|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-590 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 703.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 13 KAYDARLMKRLIHYLSPYKMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFH 92
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 93 FYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDA 172
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 173 KLALITLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTI 252
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 253 LYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLLDKV 332
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 333 DEIPDKPDAIAPAYVRGEIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDG 412
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 413 INIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQ 492
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 493 KQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQL 572
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*...
gi 931518516 573 LRKHGIYYKLYQLQYRDQ 590
Cdd:COG1132 562 LARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-586 |
1.92e-178 |
|
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: 522.09 E-value: 1.92e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 21 KRLIHYLSPYKMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTG 100
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 101 QKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTtDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLT 180
Cdd:COG2274 225 QRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 181 IMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYP 260
Cdd:COG2274 304 LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLST 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 261 AVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLLDKVDEIPDKPD 340
Cdd:COG2274 384 LSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRS 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 341 AIAPAYVRGEIEFKNVWFAY-KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT 419
Cdd:COG2274 464 KLSLPRLKGDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 420 KESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFA 499
Cdd:COG2274 544 PASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIA 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 500 RVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIY 579
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
....*..
gi 931518516 580 YKLYQLQ 586
Cdd:COG2274 704 AELVQQQ 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
18-587 |
1.28e-145 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 433.36 E-value: 1.28e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 18 RLMKRLIHYLSPYKMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMY 97
Cdd:TIGR02204 4 RPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 98 MTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALI 177
Cdd:TIGR02204 84 WLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 178 TLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSI 257
Cdd:TIGR02204 164 VLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 258 FYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLLDKVDEI-- 335
Cdd:TIGR02204 244 LTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIka 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 336 PDKPDAIaPAYVRGEIEFKNVWFAY--KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGI 413
Cdd:TIGR02204 324 PAHPKTL-PVPLRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 414 NIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQK 493
Cdd:TIGR02204 403 DLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 494 QLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLL 573
Cdd:TIGR02204 483 QRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELI 562
|
570
....*....|....
gi 931518516 574 RKHGIYYKLYQLQY 587
Cdd:TIGR02204 563 AKGGLYARLARLQF 576
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
21-589 |
1.27e-129 |
|
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: 392.16 E-value: 1.27e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 21 KRLIHYLSPYKMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTG 100
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 101 QKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLT 180
Cdd:TIGR02203 83 NKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 181 IMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYP 260
Cdd:TIGR02203 163 MLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 261 AVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLLDKvdeiPDKPD 340
Cdd:TIGR02203 243 ITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDS----PPEKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 341 A--IAPAYVRGEIEFKNVWFAYKDEEW-VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEH 417
Cdd:TIGR02203 319 TgtRAIERARGDVEFRNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 418 ITKESLRKHIGVVLQDVFLFSGSVRDNIALTN-SKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLI 496
Cdd:TIGR02203 399 YTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 497 SFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKH 576
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558
|
570
....*....|...
gi 931518516 577 GIYYKLYQLQYRD 589
Cdd:TIGR02203 559 GLYAQLHNMQFRE 571
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
34-325 |
5.48e-127 |
|
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: 375.19 E-value: 5.48e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMP--GDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQI 111
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPgqGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 112 FKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFI 191
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 192 FKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAIT 271
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 931518516 272 LIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-577 |
4.20e-122 |
|
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: 372.17 E-value: 4.20e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 21 KRLIHYLSPYKMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPG-DFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMT 99
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGaPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 100 GQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDAL--------NEMFTSGVVTIlgdillllglATMMFVF- 170
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALdgyfarylPQLFLAALVPL----------LILVAVFp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 171 -DAKLALITLTIMPL--LFITAF--IFKIKAREGFRSIRILIAkinSFLqENITGMKIVQLFNREDKNYRQFERINADHL 245
Cdd:COG4988 156 lDWLSGLILLVTAPLipLFMILVgkGAAKASRRQWRALARLSG---HFL-DRLRGLTTLKLFGRAKAEAERIAEASEDFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 246 KAYLRT--ILYFSIFypAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSE 323
Cdd:COG4988 232 KRTMKVlrVAFLSSA--VLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 324 RIFKLLDKVDEIPDKPDAIAPAYVRGEIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQV 403
Cdd:COG4988 310 KIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 404 QKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLE 483
Cdd:COG4988 390 YSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 484 RGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRI 563
Cdd:COG4988 470 GGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRI 549
|
570
....*....|....
gi 931518516 564 REEGTHQQLLRKHG 577
Cdd:COG4988 550 VEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
349-577 |
5.67e-119 |
|
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: 351.91 E-value: 5.67e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 349 GEIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIG 428
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 VVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRI 508
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 509 LVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHG 577
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-587 |
5.28e-112 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 347.01 E-value: 5.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 21 KRLIHYLSPYKMQVIYAALLLVC-----TSIFTLARPLLTQ--YAIDNYV---MPgdfdgLTIIAglFIVIAGL-NFIFQ 89
Cdd:PRK11176 14 RRLWPTIAPFKAGLIVAGVALILnaasdTFMLSLLKPLLDDgfGKADRSVlkwMP-----LVVIG--LMILRGItSFISS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 90 YFhfyLMYMTGQKVMyDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFV 169
Cdd:PRK11176 87 YC---ISWVSGKVVM-TMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 170 FDAKLALITLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYL 249
Cdd:PRK11176 163 YSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 250 RTILYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQL-VGF-IMAAQMfyRPIEDLSEKYNILQSAMASSERIFK 327
Cdd:PRK11176 243 KMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTItVVFsSMIALM--RPLKSLTNVNAQFQRGMAACQTLFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 328 LLDKVDEIPDKPDAIAPAyvRGEIEFKNVWFAYKD-EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKG 406
Cdd:PRK11176 321 ILDLEQEKDEGKRVIERA--KGDIEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 407 EILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIAL-TNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERG 485
Cdd:PRK11176 399 EILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 486 SNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIRE 565
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
570 580
....*....|....*....|..
gi 931518516 566 EGTHQQLLRKHGIYYKLYQLQY 587
Cdd:PRK11176 559 RGTHAELLAQNGVYAQLHKMQF 580
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
351-583 |
7.78e-112 |
|
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: 333.81 E-value: 7.78e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAY-KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGV 429
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRIL 509
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 510 VLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLY 583
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-586 |
4.58e-111 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 344.78 E-value: 4.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 20 MKRLIHYLSPYKMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDgLTIIAGL---FIVIAGLNFIFQYFHFYLM 96
Cdd:PRK10790 11 LKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLP-LGLVAGLaaaYVGLQLLAAGLHYAQSLLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 97 YMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLAL 176
Cdd:PRK10790 90 NRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 177 ITLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTI-LYF 255
Cdd:PRK10790 170 VAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLrLDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 256 SIFYPAVEVLSA-VAITLIIWFGGLDILTNNLtwGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLLDKVDE 334
Cdd:PRK10790 250 FLLRPLLSLFSAlILCGLLMLFGFSASGTIEV--GVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 335 ipDKPDAIAPaYVRGEIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGIN 414
Cdd:PRK10790 328 --QYGNDDRP-LQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 415 IEHITKESLRKHIGVVLQDVFLFSGSVRDNIALtNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQ 494
Cdd:PRK10790 405 LSSLSHSVLRQGVAMVQQDPVVLADTFLANVTL-GRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 495 LISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLR 574
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA 563
|
570
....*....|..
gi 931518516 575 KHGIYYKLYQLQ 586
Cdd:PRK10790 564 AQGRYWQMYQLQ 575
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
33-586 |
1.29e-110 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 346.73 E-value: 1.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 33 QVIYAALLLvctSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIF 112
Cdd:TIGR01846 143 EVLLISLAL---QLFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLY 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 113 KHLQRLSLSFFDKTPIGRLVTRLTtDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIF 192
Cdd:TIGR01846 220 RHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 193 KIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITL 272
Cdd:TIGR01846 299 GPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAI 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 273 IIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLLDKVDEiPDKPDAIAPAYVRGEIE 352
Cdd:TIGR01846 379 LLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTE-PRSAGLAALPELRGAIT 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 353 FKNVWFAYK-DEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVL 431
Cdd:TIGR01846 458 FENIRFRYApDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 432 QDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVL 511
Cdd:TIGR01846 538 QENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIF 617
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 512 DEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLYQLQ 586
Cdd:TIGR01846 618 DEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-591 |
3.69e-110 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 342.96 E-value: 3.69e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 16 DARLMKRLIHYLSPYKMQVIYAALLLVCTSI-FTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGL----NFIFQY 90
Cdd:COG5265 17 DLLLRLLLLLLLPPYLRRRRRALAALLLLLLaAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAYGLlrllSVLFGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 91 FHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFF--DKT-PIGRLVTRLTTDVDAL-NEMFTSGVVTILGDILLLlglATM 166
Cdd:COG5265 97 LRDALFARVTQRAVRRLALEVFRHLHALSLRFHleRQTgGLSRDIERGTKGIEFLlRFLLFNILPTLLEIALVA---GIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 167 MFVFDAKLALITLtIMPLLFItAFIFKI-KAREGFRsiriliAKINSflQENITGMKI---------VQLFNREDKNYRQ 236
Cdd:COG5265 174 LVKYDWWFALITL-VTVVLYI-AFTVVVtEWRTKFR------REMNE--ADSEANTRAvdsllnyetVKYFGNEAREARR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 237 FERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVgFIMAAQM-FYRPIEDLSEKYNIL 315
Cdd:COG5265 244 YDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFV-LVNAYLIqLYIPLNFLGFVYREI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 316 QSAMASSERIFKLLDKVDEIPDKPDAIAPAYVRGEIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVIS 395
Cdd:COG5265 323 RQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 396 LLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDR 475
Cdd:COG5265 403 LLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 476 DYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERI 555
Cdd:COG5265 483 GYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEI 562
|
570 580 590
....*....|....*....|....*....|....*.
gi 931518516 556 IVMHKGRIREEGTHQQLLRKHGIYYKLYQLQYRDQE 591
Cdd:COG5265 563 LVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEE 598
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
33-325 |
2.46e-109 |
|
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: 329.81 E-value: 2.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 33 QVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIF 112
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 113 KHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIF 192
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 193 KIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITL 272
Cdd:cd18545 161 RRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTAL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 931518516 273 IIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-582 |
3.38e-108 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 340.93 E-value: 3.38e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 17 ARLMKRLIHYLSPYKMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLM 96
Cdd:TIGR00958 146 ADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 97 YMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLAL 176
Cdd:TIGR00958 226 NYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTM 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 177 ITLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFS 256
Cdd:TIGR00958 306 VTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 257 IFYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLLDKVDEIP 336
Cdd:TIGR00958 386 GYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 337 dKPDAIAPAYVRGEIEFKNVWFAY--KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGIN 414
Cdd:TIGR00958 466 -LTGTLAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 415 IEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQ 494
Cdd:TIGR00958 545 LVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQ 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 495 LISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRlmHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLR 574
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
....*...
gi 931518516 575 KHGIYYKL 582
Cdd:TIGR00958 703 DQGCYKHL 710
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-585 |
3.87e-100 |
|
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: 315.55 E-value: 3.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 18 RLMKRLIHYLSPYKMQVIYAALLLVCT-----SIFTLARPLLTQYAidnyVMPGDFDgltiiagLFIVIAGLNF------ 86
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTllagiGLLALSGWLIAAAA----LAPPILN-------LFVPIVGVRAfaigrt 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 87 IFQYF-----H---FylmymtgqKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMF-------TSGVV 151
Cdd:COG4987 70 VFRYLerlvsHdatL--------RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYlrvllplLVALL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 152 TILGDillllglATMMFVFDAKLALITLTIM-PLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNRE 230
Cdd:COG4987 142 VILAA-------VAFLAFFSPALALVLALGLlLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGAL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 231 DKNYRQFERINADHLKAYLR--TILYFSIFypAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDL 308
Cdd:COG4987 215 DRALARLDAAEARLAAAQRRlaRLSALAQA--LLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 309 SEKYNILQSAMASSERIFKLLDKVDEIPDkPDAIAPAYVRGEIEFKNVWFAY-KDEEWVLKDISFKVKEGEKVAVVGATG 387
Cdd:COG4987 293 PAAAQHLGRVRAAARRLNELLDAPPAVTE-PAEPAPAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 388 AGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAH 467
Cdd:COG4987 372 SGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 468 QFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLS 547
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
570 580 590
....*....|....*....|....*....|....*...
gi 931518516 548 TIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLYQL 585
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
351-586 |
9.46e-100 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 303.00 E-value: 9.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVV 430
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILV 510
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 511 LDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLYQLQ 586
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
351-586 |
1.71e-99 |
|
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: 302.54 E-value: 1.71e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAY--KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIG 428
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 VVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRI 508
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 509 LVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLYQLQ 586
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-592 |
4.95e-94 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 300.34 E-value: 4.95e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 18 RLMKRLIHYLSPYKMQVIYAALLLVCTSIFTLARPLLTQYAIDnyVMPGDFDGLTIIA-----GLFIVIAGlnfIFQYFH 92
Cdd:PRK13657 5 RLYARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIID--AISGKGDIFPLLAawagfGLFNIIAG---VLVARH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 93 F-YLMYMTGQKVMydirSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFD 171
Cdd:PRK13657 80 AdRLAHRRRLAVL----TEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 172 AKLALItLTIMPLLF--ITAFIFKiKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYL 249
Cdd:PRK13657 156 WRLSLV-LVVLGIVYtlITTLVMR-KTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 250 RTILYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLL 329
Cdd:PRK13657 234 PVLSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 330 DKVDEIPDKPDAIAPAYVRGEIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEIL 409
Cdd:PRK13657 314 DAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 410 IDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFS 489
Cdd:PRK13657 394 IDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 490 TGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTH 569
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSF 553
|
570 580
....*....|....*....|...
gi 931518516 570 QQLLRKHGIYYKLYQLQYRDQET 592
Cdd:PRK13657 554 DELVARGGRFAALLRAQGMLQED 576
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
34-582 |
4.42e-87 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 285.30 E-value: 4.42e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVctsIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:TIGR03796 159 LLLAGLLLV---LPGLVIPAFSQIFVDEILVQGRQDWLRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLW 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTTDvDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTiMPLLFITAFIFK 193
Cdd:TIGR03796 236 HILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIA-FAAINVLALQLV 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKARE-GFRSIRILIAKINSFlqeNITGMKIVQLFNR---EDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVA 269
Cdd:TIGR03796 314 SRRRVdANRRLQQDAGKLTGV---AISGLQSIETLKAsglESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLN 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 270 ITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERifklLDKV----------DEIPDKP 339
Cdd:TIGR03796 391 SALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNR----LDDVlrnpvdplleEPEGSAA 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 340 DAIAPAYVRGEIEFKNVWFAY-KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHI 418
Cdd:TIGR03796 467 TSEPPRRLSGYVELRNITFGYsPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 419 TKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISF 498
Cdd:TIGR03796 547 PREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEI 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 499 ARVLVYNPRILVLDEATSNIDTETEILIQKALNRlmhkR--TSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKH 576
Cdd:TIGR03796 627 ARALVRNPSILILDEATSALDPETEKIIDDNLRR----RgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
....*.
gi 931518516 577 GIYYKL 582
Cdd:TIGR03796 703 GAYARL 708
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
37-325 |
5.76e-87 |
|
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: 272.06 E-value: 5.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQ 116
Cdd:cd18546 4 ALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIKA 196
Cdd:cd18546 84 RLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 197 REGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWF 276
Cdd:cd18546 164 SRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 931518516 277 GGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18546 244 GAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
34-325 |
3.71e-86 |
|
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: 270.19 E-value: 3.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFK 193
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLI 273
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 274 IWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
351-586 |
1.99e-85 |
|
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: 266.27 E-value: 1.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYK-DEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGV 429
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRIL 509
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 510 VLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLYQLQ 586
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
349-568 |
6.48e-85 |
|
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: 263.97 E-value: 6.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 349 GEIEFKNVWFAYKDEE-WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHI 427
Cdd:cd03244 1 GDIEFKNVSLRYRPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSGSVRDNIALTNSKiTDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPR 507
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEY-SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGT 568
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
34-583 |
7.05e-80 |
|
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: 266.22 E-value: 7.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIftlARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:TIGR01193 161 IVIAAIIVTLISI---AGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTtDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFK 193
Cdd:TIGR01193 238 HLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLI 273
Cdd:TIGR01193 317 RTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 274 IWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLLDKVDEIPDKPDAIAPAYVRGEIEF 353
Cdd:TIGR01193 397 LWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVI 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 354 KNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQD 433
Cdd:TIGR01193 477 NDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQE 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 434 VFLFSGSVRDNIAL-TNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLD 512
Cdd:TIGR01193 557 PYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 513 EATSNIDTETEILIQKALNRLMHKrTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLY 583
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
351-562 |
9.87e-80 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 248.84 E-value: 9.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEE-WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGV 429
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSGSVRDNIaltnskitdaeliraakdvhahqfiekldrdydeevlergsnFSTGQKQLISFARVLVYNPRIL 509
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518516 510 VLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGR 562
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
30-558 |
2.70e-77 |
|
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: 254.52 E-value: 2.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 30 YKMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPG-DFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIR 108
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGePLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 109 SQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFIt 188
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPI- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 189 aFIFKI------KAREGFRSIriliAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRT--ILYFSIFyp 260
Cdd:TIGR02857 160 -FMILIgwaaqaAARKQWAAL----SRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVlrIAFLSSA-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 261 AVEVLSAVAITLIIWFGGLDILTNNLTWGQ-LVGFIMAAQmFYRPIEDLSEKYNILQSAMASSERIFKLLDKvDEIPDKP 339
Cdd:TIGR02857 233 VLELFATLSVALVAVYIGFRLLAGDLDLATgLFVLLLAPE-FYLPLRQLGAQYHARADGVAAAEALFAVLDA-APRPLAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 340 DAIAPAYVRGEIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT 419
Cdd:TIGR02857 311 KAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 420 KESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFA 499
Cdd:TIGR02857 391 ADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 500 RVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVM 558
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
42-586 |
5.74e-75 |
|
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: 252.57 E-value: 5.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 42 VCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFH-FYLMYMTGQkVMYDIRSQIFKHLQRLSL 120
Cdd:TIGR03797 146 LLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQsLAVLRLETR-MDASLQAAVWDRLLRLPV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 121 SFFDKTPIGRLVTRlTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTImplLFITAFIFKIKAREGF 200
Cdd:TIGR03797 225 SFFRQYSTGDLASR-AMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVAL---ALVAIAVTLVLGLLQV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 201 RSIRILIA---KINSFLQENITGM-KI------VQLFNREDKNYRQFERI--NADHLKAYLRTILyfsifypavEVLSAV 268
Cdd:TIGR03797 301 RKERRLLElsgKISGLTVQLINGIsKLrvagaeNRAFARWAKLFSRQRKLelSAQRIENLLTVFN---------AVLPVL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 269 AITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSekyNILQSAMASS---ERIFKLLDKVDEIP-DKPDaiaP 344
Cdd:TIGR03797 372 TSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLS---NTLISILAVIplwERAKPILEALPEVDeAKTD---P 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 345 AYVRGEIEFKNVWFAY-KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL 423
Cdd:TIGR03797 446 GKLSGAIEVDRVTFRYrPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 424 RKHIGVVLQDVFLFSGSVRDNIALTNSkITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLV 503
Cdd:TIGR03797 526 RRQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 504 YNPRILVLDEATSNIDTETEILIQKALNRLmhKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLY 583
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLA 682
|
...
