gi 339895787 658 VRNPPVLILDEATSALDAES 677
Cdd:COG2884 153 VNRPELLLADEPTGNLDPET 172
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
506-674 |
3.88e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 110.53 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAYDHKYLHRV- 581
Cdd:COG3638 5 LRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTllrCLNGLV---EPTSGEILVDGQDVTALRGRALRRLr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 --ISLVSQEPVLFAR-SITDNISYG-LPTVPF----EMVVEAAQKANAHGFI--MELQDgystETGEKGAQLSGGQKQRV 651
Cdd:COG3638 80 rrIGMIFQQFNLVPRlSVLTNVLAGrLGRTSTwrslLGLFPPEDRERALEALerVGLAD----KAYQRADQLSGGQQQRV 155
|
170 180
....*....|....*....|...
gi 339895787 652 AMARALVRNPPVLILDEATSALD 674
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLD 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
522-674 |
1.17e-26 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 109.66 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFA-RSI 596
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 597 TDNISYGLPT--VP----FEMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:cd03294 120 LENVAFGLEVqgVPraerEERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
....
gi 339895787 671 SALD 674
Cdd:cd03294 189 SALD 192
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
504-674 |
2.00e-26 |
|
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: 108.54 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFA-RSITDNISyglpTVP-FEMVVEAAQKANAHGFI-------MELQDGYStetgekgAQLSGGQKQRVAMA 654
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIA----LVPkLLKWPKEKIRERADELLalvgldpAEFADRYP-------HELSGGQQQRVGVA 147
|
170 180
....*....|....*....|
gi 339895787 655 RALVRNPPVLILDEATSALD 674
Cdd:cd03295 148 RALAADPPLLLMDEPFGALD 167
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
250-681 |
4.93e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 114.84 E-value: 4.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 250 FTLIFARLNI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSwQ 327
Cdd:PLN03130 975 YWLIMSSLYAakRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVS-T 1053
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 328 LSLVTFMgfPIIMMVSNIYgKYYKRLSKEVQ--NALARASNTAE--ETISAMKTVRSFANEEEEAEVYLRKLQQvyklNR 403
Cdd:PLN03130 1054 ISLWAIM--PLLVLFYGAY-LYYQSTAREVKrlDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDN----NI 1126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 404 KEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFI 483
Cdd:PLN03130 1127 RFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAV 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 484 DRQPTMVHDGSLAPDHLE-----------GRVDFENVTFTYRTR--PhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 550
Cdd:PLN03130 1207 ERVGTYIDLPSEAPLVIEnnrpppgwpssGSIKFEDVVLRYRPElpP---VLHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 551 ILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQKANAHGFI 625
Cdd:PLN03130 1284 ALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD------PFNEhndadLWESLERAHLKDVI 1357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 339895787 626 MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PLN03130 1358 RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI 1413
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
506-678 |
5.19e-26 |
|
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: 106.46 E-value: 5.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhrvISLV 585
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVL---FARSITDNISYGL-PTVPFEMVVEAAQKANahgfIMELQDgySTETGEKG----AQLSGGQKQRVAMARAL 657
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLyGHKGLFRRLSKADKAK----VDEALE--RVGLSELAdrqiGELSGGQQQRVLLARAL 147
|
170 180
....*....|....*....|.
gi 339895787 658 VRNPPVLILDEATSALDAESE 678
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQ 168
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
521-675 |
5.39e-26 |
|
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: 107.04 E-value: 5.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SITDN 599
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 600 ISYGL-------PTVPfEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:cd03299 92 IAYGLkkrkvdkKEIE-RKVLEIAEMLG----IDHLLN-------RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
...
gi 339895787 673 LDA 675
Cdd:cd03299 160 LDV 162
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
503-681 |
7.83e-26 |
|
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: 105.33 E-value: 7.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 503 RVDFENVTFT---YRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--GRVLLDGKPISAYDHKY 577
Cdd:cd03213 3 TLSFRNLTVTvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 578 LhrvISLVSQEPVLFARSitdnisyglpTVpFEMVVEAAqkanahgfimELQdgystetgekgaQLSGGQKQRVAMARAL 657
Cdd:cd03213 83 I---IGYVPQDDILHPTL----------TV-RETLMFAA----------KLR------------GLSGGERKRVSIALEL 126
|
170 180
....*....|....*....|....
gi 339895787 658 VRNPPVLILDEATSALDAESEYLI 681
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQV 150
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
504-675 |
8.84e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 105.80 E-value: 8.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 583
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRN 660
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKLrkVPKDEIDERVREVAELLQIEHLLD-------RKPKQLSGGQRQRVALGRAIVRE 148
|
170
....*....|....*
gi 339895787 661 PPVLILDEATSALDA 675
Cdd:cd03301 149 PKVFLMDEPLSNLDA 163
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
504-674 |
1.10e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.00 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEP--VLFARSITDNISYGLPTV---PFEM---VVEAAQKANAHGFImelqdgystetgEKGAQ-LSGGQKQRVAMA 654
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKkvpPKKMkdiIDDLAKKVGMEDYL------------DKEPQnLSGGQKQRVAIA 154
|
170 180
....*....|....*....|
gi 339895787 655 RALVRNPPVLILDEATSALD 674
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLD 174
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
504-676 |
1.36e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 105.18 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQV-LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLH 579
Cdd:cd03292 1 IEFINVTKTY---PNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 RVISLVSQE-PVLFARSITDNisyglptVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARA 656
Cdd:cd03292 78 RKIGVVFQDfRLLPDRNVYEN-------VAFALEVTGVPPREIRKRVPAALElvGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180
....*....|....*....|
gi 339895787 657 LVRNPPVLILDEATSALDAE 676
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPD 170
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
506-677 |
1.63e-25 |
|
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: 105.73 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAYDHKYLHRV- 581
Cdd:cd03256 3 VENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTllrCLNGLV---EPTSGSVLIDGTDINKLKGKALRQLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 --ISLVSQEPVLFAR-SITDNISYG-LPTVP-----FEMVVEAA-QKANAhgfIMElQDGYSTETGEKGAQLSGGQKQRV 651
Cdd:cd03256 78 rqIGMIFQQFNLIERlSVLENVLSGrLGRRStwrslFGLFPKEEkQRALA---ALE-RVGLLDKAYQRADQLSGGQQQRV 153
|
170 180
....*....|....*....|....*.
gi 339895787 652 AMARALVRNPPVLILDEATSALDAES 677
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPAS 179
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
504-674 |
1.83e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 106.27 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG-----GRVLLDGKPIsaYDHKY- 577
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI--YERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 578 ---LHRVISLVSQEPVLFARSITDNISYGL------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAQLSGGQK 648
Cdd:PRK14258 83 lnrLRRQVSMVHPKPNLFPMSVYDNVAYGVkivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180
....*....|....*....|....*.
gi 339895787 649 QRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLD 182
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
519-674 |
5.30e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.64 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITD 598
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895787 599 NISYglptvPFEMvveAAQKANAHGFIMELQD-GYSTETGEKG-AQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK10247 100 NLIF-----PWQI---RNQQPDPAIFLDDLERfALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
519-673 |
5.80e-25 |
|
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: 103.67 E-value: 5.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SI 596
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 597 TDNIsyglptvpfEMVVEAAQKANAHgFIME--------LQDGYSTetgeKGAQLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:cd03224 93 EENL---------LLGAYARRRAKRK-ARLErvyelfprLKERRKQ----LAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
....*
gi 339895787 669 ATSAL 673
Cdd:cd03224 159 PSEGL 163
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
504-676 |
9.44e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 106.04 E-value: 9.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPlEGGRVLLDGKPISAYDHKYL- 578
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER--P-TSGRVLVDGQDLTALSEKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 579 --HRVISLVSQE-PVLFARSITDNISYglptvPFEMVVEAAQKANAHgfIMELQD--GYSTETGEKGAQLSGGQKQRVAM 653
Cdd:PRK11153 79 kaRRQIGMIFQHfNLLSSRTVFDNVAL-----PLELAGTPKAEIKAR--VTELLElvGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180
....*....|....*....|...
gi 339895787 654 ARALVRNPPVLILDEATSALDAE 676
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPA 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
517-680 |
1.53e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.80 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVSQEPV 590
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdAQAAG-----IAIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 591 LFA-RSITDNISYG-LPTVPF-----EMVVEAAQKANAHGFIMELqdgySTETGEkgaqLSGGQKQRVAMARALVRNPPV 663
Cdd:COG1129 90 LVPnLSVAENIFLGrEPRRGGlidwrAMRRRARELLARLGLDIDP----DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170
....*....|....*...
gi 339895787 664 LILDEATSAL-DAESEYL 680
Cdd:COG1129 162 LILDEPTASLtEREVERL 179
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
507-675 |
2.89e-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: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTY-RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRviSLV 585
Cdd:COG4525 7 RHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---R--GVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVLFA-RSITDNISYGLPtvpFEMVVEAAQKANAHGFI--MELQDgysteTGEKG-AQLSGGQKQRVAMARALVRNP 661
Cdd:COG4525 82 FQKDALLPwLNVLDNVAFGLR---LRGVPKAERRARAEELLalVGLAD-----FARRRiWQLSGGMRQRVGIARALAADP 153
|
170
....*....|....
gi 339895787 662 PVLILDEATSALDA 675
Cdd:COG4525 154 RFLLMDEPFGALDA 167
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
504-674 |
3.41e-24 |
|
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: 101.81 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-- 581
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 -ISLVSQEPVLF-ARSITDNISYGL---PTVPFEMVVE-AAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMAR 655
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPLrehTRLSEEEIREiVLEKLEAVG-LRGAEDLYP-------AELSGGMKKRVALAR 149
|
170
....*....|....*....
gi 339895787 656 ALVRNPPVLILDEATSALD 674
Cdd:cd03261 150 ALALDPELLLYDEPTAGLD 168
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
504-674 |
4.96e-24 |
|
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: 100.65 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTQVLQnvsfsLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 583
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT-----FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNISYGL-PTVPFEMVVEAAQKANAHgfimelQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLsPGLKLTAEDRQAIEVALA------RVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170
....*....|...
gi 339895787 662 PVLILDEATSALD 674
Cdd:cd03298 148 PVLLLDEPFAALD 160
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
524-681 |
8.47e-24 |
|
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: 100.06 E-value: 8.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 524 NVSFSLsPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKylhRVISLVSQEPVLFAR-S 595
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQ---RKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 596 ITDNISYGLPTV-PFEMVVEAAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:cd03297 92 VRENLAFGLKRKrNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
....*..
gi 339895787 675 AESEYLI 681
Cdd:cd03297 164 RALRLQL 170
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
504-676 |
9.00e-24 |
|
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: 100.49 E-value: 9.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVIS 583
Cdd:cd03296 3 IEVRNVSKRF---GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNISYGLPTVP-FEMVVEAAQKANAHGFIMELQ-DGYSTETGekgAQLSGGQKQRVAMARALVRN 660
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPrSERPPEAEIRAKVHELLKLVQlDWLADRYP---AQLSGGQRQRVALARALAVE 154
|
170
....*....|....*.
gi 339895787 661 PPVLILDEATSALDAE 676
Cdd:cd03296 155 PKVLLLDEPFGALDAK 170
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
507-674 |
9.64e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.43 E-value: 9.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPhtqvlqnVSFSLS--PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKpisayDHKYL---HRV 581
Cdd:PRK10771 5 TDITWLYHHLP-------MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ISLVSQEPVLFAR-SITDNISYGL-PTVPF-----EMVVEAAQKANAHGFIMELQdgystetgekgAQLSGGQKQRVAMA 654
Cdd:PRK10771 73 VSMLFQENNLFSHlTVAQNIGLGLnPGLKLnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALA 141
|
170 180
....*....|....*....|
gi 339895787 655 RALVRNPPVLILDEATSALD 674
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALD 161
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
235-462 |
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 339895787 235 LAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKV 314
Cdd:cd18558 68 IGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 315 TGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRK 394
Cdd:cd18558 148 GTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQN 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895787 395 LQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLI----AFIIYEFVLGDCMESV 462
Cdd:cd18558 228 LEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLtvffSVLIGAFSAGQQVPSI 299
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
507-674 |
1.18e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.58 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 586
Cdd:COG4559 5 ENLSVRLGGR---TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 Q-----------EPVLFARsitdnISYGLPTVPFEMVVEAAqkanahgfiMELqdgysTETGEKGA----QLSGGQKQRV 651
Cdd:COG4559 82 QhsslafpftveEVVALGR-----APHGSSAAQDRQIVREA---------LAL-----VGLAHLAGrsyqTLSGGEQQRV 142
|
170 180 190
....*....|....*....|....*....|
gi 339895787 652 AMARAL------VRNPP-VLILDEATSALD 674
Cdd:COG4559 143 QLARVLaqlwepVDGGPrWLFLDEPTSALD 172
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
188-450 |
1.48e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 101.48 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18568 7 ILLASLLLQLLGL---ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYG 347
Cdd:cd18568 84 HLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 348 KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE-----EAEvYLRKLQQVYKLNRKEAAAYMyyvwGSGLTLLV 422
Cdd:cd18568 163 PKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPirwrwENK-FAKALNTRFRGQKLSIVLQL----ISSLINHL 237
|
250 260
....*....|....*....|....*...
gi 339895787 423 VQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18568 238 GTIAVLWYGAYLVISGQLTIGQLVAFNM 265
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
507-676 |
1.77e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.09 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE---GGRVLLDGKPISAYdhKYLHRVIS 583
Cdd:COG4136 5 ENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNISYGLP-TVPFE----MVVEAAQKANAHGFimelqdgystetGEKG-AQLSGGQKQRVAMARA 656
Cdd:COG4136 80 ILFQDDLLFPHlSVGENLAFALPpTIGRAqrraRVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRA 147
|
170 180
....*....|....*....|
gi 339895787 657 LVRNPPVLILDEATSALDAE 676
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAA 167
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
185-448 |
2.85e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 100.66 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 185 VAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNC 264
Cdd:cd18555 4 LISILLLSLLLQLLTL---LIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 265 LFRSLVSQETSFFDENRTGDLISRLTSdTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANS-NVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQ 424
Cdd:cd18555 160 LTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAP 239
|
250 260
....*....|....*....|....
gi 339895787 425 VSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18555 240 LLILWIGAYLVINGELTLGELIAF 263
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
182-451 |
3.66e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 100.23 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRL 261
Cdd:cd18567 1 KRALLQILLLSLALELFAL---ASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 262 RNCLFRSLVSQETSFFdENR-TGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18567 78 TSNLFRHLLRLPLSYF-EKRhLGDIVSRFGSLDEIQQTLTTGFVEALL-DGLMAILTLVMMFLYSPKLALIVLAAVALYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTL 420
Cdd:cd18567 156 LLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLF 235
|
250 260 270
....*....|....*....|....*....|.
gi 339895787 421 LVVQVSILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18567 236 GLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
188-451 |
3.71e-23 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 100.72 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKS---------------MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTL 252
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEAsflplvpaslgpadpRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 253 IFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 332
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 333 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvYLRKLQQVYKLNRKEA----AA 408
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERE-RVADASEEYRDANWRAirlrAA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 339895787 409 Y---MYYVWGSGLtllvvqVSILYYGGHLVISG------QMTSGNLIAFIIY 451
Cdd:cd18565 240 FfpvIRLVAGAGF------VATFVVGGYWVLDGpplftgTLTVGTLVTFLFY 285
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
518-676 |
4.43e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.31 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaydhkYLH---RVISLVSQEPVLFaR 594
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-----RLHardRKVGFVFQHYALF-R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 SIT--DNISYGLPTVPfemvveAAQKANAHGF---IMELQDGYSTE--TGEKGAQLSGGQKQRVAMARALVRNPPVLILD 667
Cdd:PRK10851 88 HMTvfDNIAFGLTVLP------RRERPNAAAIkakVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
....*....