gi 931518516 584 QLQ 586
Cdd:TIGR03797 683 RRQ 685
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
39-586 |
1.23e-73 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 246.16 E-value: 1.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 39 LLLVCTSIFTLARPLLTQYAIDNyVMPGDFDGLTIIA--GLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQ 116
Cdd:PRK10789 2 ALLIIIAMLQLIPPKVVGIIVDG-VTEQHMTTGQILMwiGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFV-FDAKLALITLTIMPLLFITAFIFKIK 195
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRYGDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 196 AREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIW 275
Cdd:PRK10789 161 LHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 276 FGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIFKLLDKVDEIPDKPDAIAPAyvRGEIEFKN 355
Cdd:PRK10789 241 GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEG--RGELDVNI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 356 VWFAY-KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDV 434
Cdd:PRK10789 319 RQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 435 FLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEA 514
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 515 TSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLYQLQ 586
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
349-563 |
1.37e-73 |
|
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: 234.79 E-value: 1.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 349 GEIEFKNVWFAYKDEEW-VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHI 427
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPR 507
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRI 563
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
34-325 |
2.00e-71 |
|
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: 231.55 E-value: 2.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFK 193
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLI 273
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 274 IWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
37-325 |
1.95e-70 |
|
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: 229.21 E-value: 1.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVMPG------DFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQ 110
Cdd:cd18547 4 VIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 111 IFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAF 190
Cdd:cd18547 84 LFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 191 IFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAI 270
Cdd:cd18547 164 FIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 271 TLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18547 244 VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
34-325 |
7.60e-68 |
|
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: 222.30 E-value: 7.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFK 193
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLI 273
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 274 IWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
37-325 |
3.23e-67 |
|
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: 221.23 E-value: 3.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVM---------------PGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQ 101
Cdd:cd18564 4 ALLALLLETALRLLEPWPLKVVIDDVLGdkplpgllglapllgPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 102 KVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTI 181
Cdd:cd18564 84 RVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 182 MPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPA 261
Cdd:cd18564 164 APLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 262 VEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18564 244 VDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
31-325 |
7.57e-67 |
|
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: 219.66 E-value: 7.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 31 KMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQ 110
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 111 IFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAF 190
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 191 IFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAI 270
Cdd:cd18540 161 YFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIAT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 271 TLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18540 241 ALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
342-563 |
1.01e-66 |
|
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: 216.95 E-value: 1.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 342 IAPAYVRGEIEFKNVWFAY--KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT 419
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 420 KESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFA 499
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 500 RVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRI 563
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
102-584 |
3.13e-65 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 223.55 E-value: 3.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 102 KVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEM-------FTSGVVtilgdillllGLATMMF---VFD 171
Cdd:PRK11160 90 RVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLylrlispLVAALV----------VILVLTIglsFFD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 172 AKLALITLTIM-PLLFITAFIF----KIKAREGFRSIRILIAKINSFLQenitGMKIVQLFNREDKnYRQfeRINA--DH 244
Cdd:PRK11160 160 LTLALTLGGILlLLLLLLPLLFyrlgKKPGQDLTHLRAQYRVQLTEWLQ----GQAELTLFGAEDR-YRQ--QLEQteQQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 245 LKAYLRTILYFSIFYPAVEVL-SAVAITLIIWFGGlDILTNNLTWGQLVGFI----MAAQMFYRPIedlSEKYNILQSAM 319
Cdd:PRK11160 233 WLAAQRRQANLTGLSQALMILaNGLTVVLMLWLAA-GGVGGNAQPGALIALFvfaaLAAFEALMPV---AGAFQHLGQVI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 320 ASSERIFKLLDKVDEIpDKPDAIAPAYVRGEIEFKNVWFAYKDEEW-VLKDISFKVKEGEKVAVVGATGAGKTTVISLLT 398
Cdd:PRK11160 309 ASARRINEITEQKPEV-TFPTTSTAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 399 RFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEkldrdyD 478
Cdd:PRK11160 388 RAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLE------D 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 479 EEVL-----ERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVE 553
Cdd:PRK11160 462 DKGLnawlgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541
|
490 500 510
....*....|....*....|....*....|.
gi 931518516 554 RIIVMHKGRIREEGTHQQLLRKHGIYYKLYQ 584
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
37-325 |
3.69e-62 |
|
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: 207.39 E-value: 3.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLAR---PLLTQYAIDN-YVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIF 112
Cdd:cd18778 1 LILTLLCALLSTLLGlvpPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 113 KHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIF 192
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 193 KIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITL 272
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 931518516 273 IIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-325 |
7.02e-62 |
|
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: 206.59 E-value: 7.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMP----GDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRS 109
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQlgpgGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 110 QIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITA 189
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 190 FIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVA 269
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 270 ITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
117-582 |
1.21e-61 |
|
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: 221.74 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSgVVTILGDILLLLGLATMMFVFDAKLAliTLTIMPLLFITAFI---FK 193
Cdd:TIGR00957 1050 RSPMSFFERTPSGNLVNRFSKELDTVDSMIPP-VIKMFMGSLFNVIGALIVILLATPIA--AVIIPPLGLLYFFVqrfYV 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREdknyRQFERINADHLKAYLRTilyfsiFYPAVEVLSAVAITL- 272
Cdd:TIGR00957 1127 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQ----ERFIHQSDLKVDENQKA------YYPSIVANRWLAVRLe 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 273 -----IIWFGGL--DILTNNLTWGqLVGFIMAAQM---FYrpIEDLSEKYNILQSAMASSERIFKLLDKVDEIPDKPDAI 342
Cdd:TIGR00957 1197 cvgncIVLFAALfaVISRHSLSAG-LVGLSVSYSLqvtFY--LNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQET 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 343 APAYV---RGEIEFKNVWFAYK-DEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHI 418
Cdd:TIGR00957 1274 APPSGwppRGRVEFRNYCLRYReDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI 1353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 419 TKESLRKHIGVVLQDVFLFSGSVRDNIAlTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISF 498
Cdd:TIGR00957 1354 GLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCL 1432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 499 ARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGI 578
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGI 1512
|
....
gi 931518516 579 YYKL 582
Cdd:TIGR00957 1513 FYSM 1516
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
35-325 |
3.01e-59 |
|
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: 199.56 E-value: 3.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 35 IYAALLLVCTSIFTLARPLLTQYAIDNYVMPG-DFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFK 193
Cdd:cd18541 82 HLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLI 273
Cdd:cd18541 162 KKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 274 IWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18541 242 LWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
349-568 |
2.25e-58 |
|
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: 194.17 E-value: 2.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 349 GEIEFKNVWFAYK-DEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHI 427
Cdd:cd03369 5 GEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSGSVRDNIALTNsKITDAELIRAAKdvhahqfiekldrdydeeVLERGSNFSTGQKQLISFARVLVYNPR 507
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGT 568
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
37-325 |
2.83e-56 |
|
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: 191.54 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQ 116
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIKA 196
Cdd:cd18576 81 RLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 197 REGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWF 276
Cdd:cd18576 161 RKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 931518516 277 GGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18576 241 GGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
304-575 |
4.43e-55 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 196.12 E-value: 4.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 304 PIEDLSEKYNILQSAMASSERIFKLLDKVDEIPDKPDAIAPayvRGEIEFKNVWFAYK-DEEWVLKDISFKVKEGEKVAV 382
Cdd:COG4618 287 PIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPLPRP---KGRLSVENLTVVPPgSKRPILRGVSFSLEPGEVLGV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 383 VGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIA-LTNskITDAELIRAA 461
Cdd:COG4618 364 IGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIArFGD--ADPEKVVAAA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 462 KDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRL-MHKRTSV 540
Cdd:COG4618 442 KLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVV 521
|
250 260 270
....*....|....*....|....*....|....*
gi 931518516 541 IIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRK 575
Cdd:COG4618 522 VITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
351-576 |
9.22e-55 |
|
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: 185.61 E-value: 9.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVV 430
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVF--LFSGSVRDNIA--LTNSKITDAELIRAAKDVhahqfIEKLDRdydEEVLERG-SNFSTGQKQLISFARVLVYN 505
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAfgPENLGLPREEIRERVEEA-----LELVGL---EHLADRPpHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 506 PRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLSTI-KNVERIIVMHKGRIREEGTHQQLLRKH 576
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
117-577 |
3.91e-54 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 199.43 E-value: 3.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNEmftsGVVTILGDILLLLGLATMMFVFDAKLALITL-TIMPLL--FITAFIF- 192
Cdd:PLN03232 995 RAPMLFFHTNPTGRVINRFSKDIGDIDR----NVANLMNMFMNQLWQLLSTFALIGTVSTISLwAIMPLLilFYAAYLYy 1070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 193 KIKAREGFRSIRILIAKINSFLQENITGMKIVQLFnredKNYRQFERINADHLKAYLRTIL-------YFSIfypAVEVL 265
Cdd:PLN03232 1071 QSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAY----KAYDRMAKINGKSMDNNIRFTLantssnrWLTI---RLETL 1143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 266 SAVAITLIIWFGgldILTNNLTWGQlVGF--IMAAQMFYRP-IEDLSEkyNILQSA------MASSERIFKLLDKVDEIP 336
Cdd:PLN03232 1144 GGVMIWLTATFA---VLRNGNAENQ-AGFasTMGLLLSYTLnITTLLS--GVLRQAskaensLNSVERVGNYIDLPSEAT 1217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 337 D-----KPDAIAPAyvRGEIEFKNVWFAYKDE-EWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILI 410
Cdd:PLN03232 1218 AiiennRPVSGWPS--RGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI 1295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 411 DGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIAlTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFST 490
Cdd:PLN03232 1296 DDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSV 1374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 491 GQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQ 570
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQ 1454
|
....*..
gi 931518516 571 QLLRKHG 577
Cdd:PLN03232 1455 ELLSRDT 1461
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
102-546 |
1.30e-53 |
|
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: 191.42 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 102 KVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTI 181
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 182 MPL-LFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTilyfsifyp 260
Cdd:TIGR02868 163 LLLaGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRA--------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 261 avEVLSAVAITLIIWFGGLDILTNNLTW------GQLVGFIMAAQMF--------YRPIEDLSEKyniLQSAMASSERIF 326
Cdd:TIGR02868 234 --AAATALGAALTLLAAGLAVLGALWAGgpavadGRLAPVTLAVLVLlplaafeaFAALPAAAQQ---LTRVRAAAERIV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 327 KLLDKVDEIPDKPDAIAPAYVRGE--IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQ 404
Cdd:TIGR02868 309 EVLDAAGPVAEGSAPAAGAVGLGKptLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 405 KGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLER 484
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 485 GSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRL 546
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
38-591 |
7.65e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 190.44 E-value: 7.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 38 ALLLVCTSIFtLARpLLTQYAIDNyVMPGDF-DGLTIIAGLFIVIAGLNFIFQYFHFylmyMTGQKVMYDIRSQIFKHLQ 116
Cdd:PRK11174 35 GLLLIAQAWL-LAT-ILQALIIEN-IPREALlPPFILLILLFVLRALLAWLRERVGF----KAGQHIRQQIRQQVLDKLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNE--------MFTSGVVTIlgdillllglATMMFVFDAKLA--LITLTIMPLLF 186
Cdd:PRK11174 108 QLGPAWIQGKPAGSWATLVLEQVEDMHDfyarylpqMALAVLVPL----------LILIAVFPINWAagLILLGTAPLIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 187 ITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKaylRT--ILYFSIFYPAV-E 263
Cdd:PRK11174 178 LFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQ---RTmeVLRMAFLSSAVlE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 264 VLSAVAITLI-IWFG--GLDILtNNLTWGQLV----GF---IMAAQmFYRPIEDLSEKYNILQSAMASSERIFKLLDKVD 333
Cdd:PRK11174 255 FFASISIALVaVYFGfsYLGEL-NFGHYGTGVtlfaGFfvlILAPE-FYQPLRDLGTFYHAKAQAVGAAESLVTFLETPL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 334 EIPDKPDAIAPAYVRGEIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRF--YQvqkGEILID 411
Cdd:PRK11174 333 AHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKIN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 412 GINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTG 491
Cdd:PRK11174 410 GIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVG 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 492 QKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQ 571
Cdd:PRK11174 490 QAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAE 569
|
570 580
....*....|....*....|
gi 931518516 572 LLRKHGIYYKLyqLQYRDQE 591
Cdd:PRK11174 570 LSQAGGLFATL--LAHRQEE 587
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
351-563 |
3.19e-52 |
|
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: 176.64 E-value: 3.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKD-EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGV 429
Cdd:cd03246 1 LEVENVSFRYPGaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSGSVRDNIaltnskitdaeliraakdvhahqfiekldrdydeevlergsnFSTGQKQLISFARVLVYNPRIL 509
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 510 VLDEATSNIDTETEILIQKALNRL-MHKRTSVIIAHRLSTIKNVERIIVMHKGRI 563
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
117-577 |
1.32e-51 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 191.88 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRL---TTDVDALNEMFTSGVVTILGDILLLlglatmmFVFDAKLALITL-TIMPLL--FITAF 190
Cdd:PLN03130 998 RAPMSFFHTNPLGRIINRFakdLGDIDRNVAVFVNMFLGQIFQLLST-------FVLIGIVSTISLwAIMPLLvlFYGAY 1070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 191 I-FKIKAREGFRSIRILIAKINSFLQENITGMKIVqlfnREDKNYRQFERINADHLKAYLRTIL-------YFSIfypAV 262
Cdd:PLN03130 1071 LyYQSTAREVKRLDSITRSPVYAQFGEALNGLSTI----RAYKAYDRMAEINGRSMDNNIRFTLvnmssnrWLAI---RL 1143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 263 EVLSAvaitLIIWF-GGLDILTNNLTWGQlVGFimAAQMFYRpiedLSEKYNI--LQSA---MAS-SERIFKLLDKVDEI 335
Cdd:PLN03130 1144 ETLGG----LMIWLtASFAVMQNGRAENQ-AAF--ASTMGLL----LSYALNItsLLTAvlrLASlAENSLNAVERVGTY 1212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 336 PDKPdAIAPAYVR-----------GEIEFKNVWFAYKDE-EWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQV 403
Cdd:PLN03130 1213 IDLP-SEAPLVIEnnrpppgwpssGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL 1291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 404 QKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKiTDAELIRAAKDVHAHQFIEKLDRDYDEEVLE 483
Cdd:PLN03130 1292 ERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSE 1370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 484 RGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRI 563
Cdd:PLN03130 1371 AGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
490
....*....|....