gi 339895787 668 EATSALDAE 676
Cdd:PRK10851 162 EPFGALDAQ 170
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
504-681 |
4.74e-23 |
|
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: 95.96 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaydhkylhrvis 583
Cdd:cd03216 1 LELRGITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 lvsqepvlfARSITDNISYGLPTVPfemvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03216 66 ---------FASPRDARRAGIAMVY---------------------------------QLSVGERQMVEIARALARNARL 103
|
170
....*....|....*....
gi 339895787 664 LILDEATSAL-DAESEYLI 681
Cdd:cd03216 104 LILDEPTAALtPAEVERLF 122
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
504-676 |
6.67e-23 |
|
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: 97.26 E-value: 6.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGkVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVIS 583
Cdd:cd03264 1 LQLENLTKRY---GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL-RRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNISY-----GLP--TVPfEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPskEVK-ARVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQ 143
|
170 180
....*....|....*....|.
gi 339895787 656 ALVRNPPVLILDEATSALDAE 676
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPE 164
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
512-674 |
7.47e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 7.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 512 TYRtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVL 591
Cdd:PRK13548 9 SVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 592 -FARSITDNISYGL-----PTVPFEMVVEAAqkanahgfiMELQD--GYStetGEKGAQLSGGQKQRVAMARALVR---- 659
Cdd:PRK13548 88 sFPFTVEEVVAMGRaphglSRAEDDALVAAA---------LAQVDlaHLA---GRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170
....*....|....*..
gi 339895787 660 --NPPVLILDEATSALD 674
Cdd:PRK13548 156 dgPPRWLLLDEPTSALD 172
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
504-676 |
8.14e-23 |
|
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: 98.66 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-KPISAYDHKYLHRVI 582
Cdd:TIGR04520 1 IEVENVSFSY-PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALV 658
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEALK---LVGMEDFRDREP----HLLSGGQKQRVAIAGVLA 152
|
170
....*....|....*...
gi 339895787 659 RNPPVLILDEATSALDAE 676
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPK 170
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
521-681 |
1.22e-22 |
|
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: 97.12 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITD 598
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 599 NI---------SYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEA 669
Cdd:cd03219 95 NVmvaaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170
....*....|...
gi 339895787 670 TSAL-DAESEYLI 681
Cdd:cd03219 171 AAGLnPEETEELA 183
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
507-674 |
1.52e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 586
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPvLFARSIT--DNISYGL-PTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMA 654
Cdd:PRK11231 83 QHH-LTPEGITvrELVAYGRsPWLSLwgrlsaednARVNQAMEQTR----INHLADRRLTD-------LSGGQRQRAFLA 150
|
170 180
....*....|....*....|
gi 339895787 655 RALVRNPPVLILDEATSALD 674
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLD 170
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
189-448 |
2.21e-22 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 97.95 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 189 VAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMdqfSTAVVIVCLLAIGSSFAA---GIRGGIFTLIFARLNIRLRNCL 265
Cdd:cd18588 8 LLASLFLQLFALV---TPLFFQVIIDKVLVHRSL---STLDVLAIGLLVVALFEAvlsGLRTYLFSHTTNRIDAELGARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 266 FRSLVSQETSFFDENRTGDLISR----------LTSDT-TMVSDLVSqnINVFLrntvkvtgvvVFMFSLSWQLSLVTFM 334
Cdd:cd18588 82 FRHLLRLPLSYFESRQVGDTVARvrelesirqfLTGSAlTLVLDLVF--SVVFL----------AVMFYYSPTLTLIVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 335 GFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVW 414
Cdd:cd18588 150 SLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQ 229
|
250 260 270
....*....|....*....|....*....|....
gi 339895787 415 GSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18588 230 IVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
504-681 |
2.51e-22 |
|
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: 96.03 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsAYDHKYLHRVIS 583
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNISY-----GLPTVPFEMVVEAAQKanahgfIMELQDGYSTETGekgaQLSGGQKQRVAMARAL 657
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180
....*....|....*....|....
gi 339895787 658 VRNPPVLILDEATSALDAESEYLI 681
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAI 172
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
506-677 |
2.57e-22 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 96.60 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfypLEGGRVLLDGKPISAYDHKYLHRV- 581
Cdd:TIGR02315 4 VENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTllrCINRLVE---PSSGSILLEGTDITKLRGKKLRKLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 --ISLVSQEPVLFAR-SITDNISYG----LPTVP--FEMVVEAaQKANAhgfiMELQD--GYSTETGEKGAQLSGGQKQR 650
Cdd:TIGR02315 79 rrIGMIFQHYNLIERlTVLENVLHGrlgyKPTWRslLGRFSEE-DKERA----LSALErvGLADKAYQRADQLSGGQQQR 153
|
170 180
....*....|....*....|....*..
gi 339895787 651 VAMARALVRNPPVLILDEATSALDAES 677
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKT 180
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
504-676 |
3.25e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.74 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRT-RPHTqvLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI 582
Cdd:PRK13648 8 IVFKNVSFQYQSdASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEPV-LFARSITD-NISYGLP--TVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAqLSGGQKQRVAMARALV 658
Cdd:PRK13648 86 GIVFQNPDnQFVGSIVKyDVAFGLEnhAVPYDEMHRRVSEA------LKQVDMLERADYEPNA-LSGGQKQRVAIAGVLA 158
|
170
....*....|....*...
gi 339895787 659 RNPPVLILDEATSALDAE 676
Cdd:PRK13648 159 LNPSVIILDEATSMLDPD 176
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
504-676 |
4.03e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.72 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALVR 659
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEALE---LVGMQDFKEREP----ARLSGGQKQRVAIAGAVAM 157
|
170
....*....|....*..
gi 339895787 660 NPPVLILDEATSALDAE 676
Cdd:PRK13650 158 RPKIIILDEATSMLDPE 174
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
507-674 |
5.37e-22 |
|
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: 95.30 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV 585
Cdd:cd03218 4 ENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVLFAR-SITDNISYGLPTVPFEmvvEAAQKANAHGFIMELQdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 664
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLS---KKEREEKLEELLEEFH--ITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170
....*....|
gi 339895787 665 ILDEATSALD 674
Cdd:cd03218 156 LLDEPFAGVD 165
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
504-674 |
6.09e-22 |
|
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: 95.43 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-- 581
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 -ISLVSQEPVLFArSIT--DNISYGL---PTVPFEMVVEAAqkanahgfIMELQdgystETGEKGA------QLSGGQKQ 649
Cdd:COG1127 83 rIGMLFQGGALFD-SLTvfENVAFPLrehTDLSEAEIRELV--------LEKLE-----LVGLPGAadkmpsELSGGMRK 148
|
170 180
....*....|....*....|....*
gi 339895787 650 RVAMARALVRNPPVLILDEATSALD 674
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLD 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
507-675 |
7.66e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.54 E-value: 7.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRVIsLVS 586
Cdd:PRK11248 5 SHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGV-VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPVLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfimelqdgystETGEKGA------QLSGGQKQRVAMARALV 658
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLagVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIARALA 144
|
170
....*....|....*..
gi 339895787 659 RNPPVLILDEATSALDA 675
Cdd:PRK11248 145 ANPQLLLLDEPFGALDA 161
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
524-677 |
7.99e-22 |
|
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: 97.48 E-value: 7.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsaYD---------HKylhRVISLVSQEPVLFA- 593
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDsargiflppHR---RRIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 594 RSITDNISYGL-------PTVPFEMVVEAAQkanahgfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:COG4148 92 LSVRGNLLYGRkrapraeRRISFDEVVELLG-------IGHLLDRRP-------ATLSGGERQRVAIGRALLSSPRLLLM 157
|
170
....*....|.
gi 339895787 667 DEATSALDAES 677
Cdd:COG4148 158 DEPLAALDLAR 168
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
507-675 |
8.43e-22 |
|
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: 96.66 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP---LEGGRVLLDGKPISAYDHKYLHRV- 581
Cdd:COG0444 5 RNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKIr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ---ISLVSQE------PVLfarsitdnisyglpTVpFEMVVEAaqkanahgfiMELQDGYSTETGEKGA----------- 641
Cdd:COG0444 85 greIQMIFQDpmtslnPVM--------------TV-GDQIAEP----------LRIHGGLSKAEARERAiellervglpd 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 339895787 642 ----------QLSGGQKQRVAMARALVRNPPVLILDEATSALDA 675
Cdd:COG0444 140 perrldryphELSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
519-677 |
1.26e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.59 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILENFYPLE--GGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFA 593
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 594 R-SITDNISYGLP--------TVPFEMVVEAAQKAnahgfimELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 664
Cdd:PRK14247 96 NlSIFENVALGLKlnrlvkskKELQERVRWALEKA-------QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170
....*....|...
gi 339895787 665 ILDEATSALDAES 677
Cdd:PRK14247 169 LADEPTANLDPEN 181
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
514-674 |
2.10e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 95.95 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYL---HRVISLVSQEPv 590
Cdd:COG4608 26 RTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 591 lFA-----RSITDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGA-QLSGGQKQRVAMARALVRNPP 662
Cdd:COG4608 105 -YAslnprMTVGDIIAEPL------RIHGLASKAERRERVAELLElvGLRPEHADRYPhEFSGGQRQRIGIARALALNPK 177
|
170
....*....|..
gi 339895787 663 VLILDEATSALD 674
Cdd:COG4608 178 LIVCDEPVSALD 189
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
520-681 |
2.37e-21 |
|
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: 93.95 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDhkyLHRVISL-VS---QEPVLFAR- 594
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP---PHRIARLgIArtfQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 SITDNI--------SYGLPTVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 664
Cdd:COG0411 95 TVLENVlvaaharlGRGLLAALLRLPRARREEREARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170
....*....|....*...
gi 339895787 665 ILDEATSAL-DAESEYLI 681
Cdd:COG0411 175 LLDEPAAGLnPEETEELA 192
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
504-674 |
2.49e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.70 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 581
Cdd:PRK13635 6 IRVEHISFRY---PDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ISLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHgfiMELQDGYSTETgekgAQLSGGQKQRVAMARAL 657
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLENigVPREEMVERVDQALRQ---VGMEDFLNREP----HRLSGGQKQRVAIAGVL 155
|
170
....*....|....*..
gi 339895787 658 VRNPPVLILDEATSALD 674
Cdd:PRK13635 156 ALQPDIIILDEATSMLD 172
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
507-676 |
9.12e-21 |
|
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: 91.12 E-value: 9.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVS 586
Cdd:cd03268 4 NDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 qEPVLF-ARSITDNISYglptvpfemvveaaqKANAHGF----IMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVR 659
Cdd:cd03268 80 -APGFYpNLTARENLRL---------------LARLLGIrkkrIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170
....*....|....*..
gi 339895787 660 NPPVLILDEATSALDAE 676
Cdd:cd03268 144 NPDLLILDEPTNGLDPD 160
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
510-675 |
9.45e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.59 E-value: 9.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 510 TFTYRT----RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPvlfarsitdNISYGlPTVPFEMVVEAAQKANAH-----------------GFIMELQDGYSTEtgekgaqLSGGQK 648
Cdd:COG4167 93 FQDP---------NTSLN-PRLNIGQILEEPLRLNTDltaeereerifatlrlvGLLPEHANFYPHM-------LSSGQK 155
|
170 180
....*....|....*....|....*..
gi 339895787 649 QRVAMARALVRNPPVLILDEATSALDA 675
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDM 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
514-674 |
1.12e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYLHRVISLVSQEP- 589
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 590 --VLFARSITDNIsyGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTEtgeKGAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:PRK10419 100 saVNPRKTVREII--REPLRHLLSLDKAERLARASEMLraVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLI 174
|
....*....
gi 339895787 666 LDEATSALD 674
Cdd:PRK10419 175 LDEAVSNLD 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
521-681 |
1.39e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK----YL-HRvislVSQEPVLfarS 595
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHR----NAMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 596 ITDNIS-----YGlptvPFEMVVEAAQKANAHGFIMELQDGYstetgekgaqLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:PRK13539 90 VAENLEfwaafLG----GEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170
....*....|.
gi 339895787 671 SALDAESEYLI 681
Cdd:PRK13539 156 AALDAAAVALF 166
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
522-674 |
1.54e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.77 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP---LEGgRVLLDGKPISA--YDHKYLHRVISLVSQEPVLFA 593
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPgfrVEG-KVTFHGKNLYApdVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 594 RSITDNISYGlPTV-----PFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:PRK14243 105 KSIYDNIAYG-ARIngykgDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
....*.
gi 339895787 669 ATSALD 674
Cdd:PRK14243 178 PCSALD 183
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
504-674 |
1.83e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 93.86 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 583
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNISYGL--PTVPFE----MVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAMARA 656
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGLrmQKTPAAeitpRVMEALRMVQLEEFA-----------QRKPHQLSGGQQQRVAIARA 158
|
170
....*....|....*...
gi 339895787 657 LVRNPPVLILDEATSALD 674
Cdd:PRK09452 159 VVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
507-674 |
2.39e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.68 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKYLHRV---IS 583
Cdd:PRK13639 3 ETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVrktVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfiMElqdGYstetgEKGA--QLSGGQKQRVAMA 654
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGplnlgLSKEEVEKRVKEALKAVG----ME---GF-----ENKPphHLSGGQKKRVAIA 149
|
170 180
....*....|....*....|
gi 339895787 655 RALVRNPPVLILDEATSALD 674
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLD 169
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
507-677 |
2.42e-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: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENV--TFTYRTRPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSS---CvnILENFYPlEGGRVLL--DGKPI---SAYD 574
Cdd:COG4778 8 ENLskTFTLHLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTllkC--IYGNYLP-DSGSILVrhDGGWVdlaQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 575 HKYLH---RVISLVSQepvlFARSItdnisyglPTVP-FEMVVEAAqkanahgfimeLQDGYSTETG-EKGAQL------ 643
Cdd:COG4778 85 REILAlrrRTIGYVSQ----FLRVI--------PRVSaLDVVAEPL-----------LERGVDREEArARARELlarlnl 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 339895787 644 ------------SGGQKQRVAMARALVRNPPVLILDEATSALDAES 677
Cdd:COG4778 142 perlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN 187
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
520-674 |
3.11e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.61 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 520 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP--LEGGRVLLDGKPISA--YDHKYLHRVISLVSQEPVLF 592
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 593 ARSITDNISYGL------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:PRK14239 99 PMSIYENVVYGLrlkgikDKQVLDEAVEKSLKGAS------IWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
....*...
gi 339895787 667 DEATSALD 674
Cdd:PRK14239 173 DEPTSALD 180
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
506-680 |
3.45e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpisaydhkylHRVISLV 585
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVLFA-RSITDNISYGLPTV-------------PFEMVVEAAQKANAHGfIMELQDGYSTET--------------- 636
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELraleaeleeleakLAEPDEDLERLAELQE-EFEALGGWEAEAraeeilsglgfpeed 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 339895787 637 -GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES-----EYL 680
Cdd:COG0488 146 lDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFL 195
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
518-670 |
3.48e-20 |
|
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: 90.04 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-S 595
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 596 ITDNISYGLPTVPFEMVVEAAQKanahgFIMEL---------QdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRADLE-----RVYELfprlkerrrQ---------RAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
....
gi 339895787 667 DEAT 670
Cdd:COG0410 161 DEPS 164
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
507-676 |
5.39e-20 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 89.42 E-value: 5.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENfypLE---GGRVLLDGKPISAYDHKYLHRV- 581
Cdd:COG4181 12 RGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG---LDrptSGTVRLAGQDLFALDEDARARLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ---ISLVSQE----PVLFARsitDNIsyglpTVPFEM--VVEAAQKANAhgfimELQD-GYSTETGEKGAQLSGGQKQRV 651
Cdd:COG4181 89 arhVGFVFQSfqllPTLTAL---ENV-----MLPLELagRRDARARARA-----LLERvGLGHRLDHYPAQLSGGEQQRV 155
|
170 180
....*....|....*....|....*
gi 339895787 652 AMARALVRNPPVLILDEATSALDAE 676
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAA 180
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
504-674 |
5.50e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.54 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVR 659
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIAL 157
|
170
....*....|....*
gi 339895787 660 NPPVLILDEATSALD 674
Cdd:PRK13642 158 RPEIIILDESTSMLD 172
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
508-674 |
8.11e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 89.86 E-value: 8.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 508 NVTFTYRT------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYL 578
Cdd:TIGR02769 7 DVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 579 HRVISLVSQE-PVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGfIMELQDGYSTETGEKGAQLSGGQKQRVAMARAL 657
Cdd:TIGR02769 87 RRDVQLVFQDsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAE-LLDMVGLRSEDADKLPRQLSGGQLQRINIARAL 165
|
170
....*....|....*..