gi 931518516 564 REEGTHQQLLRKHG 577
Cdd:PLN03130 1451 VEFDTPENLLSNEG 1464
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
38-324 |
2.92e-51 |
|
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: 178.41 E-value: 2.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 38 ALLLVC---TSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKH 114
Cdd:cd18549 5 FLDLFCavlIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 115 LQRLSLSFFDKTPIGRLVTRLTTDVDALNEM--------FTSGVVtilgdillLLGLATMMFVFDAKLALITLTIMPLLF 186
Cdd:cd18549 85 LQKLSFSFFDNNKTGQLMSRITNDLFDISELahhgpedlFISIIT--------IIGSFIILLTINVPLTLIVFALLPLMI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 187 ITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLS 266
Cdd:cd18549 157 IFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFT 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 267 AVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSER 324
Cdd:cd18549 237 NLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-568 |
4.30e-48 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 181.38 E-value: 4.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 78 FIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPigrlVTRLTTDVDALNEMFTSGVVTILGDI 157
Cdd:PTZ00265 103 LVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNP----GSKLTSDLDFYLEQVNAGIGTKFITI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 158 LLLLGLATMMFVF----DAKLALITLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKN 233
Cdd:PTZ00265 179 FTYASAFLGLYIWslfkNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 234 YRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWFGgLDILTNNLTWGQ-------------LVGFIMAAQM 300
Cdd:PTZ00265 259 LKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYG-TRIIISDLSNQQpnndfhggsvisiLLGVLISMFM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 301 FYRPIEDLSEkyniLQSAMASSERIFKLLDKVDEIPDKPDAIAPAYVRgEIEFKNVWFAY---KDEEwVLKDISFKVKEG 377
Cdd:PTZ00265 338 LTIILPNITE----YMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYdtrKDVE-IYKDLNFTLTEG 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 378 EKVAVVGATGAGKTTVISLLTRFYQVQKGEILI-DGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNI----------- 445
Cdd:PTZ00265 412 KTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdle 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 446 ALTN----------------------------------------------SKITDAELIRAAKDVHAHQFIEKLDRDYDE 479
Cdd:PTZ00265 492 ALSNyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyQTIKDSEVVDVSKKVLIHDFVSALPDKYET 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 480 EVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLM--HKRTSVIIAHRLSTIKNVERIIV 557
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFV 651
|
570
....*....|.
gi 931518516 558 MHKgriREEGT 568
Cdd:PTZ00265 652 LSN---RERGS 659
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
37-325 |
1.91e-47 |
|
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: 167.74 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQ 116
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIKA 196
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 197 REGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWF 276
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 931518516 277 GGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
352-562 |
6.71e-47 |
|
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: 163.79 E-value: 6.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 352 EFKNVWFAYKD-EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVV 430
Cdd:cd03225 1 ELKNLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQ--DVFLFSGSVRDNIA--LTNSKITDAELIRAAKDVhahqfIEKLDrdyDEEVLERG-SNFSTGQKQLISFARVLVYN 505
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAfgLENLGLPEEEIEERVEEA-----LELVG---LEGLRDRSpFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 506 PRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLSTIKNV-ERIIVMHKGR 562
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-325 |
3.27e-46 |
|
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: 164.58 E-value: 3.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFI-TAFIF 192
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLpTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 193 KIK---AREGFRsiriLIAKINSFLQE--NITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSA 267
Cdd:cd18550 161 RRRrklTREQQE----KLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 268 VAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18550 237 IGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
34-325 |
6.52e-46 |
|
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: 163.72 E-value: 6.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTTDVD----ALNEMFTSGVvtilgdillllgLATMMFVF--------DAKLALITLTI 181
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTqvqnFVMMLLRMLV------------RAPIMLIGaiimafriNPKLALILLVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 182 MPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPA 261
Cdd:cd18548 149 IPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 262 VEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFI-----------MAAQMFyrpiedlsekyNILQSAMASSERI 325
Cdd:cd18548 229 MMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFInylmqilmslmMLSMVF-----------VMLPRASASAKRI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
34-305 |
3.30e-45 |
|
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: 161.27 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFD--GLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQI 111
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 112 FKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFI 191
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 192 FKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAIT 271
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 931518516 272 LIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPI 305
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-325 |
1.33e-43 |
|
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: 158.11 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDG---------------LTIIAGLFIVIAGLNFIFQYFHFYLMYM 98
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLplvpaslgpadprgqLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 99 TGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALIT 178
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 179 LTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIF 258
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 259 YPAVEVLSAVAITLIIWFGGLDILTNN------LTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18565 241 FPVIRLVAGAGFVATFVVGGYWVLDGPplftgtLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
351-567 |
8.35e-43 |
|
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: 151.70 E-value: 8.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEE-WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIeHITKESLRKHIGV 429
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSGSVRDNIaltnskitdaeliraakdvhahqfiekldrdydeevlerGSNFSTGQKQLISFARVLVYNPRIL 509
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 510 VLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEG 567
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
34-325 |
1.74e-42 |
|
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: 154.56 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTTDVDALNeMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFK 193
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQ-RFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERiNADHL-KAYLRTILYFSIFYPAVEVLSAVAITL 272
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEA-AARRLrATRLRAARLRARFWPLLEALPELGLAA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 931518516 273 IIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18543 239 VLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
37-325 |
4.92e-42 |
|
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: 153.02 E-value: 4.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQ 116
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKika 196
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFG--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 197 regfRSIRIL-------IAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVA 269
Cdd:cd18575 158 ----RRVRRLsrasqdrLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 270 ITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18575 234 IVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
351-577 |
6.92e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 151.16 E-value: 6.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEeWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKEsLRKHIGVV 430
Cdd:COG4555 2 IEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIALTNS--KITDAELIRAAKDVhAHQFieKLDRDYDEEVlergSNFSTGQKQLISFARVLVYNPR 507
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEEL-IELL--GLEEFLDRRV----GELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLSTIKNV-ERIIVMHKGRIREEGTHQQLLRKHG 577
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
367-516 |
8.50e-42 |
|
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: 147.79 E-value: 8.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSG-SVRDNI 445
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 446 ALTnskITDAELIRAAKDVHAHQFIEKLDRDY--DEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATS 516
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-585 |
1.28e-41 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 162.12 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 79 IVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDK---TPiGRLVTRLTTDVDALNEMFTSGVVTILG 155
Cdd:PTZ00265 873 LVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFTH 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 156 DILLLLGLATMMFVFdakLALITLTIMPLLFITAFIFKIKAREGfRSIRILIAKIN------------------SFL-QE 216
Cdd:PTZ00265 952 FIVLFLVSMVMSFYF---CPIVAAVLTGTYFIFMRVFAIRARLT-ANKDVEKKEINqpgtvfaynsddeifkdpSFLiQE 1027
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 217 NITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLtwgqLVGFIM 296
Cdd:PTZ00265 1028 AFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTI----LVDDFM 1103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 297 AAQMFYRPIEDLSEKYNIL----QSAMASSERIFKLLDKVDEIPDKPDA----IAPAYVRGEIEFKNVWFAYKDEEWV-- 366
Cdd:PTZ00265 1104 KSLFTFLFTGSYAGKLMSLkgdsENAKLSFEKYYPLIIRKSNIDVRDNGgiriKNKNDIKGKIEIMDVNFRYISRPNVpi 1183
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQK----------------------------------------- 405
Cdd:PTZ00265 1184 YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltke 1263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 406 -------------GEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEK 472
Cdd:PTZ00265 1264 ggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIES 1343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 473 LDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHK--RTSVIIAHRLSTIK 550
Cdd:PTZ00265 1344 LPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIITIAHRIASIK 1423
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 931518516 551 NVERIIVMHK-----GRIREEGTHQQLLR-KHGIYYKLYQL 585
Cdd:PTZ00265 1424 RSDKIVVFNNpdrtgSFVQAHGTHEELLSvQDGVYKKYVKL 1464
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
34-325 |
5.47e-41 |
|
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: 150.28 E-value: 5.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNyVMPGDFDGLTIIagLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDA-LSAGGSSGGLLA--LLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFK 193
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLI 273
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 274 IWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18551 238 LGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
349-579 |
3.23e-40 |
|
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: 147.36 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 349 GEIEFKNVWFAYKDE-EWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHI 427
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSGSVRDNIAlTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPR 507
Cdd:cd03288 98 SIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLL-RKHGIY 579
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVF 249
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
351-576 |
1.22e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.82 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKEsLRKHIGVV 430
Cdd:COG1131 1 IEVRGLTKRYGDKT-ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIaltnskitdaELIRAAKDVHAHQFIEKLDrdydeEVLE----------RGSNFSTGQKQLISFA 499
Cdd:COG1131 79 PQEPALYPDlTVRENL----------RFFARLYGLPRKEARERID-----ELLElfgltdaadrKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 500 RVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLSTIKNV-ERIIVMHKGRIREEGTHQQLLRKH 576
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
31-325 |
1.57e-39 |
|
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: 146.44 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 31 KMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQ 110
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 111 IFKHLQRLSLSFFDKTPIGRLVTRLTtDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAF 190
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 191 IFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAI 270
Cdd:cd18570 160 LFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 271 TLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18570 240 LLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
77-582 |
2.65e-39 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 154.94 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 77 LFIVIAG-LNFIFQ-YFHFYLMYMtGQKVMYDIrsqIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTsgvVTIL 154
Cdd:PTZ00243 1005 LGIVLLGtFSVPLRfFLSYEAMRR-GSRNMHRD---LLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLP---MSYL 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 155 GDILLLLGLATMMFVFDAKLALITLTIMPLLFI---TAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNRED 231
Cdd:PTZ00243 1078 YLLQCLFSICSSILVTSASQPFVLVALVPCGYLyyrLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAH 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 232 KNYRQ-FERINADHLKAYLRTIL--YFSIfypAVEVLSAVAITLIIWFGglDILTNNLTWGQLVGFI-----MAAQmfyr 303
Cdd:PTZ00243 1158 LVMQEaLRRLDVVYSCSYLENVAnrWLGV---RVEFLSNIVVTVIALIG--VIGTMLRATSQEIGLVslsltMAMQ---- 1228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 304 piedLSEKYNIL-------QSAMASSERIFKLLDKV--------DEI---------------------PDKPDAIAPAYV 347
Cdd:PTZ00243 1229 ----TTATLNWLvrqvatvEADMNSVERLLYYTDEVphedmpelDEEvdalerrtgmaadvtgtvviePASPTSAAPHPV 1304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 348 R-GEIEFKNVWFAYKDE-EWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRK 425
Cdd:PTZ00243 1305 QaGSLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 426 HIGVVLQDVFLFSGSVRDNIAlTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYN 505
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKK 1463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 506 PRILVL-DEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQL-LRKHGIYYKL 582
Cdd:PTZ00243 1464 GSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSM 1542
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
318-574 |
5.64e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.05 E-value: 5.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 318 AMASSERIFKLLDKVDEIPDKPDAIAPAYVRGE-----IEFKNVWFAYKDEEW----VLKDISFKVKEGEKVAVVGATGA 388
Cdd:COG1123 223 EDGPPEEILAAPQALAAVPRLGAARGRAAPAAAaaeplLEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGS 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 389 GKTTVISLLTRFYQVQKGEILIDGINIEHITKES---LRKHIGVVLQDVF--LFSG-SVRDNIA--LTNSKITDAELIRA 460
Cdd:COG1123 303 GKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreLRRRVQMVFQDPYssLNPRmTVGDIIAepLRLHGLLSRAERRE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 461 akdvHAHQFIEK--LDRDYdeevLER-GSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRL--MH 535
Cdd:COG1123 383 ----RVAELLERvgLPPDL----ADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrEL 454
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 931518516 536 KRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLR 574
Cdd:COG1123 455 GLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFA 494
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
351-567 |
4.69e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.19 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKES---LRKHI 427
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDV-FLFSGSVRDNIA--LTNSKITDAELIRAAKDV--------HAHQFIEKLdrdydeevlergsnfSTGQKQLI 496
Cdd:COG2884 82 GVVFQDFrLLPDRTVYENVAlpLRVTGKSRKEIRRRVREVldlvglsdKAKALPHEL---------------SGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 497 SFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLSTIKNVE-RIIVMHKGRIREEG 567
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkRVLELEDGRLVRDE 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
351-572 |
1.04e-37 |
|
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: 139.24 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQK-----GEILIDGINIEH--ITKESL 423
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 424 RKHIGVVLQDVFLFSGSVRDNIALT-------NSKITDAELIRAAKDVhahqfiekldrDYDEEVLER--GSNFSTGQKQ 494
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKA-----------ALWDEVKDRlhALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 495 LISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQL 572
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
351-567 |
1.59e-37 |
|
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: 138.79 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEW---VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL---R 424
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 425 KHIGVVLQDVFL---FSGSVRDNIaltnskitdAELIRAAKDVHAHQFIEKLDRDY------DEEVLERGSN-FSTGQKQ 494
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQI---------AEPLRIHGKLSKKEARKEAVLLLlvgvglPEEVLNRYPHeLSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 495 LISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRL--MHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
351-563 |
1.06e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 134.83 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIeHITKESLRKHIGVV 430
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIaltnskitdaeliraakdvhahqfiekldrdydeevlergsNFSTGQKQLISFARVLVYNPRIL 509
Cdd:cd03230 79 PEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 510 VLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLSTIKNV-ERIIVMHKGRI 563
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
352-562 |
2.81e-36 |
|
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: 133.14 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 352 EFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVL 431
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 432 QdvflfsgsvrdnialtnskitdaeliraakdvhahqfiekldrdydeevlergsnFSTGQKQLISFARVLVYNPRILVL 511
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518516 512 DEATSNIDTETEILIQKALNRLM-HKRTSVIIAHRLSTIKNV-ERIIVMHKGR 562
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
351-576 |
3.06e-36 |
|
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: 142.35 E-value: 3.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAY-KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTV---ISLLTRFYQVQKGEILIDGINIEHITKESLRKH 426
Cdd:COG1123 5 LEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLalaLMGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 427 IGVVLQDVF--LFSGSVRDNIA--LTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEvlergsnFSTGQKQLISFARVL 502
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAVGLERRLDRYPHQ-------LSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 503 VYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLRKH 576
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
349-579 |
3.21e-35 |
|
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: 133.83 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 349 GEIEFKNVWFAYKDE-EWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQkGEILIDGINIEHITKESLRKHI 427
Cdd:cd03289 1 GQMTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSGSVRDNIAlTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPR 507
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIY 579
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
351-573 |
3.32e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.58 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEE-WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGV 429
Cdd:PRK13632 8 IKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQ--DVFLFSGSVRDNIA--LTNSKITDAELIRAAKDVHAHQFIEK-LDRDydeevlerGSNFSTGQKQLISFARVLVY 504
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAfgLENKKVPPKKMKDIIDDLAKKVGMEDyLDKE--------PQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 505 NPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA--HRLSTIKNVERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
351-574 |
1.93e-34 |
|
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: 130.31 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKE---SLRKHI 427
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSG-SVRDNIAL---TNSKITDAELIRAAKdvhahqfiEKLdrdydEEVLERG------SNFSTGQKQLIS 497
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFplrEHTRLSEEEIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 498 FARVLVYNPRILVLDEATSNID----TETEILIQKaLNRLMHKrTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQL 572
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpiasGVIDDLIRS-LKKELGL-TSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEEL 224
|
..
gi 931518516 573 LR 574
Cdd:cd03261 225 RA 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
103-573 |
8.36e-34 |
|
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: 138.12 E-value: 8.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 103 VMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGV---VTILGDILLLLGLATMM--FVFDAKLALI 177
Cdd:TIGR01271 956 VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLfdfIQLTLIVLGAIFVVSVLqpYIFIAAIPVA 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 178 TLTIMPLLFITAFIFKIKAREG-FRSiriliaKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKA---YLRTIL 253
Cdd:TIGR01271 1036 VIFIMLRAYFLRTSQQLKQLESeARS------PIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANwflYLSTLR 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 254 YFSIFYPAVEVLSAVAITLIiwfgglDILTNNLTWGQlVGFIMAAQMFYRPIEDLSEKYNI-LQSAMASSERIFKLLDKV 332
Cdd:TIGR01271 1110 WFQMRIDIIFVFFFIAVTFI------AIGTNQDGEGE-VGIILTLAMNILSTLQWAVNSSIdVDGLMRSVSRVFKFIDLP 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 333 DEIPD-----KPDAIAPAYV------------RGEIEFKNVWFAY-KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVI 394
Cdd:TIGR01271 1183 QEEPRpsgggGKYQLSTVLVienphaqkcwpsGGQMDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLL 1262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 395 SLLTRFYQVQkGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNIAlTNSKITDAELIRAAKDVHAHQFIEKLD 474
Cdd:TIGR01271 1263 SALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFP 1340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 475 RDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVER 554
Cdd:TIGR01271 1341 DKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQ 1420
|
490
....*....|....*....