gi 339895787 658 VRNPPVLILDEATSALD 674
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLD 182
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
520-676 |
8.48e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.42 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 520 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEG----GRVLLDG-KPISAYDH--KYLHRVISLVSQEP 589
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ--PEAGtirvGDITIDTaRSLSQQKGliRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 590 VLFA-RSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:PRK11264 95 NLFPhRTVLENIIEG----PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
....*...
gi 339895787 669 ATSALDAE 676
Cdd:PRK11264 171 PTSALDPE 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
514-674 |
9.69e-20 |
|
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: 93.21 E-value: 9.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSC----VNILENfypleGGRVLLDGKPISAYDHKYLHRV---ISLVS 586
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRALRPLrrrMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPvlFA-----RSITDNISYGLpTVPF---------EMVVEAAQKAnahGFIMELQDGYSTEtgekgaqLSGGQKQRVA 652
Cdd:COG4172 369 QDP--FGslsprMTVGQIIAEGL-RVHGpglsaaerrARVAEALEEV---GLDPAARHRYPHE-------FSGGQRQRIA 435
|
170 180
....*....|....*....|..
gi 339895787 653 MARALVRNPPVLILDEATSALD 674
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALD 457
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
188-450 |
1.79e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 89.56 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18566 7 VLLASLFINILALA---TPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrntvKVTGVVVF---MFSLSWQLSLVTFMGFPIIMMVSN 344
Cdd:cd18566 84 HLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALL----DLPFVLIFlglIWYLGGKLVLVPLVLLGLFVLVAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 345 IYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQ----VYKLNRKEAAAYMyyvwGSGLTL 420
Cdd:cd18566 160 LLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANaayaGFKVAKINAVAQT----LGQLFS 235
|
250 260 270
....*....|....*....|....*....|
gi 339895787 421 LVVQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18566 236 QVSMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
521-675 |
2.16e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNI---LENfyPLEGgRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SI 596
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLvagLEK--PTEG-QIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 597 TDNISYGLPT--VPFE----MVVEAAQKANAHGFimelQDGYSTetgekgaQLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:PRK11432 96 GENVGYGLKMlgVPKEerkqRVKEALELVDLAGF----EDRYVD-------QISGGQQQRVALARALILKPKVLLFDEPL 164
|
....*
gi 339895787 671 SALDA 675
Cdd:PRK11432 165 SNLDA 169
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
507-668 |
2.32e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.78 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV 585
Cdd:COG1137 7 ENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVLFaRSIT--DNIsyglptvpfEMVVE------AAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARAL 657
Cdd:COG1137 84 PQEASIF-RKLTveDNI---------LAVLElrklskKEREERLEELLEEFGITHLRKS--KAYSLSGGERRRVEIARAL 151
|
170
....*....|.
gi 339895787 658 VRNPPVLILDE 668
Cdd:COG1137 152 ATNPKFILLDE 162
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
182-450 |
2.73e-19 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 88.80 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRL 261
Cdd:cd18782 1 RRALIEVLALSFVVQLLGL---ANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 262 RNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 341
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 342 VSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEE----EEAEVYLRKLQQVYKLNRKEAAAYMYyvwgSG 417
Cdd:cd18782 157 LTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELkarwRWQNRYARSLGEGFKLTVLGTTSGSL----SQ 232
|
250 260 270
....*....|....*....|....*....|...
gi 339895787 418 LTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18782 233 FLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRI 265
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
507-674 |
3.34e-19 |
|
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: 86.65 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYR-TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-----KPISAydhkylHR 580
Cdd:cd03266 5 DALTKRFRdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEA------RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VISLVSQEPVLFAR-SITDNISY-----GLptvpfemvveaaQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVA 652
Cdd:cd03266 79 RLGFVSDSTGLYDRlTARENLEYfaglyGL------------KGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVA 146
|
170 180
....*....|....*....|..
gi 339895787 653 MARALVRNPPVLILDEATSALD 674
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLD 168
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
518-670 |
4.17e-19 |
|
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: 86.81 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-S 595
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 596 ITDNISYGLPTVPfemvveaAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:TIGR03410 92 VEENLLTGLAALP-------RRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
506-678 |
4.98e-19 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 84.90 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFtyRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVlldgkpisaydHKYLHRVISLV 585
Cdd:cd03223 3 LENLSL--ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVLFARSITDNISYglptvPFEMVveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 665
Cdd:cd03223 70 PQRPYLPLGTLREQLIY-----PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170
....*....|...
gi 339895787 666 LDEATSALDAESE 678
Cdd:cd03223 115 LDEATSALDEESE 127
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
518-675 |
8.49e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.02 E-value: 8.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI----SAYDHKYLHRVISLVSQepvlFA 593
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRNQKLGFIYQ----FH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 594 RSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK11629 97 HLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
..
gi 339895787 674 DA 675
Cdd:PRK11629 177 DA 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
514-674 |
9.20e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYL---HRVISLVSQEP- 589
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 590 -VLFAR-SITDNISYGL----PTVpfemvvEAAQKANAHGFIMElQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPP 662
Cdd:PRK15134 373 sSLNPRlNVLQIIEEGLrvhqPTL------SAAQREQQVIAVME-EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPS 445
|
170
....*....|..
gi 339895787 663 VLILDEATSALD 674
Cdd:PRK15134 446 LIILDEPTSSLD 457
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
522-681 |
1.05e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVSQEPVLFAR- 594
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdAIALG-----IGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 SITDNISYGLPTVPFEMV--VEAAQKanahgfIMELQDGYstetG------EKGAQLSGGQKQRVAMARALVRNPPVLIL 666
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLdrKAARAR------IRELSERY----GldvdpdAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170
....*....|....*.
gi 339895787 667 DEATSAL-DAESEYLI 681
Cdd:COG3845 166 DEPTAVLtPQEADELF 181
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
510-674 |
1.40e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.00 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 510 TFTYRT----RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 585
Cdd:PRK15112 13 TFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPvlfARSITDNISYG-LPTVPFEMVVEAAQKANAHGFIMEL-QDGYSTE-TGEKGAQLSGGQKQRVAMARALVRNPP 662
Cdd:PRK15112 93 FQDP---STSLNPRQRISqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPK 169
|
170
....*....|..
gi 339895787 663 VLILDEATSALD 674
Cdd:PRK15112 170 VIIADEALASLD 181
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
504-677 |
1.57e-18 |
|
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: 85.52 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL--ENfYPLEGGRVLLDGKPISAYDHKYLHRV 581
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgDL-PPTYGNDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ISLVSQEpvlFARSITDNIsyglpTVpFEMV-------------VEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQK 648
Cdd:COG1119 80 IGLVSPA---LQLRFPRDE-----TV-LDVVlsgffdsiglyrePTDEQRERARELLELL--GLAHLADRPFGTLSQGEQ 148
|
170 180
....*....|....*....|....*....
gi 339895787 649 QRVAMARALVRNPPVLILDEATSALDAES 677
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGA 177
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
230-668 |
2.05e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 89.09 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 230 VIVCLLAIGSSFAAGIRggiFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSqNINVFLR 309
Cdd:COG4615 55 AGLLVLLLLSRLASQLL---LTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 310 NTVKVTGVVVFMFSLSWQLSLVTFmgfpiIMMVSNIYGkyYKRLSKEVQNALARASNTAEETISAMKTV----------- 378
Cdd:COG4615 131 SVALVLGCLAYLAWLSPPLFLLTL-----VLLGLGVAG--YRLLVRRARRHLRRAREAEDRLFKHFRALlegfkelklnr 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 379 ---RSFANEEeeaevYLRKLQQVYKLNRKEAAAYMYYV-WGSgLTLLVVQVSILYYGGHLV-ISGQMTSGnlIAFIIYeF 453
Cdd:COG4615 204 rrrRAFFDED-----LQPTAERYRDLRIRADTIFALANnWGN-LLFFALIGLILFLLPALGwADPAVLSG--FVLVLL-F 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 454 VLGDcMESVGSVYSGLMQGVGAAEKVFEF---IDRQPTMVHDGSLAPDHLE-GRVDFENVTFTYRTRPHTQ--VLQNVSF 527
Cdd:COG4615 275 LRGP-LSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDEgfTLGPIDL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 528 SLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA--YDHkYLHRvISLVSQEPVLFARsitdniSYGLP 605
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREA-YRQL-FSAVFSDFHLFDR------LLGLD 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895787 606 TVPfemvveAAQKANAHGFIMELQ------DGYSTETgekgaQLSGGQKQRVAMARALVRNPPVLILDE 668
Cdd:COG4615 426 GEA------DPARARELLERLELDhkvsveDGRFSTT-----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
504-675 |
2.11e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.21 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNI---LEnfyPLEGGRVLLDGKPISAYDHKylHR 580
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLE---RITSGEIWIGGRVVNELEPA--DR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VISLVSQEPVLFAR-SITDNISYGLPT--VP----FEMVVEAAQkanahgfIMELQ---DgystetgEKGAQLSGGQKQR 650
Cdd:PRK11650 77 DIAMVFQNYALYPHmSVRENMAYGLKIrgMPkaeiEERVAEAAR-------ILELEpllD-------RKPRELSGGQRQR 142
|
170 180
....*....|....*....|....*
gi 339895787 651 VAMARALVRNPPVLILDEATSALDA 675
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
525-681 |
2.40e-18 |
|
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: 87.09 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 525 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKylhRVISLVSQEPVLFAR-SI 596
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEK---RRIGYVFQEARLFPHlSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 597 TDNISYGL--PTVPFEMVVEAAqkanahgfIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:TIGR02142 93 RGNLRYGMkrARPSERRISFER--------VIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
....*..
gi 339895787 675 AESEYLI 681
Cdd:TIGR02142 164 DPRKYEI 170
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
521-681 |
2.74e-18 |
|
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: 83.70 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsAYDHKYLHRVISLVSQEPVLFAR-SITDN 599
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 600 ISYGLPTVPFEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 679
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNGF-----------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
..
gi 339895787 680 LI 681
Cdd:cd03231 163 RF 164
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
516-677 |
2.75e-18 |
|
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: 83.56 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 516 RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVISLVSQEPVLFAR- 594
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 SITDNISYGLPTVPFE--MVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:TIGR01189 89 SALENLHFWAAIHGGAqrTIEDALAAVGLTGF-----------EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
....*
gi 339895787 673 LDAES 677
Cdd:TIGR01189 158 LDKAG 162
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
256-675 |
4.10e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 89.26 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 256 RLNIRLRNCLFRSLVSQETSFFDENR----TGDLISRLTSDTTMVSdLVSQNINVFLRNTVKVTgvvVFMFSLSWQLSLV 331
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDANALQ-QIAEQLHGLWSAPFRII---VSMVLLYQQLGVA 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 332 TFMGFPIIMMV---SNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE----------EAEVYLRKLQQV 398
Cdd:PLN03232 443 SLFGSLILFLLiplQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSfesriqgirnEELSWFRKAQLL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 399 YKLNrkeaaAYMyyvwgsgLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEK 478
Cdd:PLN03232 523 SAFN-----SFI-------LNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 479 VFE-FIDRQPTMVHDGSLAPDhlEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFY 556
Cdd:PLN03232 591 IEElLLSEERILAQNPPLQPG--APAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELS 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 557 PLEGGRVLLDGKpisaydhkylhrvISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGfiMELQDGYS-TE 635
Cdd:PLN03232 669 HAETSSVVIRGS-------------VAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTE 733
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 339895787 636 TGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 675
Cdd:PLN03232 734 IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
504-674 |
4.18e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.79 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKAnahgfiMELQDgysteTGEKGA-QLSGGQKQRVAMAR 655
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKA------VRMWD-----FRDKPPyHLSYGQKKRVAIAG 151
|
170
....*....|....*....
gi 339895787 656 ALVRNPPVLILDEATSALD 674
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLD 170
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
507-675 |
5.54e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.03 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGGRVLLDGKpisaydhkylhrvISLV 585
Cdd:PLN03130 618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVLFARSITDNISYGLPTVP--FEMVVEAAqkANAHGFIMeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 663
Cdd:PLN03130 685 PQVSWIFNATVRDNILFGSPFDPerYERAIDVT--ALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
170
....*....|..
gi 339895787 664 LILDEATSALDA 675
Cdd:PLN03130 762 YIFDDPLSALDA 773
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
521-674 |
6.62e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.04 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SITDN 599
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 600 ISYGLPTVPFEMVvEAAQKANAHGFIMELQDGysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK11607 112 IAFGLKQDKLPKA-EIASRVNEMLGLVHMQEF----AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
513-674 |
1.04e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.13 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 513 YRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHK---YLHRVISLVSQEP 589
Cdd:PRK13636 13 YNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmKLRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 590 --VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:PRK13636 92 dnQLFSASVYQDVSFGAVNlkLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
....*....
gi 339895787 666 LDEATSALD 674
Cdd:PRK13636 165 LDEPTAGLD 173
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
504-681 |
1.51e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 83.31 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY---PLEGGRVLLDGKPISAYDHKYLHR 580
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VISLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDGystetgeKGAQLSGGQKQRVAMARA 656
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLADVGMLDYIDS-------EPANLSGGQKQRVAIAGI 157
|
170 180
....*....|....*....|....*
gi 339895787 657 LVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQI 182
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
261-451 |
1.56e-17 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 83.62 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 261 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 340
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 341 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAaymyyvWgSGLTL 420
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTR------W-NAKTF 233
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895787 421 LVVQVS-------ILYYGGHLVISGQMTSGNLIAFIIY 451
Cdd:cd18554 234 SAVNTItdlapllVIGFAAYLVIEGNLTVGTLVAFVGY 271
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
500-681 |
1.70e-17 |
|
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: 82.65 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 500 LEGRVDFENVTFTYRT--RPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY 577
Cdd:cd03288 16 LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 578 LHRVISLVSQEPVLFARSITDNISyglP--TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 655
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNLD---PecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180
....*....|....*....|....*.
gi 339895787 656 ALVRNPPVLILDEATSALDAESEYLI 681
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENIL 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
505-674 |
2.94e-17 |
|
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: 85.51 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 505 DFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGKPISAYDHKYLH 579
Cdd:COG4172 8 SVEDLSVAFGQGGGtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 RV----ISLVSQEPV-----LFarSITDNISYGLptvpfeMVVEAAQKANAHGFIMELQDgystETGEKGA--------- 641
Cdd:COG4172 88 RIrgnrIAMIFQEPMtslnpLH--TIGKQIAEVL------RLHRGLSGAAARARALELLE----RVGIPDPerrldayph 155
|
170 180 190
....*....|....*....|....*....|...
gi 339895787 642 QLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
521-680 |
3.74e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SITD 598
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 599 NISYGLPTVPfemvvEAAQKANAhgFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD-AES 677
Cdd:PRK15439 106 NILFGLPKRQ-----ASMQKMKQ--LLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
...
gi 339895787 678 EYL 680
Cdd:PRK15439 177 ERL 179
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
520-681 |
4.09e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 80.78 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN---FYPLEGGRVLLDGKPISAYDHKYlhrVISLVSQEPVlFARSI 596
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQK---CVAYVRQDDI-LLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 597 T--DNISYglpTVPFEMVVEA--AQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:cd03234 97 TvrETLTY---TAILRLPRKSsdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
....*....