gi 931518516 555 IIVMHKGRIREEGTHQQLL 573
Cdd:TIGR01271 1421 FLVIEGSSVKQYDSIQKLL 1439
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
351-567 |
3.58e-33 |
|
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: 126.09 E-value: 3.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKEslRKHIGVV 430
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIA--LTNSKITDAELIRAAKdvhahqfiEKLDRDYDEEVLER-GSNFSTGQKQLISFARVLVYNP 506
Cdd:cd03259 78 FQDYALFPHlTVAENIAfgLKLRGVPKAEIRARVR--------ELLELVGLEGLLNRyPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 507 RILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAH------RLStiknvERIIVMHKGRIREEG 567
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHdqeealALA-----DRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
351-563 |
4.94e-33 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 126.07 E-value: 4.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEE---WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL---- 423
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 424 RKHIGVVLQDVFLFSG-SVRDNIAL----TNSKITDAELIraakdvhAHQFIEKLDRdydEEVLERG-SNFSTGQKQLIS 497
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllAGVPKKERRER-------AEELLERVGL---GDRLNHYpSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 498 FARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR-TSVIIA-HRLSTIKNVERIIVMHKGRI 563
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
351-575 |
4.96e-33 |
|
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: 126.54 E-value: 4.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKD---EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL---R 424
Cdd:cd03258 2 IELKNVSKVFGDtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 425 KHIGVVLQDVFLFSG-SVRDNIA--LTNSKITDAELIRAAKDVHAHQFIEKLDRDYDeevlergSNFSTGQKQLISFARV 501
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVAlpLEIAGVPKAEIEERVLELLELVGLEDKADAYP-------AQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 502 LVYNPRILVLDEATSNIDTET--EILiqkALNRLMHKR---TSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLRK 575
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETtqSIL---ALLRDINRElglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
33-325 |
7.13e-33 |
|
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: 127.68 E-value: 7.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 33 QVIYAALLLvctSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIF 112
Cdd:cd18568 6 EILLASLLL---QLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 113 KHLQRLSLSFFDKTPIGRLVTRLTTDvDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIF 192
Cdd:cd18568 83 KHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 193 KIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITL 272
Cdd:cd18568 162 SPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 931518516 273 IIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18568 242 VLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
34-325 |
7.91e-33 |
|
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: 127.63 E-value: 7.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFK 113
Cdd:cd18555 4 LISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 114 HLQRLSLSFFDKTPIGRLVTRLTtDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFK 193
Cdd:cd18555 84 HLLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLI 273
Cdd:cd18555 163 KKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 274 IWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18555 243 LWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
351-574 |
1.37e-32 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 125.49 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVV 430
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIALTNSKItdaELIRAAKDVHAHQFIEKLDRDyDEEVLER-GSNFSTGQKQLISFARVLVYNPRI 508
Cdd:cd03295 81 IQQIGLFPHmTVEENIALVPKLL---KWPKEKIRERADELLALVGLD-PAEFADRyPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 509 LVLDEATSNIDTETEILIQ---KALNRLMHKrTSVIIAHRL-STIKNVERIIVMHKGRIREEGTHQQLLR 574
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQeefKRLQQELGK-TIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
49-325 |
1.73e-32 |
|
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: 126.76 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 49 LARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIF-------QYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLS 121
Cdd:cd18554 16 LLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFlilrppvEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 122 FFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIKAREGFR 201
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 202 SIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDI 281
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLV 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 931518516 282 LTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18554 256 IEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
351-562 |
2.98e-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: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEW----VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniehitkeslrkH 426
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 427 IGVVLQDVFLFSGSVRDNIALtnSKITDAELIRAAkdVHAHQfiekLDRDYDE-------EVLERGSNFSTGQKQLISFA 499
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILF--GKPFDEERYEKV--IKACA----LEPDLEIlpdgdltEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 500 RVLVYNPRILVLDEATSNIDTETEI-LIQKALN-RLMHKRTSVIIAHRLSTIKNVERIIVMHKGR 562
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRhIFENCILgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
351-562 |
2.41e-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: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKES--LRKHIG 428
Cdd:cd03229 1 LELKNVSKRYGQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 VVLQDVFLFSG-SVRDNIALTnskitdaeliraakdvhahqfiekldrdydeevlergsnFSTGQKQLISFARVLVYNPR 507
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRL--MHKRTSVIIAHRLSTIKNV-ERIIVMHKGR 562
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
351-574 |
3.65e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.82 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKD-EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGV 429
Cdd:PRK13635 6 IRVEHISFRYPDaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQ--DVFLFSGSVRDNIA--LTNSKITDAELIR----AAKDVHAHQFiekLDRDydeevlerGSNFSTGQKQLISFARV 501
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAfgLENIGVPREEMVErvdqALRQVGMEDF---LNRE--------PHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 502 LVYNPRILVLDEATSNIDTETEILIQKALNRLM-HKRTSVI-IAHRLSTIKNVERIIVMHKGRIREEGTHQQLLR 574
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
351-563 |
2.13e-30 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 118.40 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKE--SLRKHIG 428
Cdd:cd03262 1 IEIKNLHKSFGDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 VVLQDVFLFSG-SVRDNIAL---TNSKITDAELIRAAKDV--------HAHQFIEKLdrdydeevlergsnfSTGQKQLI 496
Cdd:cd03262 80 MVFQQFNLFPHlTVLENITLapiKVKGMSKAEAEERALELlekvgladKADAYPAQL---------------SGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 497 SFARVLVYNPRILVLDEATSNIDTET--EILiqKALNRLMH-KRTSVIIAHRLSTIKNV-ERIIVMHKGRI 563
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELvgEVL--DVMKDLAEeGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
351-576 |
3.18e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.04 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHitkesLRKHIGVV 430
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQ-------------DVFLfSGSVRDNIALTNSKITDAELIRAA-KDVHAHQFiekLDRDYDEevlergsnFSTGQKQLI 496
Cdd:COG1121 81 PQraevdwdfpitvrDVVL-MGRYGRRGLFRRPSRADREAVDEAlERVGLEDL---ADRPIGE--------LSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 497 SFARVLVYNPRILVLDEATSNIDTETEILIQKALNRL-MHKRTSVIIAHRLSTI-KNVERIIVMHKGRIReEGTHQQLLR 574
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLLNRGLVA-HGPPEEVLT 227
|
..
gi 931518516 575 KH 576
Cdd:COG1121 228 PE 229
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
33-325 |
5.99e-30 |
|
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: 119.53 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 33 QVIYAALLLvctSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVmyDIR--SQ 110
Cdd:cd18588 6 EVLLASLFL---QLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRI--DAElgAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 111 IFKHLQRLSLSFFDKTPIGRLVTRLTtDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAF 190
Cdd:cd18588 81 LFRHLLRLPLSYFESRQVGDTVARVR-ELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 191 ----IFKIKAREGFRsiriLIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLS 266
Cdd:cd18588 160 lvtpILRRRLEEKFQ----RGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQ 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 267 AVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18588 236 KLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
38-325 |
6.47e-30 |
|
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: 119.54 E-value: 6.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 38 ALLLVCTSIfTLARPLLTQYAID---NYVMPGDFDGLT------IIAGLFIVIAGLNFIfqyfHFYLMYMTGQKVMYDIR 108
Cdd:cd18573 3 ALLLVSSAV-TMSVPFAIGKLIDvasKESGDIEIFGLSlktfalALLGVFVVGAAANFG----RVYLLRIAGERIVARLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 109 SQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFIT 188
Cdd:cd18573 78 KRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 189 AFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAV 268
Cdd:cd18573 158 AVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 269 AITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18573 238 SLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
352-567 |
1.00e-29 |
|
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: 115.61 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 352 EFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVL 431
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 432 QdvflfsgsvrdniALTNSKITDaeliraakdvhahqfieKLDRDYDEevlergsnFSTGQKQLISFARVLVYNPRILVL 511
Cdd:cd03214 80 Q-------------ALELLGLAH-----------------LADRPFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 512 DEATSNIDTETEILIQKALNRLMHKR-TSVII-------AHRLStiknvERIIVMHKGRIREEG 567
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERgKTVVMvlhdlnlAARYA-----DRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
351-575 |
1.55e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.93 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEW-VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGV 429
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDV-FLFSGS-VRDNIA--LTNSKITDAELIRAAKDVHAHqfIEKLDR-DYDEEVLergsnfSTGQKQLISFARVLVY 504
Cdd:PRK13648 88 VFQNPdNQFVGSiVKYDVAfgLENHAVPYDEMHRRVSEALKQ--VDMLERaDYEPNAL------SGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 505 NPRILVLDEATSNIDTETeiliQKALNRLMHKR------TSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRK 575
Cdd:PRK13648 160 NPSVIILDEATSMLDPDA----RQNLLDLVRKVksehniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
366-574 |
1.56e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 116.77 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHItKESLRKHIGVV--LQDVFLFSG-SVR 442
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARLGIGrtFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 443 DN--IALTNSKITDAELIRAAKDVHAHqfiekldRDYDEEVLER----------GSNFSTGQKQLISFARVLVYNPRILV 510
Cdd:cd03219 94 ENvmVAAQARTGSGLLLARARREEREA-------RERAEELLERvgladladrpAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 511 LDEATSNI-DTETEILIQ--KALNRlmHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLR 574
Cdd:cd03219 167 LDEPAAGLnPEETEELAEliRELRE--RGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
42-325 |
1.62e-29 |
|
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: 118.46 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 42 VCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLS 121
Cdd:cd18782 12 FVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 122 FFDKTPIGRLVTRLtTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIKAREGFR 201
Cdd:cd18782 92 FFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 202 SIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDI 281
Cdd:cd18782 171 RRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 931518516 282 LTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18782 251 LRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
351-566 |
1.70e-29 |
|
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: 116.03 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEW---VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIehitkESLRKHI 427
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFS-GSVRDNIALTnskITDAELIRAAKDVHAHQFIEKLD-----RDYDEEVlergsnfSTGQKQLISFARV 501
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELLELVGlsgfeNAYPHQL-------SGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 502 LVYNPRILVLDEATSNIDTETEILIQKALNRLM--HKRTSVIIAH------RLSTiknveRIIVMHK--GRIREE 566
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTHdideavFLAD-----RVVVLSArpGRIVAE 215
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
58-335 |
1.75e-29 |
|
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: 118.71 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 58 AIDNYVMPGDF---DGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDK---TPiGRL 131
Cdd:cd18578 35 LISVFSLPDDDelrSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDpenST-GAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 132 VTRLTTDVDALNEMFTS--GVVTilgdillllGLATMM-------FVFDAKLALITLTIMPLLFITAFIFkIKAREGF-R 201
Cdd:cd18578 114 TSRLSTDASDVRGLVGDrlGLIL---------QAIVTLvagliiaFVYGWKLALVGLATVPLLLLAGYLR-MRLLSGFeE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 202 SIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDI 281
Cdd:cd18578 184 KNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLV 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 282 LTNNLTWGQ--------LVGFIMAAQMF-YRPieDLSekynilqSAMASSERIFKLLDKVDEI 335
Cdd:cd18578 264 ANGEYTFEQffivfmalIFGAQSAGQAFsFAP--DIA-------KAKAAAARIFRLLDRKPEI 317
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
352-561 |
3.41e-29 |
|
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: 114.94 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 352 EFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHItkeslRKHIGVVL 431
Cdd:cd03235 1 EVEDLTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 432 Q--DV-FLFSGSVRDNIALtnskitdaeliRAAKDVHAHQFIEKLDRDYDEEVLERG----------SNFSTGQKQLISF 498
Cdd:cd03235 75 QrrSIdRDFPISVRDVVLM-----------GLYGHKGLFRRLSKADKAKVDEALERVglseladrqiGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 499 ARVLVYNPRILVLDEATSNIDTETEILIQKALNRL-MHKRTSVIIAHRLSTI-KNVERIIVMHKG 561
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
366-567 |
8.40e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.12 E-value: 8.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT-KESLRKHIGVVLQDVFLFSG-SVRD 443
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 444 NIAL----TNSKITD-AELIRAAKDVhahqfIEKLDRDYDeeVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNI 518
Cdd:COG1129 99 NIFLgrepRRGGLIDwRAMRRRAREL-----LARLGLDID--PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 519 -DTETEILIqKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:COG1129 172 tEREVERLF-RIIRRLKAQGVAIIyISHRLDEVFEIaDRVTVLRDGRLVGTG 222
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
37-325 |
2.38e-28 |
|
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: 114.95 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQ 116
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIKA 196
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 197 REGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWF 276
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 931518516 277 GGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
351-563 |
2.59e-28 |
|
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: 112.50 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKES---LRKHI 427
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSG-SVRDNIALTnSKITDAELIRAAKDVHAhqFIEKLD-----RDYDEEVlergsnfSTGQKQLISFARV 501
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFA-LEVTGVPPREIRKRVPA--ALELVGlshkhRALPAEL-------SGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 502 LVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNV--ERIIVMHKGRI 563
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
351-568 |
6.16e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 115.20 E-value: 6.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKEslRKHIGVV 430
Cdd:COG3842 6 LELENVSKRYGDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIA--LTNSKITDAELIRAAKDV--------HAHQFIEKLdrdydeevlergsnfSTGQKQLISFA 499
Cdd:COG3842 83 FQDYALFPHlTVAENVAfgLRMRGVPKAEIRARVAELlelvglegLADRYPHQL---------------SGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 500 RVLVYNPRILVLDEATSNIDTET------EIL-IQKALNrlmhkRTSVIIAH------RLSTiknveRIIVMHKGRIREE 566
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLreemreELRrLQRELG-----ITFIYVTHdqeealALAD-----RIAVMNDGRIEQV 217
|
..
gi 931518516 567 GT 568
Cdd:COG3842 218 GT 219
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
39-312 |
6.22e-28 |
|
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: 113.71 E-value: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 39 LLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRL 118
Cdd:cd18567 9 LLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 119 SLSFFDKTPIGRLVTRLTTdVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFkikare 198
Cdd:cd18567 89 PLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLAL------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 199 gFRSIR-------ILIAKINSFLQENITGMKIVQLFNREDKNYRQF-----ERINADHLKAYLRtiLYFSIFYPAVEVLS 266
Cdd:cd18567 162 -YPPLRrateeqiVASAKEQSHFLETIRGIQTIKLFGREAEREARWlnllvDAINADIRLQRLQ--ILFSAANGLLFGLE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 931518516 267 AVaitLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKY 312
Cdd:cd18567 239 NI---LVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKL 281
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
351-572 |
8.34e-28 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 111.44 E-value: 8.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEW-VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIeHITKESLRKHIGV 429
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSG-SVRDNIAL------TNSKITDAELIRAAKDVhahQFIEKLDRdydeevleRGSNFSTGQKQLISFARVL 502
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkgLPKSEIKEEVELLLRVL---GLTDKANK--------RARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 503 VYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAH------RLSTiknveRIIVMHKGRIREEGTHQQL 572
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeALCD-----RIAIMSDGKLRCIGSPQEL 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
351-567 |
1.83e-27 |
|
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: 111.33 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRF-YQVQKGEILIDGINIEHITKESLRKHIGV 429
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 V---LQDVFLFSGSVRDNI--ALTNS-----KITDAELIRAAKDVHAHQFIEKLDRDYDEevlergsnFSTGQKQLISFA 499
Cdd:COG1119 83 VspaLQLRFPRDETVLDVVlsGFFDSiglyrEPTDEQRERARELLELLGLAHLADRPFGT--------LSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 500 RVLVYNPRILVLDEATSNIDTE-TEILIQkALNRLMHK--RTSVIIAHRLSTI-KNVERIIVMHKGRIREEG 567
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGaRELLLA-LLDKLAAEgaPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAG 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
351-555 |
2.92e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 109.49 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIeHITKESLRKHIGVV 430
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNI----ALTNSKITDAELIRAAKDV----HAHQFIEKLdrdydeevlergsnfSTGQKQLISFARV 501
Cdd:COG4133 81 GHADGLKPElTVRENLrfwaALYGLRADREAIDEALEAVglagLADLPVRQL---------------SAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 502 LVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLSTIKNVERI 555
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
351-572 |
3.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.36 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKD--EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKES---LRK 425
Cdd:PRK13650 5 IEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENvwdIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 426 HIGVVLQ--DVFLFSGSVRDNIA--LTNSKITDAELIRAAKdvHAHQFIEKLDRDYDEEvlergSNFSTGQKQLISFARV 501
Cdd:PRK13650 82 KIGMVFQnpDNQFVGATVEDDVAfgLENKGIPHEEMKERVN--EALELVGMQDFKEREP-----ARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 502 LVYNPRILVLDEATSNIDTETEI-LIQKALN-RLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQL 572
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLeLIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
364-575 |
5.19e-27 |
|
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: 109.73 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 364 EWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKEslRKHIGVVLQDVFLFSG-SVR 442
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 443 DNIA-----LTNSKITDAELIraakdvhaHQFIEKLDRDydeEVLERG-SNFSTGQKQLISFARVLVYNPRILVLDEATS 516
Cdd:cd03299 90 KNIAyglkkRKVDKKEIERKV--------LEIAEMLGID---HLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 517 NIDTETEILIQKALNRLMHK-RTSVI-IAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLRK 575
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEfGVTVLhVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
351-568 |
1.43e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.94 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNV---WFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL---R 424
Cdd:COG1135 2 IELENLsktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 425 KHIGVVLQDVFLFSG-SVRDNIA--LTNSKITDAEliRAAKdVhahqfiekldrdydEEVLER-G---------SNFSTG 491
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVAlpLEIAGVPKAE--IRKR-V--------------AELLELvGlsdkadaypSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 492 QKQLISFARVLVYNPRILVLDEATSNIDTET--EIL-----IQKALNrLmhkrTSVIIAHRLSTIKNV-ERIIVMHKGRI 563
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETtrSILdllkdINRELG-L----TIVLITHEMDVVRRIcDRVAVLENGRI 219
|
....*
gi 931518516 564 REEGT 568
Cdd:COG1135 220 VEQGP 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
351-575 |
3.89e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.28 E-value: 3.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVV 430
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDV--FLFSGSVRDNIAL--TNSKITDAELIR----AAKDVHAHQFIEKLDRdydeevlergsNFSTGQKQLISFARVL 502
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFgpVNMGLDKDEVERrveeALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 503 VYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLS-TIKNVERIIVMHKGRIREEGTHQQLLRK 575
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
351-574 |
4.29e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.21 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKD----EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINI--EHITKESLR 424
Cdd:PRK13637 3 IKIENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 425 KHIGVVLQ--DVFLFSGSVRDNIAL--TNSKITDAELiraAKDVHAHQFIEKLDRdydeEVLERGSNF--STGQKQLISF 498
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFgpINLGLSEEEI---ENRVKRAMNIVGLDY----EDYKDKSPFelSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 499 ARVLVYNPRILVLDEATSNIDTET--EILiqkALNRLMHKR---TSVIIAHRLSTI-KNVERIIVMHKGRIREEGTHQQL 572
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGrdEIL---NKIKELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREV 232
|
..
gi 931518516 573 LR 574
Cdd:PRK13637 233 FK 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
366-573 |
5.83e-26 |
|
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: 105.98 E-value: 5.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKES----LRKHIGVVLQDVFLFSG-S 440
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG---RDITGLPpherARAGIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 441 VRDNIALtnskitdAELIRAAKDVHAhqfieKLDRDYD-----EEVLER-GSNFSTGQKQLISFARVLVYNPRILVLDEA 514
Cdd:cd03224 92 VEENLLL-------GAYARRRAKRKA-----RLERVYElfprlKERRKQlAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 515 TS----NIDTEteilIQKALNRLMHKRTSVII----AHRLSTIknVERIIVMHKGRIREEGTHQQLL 573
Cdd:cd03224 160 SEglapKIVEE----IFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELL 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
351-573 |
7.33e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.38 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITK-ESLRKHIGV 429
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDV-FLFSG-SVRDNIALTNSKITDAEL-IRaakdvhahqfiEKLDRDYDEEVLER-----GSNFSTGQKQLISFARV 501
Cdd:PRK13644 82 VFQNPeTQFVGrTVEEDLAFGPENLCLPPIeIR-----------KRVDRALAEIGLEKyrhrsPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 502 LVYNPRILVLDEATSNIDTETEILIQKALNRLMHK-RTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
351-572 |
1.06e-25 |
|
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: 105.78 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKEslRKHIGVV 430
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIA--LTNSKITDAELIRAAKDV--------HAHQFIEKLdrdydeevlergsnfSTGQKQLISFA 499
Cdd:cd03300 78 FQNYALFPHlTVFENIAfgLRLKKLPKAEIKERVAEAldlvqlegYANRKPSQL---------------SGGQQQRVAIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 500 RVLVYNPRILVLDEATSNIDTETEILIQKALNRLmHKR---TSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQL 572
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRL-QKElgiTFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
351-575 |
1.16e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.81 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKD-EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFY---QVQKGEILIDGINIEHITKESLRKH 426
Cdd:PRK13640 6 VEFKHVSFTYPDsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 427 IGVVLQ--DVFLFSGSVRDNIA--LTNSKITDAELIRAAKDVHAHqfIEKLDRDYDEEvlergSNFSTGQKQLISFARVL 502
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAfgLENRAVPRPEMIKIVRDVLAD--VGMLDYIDSEP-----ANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 503 VYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRK 575
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
351-572 |
1.71e-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: 105.34 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL---RKHI 427
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSG-SVRDNI---ALTNSKI--------TDAELIRAakdvhahqfIEKLDR-DYDEEVLERGSNFSTGQKQ 494
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVlsgRLGRRSTwrslfglfPKEEKQRA---------LAALERvGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 495 LISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRL-MHKRTSVIIA-HRLSTIK-NVERIIVMHKGRIREEGTHQQ 571
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSlHQVDLAReYADRIVGLKDGRIVFDGPPAE 231
|
.
gi 931518516 572 L 572
Cdd:cd03256 232 L 232
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
54-325 |
1.76e-25 |
|
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: 106.79 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 54 LTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVT 133
Cdd:cd18577 29 FTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 134 RLTTDVDALNE--------------MFTSGVVTIlgdillllglatmmFVFDAKLALITLTIMPLLFITAFIFKIKAREG 199
Cdd:cd18577 109 RLTSDTNLIQDgigeklglliqslsTFIAGFIIA--------------FIYSWKLTLVLLATLPLIAIVGGIMGKLLSKY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 200 FRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWFGGL 279
Cdd:cd18577 175 TKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSR 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 931518516 280 DILTNNLTWGQLV----GFIMAAQMfyrpIEDLSEKYNILQSAMASSERI 325
Cdd:cd18577 255 LVRDGEISPGDVLtvffAVLIGAFS----LGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
350-563 |
2.07e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.78 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 350 EIEFKNV-----WFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLT--RFYQVQKGEILIDGINIEhitKES 422
Cdd:cd03213 3 TLSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 LRKHIGVVLQ-DVFLFSGSVRDNIALTnskitdAELiraakdvhahqfiekldrdydeevleRGsnFSTGQKQLISFARV 501
Cdd:cd03213 80 FRKIIGYVPQdDILHPTLTVRETLMFA------AKL--------------------------RG--LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 502 LVYNPRILVLDEATSNIDTETEILIQKALNRLMHK-RTSVIIAHRLST--IKNVERIIVMHKGRI 563
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
78-584 |
4.36e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 110.84 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 78 FIVIAGLNF--IFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMftsGVVTILG 155
Cdd:PLN03232 345 FLIFFGVTFgvLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQI---AEQLHGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 156 DILLLLGLATMMFVFD----AKL--ALITLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLqeniTGMKIVQLFNR 229
Cdd:PLN03232 422 WSAPFRIIVSMVLLYQqlgvASLfgSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEIL----ASMDTVKCYAW 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 230 EDKNYRQFERINADHLKAYLRTILYFSifYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLS 309
Cdd:PLN03232 498 EKSFESRIQGIRNEELSWFRKAQLLSA--FNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLP 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 310 EKYNILQSAMASSERIFKLLDKVDEI--PDKP-DAIAPAyvrgeIEFKNVWFAY--KDEEWVLKDISFKVKEGEKVAVVG 384
Cdd:PLN03232 576 NLLSQVVNANVSLQRIEELLLSEERIlaQNPPlQPGAPA-----ISIKNGYFSWdsKTSKPTLSDINLEIPVGSLVAIVG 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 385 ATGAGKTTVIS-LLTRFYQVQKGEILIdginiehitkeslRKHIGVVLQDVFLFSGSVRDNIaLTNSKITDAELIRAAkD 463
Cdd:PLN03232 651 GTGEGKTSLISaMLGELSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENI-LFGSDFESERYWRAI-D 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 464 VHAHQFIEKLDRDYD-EEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTE-TEILIQKALNRLMHKRTSVI 541
Cdd:PLN03232 716 VTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVL 795
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 931518516 542 IAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKLYQ 584
Cdd:PLN03232 796 VTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
366-568 |
4.74e-25 |
|
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: 104.35 E-value: 4.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHiTKESLRKHIGVV--LQDVFLFSG-SVR 442
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG-LPPHRIARLGIArtFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 443 DNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLER----------GSNFSTGQKQLISFARVLVYNPRILVLD 512
Cdd:COG0411 98 ENVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERvgladradepAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 513 EATS--NiDTETEILIQ--KALNRlMHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGT 568
Cdd:COG0411 178 EPAAglN-PEETEELAEliRRLRD-ERGITILLIEHDMDLVMGLaDRIVVLDFGRVIAEGT 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
354-563 |
5.37e-25 |
|
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: 102.72 E-value: 5.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 354 KNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINiehITKESLRKHIGVVLQD 433
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 434 V--FLFSGSVRDNIALTNsKITDAELIRAA---KDVHAHQFIEKLDRDydeevlergsnFSTGQKQLISFARVLVYNPRI 508
Cdd:cd03226 80 VdyQLFTDSVREELLLGL-KELDAGNEQAEtvlKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 509 LVLDEATSNIDTETEILIQKALNRLM-HKRTSVIIAHRLSTIKNV-ERIIVMHKGRI 563
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
350-575 |
9.08e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.72 E-value: 9.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 350 EIEFKNVWFAYKD----EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKE---- 421
Cdd:PRK13634 2 DITFQKVEHRYQYktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 422 SLRKHIGVVLQdvF----LFSGSVRDNIAL--TNSKITDAELIRAAKDVhahqfIEKLdrDYDEEVLERgSNF--STGQK 493
Cdd:PRK13634 82 PLRKKVGIVFQ--FpehqLFEETVEKDICFgpMNFGVSEEDAKQKAREM-----IELV--GLPEELLAR-SPFelSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 494 QLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLSTIKN-VERIIVMHKGRIREEGTHQ 570
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*
gi 931518516 571 QLLRK 575
Cdd:PRK13634 232 EIFAD 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
351-568 |
1.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.00 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHiTKESL---RKHI 427
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSLlevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQ--DVFLFSGSVRDNIAL--TNSKITDAELIRAAKDVHAHQFIEkldrDYDEEVLErgsNFSTGQKQLISFARVLV 503
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEDVAFgpLNLGLSKEEVEKRVKEALKAVGME----GFENKPPH---HLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 504 YNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLSTI-KNVERIIVMHKGRIREEGT 568
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
349-575 |
1.40e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.16 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 349 GEIEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKESLRK-HI 427
Cdd:COG3839 2 ASLELENVSKSYGGVE-ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTDLPPKDrNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLF-SGSVRDNIA--LTNSKITDAElIR-----AAKDVHahqfIEK-LDRdydeevleRGSNFSTGQKQLISF 498
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIAfpLKLRKVPKAE-IDrrvreAAELLG----LEDlLDR--------KPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 499 ARVLVYNPRILVLDEATSNID------TETEIliqKALnrlmHKR---TSVIIAHRLstiknVE------RIIVMHKGRI 563
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDaklrveMRAEI---KRL----HRRlgtTTIYVTHDQ-----VEamtladRIAVMNDGRI 212
|
250
....*....|..
gi 931518516 564 REEGTHQQLLRK 575
Cdd:COG3839 213 QQVGTPEELYDR 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
367-575 |
3.01e-24 |
|
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: 102.34 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL----RKHIGVVLQDVFLFSG-SV 441
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIA--LTNSKITDAELIRAAKDV--------HAHQFIEKLdrdydeevlergsnfSTGQKQLISFARVLVYNPRILVL 511
Cdd:cd03294 120 LENVAfgLEVQGVPRAEREERAAEAlelvglegWEHKYPDEL---------------SGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 512 DEATSNIDTETEILIQKALNRL--MHKRTSVIIAHRLS-TIKNVERIIVMHKGRIREEGTHQQLLRK 575
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
366-574 |
4.92e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFL-FSGSVRDN 444
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IAL-----TNSKITDAELIRAAkdvhahqfIEKLD------RDYDEevlergsnFSTGQKQLISFARVLV------YNPR 507
Cdd:PRK13548 97 VAMgraphGLSRAEDDALVAAA--------LAQVDlahlagRDYPQ--------LSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKR-TSVI-IAHRLstikNV-----ERIIVMHKGRIREEGTHQQLLR 574
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAHERgLAVIvVLHDL----NLaaryaDRIVLLHQGRLVADGTPAEVLT 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
351-573 |
5.43e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.94 E-value: 5.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIE--HITKESLRKHIG 428
Cdd:PRK09493 2 IEFKNVSKHFGPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 VVLQDVFLFSG-SVRDNIALTNSKITDAEliRAAKDVHAHQFIEKLDrdydeeVLERG----SNFSTGQKQLISFARVLV 503
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFGPLRVRGAS--KEEAEKQARELLAKVG------LAERAhhypSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 504 YNPRILVLDEATSNIDTEteiLIQKALnRLMHK-----RTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPE---LRHEVL-KVMQDlaeegMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
366-567 |
5.76e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 100.13 E-value: 5.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKhIGVVLQDVFLFSG-SVRDN 444
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IALTnskitdAELIRAAKDvHAHQFIEKLDRDYD-EEVLE-RGSNFSTGQKQLISFARVLVYNPRILVLDEATSNID-TE 521
Cdd:cd03266 99 LEYF------AGLYGLKGD-ELTARLEELADRLGmEELLDrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931518516 522 TEILIQkALNRLMHKRTSVIIA-HRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:cd03266 172 TRALRE-FIRQLRALGKCILFStHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
28-296 |
6.74e-24 |
|
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: 102.28 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 28 SPYKMQVIYAALLLvctSIFTLARPLLTQYAIDNYVMPGDFDGLT-IIAGLFIVIaGLNFIFQYFHFYLMYMTGQKVMYD 106
Cdd:cd18566 1 RPLLPQVLLASLFI---NILALATPLFILQVYDRVIPNESIPTLQvLVIGVVIAI-LLESLLRLLRSYILAWIGARFDHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 107 IRSQIFKHLQRLSLSFFDKTPIGRLVTRLTtDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLF 186
Cdd:cd18566 77 LSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 187 ITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLS 266
Cdd:cd18566 156 LVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFS 235
|
250 260 270
....*....|....*....|....*....|
gi 931518516 267 AVAITLIIWFGGLDILTNNLTWGQLVGFIM 296
Cdd:cd18566 236 QVSMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
366-563 |
1.76e-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: 97.11 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT-KESLRKHIGVVlqdvflfsgsvrdn 444
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMV-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 ialtnskitdaeliraakdvhaHQFiekldrdydeevlergsnfSTGQKQLISFARVLVYNPRILVLDEATSNI-DTETE 523
Cdd:cd03216 81 ----------------------YQL-------------------SVGERQMVEIARALARNARLLILDEPTAALtPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931518516 524 ILIqKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGRI 563
Cdd:cd03216 120 RLF-KVIRRLRAQGVAVIfISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
225-561 |
2.78e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.12 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 225 QLFNREDKNYRQFERINAdHLKAYLRTILYFSIFYPAVevlsavaITLIIWFGGldiltnNLTWGQLvgfIMAAQMFYRP 304
Cdd:COG4178 249 RRFDAVIANWRRLIRRQR-NLTFFTTGYGQLAVIFPIL-------VAAPRYFAG------EITLGGL---MQAASAFGQV 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 305 IEDLS---EKYNILQSAMASSERIFKL---LDKVDEIPDKPDAIAPAyVRGEIEFKNVWFAYKDEEWVLKDISFKVKEGE 378
Cdd:COG4178 312 QGALSwfvDNYQSLAEWRATVDRLAGFeeaLEAADALPEAASRIETS-EDGALALEDLTLRTPDGRPLLEDLSLSLKPGE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 379 KVAVVGATGAGKTTVISLLTRFYQVQKGEILidginiehitkeslRKHIGVVL---QDVFLFSGSVRDNIA--LTNSKIT 453
Cdd:COG4178 391 RLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------------RPAGARVLflpQRPYLPLGTLREALLypATAEAFS 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 454 DAELIRAAKDVHAHQFIEKLDRDYD-EEVLergsnfSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNR 532
Cdd:COG4178 457 DAELREALEAVGLGHLAERLDEEADwDQVL------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
330 340
....*....|....*....|....*....