gi 339895787 673 LDAESEYLI 681
Cdd:cd03234 174 LDSFTALNL 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
495-675 |
4.62e-17 |
|
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: 85.77 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 495 LAPDHLEGR---------VDFENVTFTY-RTRPHTqvLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgrv 563
Cdd:TIGR00957 619 LEPDSIERRtikpgegnsITVHNATFTWaRDLPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEG--- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 564 lldgkpisaydHKYLHRVISLVSQEPVLFARSITDNISYGLPTVP--FEMVVEAAqkanahGFIMELQ---DGYSTETGE 638
Cdd:TIGR00957 694 -----------HVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEkyYQQVLEAC------ALLPDLEilpSGDRTEIGE 756
|
170 180 190
....*....|....*....|....*....|....*..
gi 339895787 639 KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 675
Cdd:TIGR00957 757 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
507-675 |
5.79e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkyLHRVISLVS 586
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPVLFA-RSITDNISYGLptvpfemvvEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGL---------KGQWRDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170
....*....|
gi 339895787 666 LDEATSALDA 675
Cdd:PRK11247 157 LDEPLGALDA 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
504-680 |
5.81e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-I 582
Cdd:PRK09700 6 ISMAGIGKSF---GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQE-PVLFARSITDNISYG-LPT-----VPF----EMVVEAAqkanahgfIMELQDGYSTETGEKGAQLSGGQKQRV 651
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGrHLTkkvcgVNIidwrEMRVRAA--------MMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190
....*....|....*....|....*....|
gi 339895787 652 AMARALVRNPPVLILDEATSAL-DAESEYL 680
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLtNKEVDYL 184
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
501-678 |
6.86e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 501 EGRVDFENVTFTyrtRPHTQVL-QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL-DGKPISaydhkyl 578
Cdd:COG4178 360 DGALALEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 579 hrvisLVSQEPVLFARSITDNISYGLPTVPF--EMVVEAAQKANAHGFIMELQdgystETGEKGAQLSGGQKQRVAMARA 656
Cdd:COG4178 430 -----FLPQRPYLPLGTLREALLYPATAEAFsdAELREALEAVGLGHLAERLD-----EEADWDQVLSLGEQQRLAFARL 499
|
170 180
....*....|....*....|..
gi 339895787 657 LVRNPPVLILDEATSALDAESE 678
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENE 521
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
504-676 |
7.42e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.44 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILEnfYPLEGGRVLLDGK-----PISAYDH 575
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLrvlNLLE--TPDSGQLNIAGHQfdfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 576 KYLHRVISLVSQEPVLFA-RSITDNISYGlPTVPFEMVVEAAQ-KANAHGFIMELQDgystETGEKGAQLSGGQKQRVAM 653
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPhLTVMENLIEA-PCKVLGLSKEQAReKAMKLLARLRLTD----KADRFPLHLSGGQQQRVAI 152
|
170 180
....*....|....*....|...
gi 339895787 654 ARALVRNPPVLILDEATSALDAE 676
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPE 175
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
517-681 |
7.57e-17 |
|
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: 80.07 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV-NILENFYPLEG----GRVLLDGKPISAYDHKYLHRViSLVSQEPVL 591
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRYSV-AYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 592 FARSITDNISYGLP--TVPFEMVVEAAqkaNAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 669
Cdd:cd03290 91 LNATVEENITFGSPfnKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170
....*....|...
gi 339895787 670 TSALDAE-SEYLI 681
Cdd:cd03290 168 FSALDIHlSDHLM 180
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
504-681 |
8.48e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 8.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA-YDHKYLHR 580
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 V---ISLVSQ--EPVLFARSITDNISYGLPTvpFEMVVEAAqKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMA 654
Cdd:PRK13646 83 VrkrIGMVFQfpESQLFEDTVEREIIFGPKN--FKMNLDEV-KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180
....*....|....*....|....*..
gi 339895787 655 RALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQV 184
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
505-674 |
8.83e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 8.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 505 DFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG------GRVLLDGKPISAYDHKYL 578
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 579 HRVISLVSQEPVLFAR-SITDNISYGLPTVPFE-------MVVEAAQKAnahGFIMELQDGYSTetgeKGAQLSGGQKQR 650
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKekreikkIVEECLRKV---GLWKEVYDRLNS----PASQLSGGQQQR 161
|
170 180
....*....|....*....|....
gi 339895787 651 VAMARALVRNPPVLILDEATSALD 674
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMID 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
507-674 |
1.07e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.94 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV 585
Cdd:PRK10895 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVLFAR-SITDNIsygLPTVPFEMVVEAAQKANAHGFIME------LQDGYstetgekGAQLSGGQKQRVAMARALV 658
Cdd:PRK10895 84 PQEASIFRRlSVYDNL---MAVLQIRDDLSAEQREDRANELMEefhiehLRDSM-------GQSLSGGERRRVEIARALA 153
|
170
....*....|....*.
gi 339895787 659 RNPPVLILDEATSALD 674
Cdd:PRK10895 154 ANPKFILLDEPFAGVD 169
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
522-675 |
1.12e-16 |
|
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: 79.82 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLhrvisLVSQEPVLFA-RSITDNI 600
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 601 SYGLPTVPFEMVVEAAQKANAHGFIMElqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 675
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALV---GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
506-681 |
1.68e-16 |
|
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: 78.05 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN--FYPLEGGRVLLDGKPISaydhKYLHRVI 582
Cdd:cd03232 6 WKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD----KNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEPVLFarsitdnisyglptvPFEMVVEAAQ-KANAHGfimelqdgystetgekgaqLSGGQKQRVAMARALVRNP 661
Cdd:cd03232 82 GYVEQQDVHS---------------PNLTVREALRfSALLRG-------------------LSVEQRKRLTIGVELAAKP 127
|
170 180
....*....|....*....|
gi 339895787 662 PVLILDEATSALDAESEYLI 681
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNI 147
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
504-674 |
2.14e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.17 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAY----DHKY 577
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 578 LHRVISLVSQ--EPVLFARSITDNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMA 654
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQN--FGVSQEEAEALAREKLALV---GISESLFEKNPfELSGGQMRRVAIA 157
|
170 180
....*....|....*....|
gi 339895787 655 RALVRNPPVLILDEATSALD 674
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
504-678 |
2.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSScvnILENFYPL---EGGRVLLDGKPISAYDH--- 575
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKST---LMQHFNALlkpSSGTITIAGYHITPETGnkn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 576 -KYLHRVISLVSQ--EPVLFARSITDNISYGLPTVPFEmvvEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRV 651
Cdd:PRK13641 80 lKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFS---EDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180
....*....|....*....|....*..
gi 339895787 652 AMARALVRNPPVLILDEATSALDAESE 678
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
511-678 |
3.80e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.89 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 511 FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-------------ILENFY---PLEGGRVLLDGKPISAYD 574
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigdKKNNHELITNPYSKKIKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 575 HKYLHRVISLVSQEP--VLFARSITDNISYGlPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGekgAQLSGGQKQRVA 652
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSYLERSP---FGLSGGQKRRVA 186
|
170 180
....*....|....*....|....*.
gi 339895787 653 MARALVRNPPVLILDEATSALDAESE 678
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGE 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
521-675 |
3.88e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.90 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDgkpisaydhkylhRVISLVSQEPVLFARSITDNI 600
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895787 601 SYGLPTVPFEM--VVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 675
Cdd:PTZ00243 742 LFFDEEDAARLadAVRVSQlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
502-674 |
6.61e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.13 E-value: 6.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 502 GRVDFENVTFTYRtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 581
Cdd:PTZ00243 1307 GSLVFEGVQMRYR-EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ISLVSQEPVLFARSITDNISYGLPTVPFEmVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNVDPFLEASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKG 1464
|
170
....*....|....
gi 339895787 662 PVLIL-DEATSALD 674
Cdd:PTZ00243 1465 SGFILmDEATANID 1478
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
515-674 |
1.22e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 515 TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPvlfar 594
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 sitdnisyglpTVPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ------------------LSGGQKQRVAMARA 656
Cdd:PRK09536 87 -----------SLSFEFDVRQVVEMGRTPHRSRF--DTWTETDRAAVEramertgvaqfadrpvtsLSGGERQRVLLARA 153
|
170
....*....|....*...
gi 339895787 657 LVRNPPVLILDEATSALD 674
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD 171
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
504-681 |
1.22e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.72 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydHKYLHRV-I 582
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARArI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQ----EPVLFARsitDNI-----SYGLPTVPFEMVV----EAAQ---KANAhgfimelqdgystetgeKGAQLSGG 646
Cdd:PRK13536 117 GVVPQfdnlDLEFTVR---ENLlvfgrYFGMSTREIEAVIpsllEFARlesKADA-----------------RVSDLSGG 176
|
170 180 190
....*....|....*....|....*....|....*
gi 339895787 647 QKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
506-680 |
1.23e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI---SAYDHkyLHRVI 582
Cdd:PRK11288 7 FDGIGKTF---PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAA--LAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQE----PVLfarSITDNISYG-LPTvPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARAL 657
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGqLPH-KGGIVNRRLLNYEAREQLEHLGVDIDPDT--PLKYLSIGQRQMVEIAKAL 155
|
170 180
....*....|....*....|....
gi 339895787 658 VRNPPVLILDEATSALDA-ESEYL 680
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSArEIEQL 179
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
504-676 |
1.67e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.07 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLHR 580
Cdd:PRK10908 2 IRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 VISLVSQEP-VLFARSITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARAL 657
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVA--IP-----LIIAGASGDDIRRRVSAALDkvGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170
....*....|....*....
gi 339895787 658 VRNPPVLILDEATSALDAE 676
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDA 171
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
502-678 |
1.80e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.36 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 502 GRVDFENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA-----YD 574
Cdd:PRK13645 5 KDIILDNVSYTYakKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 575 HKYLHRVISLVSQEP--VLFARSITDNISYGlptvPFEMvveAAQKANAHGFIMELQDGYS--TETGEKGA-QLSGGQKQ 649
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFG----PVNL---GENKQEAYKKVPELLKLVQlpEDYVKRSPfELSGGQKR 157
|
170 180
....*....|....*....|....*....
gi 339895787 650 RVAMARALVRNPPVLILDEATSALDAESE 678
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
516-674 |
1.88e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.08 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 516 RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH---KYLHRVISLVSQ--- 587
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQnpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 588 --------------EPVLfarsITDNISyglptvpfemVVEAAQKANAhgfiMELQDGYSTE-TGEKGAQLSGGQKQRVA 652
Cdd:PRK11308 103 gslnprkkvgqileEPLL----INTSLS----------AAERREKALA----MMAKVGLRPEhYDRYPHMFSGGQRQRIA 164
|
170 180
....*....|....*....|..
gi 339895787 653 MARALVRNPPVLILDEATSALD 674
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALD 186
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
507-674 |
1.93e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.40 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY--LHRVI 582
Cdd:PRK13637 6 ENLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEP--VLFARSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQdGYSTET-GEKGA-QLSGGQKQRVAMARALV 658
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAFG----PINLGLSEEEIENRVKRAMNIV-GLDYEDyKDKSPfELSGGQKRRVAIAGVVA 160
|
170
....*....|....*.
gi 339895787 659 RNPPVLILDEATSALD 674
Cdd:PRK13637 161 MEPKILILDEPTAGLD 176
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
504-674 |
2.18e-15 |
|
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: 75.39 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHkylHRvIS 583
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR---NR-IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLF-ARSITDNISY-----GLPTvpfemvvEAAQKANAHGF----IMELQDgystetgEKGAQLSGGQKQRVAM 653
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlaqlkGLKK-------EEARRRIDEWLerleLSEYAN-------KRVEELSKGNQQKVQF 139
|
170 180
....*....|....*....|.
gi 339895787 654 ARALVRNPPVLILDEATSALD 674
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLD 160
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
507-674 |
2.18e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.75 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR-VISLV 585
Cdd:PRK10575 15 RNVSFRV---PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVLFARSITDNISYGlpTVPF------------EMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAM 653
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIG--RYPWhgalgrfgaadrEKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180
....*....|....*....|.
gi 339895787 654 ARALVRNPPVLILDEATSALD 674
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALD 179
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
507-676 |
2.49e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.21 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILEnfYPLEG-----GRVLLDGKPISAYDHKYL 578
Cdd:PRK11124 6 NGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLrvlNLLE--MPRSGtlniaGNHFDFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 579 HRVISLVSQEPVLFAR-SITDNisygLPTVPfeMVVEAAQKANAHGFIMELQDGYS-TETGEK-GAQLSGGQKQRVAMAR 655
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHlTVQQN----LIEAP--CRVLGLSKDQALARAEKLLERLRlKPYADRfPLHLSGGQQQRVAIAR 154
|
170 180
....*....|....*....|.
gi 339895787 656 ALVRNPPVLILDEATSALDAE 676
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPE 175
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
521-674 |
3.57e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEG----GRVLLDGKPISAY-DHKYLHRVISLVSQEPVLFAR 594
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 SITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
188-395 |
6.52e-15 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 76.00 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFR 267
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 268 SLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVtfmgFPIIMMVSNIYG 347
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV----LPPLLVVYYLLQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 339895787 348 KYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEEEEAEVYLRKL 395
Cdd:cd18580 157 RYYLRTSRQLRrlESESRSPlySHFSETLSGLSTIRAFGWQERFIEENLRLL 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
504-677 |
7.36e-15 |
|
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: 72.10 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVlldgkpisaydhkylhrvis 583
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 lvsqepvlfARSITDNISYglptvpFEmvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPV 663
Cdd:cd03221 58 ---------TWGSTVKIGY------FE-------------------------------QLSGGEKMRLALAKLLLENPNL 91
|
170
....*....|....
gi 339895787 664 LILDEATSALDAES 677
Cdd:cd03221 92 LLLDEPTNHLDLES 105
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
522-674 |
7.62e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFAR-SI 596
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 597 TDNISYG--LPTVPFEMVVEAAQKANAHGFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK10070 124 LDNTAFGmeLAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
232-678 |
8.33e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.41 E-value: 8.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 232 VCLLAIGSSFAagIRGGIFTL--IFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISrltsdttmvsdLVSQNINVF-- 307
Cdd:TIGR01271 128 LCLLFIVRTLL--LHPAIFGLhhLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVS-----------LLSNNLNKFde 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 308 ---LRNTVKVTGV-VVFMFSLSWQL---SLVTFMGFPIIMMV-----SNIYGKYYKRLSKEVQNALARASntaeETISAM 375
Cdd:TIGR01271 195 glaLAHFVWIAPLqVILLMGLIWELlevNGFCGLGFLILLALfqaclGQKMMPYRDKRAGKISERLAITS----EIIENI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 376 KTVRSFAnEEEEAEVYLRKLQQV-YKLNRKeaAAYMYYVWGSGL---TLLVVQVSILYYGghlvISGQMTSGNLIAFIIY 451
Cdd:TIGR01271 271 QSVKAYC-WEEAMEKIIKNIRQDeLKLTRK--IAYLRYFYSSAFffsGFFVVFLSVVPYA----LIKGIILRRIFTTISY 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 452 EFVLgdcMESVGSVYSGLMQ----GVGAAEKVFEFIDRQPTMVHDGSLAPDHLEgrvdFENVT----------------- 510
Cdd:TIGR01271 344 CIVL---RMTVTRQFPGAIQtwydSLGAITKIQDFLCKEEYKTLEYNLTTTEVE----MVNVTaswdegigelfekikqn 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 511 --------------FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgRVLLDGKpisaydh 575
Cdd:TIGR01271 417 nkarkqpngddglfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEG-KIKHSGR------- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 576 kylhrvISLVSQEPVLFARSITDNISYGLPTVPFEM--VVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQRVAM 653
Cdd:TIGR01271 489 ------ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYtsVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISL 559
|
490 500
....*....|....*....|....*
gi 339895787 654 ARALVRNPPVLILDEATSALDAESE 678
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLDVVTE 584
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
508-676 |
1.21e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 508 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEGGrVLLDGKPIS----------AYD 574
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK--PSEGS-IVVNGQTINlvrdkdgqlkVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 575 HKYLHRV---ISLVSQEPVLFAR-SITDNISYGLPTVPFEMVVEAAQKA----NAHGFIMELQDGYStetgekgAQLSGG 646
Cdd:PRK10619 84 KNQLRLLrtrLTMVFQHFNLWSHmTVLENVMEAPIQVLGLSKQEARERAvkylAKVGIDERAQGKYP-------VHLSGG 156
|
170 180 190
....*....|....*....|....*....|
gi 339895787 647 QKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPE 186
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
504-677 |
1.22e-14 |
|
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: 73.56 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVIS 583
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLfARSIT--DNIS-----YGLPTvpfemvVEAAQKanahgfIMELQDGYstETGEKGAQL----SGGQKQRVA 652
Cdd:cd03265 77 IVFQDLSV-DDELTgwENLYiharlYGVPG------AERRER------IDELLDFV--GLLEAADRLvktySGGMRRRLE 141
|
170 180
....*....|....*....|....*
gi 339895787 653 MARALVRNPPVLILDEATSALDAES 677
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQT 166
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
514-679 |
1.30e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP---LEGGRVLLDGKPIsayDHKYLHRVISLVSQepv 590
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI---DAKEMRAISAYVQQ--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 591 lfarsitDNISYGLPTVPFEMVVEAAQKANAHGFI-------------MELQDGYSTETGEKGAQ--LSGGQKQRVAMAR 655
Cdd:TIGR00955 107 -------DDLFIPTLTVREHLMFQAHLRMPRRVTKkekrervdevlqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180
....*....|....*....|....