gi 931518516 533 LMHKRTSVIIAHRLSTIKNVERIIVMHKG 561
Cdd:COG4178 531 ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
351-573 |
2.89e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.05 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQ-----VQKGEILIDG---INIEHITKES 422
Cdd:PRK11264 4 IEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDTarsLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 LRKHIGVVLQDVFLFSG-SVRDNIaLTNSKITDAElIRAAKDVHAHQFIEKLDRDYDEEVLERgsNFSTGQKQLISFARV 501
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHrTVLENI-IEGPVIVKGE-PKEEATARARELLAKVGLAGKETSYPR--RLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 502 LVYNPRILVLDEATSNIDTEteiLIQKALNRLM----HKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALF 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
351-568 |
3.93e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.03 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNV---WFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL---R 424
Cdd:PRK11153 2 IELKNIskvFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 425 KHIGVVLQDVFLFSG-SVRDNIALTnskitdAELIRAAKDvhahqFIEKldrdYDEEVLER-G---------SNFSTGQK 493
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALP------LELAGTPKA-----EIKA----RVTELLELvGlsdkadrypAQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 494 QLISFARVLVYNPRILVLDEATSNIDTET--EIL-IQKALNRLMHkRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGT 568
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATtrSILeLLKDINRELG-LTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
351-568 |
4.20e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.56 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKEslRKHIGVV 430
Cdd:PRK09452 15 VELRGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIA--LTNSKITDAELIR----AAKDVHAHQFIEKldrdydeevleRGSNFSTGQKQLISFARVLV 503
Cdd:PRK09452 92 FQSYALFPHmTVFENVAfgLRMQKTPAAEITPrvmeALRMVQLEEFAQR-----------KPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 504 YNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAH-RLSTIKNVERIIVMHKGRIREEGT 568
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
367-574 |
4.73e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 103.23 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTT----VISLLTrfyqvQKGEILIDGINIEHITKE---SLRKHIGVVLQDVFlfsG 439
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDPF---G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 440 S------VRDNIA----LTNSKITDAE---LIRAA-KDVHahqfiekLDRD----YDEEvlergsnFSTGQKQLISFARV 501
Cdd:COG4172 374 SlsprmtVGQIIAeglrVHGPGLSAAErraRVAEAlEEVG-------LDPAarhrYPHE-------FSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 502 LVYNPRILVLDEATSNIDteteILIQKA----LNRLMHKR--TSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLR 574
Cdd:COG4172 440 LILEPKLLVLDEPTSALD----VSVQAQildlLRDLQREHglAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
315-582 |
1.29e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 103.28 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 315 LQSAMASSERIFklldkvdeIPDKP-DAIAPAyvrgeIEFKNVWFAY--KDEEWVLKDISFKVKEGEKVAVVGATGAGKT 391
Cdd:PLN03130 591 LEELLLAEERVL--------LPNPPlEPGLPA-----ISIKNGYFSWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKT 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 392 TVIS-LLTRFYQVQKGEILIdginiehitkeslRKHIGVVLQDVFLFSGSVRDNIaLTNSKItDAELIRAAKDVHAhqfi 470
Cdd:PLN03130 658 SLISaMLGELPPRSDASVVI-------------RGTVAYVPQVSWIFNATVRDNI-LFGSPF-DPERYERAIDVTA---- 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 471 ekLDRDYD-------EEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTET-EILIQKALNRLMHKRTSVII 542
Cdd:PLN03130 719 --LQHDLDllpggdlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVFDKCIKDELRGKTRVLV 796
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 931518516 543 AHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIYYKL 582
Cdd:PLN03130 797 TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
367-573 |
1.31e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.49 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT----KESLRKHIGVVLQDVFLFSG-SV 441
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIA--LTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVlergsnfSTGQKQLISFARVLVYNPRILVLDEATSNID 519
Cdd:PRK10070 124 LDNTAfgMELAGINAEERREKALDALRQVGLENYAHSYPDEL-------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 520 TETEILIQKALNRLM--HKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
366-574 |
3.13e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 95.82 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHI-TKESLRKHIGVVLQDVFLFSG-SVRD 443
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 444 NIALtnskitdAELIRAAKDVHAHQFiekldrdydEEVLE-----------RGSNFSTGQKQLISFARVLVYNPRILVLD 512
Cdd:COG0410 98 NLLL-------GAYARRDRAEVRADL---------ERVYElfprlkerrrqRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 513 EAtsnidteTE----ILIQK---ALNRLMHKRTSVII-------AHRLStiknvERIIVMHKGRIREEGTHQQLLR 574
Cdd:COG0410 162 EP-------SLglapLIVEEifeIIRRLNREGVTILLveqnarfALEIA-----DRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
351-567 |
3.87e-22 |
|
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: 95.01 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHItkESLRKHIGVV 430
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIA--LTNSKITDAELIRAAKDVHAHQFIEK-LDRdydeevleRGSNFSTGQKQLISFARVLVYNP 506
Cdd:cd03301 78 FQNYALYPHmTVYDNIAfgLKLRKVPKDEIDERVREVAELLQIEHlLDR--------KPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 507 RILVLDEATSNIDTETEILIQKALNRLM--HKRTSVIIAHrlstiKNVE------RIIVMHKGRIREEG 567
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTH-----DQVEamtmadRIAVMNDGQIQQIG 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
366-567 |
4.86e-22 |
|
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: 94.59 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHitKESLRKHIGVVLQDVFLFSG-SVRDN 444
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALIEAPGFYPNlTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IaltnsKITDAELIRAAKDVHahqfiEKLDR-DYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETE 523
Cdd:cd03268 93 L-----RLLARLLGIRKKRID-----EVLDVvGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518516 524 ILIQKALNRLMHKRTSVIIA-HRLSTI-KNVERIIVMHKGRIREEG 567
Cdd:cd03268 163 KELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
351-567 |
5.68e-22 |
|
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: 94.27 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGinieHITKESLRKHIGVV 430
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNI----ALTNSKITDaelirAAKDVhaHQFIEKLD-RDYDEEVLERgsnFSTGQKQLISFARVLVY 504
Cdd:cd03269 76 PEERGLYPKmKVIDQLvylaQLKGLKKEE-----ARRRI--DEWLERLElSEYANKRVEE---LSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 505 NPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVII-AHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
365-573 |
1.09e-21 |
|
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: 94.15 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 365 WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT-KESLRKHIGVVLQDVFLFSG-SVR 442
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 443 DNI--ALTNSKITDAELIRAAKDVHAHQFIEKLdRDydeevlERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDT 520
Cdd:cd03218 94 ENIlaVLEIRGLSKKEREEKLEELLEEFHITHL-RK------SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 521 ETEILIQKALNRLMHKRTSVIIA-HRLS-TIKNVERIIVMHKGRIREEGTHQQLL 573
Cdd:cd03218 167 IAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
366-568 |
1.86e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.37 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKE---SLRKHIGVVLQDVFlfsG--- 439
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDSI---Savn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 440 ---SVRDNIALTNSKITDaeLIRAAKDVHAHQFIEKLDRDyDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATS 516
Cdd:PRK10419 104 prkTVREIIREPLRHLLS--LDKAERLARASEMLRAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 517 NIDTETEILIQKALNRLMHKRTS--VIIAHRLSTIKN-VERIIVMHKGRIREEGT 568
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVETQP 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
365-567 |
1.90e-21 |
|
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: 93.37 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 365 WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniehitKESLRKHIGVVLQDVFlfsgSVRDN 444
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------RVSSLLGLGGGFNPEL----TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IALTNS--KITDAELIRAAKDVHahQFIEkLDRDYDEEVlergSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTET 522
Cdd:cd03220 105 IYLNGRllGLSRKEIDEKIDEII--EFSE-LGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931518516 523 EiliQKALNRLMHK----RTSVIIAHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:cd03220 178 Q---EKCQRRLRELlkqgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
351-576 |
2.84e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.90 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEewvLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHiTKESLRKhIGVV 430
Cdd:COG3840 2 LRLDDLTYRYGDF---PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIAL---TNSKITDAE---LIRAAKDVhahQFIEKLDRdydeevleRGSNFSTGQKQLISFARVLV 503
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLglrPGLKLTAEQraqVEQALERV---GLAGLLDR--------LPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 504 YNPRILVLDEATSNID----TETEILIQKALNRlmHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLRKH 576
Cdd:COG3840 146 RKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
351-567 |
4.26e-21 |
|
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: 91.87 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEeWVLKDISFKVKEGeKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEhITKESLRKHIGVV 430
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDvFLFSGSVR-----DNIAL---TNSKITDAELIRAAKDVHAHQFIEKldrdydeevleRGSNFSTGQKQLISFARVL 502
Cdd:cd03264 78 PQE-FGVYPNFTvreflDYIAWlkgIPSKEVKARVDEVLELVNLGDRAKK-----------KIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 503 VYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
350-572 |
4.47e-21 |
|
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: 92.40 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 350 EIEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKESLRK-HIG 428
Cdd:cd03296 2 SIEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQErNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 VVLQDVFLFSG-SVRDNIAL------TNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVlergsnfSTGQKQLISFARV 501
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFglrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQL-------SGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 502 LVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQL 572
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
351-572 |
7.09e-21 |
|
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: 91.28 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVlKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIehiTKES--LRKHIG 428
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV---VREPreVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 VVLQDVFLFSG-SVRDNIA-------LTNSKITD--AELIRaakdvhahqFIEKLD-RDydeevlERGSNFSTGQKQLIS 497
Cdd:cd03265 77 IVFQDLSVDDElTGWENLYiharlygVPGAERREriDELLD---------FVGLLEaAD------RLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 498 FARVLVYNPRILVLDEATSNIDTETEILIQKALnRLMHKRTSVIIahrLSTIKNVE-------RIIVMHKGRIREEGTHQ 570
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI-EKLKEEFGMTI---LLTTHYMEeaeqlcdRVAIIDHGRIIAEGTPE 217
|
..
gi 931518516 571 QL 572
Cdd:cd03265 218 EL 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
351-575 |
1.26e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.22 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKE--SLRKHIG 428
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 VVLQ--DVFLFSGSVRDNIAL--TNSKITDAELIRAAKDVHAHQFIEKLdRDYDEEVLergsnfSTGQKQLISFARVLVY 504
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFgaVNLKLPEDEVRKRVDNALKRTGIEHL-KDKPTHCL------SFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 505 NPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLSTIK-NVERIIVMHKGRIREEGTHQQLLRK 575
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
351-573 |
2.00e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.69 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWV--LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKE---SLRK 425
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAEnvwNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 426 HIGVVLQ--DVFLFSGSVRDNIA--LTNSKITDAELIRAAKDvhAHQFIEKLDRDYDEEvlergSNFSTGQKQLISFARV 501
Cdd:PRK13642 82 KIGMVFQnpDNQFVGATVEDDVAfgMENQGIPREEMIKRVDE--ALLAVNMLDFKTREP-----ARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 502 LVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
351-575 |
5.71e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKD----EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKES---- 422
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 LRKHIGVVLQ--DVFLFSGSVRDNIAL--TNSKITdaelIRAAKDvHAHQFIekLDRDYDEEVLERgSNF--STGQKQLI 496
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFgpKNFKMN----LDEVKN-YAHRLL--MDLGFSRDVMSQ-SPFqmSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 497 SFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHK--RTSVIIAHRLSTI-KNVERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
..
gi 931518516 574 RK 575
Cdd:PRK13646 235 KD 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
362-574 |
5.93e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.62 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 362 DEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQkGEILIDGINIEHITKESL---RKHIGVVLQDvflfs 438
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLlpvRHRIQVVFQD----- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 439 gsvrDNIALtNSKITDAELIRAAKDVHaHQFIEKLDRD-----------YDEEVLER-GSNFSTGQKQLISFARVLVYNP 506
Cdd:PRK15134 371 ----PNSSL-NPRLNVLQIIEEGLRVH-QPTLSAAQREqqviavmeevgLDPETRHRyPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 507 RILVLDEATSNIDTETEILIQKALNRLM--HKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLR 574
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQqkHQLAYLFISHDLHVVRALcHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
37-325 |
1.03e-19 |
|
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: 90.00 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAID---NYVMPGDFDGLTIIAGLFIVIAGLNF---IFQYFHFYLMYMTGQKVMYDIRSQ 110
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDavtNHSGSGGEEALRALNQAVLILLGVVLigsIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 111 IFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAF 190
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 191 IFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQF-ERINADHLKAyLRTILYFSIFYPAVEVLSAVA 269
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYsEKINESYLLG-KKLARASGGFNGFMGAAAQLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 270 ITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18780 240 IVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
366-574 |
1.09e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDG--INIEHItKESLRKHIGVVLQD-----VFLfS 438
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSP-RDAIRAGIAYVPEDrkgegLVL-D 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 439 GSVRDNIALTN-SKITDAELI-RAAKDVHAHQFIEKLD---RDYDEEVlergSNFSTGQKQLISFARVLVYNPRILVLDE 513
Cdd:COG1129 345 LSIRENITLASlDRLSRGGLLdRRRERALAEEYIKRLRiktPSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 514 ATSNID--TETEilIQKALNRLMHKRTSVIIAhrlST-----IKNVERIIVMHKGRI-----REEGTHQQLLR 574
Cdd:COG1129 421 PTRGIDvgAKAE--IYRLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRIvgeldREEATEEAIMA 488
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
367-562 |
1.44e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIeHIT--KESLRKHIGVVLQDVFLFSG-SVRD 443
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRspRDAIALGIGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 444 NIALTNSKiTDAELIRAAKdvhAHQFIEKLDRDY------DEEVlergSNFSTGQKQLISFARVLVYNPRILVLDEATSN 517
Cdd:COG3845 100 NIVLGLEP-TKGGRLDRKA---ARARIRELSERYgldvdpDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931518516 518 I-DTETEILIqKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGR 562
Cdd:COG3845 172 LtPQEADELF-EILRRLAAEGKSIIfITHKLREVMAIaDRVTVLRRGK 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
367-567 |
1.83e-19 |
|
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: 87.35 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVK---EGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDG---------INIEhitkeSLRKHIGVVLQDV 434
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkINLP-----PQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 435 FLFSG-SVRDNIALTNSKITDAELiraaKDvhahQFIEKLDRDYDEEVLERG-SNFSTGQKQLISFARVLVYNPRILVLD 512
Cdd:cd03297 85 ALFPHlNVRENLAFGLKRKRNRED----RI----SVDELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 513 EATSNIDTETEILIQKALNRlMHKR---TSVIIAHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQ-IKKNlniPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-579 |
2.39e-19 |
|
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: 92.70 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 3 DKYSEEEVL-----GKAYDARLMKRLIHYLSPY-KMQVIYAALllvcTSIFTLARPLLTQYAID--NYVMPGDFDGLtII 74
Cdd:TIGR00957 286 DANEEVEALivkspHKPRKPSLFKVLYKTFGPYfLMSFCFKAI----HDLMMFIGPQILSLLIRfvNDPMAPDWQGY-FY 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 75 AGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTtdVDALNEMFTSGVVTIL 154
Cdd:TIGR00957 361 TGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMS--VDAQRFMDLATYINMI 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 155 GDILLLLGLATMMFVFD---AKLALITLTIMPLLFITAFIFKIKAREgfrsIRILIAKIN--SFLQENITGMKIVQLFNR 229
Cdd:TIGR00957 439 WSAPLQVILALYFLWLNlgpSVLAGVAVMVLMVPLNAVMAMKTKTYQ----VAHMKSKDNriKLMNEILNGIKVLKLYAW 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 230 EDKNYRQFERINADHLKAyLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYR-PIEDL 308
Cdd:TIGR00957 515 ELAFLDKVEGIRQEELKV-LKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRfPLNIL 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 309 SEKYNILQSAMASSERIFKLLDKvDEIpdKPDAIAPAYVR-GE---IEFKNVWFAY-KDEEWVLKDISFKVKEGEKVAVV 383
Cdd:TIGR00957 594 PMVISSIVQASVSLKRLRIFLSH-EEL--EPDSIERRTIKpGEgnsITVHNATFTWaRDLPPTLNGITFSIPEGALVAVV 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 384 GATGAGKTTVISLLTRFYQVQKGEILIDGiniehitkeslrkHIGVVLQDVFLFSGSVRDNI----ALTNSKITdaELIR 459
Cdd:TIGR00957 671 GQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENIlfgkALNEKYYQ--QVLE 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 460 AAKDVHAHQFIEKLDRdydEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKAL---NRLMHK 536
Cdd:TIGR00957 736 ACALLPDLEILPSGDR---TEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKN 812
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 931518516 537 RTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLRKHGIY 579
Cdd:TIGR00957 813 KTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
362-563 |
2.80e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 87.83 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 362 DEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFL---FS 438
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 439 GSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLdrdydeEVLERG---------SNFSTGQKQLISFARVLVYNPRIL 509
Cdd:COG1101 97 MTIEENLALAYRRGKRRGLRRGLTKKRRELFRELL------ATLGLGlenrldtkvGLLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 510 VLDEATSNIDTETEILIQKALNRL--MHKRTSVIIAHRLS-TIKNVERIIVMHKGRI 563
Cdd:COG1101 171 LLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
351-572 |
3.40e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKESL---RKHI 427
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG---EPITKENIrevRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQ--DVFLFSGSVRDNIALTNSKI-TDAELIraakdvhAHQFIEKLDRDYDEEVLERGS-NFSTGQKQLISFARVLV 503
Cdd:PRK13652 81 GLVFQnpDDQIFSPTVEQDIAFGPINLgLDEETV-------AHRVSSALHMLGLEELRDRVPhHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 504 YNPRILVLDEATSNIDTETEILIQKALNRL--MHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQL 572
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
326-565 |
3.47e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 91.19 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 326 FKLLDKVDEIPDKPDAIAPAYVRG--EIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQV 403
Cdd:PRK10522 296 FNKLNKLALAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 404 QKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSgsvrdniALTNSKITDAELIRAAKDVHAHQFIEKLDRDyDEEVLE 483
Cdd:PRK10522 376 QSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD-------QLLGPEGKPANPALVEKWLERLKMAHKLELE-DGRISN 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 484 rgSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTE-TEILIQKALNRLMHKRTSVI-IAHRLSTIKNVERIIVMHKG 561
Cdd:PRK10522 448 --LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfRREFYQVLLPLLQEMGKTIFaISHDDHYFIHADRLLEMRNG 525
|
....
gi 931518516 562 RIRE 565
Cdd:PRK10522 526 QLSE 529
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
367-579 |
6.88e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.10 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINI---EHITKESLRKHIGVVLQDVFlfsGSV-- 441
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPY---GSLnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIA-------LTNSKITDAEliRAAKdvhAHQFIEKL-------DRdYDEEvlergsnFSTGQKQLISFARVLVYNPR 507
Cdd:PRK11308 108 RKKVGqileeplLINTSLSAAE--RREK---ALAMMAKVglrpehyDR-YPHM-------FSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 508 ILVLDEATSNIDteteILIQ-KALNRLM----HKRTS-VIIAHRLSTIKNV-ERIIVMHKGRIREEGThqqllrKHGIY 579
Cdd:PRK11308 175 VVVADEPVSALD----VSVQaQVLNLMMdlqqELGLSyVFISHDLSVVEHIaDEVMVMYLGRCVEKGT------KEQIF 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
366-574 |
8.45e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.22 E-value: 8.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESlrKHIGVVLQDVFLFSG-SVRDN 444
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IA-----LTNSKITDAELIRAakdvHAHQFIEKLDRDYdeeVLER-GSNFSTGQKQLISFARVLVYNPRILVLDEATSNI 518
Cdd:PRK10851 95 IAfgltvLPRRERPNAAAIKA----KVTQLLEMVQLAH---LADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 519 DTETEILIQKALNRLmH---KRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLR 574
Cdd:PRK10851 168 DAQVRKELRRWLRQL-HeelKFTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQVWR 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
351-568 |
1.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.29 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEE-----WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGI---NIEHITKes 422
Cdd:PRK13633 5 IKCKNVSYKYESNEestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsDEENLWD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 LRKHIGVVLQ--DVFLFSGSVRDNIALTNSKI-TDAELIR-----AAKDVHAHQFiekldRDYDEEVLergsnfSTGQKQ 494
Cdd:PRK13633 83 IRNKAGMVFQnpDNQIVATIVEEDVAFGPENLgIPPEEIRervdeSLKKVGMYEY-----RRHAPHLL------SGGQKQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 495 LISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLSTIKNVERIIVMHKGRIREEGT 568
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
351-575 |
1.43e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.47 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKESLR-KHIGV 429
Cdd:PRK11432 7 VVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQqRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSG-SVRDNIA--LTNSKITDAELIRAAKDVHAHQFIEKL-DRDYDEevlergsnFSTGQKQLISFARVLVYN 505
Cdd:PRK11432 83 VFQSYALFPHmSLGENVGygLKMLGVPKEERKQRVKEALELVDLAGFeDRYVDQ--------ISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 506 PRILVLDEATSNIDTEteiliqkaLNRLMHKR----------TSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLR 574
Cdd:PRK11432 155 PKVLLFDEPLSNLDAN--------LRRSMREKirelqqqfniTSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYR 226
|
.