gi 339895787 656 ALVRNPPVLILDEATSALDAESEY 679
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAY 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
522-681 |
1.33e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE--GGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SIT 597
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 598 DNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL-DAE 676
Cdd:PRK13549 101 ENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPAT--PVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtESE 178
|
....*
gi 339895787 677 SEYLI 681
Cdd:PRK13549 179 TAVLL 183
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
523-677 |
2.00e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.53 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 523 QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI----------SLVSQEPVLF 592
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpgiktELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 593 ARSITDNISYglptvpfEMVVEAAQKANAHGFiMELqdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:PRK13538 98 YQRLHGPGDD-------EALWEALAQVGLAGF-EDV----------PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
....*
gi 339895787 673 LDAES 677
Cdd:PRK13538 160 IDKQG 164
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
521-674 |
2.79e-14 |
|
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: 71.31 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEP----VLFARS 595
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895787 596 ITDNISYGlptvpfemvveaaqkanahgfimelqdgystetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:cd03215 95 VAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
504-674 |
3.36e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.60 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKylhRVIS 583
Cdd:COG4152 2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDR---RRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNISY-----GLPtvpfemvvEAAQKANAHGFI--MELQDgYSTETGEKgaqLSGGQKQRVAMAR 655
Cdd:COG4152 75 YLPEERGLYPKmKVGEQLVYlarlkGLS--------KAEAKRRADEWLerLGLGD-RANKKVEE---LSKGNQQKVQLIA 142
|
170
....*....|....*....
gi 339895787 656 ALVRNPPVLILDEATSALD 674
Cdd:COG4152 143 ALLHDPELLILDEPFSGLD 161
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
513-681 |
4.78e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 513 YRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpisaydhkylHRVISLVSQ---EP 589
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 590 VLFARSITDNISYGL---------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRN 660
Cdd:NF040873 68 DSLPLTVRDLVAMGRwarrglwrrLTRDDRAAVDDALER------VGLADLAGRQLGE----LSGGQRQRALLAQGLAQE 137
|
170 180
....*....|....*....|.
gi 339895787 661 PPVLILDEATSALDAESEYLI 681
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERI 158
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
504-676 |
4.91e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.91 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13652 4 IETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 656
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpinlgLDEETVAHRVSSALHMLG---LEELRD-------RVPHHLSGGEKKRVAIAGV 151
|
170 180
....*....|....*....|
gi 339895787 657 LVRNPPVLILDEATSALDAE 676
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQ 171
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
514-674 |
5.41e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI---SAYDHKYLHRVISLVSQEPV 590
Cdd:PRK10261 332 RVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 591 --LFAR-SITDNISYGLpTVPFEMVVEAAQKANAH-----GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPP 662
Cdd:PRK10261 412 asLDPRqTVGDSIMEPL-RVHGLLPGKAAAARVAWllervGLLPEHAWRYPHE-------FSGGQRQRICIARALALNPK 483
|
170
....*....|..
gi 339895787 663 VLILDEATSALD 674
Cdd:PRK10261 484 VIIADEAVSALD 495
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
504-681 |
6.73e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 L-----------VSQEPVLFARSitdnisYGLPT------VPfeMVVEAA---QKANAhgfimelqdgystetgeKGAQL 643
Cdd:PRK13537 85 VpqfdnldpdftVRENLLVFGRY------FGLSAaaaralVP--PLLEFAkleNKADA-----------------KVGEL 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895787 644 SGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
504-677 |
8.65e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.46 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRP--HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEGGRVLLDGKPISAYDHKYLHR 580
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 V---ISLVSQEP--VLFARSITDNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMA 654
Cdd:PRK13643 82 VrkkVGVVFQFPesQLFEETVLKDVAFGPQN--FGIPKEKAEKIAAEKLEMV---GLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180
....*....|....*....|...
gi 339895787 655 RALVRNPPVLILDEATSALDAES 677
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKA 179
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
522-674 |
9.82e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 9.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRVIS-LVSQEPVLFARSITDNI 600
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQG-EILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 601 SYGLPTVPFEMVVEA--AQKANAhgfiMELQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NPP--VLILDEATS 671
Cdd:COG4138 91 ALHQPAGASSEAVEQllAQLAEA----LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMN 162
|
...
gi 339895787 672 ALD 674
Cdd:COG4138 163 SLD 165
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
184-448 |
9.84e-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: 72.16 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 184 DVAFlvaASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFST-AVVIVCLLAIGSSFAAgIRGGIFTLIFARLNIRLR 262
Cdd:cd18783 6 DVAI---ASLILHVLAL---APPIFFQIVIDKVLVHQSYSTLYVlTIGVVIALLFEGILGY-LRRYLLLVATTRIDARLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 263 NCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNinvFLRNTVKVTGVVVF---MFSLSWQLSLVTFMGFPII 339
Cdd:cd18783 79 LRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQ---LFGTLLDATSLLVFlpvLFFYSPTLALVVLAFSALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 340 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMyyvWGSGLT 419
Cdd:cd18783 155 ALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSN---WPQTLT 231
|
250 260 270
....*....|....*....|....*....|..
gi 339895787 420 LL---VVQVSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18783 232 GPlekLMTVGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
186-395 |
1.52e-13 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 71.79 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 186 AFLVAASFFLIVAA--LGETFLPYYTGRAIDGIViQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIF---TLIFARlniR 260
Cdd:cd18605 1 LILILLSLILMQASrnLIDFWLSYWVSHSNNSFF-NFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFaygGLRAAR---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 261 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTG-VVVFMFSLSWQLSLVtfmgFPII 339
Cdd:cd18605 77 LHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGyLVVICYQLPWLLLLL----LPLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 340 MMVSNIYgKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEEEEAEVYLRKL 395
Cdd:cd18605 153 FIYYRIQ-RYYRATSRELKrlNSVNLSPlyTHFSETLKGLVTIRAFRKQERFLKEYLEKL 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
508-674 |
2.12e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 508 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAY-DHKYlHRVISLVS 586
Cdd:COG1101 8 SKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEYKR-AKYIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPVLfarsitdnisyGlpTVPfEMVVE-----AAQKANAHGFI-------------------MELQDGYSTETGekgaQ 642
Cdd:COG1101 87 QDPMM-----------G--TAP-SMTIEenlalAYRRGKRRGLRrgltkkrrelfrellatlgLGLENRLDTKVG----L 148
|
170 180 190
....*....|....*....|....*....|..
gi 339895787 643 LSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
521-674 |
2.19e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH----KYLHRVISLVSQE----PVLF 592
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaKLRAKHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 593 ARsitDNISygLPTVpfeMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:PRK10584 105 AL---ENVE--LPAL---LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
..
gi 339895787 673 LD 674
Cdd:PRK10584 177 LD 178
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
522-681 |
3.17e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.55 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP--LEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SIT 597
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 598 DNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGaQLSGGQKQRVAMARALVRNPPVLILDEATSAL-DA 675
Cdd:TIGR02633 97 ENIFLGNEiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEK 175
|
....*.
gi 339895787 676 ESEYLI 681
Cdd:TIGR02633 176 ETEILL 181
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
504-675 |
3.74e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.60 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVIS 583
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFAR-SITDNISYGLPTVPFEMVvEAAQKANAHGFImeLQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPP 662
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGLKLAGAKKE-EINQRVNQVAEV--LQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPS 153
|
170
....*....|...
gi 339895787 663 VLILDEATSALDA 675
Cdd:PRK11000 154 VFLLDEPLSNLDA 166
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
504-677 |
4.20e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLdGKPIS-AY---DHKYLH 579
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKiGYfdqHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 RvislvsqepvlfARSITDNISYGLPTvpfemvveaAQKANAHGFimeLQD-GYSTETGEKG-AQLSGGQKQRVAMARAL 657
Cdd:COG0488 392 P------------DKTVLDELRDGAPG---------GTEQEVRGY---LGRfLFSGDDAFKPvGVLSGGEKARLALAKLL 447
|
170 180
....*....|....*....|
gi 339895787 658 VRNPPVLILDEATSALDAES 677
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIET 467
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
519-677 |
7.18e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.68 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFAR 594
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 -SITDNISygLPTVpFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK10535 101 lTAAQNVE--VPAV-YAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
....
gi 339895787 674 DAES 677
Cdd:PRK10535 176 DSHS 179
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
516-674 |
7.62e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.47 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 516 RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--------GRVLLDGKPISAYDHKYLHRVISLVSQ 587
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 588 --EPVlFARSITDNISYGLptvpFEMVVEAAQKANAHGFI----MELQDGySTETGEKGAQLSGGQKQRVAMARAL---- 657
Cdd:PRK13547 91 aaQPA-FAFSAREIVLLGR----YPHARRAGALTHRDGEIawqaLALAGA-TALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180
....*....|....*....|..
gi 339895787 658 -----VRNPPVLILDEATSALD 674
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALD 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
521-670 |
9.97e-13 |
|
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: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVS----QEPV 590
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAG-----IAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 591 LFARSITDNISygLPTVP----FEMVVEAAQKANAHGFIMELQ---DGYSTETGekgaQLSGGQKQRVAMARALVRNPPV 663
Cdd:COG1129 342 VLDLSIRENIT--LASLDrlsrGGLLDRRRERALAEEYIKRLRiktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKV 415
|
....*..
gi 339895787 664 LILDEAT 670
Cdd:COG1129 416 LILDEPT 422
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
503-674 |
1.05e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 503 RVDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI 582
Cdd:PRK10253 7 RLRGEQLTLGYGKY---TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEPVLFAR-SITDNISYG-LPTVPF--------EMVVEAAQKANAhgfIMELQDgYSTETgekgaqLSGGQKQRVA 652
Cdd:PRK10253 84 GLLAQNATTPGDiTVQELVARGrYPHQPLftrwrkedEEAVTKAMQATG---ITHLAD-QSVDT------LSGGQRQRAW 153
|
170 180
....*....|....*....|..
gi 339895787 653 MARALVRNPPVLILDEATSALD 674
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLD 175
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
503-675 |
1.27e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.19 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 503 RVDFENVTFTyrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKS-SCVNILENFYP---LEGGRVLLDGKPISAYDHKyl 578
Cdd:PRK10418 4 QIELRNIALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVAPCALR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 579 HRVISLVSQEPvlfaRSITDNI----SYGLPTvpfemvVEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQ 649
Cdd:PRK10418 78 GRKIATIMQNP----RSAFNPLhtmhTHARET------CLALGKPADDATLTAALEAVGLENAARVLKLypfemSGGMLQ 147
|
170 180
....*....|....*....|....*.
gi 339895787 650 RVAMARALVRNPPVLILDEATSALDA 675
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDV 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
517-680 |
1.27e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR- 594
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 SITDNISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK10762 95 TIAENIFLGReFVNRFGRIDWKKMYAEADKLLARLNLRFSSDK--LVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
....*...
gi 339895787 674 -DAESEYL 680
Cdd:PRK10762 173 tDTETESL 180
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
504-674 |
1.31e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LvsqePVLFARSITDNisyglPTVPFEMVVEAAQKANA-HGFIMELQdgystetgekgaQLSGGQKQRVAMARALVRNPP 662
Cdd:PRK09544 82 L----PLTVNRFLRLR-----PGTKKEDILPALKRVQAgHLIDAPMQ------------KLSGGETQRVLLARALLNRPQ 140
|
170
....*....|..
gi 339895787 663 VLILDEATSALD 674
Cdd:PRK09544 141 LLVLDEPTQGVD 152
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
504-677 |
1.51e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.48 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpISAYDHKYLH--- 579
Cdd:PRK13644 2 IRLENVSYSY---PDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQgir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 RVISLVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAqkanahgfIMELQDGYSTETGEKgaQLSGGQKQRVA 652
Cdd:PRK13644 77 KLVGIVFQNPetQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRA--------LAEIGLEKYRHRSPK--TLSGGQGQCVA 146
|
170 180
....*....|....*....|....*
gi 339895787 653 MARALVRNPPVLILDEATSALDAES 677
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDS 171
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
504-668 |
1.68e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.25 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-- 581
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 -ISLVSQEPVLFAR-SITDNISY------GLPTVPFEMVVeaaqkanahgfIMELQdgystETGEKGA------QLSGGQ 647
Cdd:PRK11831 85 rMSMLFQSGALFTDmNVFDNVAYplrehtQLPAPLLHSTV-----------MMKLE-----AVGLRGAaklmpsELSGGM 148
|
170 180
....*....|....*....|.
gi 339895787 648 KQRVAMARALVRNPPVLILDE 668
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDE 169
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
185-473 |
1.86e-12 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 68.29 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 185 VAFLVAASFFLIVAalgetflPYYTGRAIDGIVIQKSMDQFSTAVVIVC--LLAIGSSFAAGIRGGIFTLIFARLNIRLR 262
Cdd:cd18582 2 LLLLVLAKLLNVAV-------PFLLKYAVDALSAPASALLAVPLLLLLAygLARILSSLFNELRDALFARVSQRAVRRLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 263 NCLFRSLVSQETSFFDENRTGDL---ISRLTSDTTMVSDLVSQNInvfLRNTVKVTGVVVFMFSL-SWQLSLVTFMGFPI 338
Cdd:cd18582 75 LRVFRHLHSLSLRFHLSRKTGALsraIERGTRGIEFLLRFLLFNI---LPTILELLLVCGILWYLyGWSYALITLVTVAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 339 IMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGL 418
Cdd:cd18582 152 YVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQAL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 419 TLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 473
Cdd:cd18582 232 IISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
501-678 |
2.55e-12 |
|
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: 70.16 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 501 EGRVDFENVTFTyrtRPHTQVL-QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYdhkylh 579
Cdd:TIGR00954 449 DNGIKFENIPLV---TPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY------ 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 rvislVSQEPVLFARSITDNISYglPTVPFEMVVEAAQKANAHGFIMELQDGY--STETGEKGAQ-----LSGGQKQRVA 652
Cdd:TIGR00954 520 -----VPQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDKDLEQILDNVQLTHilEREGGWSAVQdwmdvLSGGEKQRIA 592
|
170 180
....*....|....*....|....*.