gi 931518516 575 K 575
Cdd:PRK11432 227 Q 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-573 |
3.21e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 84.71 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 358 FAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGI------NIEHITKESLRKHIGVVL 431
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 432 QDVFLFSG-SVRDNIA--LTNSKITDAELIRaakdvhahQFIEKLDRDYD--EEVLER----GSNFSTGQKQLISFARVL 502
Cdd:PRK14246 97 QQPNPFPHlSIYDNIAypLKSHGIKEKREIK--------KIVEECLRKVGlwKEVYDRlnspASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 503 VYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
351-576 |
3.28e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKD----EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKES---- 422
Cdd:PRK13641 3 IKFENVDYIYSPgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG---YHITPETgnkn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 ---LRKHIGVVLQ--DVFLFSGSVRDNIAL--TNSKITDAEliraAKDvHAHQFIEKLdrDYDEEVLERgSNF--STGQK 493
Cdd:PRK13641 80 lkkLRKKVSLVFQfpEAQLFENTVLKDVEFgpKNFGFSEDE----AKE-KALKWLKKV--GLSEDLISK-SPFelSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 494 QLISFARVLVYNPRILVLDEATSNIDTET-EILIQKALNRLMHKRTSVIIAHRLSTI-KNVERIIVMHKGRI------RE 565
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLikhaspKE 231
|
250
....*....|.
gi 931518516 566 EGTHQQLLRKH 576
Cdd:PRK13641 232 IFSDKEWLKKH 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
351-568 |
3.42e-18 |
|
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: 87.94 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLL--TRFYQVQKGEIL------------------- 409
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 410 --------------IDGINIEHITKESLRKHIGVVLQDVFLFSG--SVRDNI--ALTNSKITDAELIRAAKD----VHAH 467
Cdd:TIGR03269 80 epcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVleALEEIGYEGKEAVGRAVDliemVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 468 QFIEKLDRDydeevlergsnFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHR 545
Cdd:TIGR03269 160 HRITHIARD-----------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHW 228
|
250 260
....*....|....*....|....
gi 931518516 546 LSTIKNV-ERIIVMHKGRIREEGT 568
Cdd:TIGR03269 229 PEVIEDLsDKAIWLENGEIKEEGT 252
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
349-602 |
3.58e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.06 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 349 GEIEFKNVWFAYKD----EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDG----INIEHITK 420
Cdd:PRK13645 5 KDIILDNVSYTYAKktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 421 -ESLRKHIGVVLQ--DVFLFSGSVRDNIALTNSKItDAELIRAAKDVHAHQFIEKLDRDYdeeVLERGSNFSTGQKQLIS 497
Cdd:PRK13645 85 vKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 498 FARVLVYNPRILVLDEATSNIDTETE---ILIQKALNRLMHKRTsVIIAHRLSTIKNV-ERIIVMHKGRIREEG------ 567
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEedfINLFERLNKEYKKRI-IMVTHNMDQVLRIaDEVIVMHEGKVISIGspfeif 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 931518516 568 THQQLLRKHGIY-YKLYQLQYRDQETGVNaVANHNV 602
Cdd:PRK13645 240 SNQELLTKIEIDpPKLYQLMYKLKNKGID-LLNKNI 274
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
366-565 |
9.44e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGSVRDNI 445
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 446 ALtnskitdAELIRaAKDVHAHQFIEKLDR-DYDEEVLERGSN-FSTGQKQLISFARVLVYNPRILVLDEATSNIDTETE 523
Cdd:PRK10247 102 IF-------PWQIR-NQQPDPAIFLDDLERfALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518516 524 ILIQKALNRLM-HKRTSVI-IAHRLSTIKNVERIIVM--HKGRIRE 565
Cdd:PRK10247 174 HNVNEIIHRYVrEQNIAVLwVTHDKDEINHADKVITLqpHAGEMQE 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
366-563 |
1.27e-17 |
|
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: 80.94 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT-KESLRKHIGVVLQD-----VFLfSG 439
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDrkregLVL-DL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 440 SVRDNIALTNSkitdaeliraakdvhahqfiekldrdydeevlergsnFSTGQKQLISFARVLVYNPRILVLDEATSNID 519
Cdd:cd03215 94 SVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931518516 520 TETEILIQKALNRLMHKRTSVIIahrLST-----IKNVERIIVMHKGRI 563
Cdd:cd03215 137 VGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
360-568 |
1.49e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.44 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 360 YKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGIN---IEhitkeslrkhIGVVLQDVFl 436
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsalLE----------LGAGFHPEL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 437 fsgSVRDNIALtNSKI---TDAELIRAAKDVHA----HQFIekldrdyDEEVlergSNFSTGQKQLISFARVLVYNPRIL 509
Cdd:COG1134 104 ---TGRENIYL-NGRLlglSRKEIDEKFDEIVEfaelGDFI-------DQPV----KTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 510 VLDEATSNIDTEteiLIQKALNRLM----HKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGT 568
Cdd:COG1134 169 LVDEVLAVGDAA---FQKKCLARIRelreSGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGD 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
363-563 |
1.49e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 81.93 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 363 EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQK---GEILIDGiniEHITKESLRKHIGVVLQDVFLFSG 439
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNG---QPRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 440 -SVRDNIALTN-------------SKITDAELIRAAKDVH-AHQFIEKLdrdydeevlergsnfSTGQKQLISFARVLVY 504
Cdd:cd03234 96 lTVRETLTYTAilrlprkssdairKKRVEDVLLRDLALTRiGGNLVKGI---------------SGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 505 NPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-H--RLSTIKNVERIIVMHKGRI 563
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
363-573 |
2.54e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 363 EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITK-------------ESLRKHIGV 429
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSG-SVRDNIalTNSKITDAELIRAAKDVHAHQFIEKLDRDyDEEVLERGSNFSTGQKQLISFARVLVYNPRI 508
Cdd:PRK10619 97 VFQHFNLWSHmTVLENV--MEAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 509 LVLDEATSNIDTEteiLIQKALnRLMHK-----RTSVIIAHRLSTIKNVE-RIIVMHKGRIREEGTHQQLL 573
Cdd:PRK10619 174 LLFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHVSsHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
369-567 |
2.74e-17 |
|
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: 81.00 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 369 DISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGinIEHITKESLRKHIGVVLQDVFLFSG-SVRDNIAL 447
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRPVSMLFQENNLFAHlTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 448 TNS---KITDAEliRAAKDVHAHQFiekldrDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEI 524
Cdd:cd03298 94 GLSpglKLTAED--RQAIEVALARV------GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518516 525 LIQKALNRLMHKR--TSVIIAHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:cd03298 166 EMLDLVLDLHAETkmTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
366-568 |
4.32e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT---KESLRKH-IGVVLQdvflFSGSV 441
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQ----FHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIALTN-------SKITDAELIRAAKDVHAHQFIEKldRDYdeevlERGSNFSTGQKQLISFARVLVYNPRILVLDEA 514
Cdd:PRK11629 100 PDFTALENvamplliGKKKPAEINSRALEMLAAVGLEH--RAN-----HRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 515 TSNIDTETEILIQKALNRLMHKRTS--VIIAHRLSTIKNVERIIVMHKGRIREEGT 568
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
367-562 |
5.25e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQV--QKGEILIDG--INIEHItKESLRKHIGVVLQDVFLFSG-SV 441
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGeeLQASNI-RDTERAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIALTNsKITDAELIRAAKDVH-AHQFIEKLDRDYDeeVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNI-D 519
Cdd:PRK13549 100 LENIFLGN-EITPGGIMDYDAMYLrAQKLLAQLKLDIN--PATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518516 520 TETEIL--IQKALNRlmHKRTSVIIAHRLSTIKNV-ERIIVMHKGR 562
Cdd:PRK13549 177 SETAVLldIIRDLKA--HGIACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
33-325 |
5.43e-17 |
|
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: 81.82 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 33 QVIYAALLLvctSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIF 112
Cdd:cd18779 6 QILLASLLL---QLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 113 KHLQRLSLSFFDKTPIGRLVTRLTTDVdALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMpLLFITAFIF 192
Cdd:cd18779 83 EHLLRLPYRFFQQRSTGDLLMRLSSNA-TIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLA-ALQVALLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 193 kikareGFRSIRILI-------AKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVL 265
Cdd:cd18779 161 ------TRRRVRELMarelaaqAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 266 SAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18779 235 RLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
351-575 |
5.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.71 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKD----EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITK----ES 422
Cdd:PRK13649 3 INLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 LRKHIGVVLQ--DVFLFSGSVRDNIAL--TNSKITDAELIRAAKdvhahqfiEKLDR-DYDEEVLERGS-NFSTGQKQLI 496
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFgpQNFGVSQEEAEALAR--------EKLALvGISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 497 SFARVLVYNPRILVLDEATSNIDTETeiliQKALNRLMHK-----RTSVIIAHRLSTIKN-VERIIVMHKGRIREEGTHQ 570
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKG----RKELMTLFKKlhqsgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPK 230
|
....*
gi 931518516 571 QLLRK 575
Cdd:PRK13649 231 DIFQD 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
371-573 |
7.15e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 371 SFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINieHITKESLRKHIGVVLQDVFLFSG-SVRDNIAL-- 447
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 448 -TNSKITDAE---LIRAAKDVHAHQFIEKLDrdydeevlergSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTE-- 521
Cdd:PRK10771 97 nPGLKLNAAQrekLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAlr 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 522 -------TEILIQKALNRLM--HkrtSVIIAHRLSTiknveRIIVMHKGRIREEGTHQQLL 573
Cdd:PRK10771 166 qemltlvSQVCQERQLTLLMvsH---SLEDAARIAP-----RSLVVADGRIAWDGPTDELL 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
367-561 |
7.60e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT-KESLRKHIGVVLQDVFLFSG-SVRDN 444
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 I---ALTNSKITDAELIRAAK-DVHAHQFIEKLD--RDYDEEVlergSNFSTGQKQLISFARVLVYNPRILVLDEATSNI 518
Cdd:PRK09700 101 LyigRHLTKKVCGVNIIDWREmRVRAAMMLLRVGlkVDLDEKV----ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518516 519 -DTETEILIQkALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKG 561
Cdd:PRK09700 177 tNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRIcDRYTVMKDG 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
370-572 |
1.48e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.65 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 370 ISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHiGVV--LQDVFLF-SGSVRDNIA 446
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVrtFQHVRLFrEMTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 447 LTNSKITDAELIRAAKDVHAHQFIEKLDRDYDEEVLER----------GSNFSTGQKQLISFARVLVYNPRILVLDEATS 516
Cdd:PRK11300 103 VAQHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLERvgllehanrqAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 517 NID-TETEILIQK-ALNRLMHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQL 572
Cdd:PRK11300 183 GLNpKETKELDELiAELRNEHNVTVLLIEHDMKLVMGIsDRIYVVNQGTPLANGTPEEI 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
351-570 |
1.78e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDG--INIEHITKE----SLR 424
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDkairELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 425 KHIGVVLQDVFLFSG-SVRDNialtnskitdaeLIRA-------AKDVHAHQFIEKLDRDYDEEVLERGS-NFSTGQKQL 495
Cdd:PRK11124 82 RNVGMVFQQYNLWPHlTVQQN------------LIEApcrvlglSKDQALARAEKLLERLRLKPYADRFPlHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 496 ISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR-TSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQ 570
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTaSRVVYMENGHIVEQGDAS 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
369-573 |
1.88e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 369 DISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQK-GEILIDG--INIEHiTKESLRKHIGVVLQD------VFLFSg 439
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGkpVKIRN-PQQAIAQGIAMVPEDrkrdgiVPVMG- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 440 sVRDNIALTN-SKITDAELIRAAKDVH-AHQFIEKLDRDYDEEVLERGsNFSTGQKQLISFARVLVYNPRILVLDEATSN 517
Cdd:PRK13549 358 -VGKNITLAAlDRFTGGSRIDDAAELKtILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 518 IDTETEILIQKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGRIR-----EEGTHQQLL 573
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQGVAIIvISSELPEVLGLsDRVLVMHEGKLKgdlinHNLTQEQVM 498
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
366-572 |
2.12e-16 |
|
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: 79.90 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEIlidginiehitKESLRkhIGVVLQDVFLFSGSVRDNI 445
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGR--ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 446 ALTNSkitdAELIRAAKDVHAHQFIEKLDR--DYDEEVL-ERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNID--T 520
Cdd:cd03291 119 IFGVS----YDEYRYKSVVKACQLEEDITKfpEKDNTVLgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 521 ETEILiQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQL 572
Cdd:cd03291 195 EKEIF-ESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
36-325 |
2.40e-16 |
|
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: 79.66 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 36 YAALLLVCTS-IFTlarPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKH 114
Cdd:cd18784 2 FFFLLAAAVGeIFI---PYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 115 LQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKI 194
Cdd:cd18784 79 IVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 195 KAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLII 274
Cdd:cd18784 159 YYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 931518516 275 WFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18784 239 YYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
366-563 |
2.74e-16 |
|
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: 78.53 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiNIEHITKESLRKHIGVVLqdvflfsGSvRDNI 445
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVF-------GQ-KTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 446 ALTNSKITDAELIRAAKDVHAHQFIEKLDRDYD----EEVLERG-SNFSTGQKQLISFARVLVYNPRILVLDEATSNIDT 520
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPPARFKKRLDELSElldlEELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518516 521 ETEILIQKALNRLMHKRTSVII--AHRLSTIKNV-ERIIVMHKGRI 563
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLltSHYMKDIEALaRRVLVIDKGRL 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
353-522 |
2.82e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 353 FKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniehitkeslRKHIGVVLQ 432
Cdd:COG0488 1 LENLSKSFGGRP-LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 433 DVFLFSG-SVRDNI----------------ALTNSKITDAELIRAAK------DVHAHQF---IEKL-------DRDYDE 479
Cdd:COG0488 69 EPPLDDDlTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAElqeefeALGGWEAearAEEIlsglgfpEEDLDR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931518516 480 EVlergSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTET 522
Cdd:COG0488 149 PV----SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-567 |
3.28e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.80 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 348 RGEIEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQ-----KGEILIDGINIEHITKES 422
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 LRKHIGVVLQ-DVFLFSGSVRDNIALtNSKITdaELIRAAKDVHAH--QFIEKldRDYDEEVLER----GSNFSTGQKQL 495
Cdd:PRK14247 80 LRRRVQMVFQiPNPIPNLSIFENVAL-GLKLN--RLVKSKKELQERvrWALEK--AQLWDEVKDRldapAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 496 ISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWG 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
333-572 |
3.85e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.65 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 333 DEIPdKPDAIAPAYVRGEIEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDG 412
Cdd:PRK11607 3 DAIP-RPQAKTRKALTPLLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 413 INIEHITkeSLRKHIGVVLQDVFLFSG-SVRDNIA--LTNSKITDAELIRAAKD----VHAHQFIEKldrdydeevleRG 485
Cdd:PRK11607 81 VDLSHVP--PYQRPINMMFQSYALFPHmTVEQNIAfgLKQDKLPKAEIASRVNEmlglVHMQEFAKR-----------KP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 486 SNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHK--RTSVIIAH-RLSTIKNVERIIVMHKGR 562
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGK 227
|
250
....*....|
gi 931518516 563 IREEGTHQQL 572
Cdd:PRK11607 228 FVQIGEPEEI 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
77-572 |
4.04e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 82.27 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 77 LFIViaglNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEmftsGVVTILGD 156
Cdd:TIGR01271 131 LFIV----RTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDE----GLALAHFV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 157 ILLLLGLATMM---------FVFDAKLALITLTIMPLLFITAFIFKIKAREGFRSIRILIAkinSFLQENITGMKIvqlF 227
Cdd:TIGR01271 203 WIAPLQVILLMgliwellevNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAIT---SEIIENIQSVKA---Y 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 228 NREDKNYRQFERINADHLK-----AYLRTILYFSIFYPA--VEVLSAVAITLIIWFGGLDILTN---NLTWGQLVG--FI 295
Cdd:TIGR01271 277 CWEEAMEKIIKNIRQDELKltrkiAYLRYFYSSAFFFSGffVVFLSVVPYALIKGIILRRIFTTisyCIVLRMTVTrqFP 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 296 MAAQMFY------RPIEDLSEK-------YNI------LQSAMAS-SERIFKLLDKVdeipdKPDAIAPAYVRGE--IEF 353
Cdd:TIGR01271 357 GAIQTWYdslgaiTKIQDFLCKeeyktleYNLttteveMVNVTASwDEGIGELFEKI-----KQNNKARKQPNGDdgLFF 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 354 KNVWFAYKDeewVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEIlidginiehitKESLRkhIGVVLQD 433
Cdd:TIGR01271 432 SNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGR--ISFSPQT 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 434 VFLFSGSVRDNIALTNSkitdAELIRAAKDVHAHQFIEKLDR--DYDEEVL-ERGSNFSTGQKQLISFARVLVYNPRILV 510
Cdd:TIGR01271 496 SWIMPGTIKDNIIFGLS----YDEYRYTSVIKACQLEEDIALfpEKDKTVLgEGGITLSGGQRARISLARAVYKDADLYL 571
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 511 LDEATSNID--TETEILiQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQL 572
Cdd:TIGR01271 572 LDSPFTHLDvvTEKEIF-ESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
354-573 |
4.07e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.01 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 354 KNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHIT-KESLRKHIGVVLQ 432
Cdd:PRK10895 7 KNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 433 DVFLFSG-SVRDNIaLTNSKITDaELIRAAKDVHAHQFIEKLDRDYDEEVLerGSNFSTGQKQLISFARVLVYNPRILVL 511
Cdd:PRK10895 86 EASIFRRlSVYDNL-MAVLQIRD-DLSAEQREDRANELMEEFHIEHLRDSM--GQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 512 DEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRL-STIKNVERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
366-544 |
1.21e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.05 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESlrkhiGVVLQDVFLFS-GSVRDN 444
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IALtnsKITDAELIRAAKDVHAHQFIEKLDRDYDEEvlERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEI 524
Cdd:PRK11248 91 VAF---GLQLAGVEKMQRLEIAHQMLKKVGLEGAEK--RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180
....*....|....*....|..