gi 339895787 653 MARALVRNPPVLILDEATSALDAESE 678
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVE 618
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
507-681 |
2.83e-12 |
|
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: 69.47 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE-GGRVLLDGKPISAYD-HKYLHRVISL 584
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 585 VSQE-------PVLfarSITDNISYG-LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 656
Cdd:TIGR02633 341 VPEDrkrhgivPIL---GVGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKM 417
|
170 180
....*....|....*....|....*
gi 339895787 657 LVRNPPVLILDEATSALDAESEYLI 681
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEI 442
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
506-674 |
3.50e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.74 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 506 FENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA----YDHKYLH 579
Cdd:PRK13634 5 FQKVEHRYqyKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 RVISLVSQ--EPVLFARSITDNISYGlPT---VPFEmvvEAAQKANAhgfIMELQdGYSTETGEKGA-QLSGGQKQRVAM 653
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFG-PMnfgVSEE---DAKQKARE---MIELV-GLPEELLARSPfELSGGQMRRVAI 156
|
170 180
....*....|....*....|.
gi 339895787 654 ARALVRNPPVLILDEATSALD 674
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
508-678 |
4.00e-12 |
|
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: 67.19 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 508 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV-NILENFYPLEGgRVLLDGKpisaydhkylhrvISLVS 586
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELEPSEG-KIKHSGR-------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPVLFARSITDNISYGLP--TVPFEMVVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 664
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSydEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170
....*....|....
gi 339895787 665 ILDEATSALDAESE 678
Cdd:cd03291 182 LLDSPFGYLDVFTE 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
260-674 |
6.24e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.17 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVvFMFSLSWQLSLVTFMGFPII 339
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAI-FVVSVLQPYIFIAAIPVAVI 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 340 MMVSNIYgkyYKRLSKEVQNALARA-SNTAEETISAMK---TVRSFANEEeeaevYLRKLqqVYK-LNRKEAAAYMYYVW 414
Cdd:TIGR01271 1038 FIMLRAY---FLRTSQQLKQLESEArSPIFSHLITSLKglwTIRAFGRQS-----YFETL--FHKaLNLHTANWFLYLST 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 415 GSGLTLLVVQVSILYYGGHLVIS---GQMTSGNL-IAFIIYEFVLGDCMESVGSVYS--GLMQGVgaaEKVFEFIDRQP- 487
Cdd:TIGR01271 1108 LRWFQMRIDIIFVFFFIAVTFIAigtNQDGEGEVgIILTLAMNILSTLQWAVNSSIDvdGLMRSV---SRVFKFIDLPQe 1184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 488 ---------------TMVHDGSLAPDHL--EGRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 550
Cdd:TIGR01271 1185 eprpsggggkyqlstVLVIENPHAQKCWpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 551 ILENFYPLEgGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQKANAHGFI 625
Cdd:TIGR01271 1264 ALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD------PYEQwsdeeIWKVAEEVGLKSVI 1336
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 339895787 626 MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:TIGR01271 1337 EQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-674 |
6.27e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.40 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG-----GRVLLDGKPISAYDHKYLH--RVISLVSQEPVLF 592
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEvrREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 593 AR-SITDNISYGL-------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 664
Cdd:PRK14267 98 PHlTIYDNVAIGVklnglvkSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170
....*....|
gi 339895787 665 ILDEATSALD 674
Cdd:PRK14267 172 LMDEPTANID 181
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
514-681 |
6.45e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.57 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 514 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY---PLEGGRVLLDGKPIS-----AYDHKYLHRVISLV 585
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIRKSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 586 SQEPVLFAR-SITDNISYG-LPTVPFEMVV----EAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVR 659
Cdd:PRK09984 92 FQQFNLVNRlSVLENVLIGaLGSTPFWRTCfswfTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180
....*....|....*....|..
gi 339895787 660 NPPVLILDEATSALDAESEYLI 681
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIV 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
499-681 |
6.95e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 499 HLEGRVDFE--NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPleG---GRVLLDGKPIS-- 571
Cdd:PRK13549 253 HTIGEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKir 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 572 ----AYDHKylhrvISLVSQE-------PVLfarSITDNISYG-LPTVPFEMVV-EAAQKANAHGFIMELQdgYSTETGE 638
Cdd:PRK13549 331 npqqAIAQG-----IAMVPEDrkrdgivPVM---GVGKNITLAaLDRFTGGSRIdDAAELKTILESIQRLK--VKTASPE 400
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 339895787 639 -KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK13549 401 lAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEI 444
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
504-677 |
1.25e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.21 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYR-TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS----CVNILENFYPLEGgRVLLDGKPISAYDHKYl 578
Cdd:cd03233 4 LSWRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVEG-DIHYNGIPYKEFAEKY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 579 HRVISLVSQEPVLFarsitdnisyglPTVPFEMVVEAAQKANAHGFImelqdgystetgeKGaqLSGGQKQRVAMARALV 658
Cdd:cd03233 82 PGEIIYVSEEDVHF------------PTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALV 134
|
170
....*....|....*....
gi 339895787 659 RNPPVLILDEATSALDAES 677
Cdd:cd03233 135 SRASVLCWDNSTRGLDSST 153
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
511-674 |
2.26e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 511 FTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHK---YLHRVISLVSQ 587
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRgllALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 588 EP--VLFARSITDNISYGLPT--VPFEMVV----EAAQKANAHGFIME-LQdgystetgekgaQLSGGQKQRVAMARALV 658
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRNlgVPEAEITrrvdEALTLVDAQHFRHQpIQ------------CLSHGQKKRVAIAGALV 152
|
170
....*....|....*.
gi 339895787 659 RNPPVLILDEATSALD 674
Cdd:PRK13638 153 LQARYLLLDEPTAGLD 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
504-681 |
3.28e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.36 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL---ENFYPLEG---------------GRVLL 565
Cdd:TIGR03269 1 IEVKNLTKKFDGK---EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmDQYEPTSGriiyhvalcekcgyvERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 566 DGKPISAYDHKYLHRVISLVSQEPVLFARsITDNIS---------YGLPTVpFEMVVEAAQKAnahgfimelqdGYSTET 636
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFWNLSDKLRRR-IRKRIAimlqrtfalYGDDTV-LDNVLEALEEI-----------GYEGKE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339895787 637 GEKGA------------------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:TIGR03269 145 AVGRAvdliemvqlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLV 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
505-674 |
3.82e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 505 DFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILEN---FYPleGGRVLLDGKPISAYDHK 576
Cdd:PRK15134 7 AIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYP--SGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 577 YLHRV----ISLVSQEPVlfarsITDNISYGLPTVPFE-------MVVEAAQkanahGFIMELQDgystETGEKGA---- 641
Cdd:PRK15134 85 TLRGVrgnkIAMIFQEPM-----VSLNPLHTLEKQLYEvlslhrgMRREAAR-----GEILNCLD----RVGIRQAakrl 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895787 642 -----QLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK15134 151 tdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
507-681 |
4.55e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTrPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLhrvISLVS 586
Cdd:PRK15056 10 NDVTVTWRN-GHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QE-------PVLfarsITDNISYG---------LPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQR 650
Cdd:PRK15056 85 QSeevdwsfPVL----VEDVVMMGryghmgwlrRAKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKR 150
|
170 180 190
....*....|....*....|....*....|.
gi 339895787 651 VAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
517-680 |
8.30e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY-LHRVISLVSQE-PVLFAR 594
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 SITDNISYG-LPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK10982 89 SVMDNMWLGrYPTKGM-FVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
....*...
gi 339895787 674 -DAESEYL 680
Cdd:PRK10982 166 tEKEVNHL 173
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
524-674 |
1.12e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.70 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA--------------YDHKYLHRVISLVsqEP 589
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpghqiarmgvvrtFQHVRLFREMTVI--EN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 590 VLFA--RSITDNISYGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTETGekgaQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:PRK11300 101 LLVAqhQQLKTGLFSGLLKTPAFRRAESEALDRAATWLerVGLLEHANRQAG----NLAYGQQRRLEIARCMVTQPEILM 176
|
....*....
gi 339895787 666 LDEATSALD 674
Cdd:PRK11300 177 LDEPAAGLN 185
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
534-674 |
1.22e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 534 VTALVGPSGSGKSSCVNILENF-YPLEG-----GRVLLD-GKPISAYDHKylhRVISLVSQEPVLFAR-SITDNISYGLp 605
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLtRPQKGrivlnGRVLFDaEKGICLPPEK---RRIGYVFQDARLFPHyKVRGNLRYGM- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339895787 606 tvpfemvveaAQKANAHgF--------IMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK11144 102 ----------AKSMVAQ-FdkivallgIEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
524-674 |
3.01e-10 |
|
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: 63.28 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGR--VLLDGKPISAYDHKYLHR-----VISLVSQEPVLFA-RS 595
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRgrakrYIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 596 ITDNI--SYGLpTVPFEM-VVEAAQKANAHGFimelQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLILDEATS 671
Cdd:TIGR03269 382 VLDNLteAIGL-ELPDELaRMKAVITLKMVGF----DEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
...
gi 339895787 672 ALD 674
Cdd:TIGR03269 457 TMD 459
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
508-674 |
3.99e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.64 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 508 NVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRV---LLDGKPISAYDH------- 575
Cdd:PRK13651 7 NIVKIFnkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 576 --------------KYLHRVISLVSQ--EPVLFARSITDNISYGlptvPFEMVV---EAAQKANAHGFIMELQDGYStet 636
Cdd:PRK13651 87 lviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVskeEAKKRAAKYIELVGLDESYL--- 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 339895787 637 gEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK13651 160 -QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
503-668 |
4.39e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 503 RVDFENVTFTYrtrphtqvlQNVSFSLSP-------GKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 575
Cdd:PRK10522 322 TLELRNVTFAY---------QDNGFSVGPinltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 576 KYLHRVISLVSQEPVLFARSITDNisyglptvPFEMVVEAAQKANAH---GFIMELQDGYSTETgekgaQLSGGQKQRVA 652
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFDQLLGPE--------GKPANPALVEKWLERlkmAHKLELEDGRISNL-----KLSKGQKKRLA 459
|
170
....*....|....*.
gi 339895787 653 MARALVRNPPVLILDE 668
Cdd:PRK10522 460 LLLALAEERDILLLDE 475
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
502-674 |
5.01e-10 |
|
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: 61.02 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 502 GRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEgGRVLLDGKPISAYDHKYLHRV 581
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 ISLVSQEPVLFARSITDNIS-YGLPTVpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRN 660
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170
....*....|....
gi 339895787 661 PPVLILDEATSALD 674
Cdd:cd03289 157 AKILLLDEPSAHLD 170
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
525-674 |
5.19e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 61.65 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 525 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPV--LFAR-SITD 598
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLasLNPRmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 599 NISYGL----PTVPFEMVVEAAQKANAH-GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PRK15079 120 IIAEPLrtyhPKLSRQEVKDRVKAMMLKvGLLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
.
gi 339895787 674 D 674
Cdd:PRK15079 193 D 193
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
188-449 |
7.42e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 60.64 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMDqFSTAVVIVCLLAIGSSFAAG-IRGGIFTLIFARLNIRLRNCLF 266
Cdd:cd18779 7 ILLASLLLQLLGLA---LPLLTGVLVDRVIPRGDRD-LLGVLGLGLAALVLTQLLAGlLRSHLLLRLRTRLDTQLTLGFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 267 RSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLrNTVKVTGVVVFMFSLSWQLSLVTfMGFPII----MMV 342
Cdd:cd18779 83 EHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALL-DGTLVLGYLALLFAQSPLLGLVV-LGLAALqvalLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 343 SNiygKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKL--QQVYKLNRKEAAAYMyyvwGSGLTL 420
Cdd:cd18779 161 TR---RRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFvdQLNASLRRGRLDALV----DALLAT 233
|
250 260 270
....*....|....*....|....*....|.
gi 339895787 421 L--VVQVSILYYGGHLVISGQMTSGNLIAFI 449
Cdd:cd18779 234 LrlAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
531-681 |
1.01e-09 |
|
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: 57.38 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 531 PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL-LDGKPISAYDHKYLHRVIslvsqepvlfarsitdnisyglptvpf 609
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339895787 610 emvveaaqkanahgfimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALL 99
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
521-679 |
1.25e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 521 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--GRVLLDGKPISaydhKYLHRVISLVSQEPVLFAR-SIT 597
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 598 DNISY-GLPTVPFEMVVEAAQKAnAHGFIMEL--QDGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSAL 673
Cdd:PLN03211 159 ETLVFcSLLRLPKSLTKQEKILV-AESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
....*.
gi 339895787 674 DAESEY 679
Cdd:PLN03211 238 DATAAY 243
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
520-677 |
1.35e-09 |
|
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: 58.31 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 520 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPI---SAYDhkylhRV---ISLVSQEPVL 591
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDItdlPPEE-----RArlgIFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 592 FarsitdnisyglPTVPFEMvveaaqkanahgFIMELQDGystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATS 671
Cdd:cd03217 89 I------------PGVKNAD------------FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
....*.
gi 339895787 672 ALDAES 677
Cdd:cd03217 134 GLDIDA 139
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
525-674 |
1.78e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 525 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRVIS-LVSQEPVLF--------ARS 595
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAGQPLEAWSAAELARHRAyLSQQQTPPFampvfqylTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 596 ITDNISYGLPTVPFEMVVEAAQkanahgfimeLQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NP--PVLILDE 668
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDE 159
|
....*.
gi 339895787 669 ATSALD 674
Cdd:PRK03695 160 PMNSLD 165
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
522-680 |
2.21e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfypleGGRVLLD-GKPISAYDhkylhRVISLVSQEPvlfARSITDN- 599
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQD-----LIVARLQQDP---PRNVEGTv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 600 --------------------ISYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GEKGAQLSGG 646
Cdd:PRK11147 84 ydfvaegieeqaeylkryhdISHLVETDPSEKNLNELAKLQE---QLDHHNLWQLENrinevlaqlgldpDAALSSLSGG 160
|
170 180 190
....*....|....*....|....*....|....*
gi 339895787 647 QKQRVAMARALVRNPPVLILDEATSALDAES-EYL 680
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
524-674 |
2.73e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEP----VLFARSITD 598
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 599 NISY-GLPTVPFEMVV--EAAQKANAHGFImelqDGYSTETGEKGAQ---LSGGQKQRVAMARALVRNPPVLILDEATSA 672
Cdd:PRK10762 350 NMSLtALRYFSRAGGSlkHADEQQAVSDFI----RLFNIKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
..
gi 339895787 673 LD 674
Cdd:PRK10762 426 VD 427
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
504-673 |
3.87e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR-VI 582
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMReAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SLVSQEPVLFAR-SITDNISYGlptvpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 661
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMG------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170
....*....|..
gi 339895787 662 PVLILDEATSAL 673
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
518-676 |
5.40e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLEGGRVLLDGKpisaydhkylhrvislVSQEpvlfaR 594
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTllrLLAGALKGTPVAGCVDVPDNQ----------------FGRE-----A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 SITDNIsygLPTVPFEMVVEAaqkANAHGfimeLQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:COG2401 101 SLIDAI---GRKGDFKDAVEL---LNAVG----LSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
..
gi 339895787 675 AE 676
Cdd:COG2401 169 RQ 170
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
507-674 |
5.96e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKpisaydHKYLHRVISLVS 586
Cdd:PRK11701 10 RGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------DGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 QEPVLFARS----ITDNISYGLptvpfEMVVEA---------AQKANAHGFI----------MELQdgySTETGEKGAQL 643
Cdd:PRK11701 81 AERRRLLRTewgfVHQHPRDGL-----RMQVSAggnigerlmAVGARHYGDIratagdwlerVEID---AARIDDLPTTF 152
|
170 180 190
....*....|....*....|....*....|.
gi 339895787 644 SGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
507-678 |
7.88e-09 |
|
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: 56.57 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRT----------------RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK 568
Cdd:cd03267 4 SNLSKSYRVyskepgligslkslfkRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 569 PISAYDHKYLHRVISLVSQE-------PVLFARSITDNIsYGLPTVPFemvveaaqKANAHGF--IMELQDGYSTETgek 639
Cdd:cd03267 84 VPWKRRKKFLRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-YDLPPARF--------KKRLDELseLLDLEELLDTPV--- 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 339895787 640 gAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 678
Cdd:cd03267 152 -RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
517-677 |
1.47e-08 |
|
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: 57.64 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFypleggrvllDGKPISAYDHKylhrvISLVSQEPVL- 591
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdKDF----------NGEARPQPGIK-----VGYLPQEPQLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 592 FARSITDNI-------------------SYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GE- 638
Cdd:TIGR03719 81 PTKTVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAAEQAELQE---IIDAADAWDLDSqleiamdalrcppWDa 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 339895787 639 KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 677
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
504-674 |
2.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.86 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTQ---VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY-LH 579
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 RVISLVSQEP--VLFARSITDNISYG---LPTVPFEM---VVEAAQKANAHGFimelqdgystetgEKGAQ--LSGGQKQ 649
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpenLGIPPEEIrerVDESLKKVGMYEY-------------RRHAPhlLSGGQKQ 151
|
170 180
....*....|....*....|....*
gi 339895787 650 RVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
464-678 |
2.80e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 464 SVYSGLMQGVGAAEKVF-----EFIDRQPTMVHdgslAPDHLEGRVDFE--NVTFTYRTRphtqvLQNVSFSLSPGKVTA 536
Cdd:PRK09700 223 SVCSGMVSDVSNDDIVRlmvgrELQNRFNAMKE----NVSNLAHETVFEvrNVTSRDRKK-----VRDISFSVCRGEILG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 537 LVGPSGSGKSSCVNILENFYPLEGGRVLLDGK---PISAYDHkyLHRVISLVSQ---EPVLFAR-SITDN--ISYGLPTV 607
Cdd:PRK09700 294 FAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDA--VKKGMAYITEsrrDNGFFPNfSIAQNmaISRSLKDG 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895787 608 PFEMVV------EAAQKANAHGFIMELQdgySTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD--AESE 678
Cdd:PRK09700 372 GYKGAMglfhevDEQRTAENQRELLALK---CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAE 447
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
508-674 |
2.99e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 508 NVTFtYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK----------PISAYDHKY 577
Cdd:PRK10261 19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 578 LHRV----ISLVSQEPVL-----------FARSItdNISYGLPTvpfEMVVEAAQKANAHGFIMELQdgysTETGEKGAQ 642
Cdd:PRK10261 98 MRHVrgadMAMIFQEPMTslnpvftvgeqIAESI--RLHQGASR---EEAMVEAKRMLDQVRIPEAQ----TILSRYPHQ 168
|
170 180 190
....*....|....*....|....*....|..
gi 339895787 643 LSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
522-680 |
3.26e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlEG---GRVLLDGKP-----ISAYDhkylHRVISLVSQE----P 589
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEVcrfkdIRDSE----ALGIVIIHQElaliP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 590 VLfarSITDNISYGLPTVPF------EMVVEAAQKANAHGfimeLQDGYSTETGEKGAqlsgGQKQRVAMARALVRNPPV 663
Cdd:NF040905 92 YL---SIAENIFLGNERAKRgvidwnETNRRARELLAKVG----LDESPDTLVTDIGV----GKQQLVEIAKALSKDVKL 160
|
170
....*....|....*...
gi 339895787 664 LILDEATSAL-DAESEYL 680
Cdd:NF040905 161 LILDEPTAALnEEDSAAL 178
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
517-677 |
3.37e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 517 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFyplEGGRVLLDGKPISaydhkYLhrvislvSQEPVL- 591
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdKEF---EGEARPAPGIKVG-----YL-------PQEPQLd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 592 FARSITDNISYGLPTVpfemvVEAAQKANAHGFIMELQDGYSTETGEKGAQ----------------------------- 642
Cdd:PRK11819 83 PEKTVRENVEEGVAEV-----KAALDRFNEIYAAYAEPDADFDALAAEQGElqeiidaadawdldsqleiamdalrcppw 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 339895787 643 ------LSGGQKQRVAMARALVRNPPVLILDEATSALDAES 677
Cdd:PRK11819 158 dakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
191-473 |
4.59e-08 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 54.92 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 191 ASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFS--TAVVIVCLLAIGSSFAAGIRggifTLIFARLN----IRLRNC 264
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESavTLILLYALLRFSSKLLKELR----SLLYRRVQqnayRELSLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 265 LFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSqninVFLRNTVK-----VTGVVVFMFSLSWQLSLVTFMGFpII 339
Cdd:cd18560 77 TFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLS----YLVFYLVPtllelIVVSVVFAFHFGAWLALIVFLSV-LL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 340 MMVSNIYG-KYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGL 418
Cdd:cd18560 152 YGVFTIKVtEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 419 TLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 473
Cdd:cd18560 232 IIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
182-447 |
5.54e-08 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 54.92 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 182 KPDVAFLVAASFFLIVAALGetfLPYYTGRAIDGIVIQKSMdqfSTAVVIvCLLAIGSSFAAGI----RGGIFTLIFARL 257
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALA---PPIFMLQVYDRVLPSGSL---STLLGL-TLGMVVLLAFDGLlrqvRSRILQRVGLRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 258 NIRLRNCLFRSLVSQETsffdENRTGDLISRLTSDTTMVSDLVSQN--INVFLRNTVKVTGVVVFMFSlSWqLSLVTFMG 335
Cdd:cd18586 74 DVELGRRVFRAVLELPL----ESRPSGYWQQLLRDLDTLRNFLTGPslFAFFDLPWAPLFLAVIFLIH-PP-LGWVALVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 336 FPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKL-NRKEAAAYMYYVW 414
Cdd:cd18586 148 APVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELqIRASDLAGAISAI 227
|
250 260 270
....*....|....*....|....*....|...
gi 339895787 415 GSGLTlLVVQVSILYYGGHLVISGQMTSGNLIA 447
Cdd:cd18586 228 GKTLR-MALQSLILGVGAYLVIDGELTIGALIA 259
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
508-674 |
7.68e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.73 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 508 NVTFTYRTRPHTQVlQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG---GRVLLDGKPISAYDHKYLHRV--- 581
Cdd:PRK09473 19 RVTFSTPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNKLrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 582 -ISLVSQEPVlfaRSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQRVAMAR 655
Cdd:PRK09473 98 qISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphefSGGMRQRVMIAM 174
|
170
....*....|....*....
gi 339895787 656 ALVRNPPVLILDEATSALD 674
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALD 193
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
505-675 |
1.05e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.14 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 505 DFENVTFTYRTrPH--TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGK---PISAYD- 574
Cdd:COG4170 5 DIRNLTIEIDT-PQgrVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIdllKLSPREr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 575 HKYLHRVISLVSQEPVLF---ARSITDNISYGLPTVPFE---MVVEAAQKANA-----------HGFIMelqDGYSTEtg 637
Cdd:COG4170 84 RKIIGREIAMIFQEPSSCldpSAKIGDQLIEAIPSWTFKgkwWQRFKWRKKRAiellhrvgikdHKDIM---NSYPHE-- 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 339895787 638 ekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDA 675
Cdd:COG4170 159 -----LTEGECQKVMIAMAIANQPRLLIADEPTNAMES 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
516-677 |
1.08e-07 |
|
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: 55.40 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 516 RPHTQVLqNVSFSLSpgKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVSQEPVLFARS 595
Cdd:TIGR01257 943 RPAVDRL-NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 596 itdnisyglpTVPFEMVVEAAQKANAH---GFIME--LQD-GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 669
Cdd:TIGR01257 1019 ----------TVAEHILFYAQLKGRSWeeaQLEMEamLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
....*...
gi 339895787 670 TSALDAES 677
Cdd:TIGR01257 1089 TSGVDPYS 1096
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
225-381 |
2.44e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 52.99 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 225 FSTAVVIVCLLAIGSSFAAGIRGgiftlifARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 304
Cdd:cd18602 59 LSLGAVILSLVTNLAGELAGLRA-------AR---RLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 305 NVFLRNTVKV-TGVVVFMFSLSWQLslvtFMGFPIImMVSNIYGKYYKRLSKEVQ--NALARA---SNTAeETISAMKTV 378
Cdd:cd18602 129 ERLLRFLLLClSAIIVNAIVTPYFL----IALIPII-IVYYFLQKFYRASSRELQrlDNITKSpvfSHFS-ETLGGLTTI 202
|
...
gi 339895787 379 RSF 381
Cdd:cd18602 203 RAF 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
524-674 |
3.15e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK-YLHRVISLVS---QEPVLFARS-ITD 598
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYLPedrQSSGLYLDApLAW 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339895787 599 NI-SYGLPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK15439 361 NVcALTHNRRGF-WIKPARENAVLERYRRAL--NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
495-674 |
3.25e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 495 LAPDhlEGRVDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlEG--------GRVLLD 566
Cdd:PRK10938 254 LPAN--EPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-QGysndltlfGRRRGS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 567 GKPIsaYDHKylhRVISLVSQEPVLFAR---SITDNI------SYGLptvpFEMVVEAAQKanahgFIMELQD--GYSTE 635
Cdd:PRK10938 328 GETI--WDIK---KHIGYVSSSLHLDYRvstSVRNVIlsgffdSIGI----YQAVSDRQQK-----LAQQWLDilGIDKR 393
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 339895787 636 TGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK10938 394 TADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
518-681 |
4.82e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 518 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILE---NFYPLEGGRVLLDGKPISAydhkYLHRVISLVSQEPVLFAR 594
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLDS----SFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 595 S-ITDNISYG----LP-TVPFE---MVVEAAQKanahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLI 665
Cdd:TIGR00956 851 StVRESLRFSaylrQPkSVSKSekmEYVEEVIK------LLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLL 924
|
170
....*....|....*..
gi 339895787 666 -LDEATSALDAESEYLI 681
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSI 941
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
504-681 |
7.16e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK-PISAYDHkylHRVI 582
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQ---HHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 SL-VSQEPVLFarsitdnISYGLPTVPfemvveaAQKANAH----GFI--MELQDGYStetgekgaqLSGGQKQRVAMAR 655
Cdd:PLN03073 584 GLdLSSNPLLY-------MMRCFPGVP-------EQKLRAHlgsfGVTgnLALQPMYT---------LSGGQKSRVAFAK 640
|
170 180
....*....|....*....|....*..
gi 339895787 656 ALVRNPPVLILDEATSALDAES-EYLI 681
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAvEALI 667
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
504-675 |
7.94e-07 |
|
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: 50.61 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRT-------------------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL 564
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 565 LDGKPISaydhkylhrVISL-VSQEPVLFARsitDNIS-----YGLPTvpfemvVEAAQKANahgFIMELqdgysTETGE 638
Cdd:cd03220 81 VRGRVSS---------LLGLgGGFNPELTGR---ENIYlngrlLGLSR------KEIDEKID---EIIEF-----SELGD 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 339895787 639 KGAQ----LSGGQKQRVAMARALVRNPPVLILDEATSALDA 675
Cdd:cd03220 135 FIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
519-674 |
8.42e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 519 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVL---- 591
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEipgv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 592 ----FARSI--TDNISYGLPTV-PFEMVVEAAQKANahgfIMELQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPPVL 664
Cdd:CHL00131 100 snadFLRLAynSKRKFQGLPELdPLEFLEIINEKLK----LVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELA 173
|
170
....*....|
gi 339895787 665 ILDEATSALD 674
Cdd:CHL00131 174 ILDETDSGLD 183
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
522-673 |
1.32e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 50.31 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNilENFYPLEGGRVLLDGKPISAYD----HKYLHRVIsLVSQEPV------- 590
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNHDriegLEHIDKVI-VIDQSPIgrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 591 -------------LF------AR--SITDNISYGLPTVP--FEMVVEAAQK-----ANAHGFIMELQD---GYSTeTGEK 639
Cdd:cd03271 88 patytgvfdeireLFcevckgKRynRETLEVRYKGKSIAdvLDMTVEEALEffeniPKIARKLQTLCDvglGYIK-LGQP 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 339895787 640 GAQLSGGQKQRVAMARALVR---NPPVLILDEATSAL 673
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGL 203
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
528-676 |
1.71e-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: 49.71 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 528 SLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKYLHRVISLVSQEpvlFARSITDnisyGLPTV 607
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGTVRD---LLSSITK----DFYTH 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895787 608 PFeMVVEAAQKanahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:cd03237 93 PY-FKTEIAKP-------LQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
522-674 |
1.75e-06 |
|
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: 48.86 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNilENFYplEGGRVLLDGKPiSAYDHKYLHRVISLvsqepvlfaRSITDNis 601
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLISFL-PKFSRNKLIFIDQL---------QFLIDV-- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 602 yGLptvpfemvveaaqkanahgfimelqdGYSTeTGEKGAQLSGGQKQRVAMARALVRNPP--VLILDEATSALD 674
Cdd:cd03238 75 -GL--------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
504-674 |
1.93e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPHTQVlQNVSFSLSPGKVTALVGPSGSGKS-SCVNILENF-YPlegGRVL-----LDGKPISAYDHK 576
Cdd:PRK11022 6 VDKLSVHFGDESAPFRAV-DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIdYP---GRVMaekleFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 577 YLHRVI----SLVSQEPVlfarsITDNISYglpTVPFEM-----VVEAAQKANAHGFIMEL--QDGYSTETGEKGA---Q 642
Cdd:PRK11022 82 ERRNLVgaevAMIFQDPM-----TSLNPCY---TVGFQImeaikVHQGGNKKTRRQRAIDLlnQVGIPDPASRLDVyphQ 153
|
170 180 190
....*....|....*....|....*....|..
gi 339895787 643 LSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
526-674 |
2.45e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 526 SFSL------SPGKVTALVGPSGSGKSSCVNILE-----NFyplegGRVllDGKP-----ISAYD----HKYLHRVIS-- 583
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKILSgelkpNL-----GDY--DEEPswdevLKRFRgtelQDYFKKLANge 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 -LVSQEP--VlfarsitDNIsyglPTVPFEMVVEAAQKANAHGFIMELQDGYSTET--GEKGAQLSGGQKQRVAMARALV 658
Cdd:COG1245 160 iKVAHKPqyV-------DLI----PKVFKGTVRELLEKVDERGKLDELAEKLGLENilDRDISELSGGELQRVAIAAALL 228
|
170
....*....|....*.
gi 339895787 659 RNPPVLILDEATSALD 674
Cdd:COG1245 229 RDADFYFFDEPSSYLD 244
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
526-674 |
2.71e-06 |
|
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: 49.29 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 526 SFSL------SPGKVTALVGPSGSGKSSCVNILENFYPLEGGRvlLDGKP-----ISAYD----HKYLHRVIS------- 583
Cdd:cd03236 14 SFKLhrlpvpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRgselQNYFTKLLEgdvkviv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 ---LVSQEPVLFARSITDNISYGLPTVPFEMVVEAaqkanahgfiMELQDGYSTETgekgAQLSGGQKQRVAMARALVRN 660
Cdd:cd03236 92 kpqYVDLIPKAVKGKVGELLKKKDERGKLDELVDQ----------LELRHVLDRNI----DQLSGGELQRVAIAAALARD 157
|
170
....*....|....
gi 339895787 661 PPVLILDEATSALD 674
Cdd:cd03236 158 ADFYFFDEPSSYLD 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
513-678 |
3.15e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 513 YRTRPHTQVL------------QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLH 579
Cdd:PRK11288 248 YRPRPLGEVRlrldglkgpglrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 580 RVISLV----SQEPVLFARSITDN--ISYGLPTVPFEMVVEAAQKA-NAHGFIMELQdgYSTETGE-KGAQLSGGQKQRV 651
Cdd:PRK11288 328 AGIMLCpedrKAEGIIPVHSVADNinISARRHHLRAGCLINNRWEAeNADRFIRSLN--IKTPSREqLIMNLSGGNQQKA 405
|
170 180
....*....|....*....|....*....
gi 339895787 652 AMARALVRNPPVLILDEATSALD--AESE 678
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDvgAKHE 434
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
504-677 |
3.62e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 583
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 584 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYstetgekgaqLSGGQKQRVAMARALVRNPPV 663
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKL 148
|
170
....*....|....
gi 339895787 664 LILDEATSALDAES 677
Cdd:PRK13540 149 WLLDEPLVALDELS 162
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
522-681 |
3.75e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQE----------PV 590
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyaylDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 591 LFARSITDNISYglpTVPFEMVVEAAQKANAHGFI--MELQD-GYSTETGekgaQLSGGQKQRVAMARALVRNPPVLILD 667
Cdd:PRK10982 344 GFNSLISNIRNY---KNKVGLLDNSRMKSDTQWVIdsMRVKTpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170
....*....|....
gi 339895787 668 EATSALDAESEYLI 681
Cdd:PRK10982 417 EPTRGIDVGAKFEI 430
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
516-677 |
3.95e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.32 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 516 RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN-FYPlEGGRVLLDGKPISAYDHKYLHRvISLV----SQ- 587
Cdd:COG4586 30 REYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGYVPFKRRKEFARR-IGVVfgqrSQl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 588 ---EPVL--FA--RSItdnisYGLPTVPF----EMVVEaaqkanahgfIMELQDGYSTETgekgAQLSGGQKQRVAMARA 656
Cdd:COG4586 108 wwdLPAIdsFRllKAI-----YRIPDAEYkkrlDELVE----------LLDLGELLDTPV----RQLSLGQRMRCELAAA 168
|
170 180
....*....|....*....|.
gi 339895787 657 LVRNPPVLILDEATSALDAES 677
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVS 189
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
234-422 |
4.53e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 49.01 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 234 LLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 313
Cdd:cd18606 43 GLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 314 VTGVVVfmfslswqLSLVTF----MGFPIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEe 385
Cdd:cd18606 123 IIGTFI--------LIIIYLpwfaIALPPLLVLYYFIANYYRASSRELKrlESILRSFvyANFSESLSGLSTIRAYGAQ- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 339895787 386 eeaEVYLRKLQqvYKLNRKEAAAYMYYV---W--------GSGLTLLV 422
Cdd:cd18606 194 ---DRFIKKNE--KLIDNMNRAYFLTIAnqrWlairldllGSLLVLIV 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
504-676 |
4.71e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.54 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRT-------------------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL 564
Cdd:COG1134 5 IEVENVSKSYRLyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 565 LDGkpisaydhkylhRVISLVSqepvL---FARSIT--DNIS-----YGLPTVP----FEMVVEAAqkanahgfimELQD 630
Cdd:COG1134 85 VNG------------RVSALLE----LgagFHPELTgrENIYlngrlLGLSRKEidekFDEIVEFA----------ELGD 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 339895787 631 -------GYSTetgekgaqlsgGQKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:COG1134 139 fidqpvkTYSS-----------GMRARLAFAVATAVDPDILLVDEVLAVGDAA 180
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
260-479 |
5.55e-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: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 260 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 339
Cdd:cd18561 70 HLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 340 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAymyYVWGSGLT 419
Cdd:cd18561 150 PLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAV---SLLSSGIM 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895787 420 LLVVQVSI---LYYGGHLVISGQMTSGNLIAFIiyeFVLGDC---MESVGSVYSGLMQGVGAAEKV 479
Cdd:cd18561 227 GLATALGTalaLGVGALRVLGGQLTLSSLLLIL---FLSREFfrpLRDLGAYWHAGYQGISAADSI 289
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
529-674 |
7.12e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 529 LSPGKVTALVGPSGSGKSSCVNILE-----NFyplegGRVllDGKP-----ISAYDHKYLHRVISLVSQEPVLFARSI-- 596
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgelipNL-----GDY--EEEPswdevLKRFRGTELQNYFKKLYNGEIKVVHKPqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 597 TDNIsyglPTVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PRK13409 169 VDLI----PKVFKGKVRELLKKVDERGKLDEVVErlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
182-448 |
1.79e-05 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 47.09 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 182 KPDVAFLVAASFFLIVAALgetFLPYYTGRAIDGIVIQKSMDQFStavvivcLLAIGSSFAAGIRGgIFTLIFARLNIRL 261
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGL---VIPVFSRIFIDDILVGGLPDWLR-------PLLLGMALTALLQG-LLTWLQQYYLLRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 262 RNCLfrSLVSQET----------SFFDENRTGDLISRLTSDTTmVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLV 331
Cdd:cd18569 70 ETKL--ALSSSSRffwhvlrlpvEFFSQRYAGDIASRVQSNDR-VANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 332 TFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEeaevYLRKL--QQVYKLNRKEAAAY 409
Cdd:cd18569 147 GIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESD----FFSRWagYQAKVLNAQQELGR 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 339895787 410 MYYVWGSGLTLL--VVQVSILYYGGHLVISGQMTSGNLIAF 448
Cdd:cd18569 223 TNQLLGALPTLLsaLTNAAILGLGGLLVMDGALTIGMLVAF 263
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
229-413 |
2.58e-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: 46.69 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 229 VVIVCLLAIGSSFAAGIRGGIFTL--------IFARLnirlrnclFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLV 300
Cdd:cd18604 46 LGIYALISLLSVLLGTLRYLLFFFgslrasrkLHERL--------LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 301 SQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMK 376
Cdd:cd18604 118 ADSLSSLLESTLSLLVILIAIVVVSPAFLLPAV----VLAALYVYIGRLYLRASRELKrlESVARSPilSHFGETLAGLV 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 339895787 377 TVRSFANEeeeaEVYLRKLQQvyKLNRKEAAAYMYYV 413
Cdd:cd18604 194 TIRAFGAE----ERFIEEMLR--RIDRYSRAFRYLWN 224
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
318-450 |
4.11e-05 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 45.89 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 318 VVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFAneeeeAE-VYLRKLQ 396
Cdd:cd18587 132 LAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALG-----AEgRMQRRWE 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 339895787 397 Q-VYKLNRKEAAAYMYYVWGSGLTLLVVQ---VSILYYGGHLVISGQMTSGNLIAFII 450
Cdd:cd18587 207 EaVAALARSSLKSRLLSSSATNFAQFVQQlvtVAIVIVGVYLISDGELTMGGLIACVI 264
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
505-676 |
4.85e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 505 DFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNI-LENFYPlEGGRVLLDGKPISAY-DHkylHRVI 582
Cdd:PRK11147 321 EMENVNYQI---DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHCGTKLEVAYfDQ---HRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 slvsQEPvlfARSITDNISYGLPTVpfeMVveAAQKANAHGFimeLQD----GYSTETGEKGaqLSGGQKQRVAMARALV 658
Cdd:PRK11147 394 ----LDP---EKTVMDNLAEGKQEV---MV--NGRPRHVLGY---LQDflfhPKRAMTPVKA--LSGGERNRLLLARLFL 456
|
170
....*....|....*...
gi 339895787 659 RNPPVLILDEATSALDAE 676
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVE 474
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
517-681 |
6.02e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 517 PHTQVLQNVSFSLSPGKVTALVGPSGSG----------KSSCVNIlenfypleGGRVLLDGKPIS------AYDHKylhr 580
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGrtelamsvfgRSYGRNI--------SGTVFKDGKEVDvstvsdAIDAG---- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 581 vISLVSQepvlfarsitDNISYGL---PTVPFEMVVEAAQKANAHGFI---MELQ--DGY-------STETGEKGAQLSG 645
Cdd:NF040905 339 -LAYVTE----------DRKGYGLnliDDIKRNITLANLGKVSRRGVIdenEEIKvaEEYrkkmnikTPSVFQKVGNLSG 407
|
170 180 190
....*....|....*....|....*....|....*.
gi 339895787 646 GQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEI 443
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
504-676 |
1.09e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 45.31 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 504 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL-DGKPISAYDHkylhrvi 582
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQ------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 583 slvSQEPVLFARSITDNISYGLPTVpfeMV--VEAAQKANAHGFIMELQDgysteTGEKGAQLSGGQKQRVAMARALVRN 660
Cdd:TIGR03719 393 ---SRDALDPNKTVWEEISGGLDII---KLgkREIPSRAYVGRFNFKGSD-----QQKKVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....*.
gi 339895787 661 PPVLILDEATSALDAE 676
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVE 477
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
526-676 |
1.42e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 526 SFSLS-------PGKVTALVGPSGSGKSSCVNILE-NFYPLEGGrvlLDGKPISAYDHKYlhrvISLVSQEPV-LFARSI 596
Cdd:PRK13409 352 DFSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAgVLKPDEGE---VDPELKISYKPQY----IKPDYDGTVeDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 597 TDNISyglpTVPFEmvVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:PRK13409 425 TDDLG----SSYYK--SEIIKPLQ----LERLLDKNVKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
193-450 |
1.55e-04 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 44.36 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 193 FFLIVAALGETFLPYYTGRAID-GIViQKSMDqFSTAVVIVCL-LAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLV 270
Cdd:cd18571 9 LGLLLGSLLQLIFPFLTQSIVDkGIN-NKDLN-FIYLILIAQLvLFLGSTSIEFIRSWILLHISSRINISIISDFLIKLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 271 SQETSFFDENRTGDLISR----------LTSDT--TMVSDLvsqNINVFlrntvkvtGVVVFMFSlsWQLSLVTFMGFPI 338
Cdd:cd18571 87 RLPISFFDTKMTGDILQRindhsriesfLTSSSlsILFSLL---NLIVF--------SIVLAYYN--LTIFLIFLIGSVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 339 IMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGL 418
Cdd:cd18571 154 YILWILLFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALF 233
|
250 260 270
....*....|....*....|....*....|....
gi 339895787 419 TLLVVQVSILYYGGHLVISGQMTSGNLIA--FII 450
Cdd:cd18571 234 INQLKNILITFLAAKLVIDGEITLGMMLAiqYII 267
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
524-674 |
1.56e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 524 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV------ISL-----VSQEPVLF 592
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVgymsqaFSLygeltVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 593 ARSitdnisYGLP--TVPfEMVVEAAQKanahgFimELQDgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 670
Cdd:NF033858 364 ARL------FHLPaaEIA-ARVAEMLER-----F--DLAD----VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 339895787 671 SALD 674
Cdd:NF033858 426 SGVD 429
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
245-385 |
3.12e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 43.46 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 245 IRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSL 324
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339895787 325 S-WqlslvTFMGFPIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEE 385
Cdd:cd18601 158 NpW-----VLIPVIPLVILFLFLRRYYLKTSREVKriEGTTRSPvfSHLSSTLQGLWTIRAYSAQE 218
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
187-473 |
7.74e-04 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 41.86 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 187 FLVAASFFLIVAALGETFLPYYTGRAIDGIV--IQKSMDQFST-AVVIVCLLAIG--SSFAAGIrggIFTLIFARLNIRL 261
Cdd:cd18556 3 LFFSILFISLLSSILISISPVILAKITDLLTssSSDSYNYIVVlAALYVITISATklLGFLSLY---LQSSLRVELIISI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 262 RNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 341
Cdd:cd18556 80 SSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFLLYAVLFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 342 VSNIY----------------GKYYKRLSKEVQNALARASNTAEETIsaMKTVRSFANEEEEAevylrklQQVY-KLNRK 404
Cdd:cd18556 160 INNTIftkkivslrndlmdagRKSYSLLTDSVKNIVAAKQNNAFDFL--FKRYEATLTNDRNS-------QKRYwKLTFK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339895787 405 EAAAymyyvwgSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 473
Cdd:cd18556 231 MLIL-------NSLLNVILFGLSFFYSLYGVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
522-590 |
8.12e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 8.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339895787 522 LQNVSFSLSPGKVTALVGPSGSGKSSCVN-----ILENFypLEGGRVLLD-GKPISAYDHkyLHRVISlVSQEPV 590
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypALANR--LNGAKTVPGrYTSIEGLEH--LDKVIH-IDQSPI 693
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
226-412 |
8.36e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 42.16 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 226 STAVVIVCLLAIgssfaagiRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNIN 305
Cdd:cd18599 66 GSILVILLLSLI--------RGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 306 VFLRNTVKVTGVVVF-MFSLSWQLslvtfMGFPIIMMVSNIYGKYYKRLSKEvqnaLARASNTAE--------ETISAMK 376
Cdd:cd18599 138 NFLQNVLLVVFSLIIiAIVFPWFL-----IALIPLAIIFVFLSKIFRRAIRE----LKRLENISRsplfshltATIQGLS 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 339895787 377 TVRSFANEEEeaevYLRKLQQVykLNRKEAAAYMYY 412
Cdd:cd18599 209 TIHAFNKEKE----FLSKFKKL--LDQNSSAFFLFN 238
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
642-674 |
1.78e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 1.78e-03
10 20 30
....*....|....*....|....*....|...
gi 339895787 642 QLSGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
643-676 |
1.80e-03 |
|
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: 39.86 E-value: 1.80e-03
10 20 30
....*....|....*....|....*....|....
gi 339895787 643 LSGGQKQRVAMARALVRNPPVLILDEATSALDAE 676
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
500-681 |
2.02e-03 |
|
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: 41.31 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 500 LEGRVDFENVTF-----TYRTRPHTQVLQNV-------------SFSLS-------PGKVTALVGPSGSGKSSCVNILEN 554
Cdd:COG1245 309 LDGYLPEENVRIrdepiEFEVHAPRREKEEEtlveypdltksygGFSLEveggeirEGEVLGIVGPNGIGKTTFAKILAG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 555 FYPLEGGRVLLDGKpISaYDHKYlhrvISLVSQEPV--LFARSITDNIsyglPTVPFEmvVEAAQKANahgfIMELQDGY 632
Cdd:COG1245 389 VLKPDEGEVDEDLK-IS-YKPQY----ISPDYDGTVeeFLRSANTDDF----GSSYYK--TEIIKPLG----LEKLLDKN 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 339895787 633 STEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 681
Cdd:COG1245 453 VKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
507-674 |
2.40e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 507 ENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKylHRvislvs 586
Cdd:NF033858 5 EGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DAR--HR------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 587 qepvlfaRSITDNISY---GL-----PTVPfemVVEAAQ---------KANAHGFIMELQDGysteTG-----EKGA-QL 643
Cdd:NF033858 72 -------RAVCPRIAYmpqGLgknlyPTLS---VFENLDffgrlfgqdAAERRRRIDELLRA----TGlapfaDRPAgKL 137
|
170 180 190
....*....|....*....|....*....|.
gi 339895787 644 SGGQKQRVAMARALVRNPPVLILDEATSALD 674
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
642-677 |
4.50e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 4.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 339895787 642 QLSGGQKQ------RVAMARALVRNPPVLILDEATSALDAES 677
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 ... |
188-449 |
5.48e-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: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 188 LVAASFFLIVAALGEtflPYYTGRAIDGIVIQKSmdqfstavvIVCLLAIGSSF-AAGIRGGIFTLIFA-RLNIRLRNCL 265
Cdd:cd18562 4 LALANVALAGVQFAE---PVLFGRVVDALSSGGD---------AFPLLALWAALgLFSILAGVLVALLAdRLAHRRRLAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 266 ----FRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMM 341
Cdd:cd18562 72 masyFEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339895787 342 VSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVyklnrkEAAAYMYYVWGSGLTLL 421
Cdd:cd18562 152 LNRLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRL------LAAQYPVLNWWALASVL 225
|
250 260 270
....*....|....*....|....*....|....
gi 339895787 422 ------VVQVSILYYGGHLVISGQMTSGNLIAFI 449
Cdd:cd18562 226 traastLTMVAIFALGAWLVQRGELTVGEIVSFV 259
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
518-552 |
8.59e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 8.59e-03
10 20 30
....*....|....*....|....*....|....*
gi 339895787 518 HTQVLQNVsfsLSPGKVTALVGPSGSGKSSCVNIL 552
Cdd:PRK01889 184 GLDVLAAW---LSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| |