gi 931518516 525 LIQKALNRLMHK--RTSVIIAH 544
Cdd:PRK11248 166 QMQTLLLKLWQEtgKQVLLITH 187
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
350-567 |
1.25e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.82 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 350 EIEFKNVWFAYKD----EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEI--LIDGINIEHITKE-- 421
Cdd:PRK13651 2 QIKVKNIVKIFNKklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 422 --------------------SLRKHIGVVLQ--DVFLFSGSVRDNIAL--TNSKITDAELIRAAKDvhahqFIEKLdrDY 477
Cdd:PRK13651 82 kvleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFgpVSMGVSKEEAKKRAAK-----YIELV--GL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 478 DEEVLERGS-NFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRL-STIKNVER 554
Cdd:PRK13651 155 DESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLdNVLEWTKR 234
|
250
....*....|...
gi 931518516 555 IIVMHKGRIREEG 567
Cdd:PRK13651 235 TIFFKDGKIIKDG 247
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
351-567 |
1.48e-15 |
|
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: 75.64 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRF--YQVQKGEILIDGINIEHI-TKESLRKHI 427
Cdd:cd03217 1 LEIKDLHVSVGGKE-ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLpPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSGsvrdnialtnskITDAELIraakdvhahqfiekldRDYDEevlergsNFSTGQKQLISFARVLVYNPR 507
Cdd:cd03217 80 FLAFQYPPEIPG------------VKNADFL----------------RYVNE-------GFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKRTSV-IIAH--RLSTIKNVERIIVMHKGRIREEG 567
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-590 |
1.56e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.46 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKESlRKHIG-------------VVLQ 432
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED-RRRIGylpeerglypkmkVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 433 DVFLfsGSVRDnialtnskITDAELIRAAKDvhahqFIEKLD-RDYDEEVLErgsNFSTGQKQLISFARVLVYNPRILVL 511
Cdd:COG4152 92 LVYL--ARLKG--------LSKAEAKRRADE-----WLERLGlGDRANKKVE---ELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 512 DEATS-----NIDteteiLIQKALNRLMHKRTSVIIA-HRLStikNVER----IIVMHKGRIREEGTHQQLLRKHGiyYK 581
Cdd:COG4152 154 DEPFSgldpvNVE-----LLKDVIRELAAKGTTVIFSsHQME---LVEElcdrIVIINKGRKVLSGSVDEIRRQFG--RN 223
|
....*....
gi 931518516 582 LYQLQYRDQ 590
Cdd:COG4152 224 TLRLEADGD 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-561 |
1.72e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQkGEILIDG--------INIEHITKES 422
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 LRKHIGVVLQDVFLFSGSVRDNIALtnskitDAELIRAAKDVHAHQFIEKLDRD---YDE---EVLERGSNFSTGQKQLI 496
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAY------GVKIVGWRPKLEIDDIVESALKDadlWDEikhKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 497 SFARVLVYNPRILVLDEATSNID----TETEILIQKAlnRLMHKRTSVIIAHRLSTIKNVERIIVMHKG 561
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSL--RLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
351-575 |
2.09e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.08 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEE----WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKES---- 422
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 LRKHIGVVLQ--DVFLFSGSVRDNIAL--TNSKITDAELIRAAKdvhahqfiEKLDR-DYDEEVLERGS-NFSTGQKQLI 496
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFgpQNFGIPKEKAEKIAA--------EKLEMvGLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 497 SFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHK-RTSVIIAHRLSTIKN-VERIIVMHKGRIREEGTHQQLLR 574
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
.
gi 931518516 575 K 575
Cdd:PRK13643 234 E 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
350-572 |
3.86e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.67 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 350 EIEFKNVWFAYKDEEwvLK---DISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL--- 423
Cdd:PRK15079 19 DIKDGKQWFWQPPKT--LKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWrav 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 424 RKHIGVVLQdvflfsgsvrDNIALTNSKITDAELIraAKDVHAHQfiEKLDRdydEEVLERGSN---------------- 487
Cdd:PRK15079 97 RSDIQMIFQ----------DPLASLNPRMTIGEII--AEPLRTYH--PKLSR---QEVKDRVKAmmlkvgllpnlinryp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 488 --FSTGQKQLISFARVLVYNPRILVLDEATSNIDteteILIQ-------KALNRLMhkRTSVI-IAHRLSTIKNV-ERII 556
Cdd:PRK15079 160 heFSGGQCQRIGIARALILEPKLIICDEPVSALD----VSIQaqvvnllQQLQREM--GLSLIfIAHDLAVVKHIsDRVL 233
|
250
....*....|....*.
gi 931518516 557 VMHKGRIREEGTHQQL 572
Cdd:PRK15079 234 VMYLGHAVELGTYDEV 249
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
360-546 |
3.89e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.58 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 360 YKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQ-----KGEILIDGINIEHITKES--LRKHIGVVLQ 432
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 433 DVFLFSGSVRDNI--ALTNSKITDAELIRAAKD---VHAHQFIEKLDRDYDEEVlergsNFSTGQKQLISFARVLVYNPR 507
Cdd:PRK14239 94 QPNPFPMSIYENVvyGLRLKGIKDKQVLDEAVEkslKGASIWDEVKDRLHDSAL-----GLSGGQQQRVCIARVLATSPK 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRL 546
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
370-574 |
3.93e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.31 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 370 ISFKVKEGEKVAVVGATGAGKTTVISLLTRF-------YQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFLFS-GSV 441
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVleptsgeVNVRVGDEWVDMTKPGPDGRGRAKRYIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIALTNSKITDAELIRaAKDVHAHQFIeKLDRDYDEEVLER-GSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDT 520
Cdd:TIGR03269 383 LDNLTEAIGLELPDELAR-MKAVITLKMV-GFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 521 ETEILIQKAlnrLMHKR-----TSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLR 574
Cdd:TIGR03269 461 ITKVDVTHS---ILKAReemeqTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEIVE 517
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
324-575 |
4.33e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 324 RIfKLLDKVDEIpDKPDAIAPAYVRGE---------IEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVI 394
Cdd:COG0488 282 RI-KALEKLERE-EPPRRDKTVEIRFPpperlgkkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 395 SLLTRFYQVQKGEILIdGINIEhitkeslrkhIGVVLQDVFLFSG--SVRDNIaltnskitdAELIRAAKDVHAHQFIEK 472
Cdd:COG0488 359 KLLAGELEPDSGTVKL-GETVK----------IGYFDQHQEELDPdkTVLDEL---------RDGAPGGTEQEVRGYLGR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 473 LDRDYDeEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTET-EILIQkALNRlmHKRTSVIIAH-R--LST 548
Cdd:COG0488 419 FLFSGD-DAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETlEALEE-ALDD--FPGTVLLVSHdRyfLDR 494
|
250 260
....*....|....*....|....*...
gi 931518516 549 IknVERIIVMHKGRIRE-EGTHQQLLRK 575
Cdd:COG0488 495 V--ATRILEFEDGGVREyPGGYDDYLEK 520
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-573 |
5.30e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 340 DAIAPAYVRGEIefkNVWFAYKDeewVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRF------YQVQkGEILIDGI 413
Cdd:PRK14271 16 DAAAPAMAAVNL---TLGFAGKT---VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRYS-GDVLLGGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 414 NI-EHITKESLRKHIGVVLQDVFLFSGSVRDNI----------------ALTNSKITDAELIRAAKDvhahqfiekldrd 476
Cdd:PRK14271 89 SIfNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVlagvrahklvprkefrGVAQARLTEVGLWDAVKD------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 477 ydeEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNV-ERI 555
Cdd:PRK14271 156 ---RLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRA 232
|
250
....*....|....*...
gi 931518516 556 IVMHKGRIREEGTHQQLL 573
Cdd:PRK14271 233 ALFFDGRLVEEGPTEQLF 250
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
365-576 |
6.71e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.68 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 365 WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINiehITKESL----RKHIGVVLQDVFLFSG- 439
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED---ITHLPMhkraRLGIGYLPQEASIFRKl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 440 SVRDNI--ALTNSKITDAEliRAAK-DVHAHQF-IEKLdRDYdeevleRGSNFSTGQKQLISFARVLVYNPRILVLDEAT 515
Cdd:COG1137 94 TVEDNIlaVLELRKLSKKE--REERlEELLEEFgITHL-RKS------KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 516 SNIDTETEILIQKALNRLMHKRTSVIIA-H--RlSTIKNVERIIVMHKGRIREEGTHQQLL-----RKH 576
Cdd:COG1137 165 AGVDPIAVADIQKIIRHLKERGIGVLITdHnvR-ETLGICDRAYIISEGKVLAEGTPEEILnnplvRKV 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
366-563 |
6.80e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.84 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL----RKHIGVVLQDVFLFSGSV 441
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 rdniALTNSKITD--AELIRAAKDVHAHQFIEKLdrDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNID 519
Cdd:PRK10535 103 ----AAQNVEVPAvyAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 931518516 520 T---ETEILIQKALNRLMHkrTSVIIAHRLSTIKNVERIIVMHKGRI 563
Cdd:PRK10535 177 ShsgEEVMAILHQLRDRGH--TVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
367-589 |
6.90e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.89 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIeHITKESLRKHIGVV-------LQDVflfsg 439
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP-FKRRKEFARRIGVVfgqrsqlWWDL----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 440 SVRDNIaltnskitdaELIRAAKDVHAHQFIEKLdrDYDEEVLERGS-------NFSTGQKQLISFARVLVYNPRILVLD 512
Cdd:COG4586 112 PAIDSF----------RLLKAIYRIPDAEYKKRL--DELVELLDLGElldtpvrQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 513 EATSNIDTETEILIQKALNRLMHKR-TSVIIA-HRLSTIKNV-ERIIVMHKGRIREEGTHQQLLRKHGiYYKLYQLQYRD 589
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFG-PYKTIVLELAE 258
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
351-545 |
8.60e-15 |
|
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: 72.19 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniehitkeslRKHIGVV 430
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSGSVRDNIALTNSKItdaeliraakdvhahqfiekldrdydeevlergsnFSTGQKQLISFARVLVYNPRILV 510
Cdd:cd03223 70 PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 931518516 511 LDEATSNIDTETEILIQKALNRLMhkrTSVI-IAHR 545
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELG---ITVIsVGHR 147
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
366-574 |
1.04e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.90 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDginiehitkeslrKHIGVVLQDVFLFSGSVRDNI 445
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 446 ALTNSKitDAEliRAAKDVHAHQF---IEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTET 522
Cdd:PTZ00243 742 LFFDEE--DAA--RLADAVRVSQLeadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518516 523 -EILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQLLR 574
Cdd:PTZ00243 818 gERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
355-567 |
1.06e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.66 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 355 NVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKE--SLRKHIGVVLQ 432
Cdd:PRK13638 6 DLWFRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 433 D--VFLFSGSVRDNIA--LTNSKITDAELIRAAKD----VHAHQFiekldRDYDEEVLergsnfSTGQKQLISFARVLVY 504
Cdd:PRK13638 85 DpeQQIFYTDIDSDIAfsLRNLGVPEAEITRRVDEaltlVDAQHF-----RHQPIQCL------SHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 505 NPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVII-AHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEIsDAVYVLRQGQILTHG 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
367-574 |
1.25e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHI-TKESLRKHIGVVLQDVFLFSG-SVRDN 444
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAsTTAALAAGVAIIYQELHLVPEmTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IAL----TNSKITDAELIRAakdvHAHQFIEKLDRDYDEEvlERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDT 520
Cdd:PRK11288 100 LYLgqlpHKGGIVNRRLLNY----EAREQLEHLGVDIDPD--TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 521 -ETEILIqKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGR-IR-----EEGTHQQLLR 574
Cdd:PRK11288 174 rEIEQLF-RVIRELRAEGRVILyVSHRMEEIFALcDAITVFKDGRyVAtfddmAQVDRDQLVQ 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
366-573 |
1.46e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFL-FSGSVRDN 444
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IAL----------TNSKITDAELIRAAKDVHAHQFIeklDRDYDEevlergsnFSTGQKQLISFARVLVYNPRILVLDEA 514
Cdd:PRK09536 98 VEMgrtphrsrfdTWTETDRAAVERAMERTGVAQFA---DRPVTS--------LSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 515 TSNIDTETEILIQKALNRLMHK-RTSVIIAHRLS-TIKNVERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
37-325 |
1.62e-14 |
|
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: 74.24 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQ 116
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 117 RLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIKA 196
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 197 REGFRSIRILIAKINSFLQENITGMKIVQLFNREDknyRQFERINADHLKAYLRTI--LYFSIFYPAV-EVLSAVAITLI 273
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASK---RRGNELAARAEDLRQATMkvLAVSLLSSGImGLATALGTALA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 274 IWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18561 238 LGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
354-579 |
1.63e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 354 KNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTrFYQ---VQK-GEILIDGiniEHITKESLRKHIGV 429
Cdd:TIGR00955 28 RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSpkgVKGsGSVLLNG---MPIDAKEMRAISAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQ-DVFLFSGSVRDNIALTnskitdAELiRAAKDVHAHQFIEKLDrdydeEVLE----------------RGSNFSTGQ 492
Cdd:TIGR00955 104 VQQdDLFIPTLTVREHLMFQ------AHL-RMPRRVTKKEKRERVD-----EVLQalglrkcantrigvpgRVKGLSGGE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 493 KQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLST--IKNVERIIVMHKGRIREEGTH 569
Cdd:TIGR00955 172 RKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGSP 251
|
250
....*....|...
gi 931518516 570 QQL---LRKHGIY 579
Cdd:TIGR00955 252 DQAvpfFSDLGHP 264
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
351-561 |
4.25e-14 |
|
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: 71.59 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL----RKH 426
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 427 IGVVLQDVFLFSGSVRDNIALTNSkiTDAELIRAAKDVHAHQ-FIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYN 505
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSP--FNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 506 PRILVLDEATSNIDTE-TEILIQKALNRLMH--KRTSVIIAHRLSTIKNVERIIVMHKG 561
Cdd:cd03290 159 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-576 |
4.45e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.71 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKeSLRKHIGVV 430
Cdd:PRK13536 42 IDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-LARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQ-DVFLFSGSVRDNIALTNSKITdaeliRAAKDVHA--HQFIE--KLDRDYDEEVlergSNFSTGQKQLISFARVLVYN 505
Cdd:PRK13536 120 PQfDNLDLEFTVRENLLVFGRYFG-----MSTREIEAviPSLLEfaRLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 506 PRILVLDEATSNIDTETEILIQKALNRLMHKRTSVII-------AHRLstiknVERIIVMHKGRIREEGTHQQLLRKH 576
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
351-563 |
4.47e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKeSLRKHIGVV 430
Cdd:PRK15439 12 LCARSISKQYSGVE-VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 L--QDVFLFSG-SVRDNIA--LTNSKITDAELIRAAKDVHAHqfiekLDRDYDEEVLErgsnfsTGQKQLISFARVLVYN 505
Cdd:PRK15439 90 LvpQEPLLFPNlSVKENILfgLPKRQASMQKMKQLLAALGCQ-----LDLDSSAGSLE------VADRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 506 PRILVLDEATSNID-TETEILIQKaLNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGRI 563
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSR-IRELLAQGVGIVfISHKLPEIRQLaDRISVMRDGTI 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
362-579 |
4.59e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.35 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 362 DEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINI-----------EHITKE-----SLRK 425
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhelitNPYSKKiknfkELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 426 HIGVVLQ--DVFLFSGSVRDNI-----ALTNSKITDAELiraakdvhAHQFIEKLDRDYDeeVLERGS-NFSTGQKQLIS 497
Cdd:PRK13631 117 RVSMVFQfpEYQLFKDTIEKDImfgpvALGVKKSEAKKL--------AKFYLNKMGLDDS--YLERSPfGLSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 498 FARVLVYNPRILVLDEATSNIDTETE-ILIQKALNRLMHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLRK 575
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTPYEIFTD 266
|
....
gi 931518516 576 HGIY 579
Cdd:PRK13631 267 QHII 270
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
351-577 |
4.60e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.37 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRF--YQVQKGEILIDGINIEHITKEsLRKHIG 428
Cdd:CHL00131 8 LEIKNLHASVNENE-ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 VVL--QDVFLFSGsvrdnialtnskITDAELIRAA----------KDVHAHQFIE----KLDR-DYDEEVLERGSN--FS 489
Cdd:CHL00131 86 IFLafQYPIEIPG------------VSNADFLRLAynskrkfqglPELDPLEFLEiineKLKLvGMDPSFLSRNVNegFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 490 TGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTS-VIIAH--RLSTIKNVERIIVMHKGRIREE 566
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSiILITHyqRLLDYIKPDYVHVMQNGKIIKT 233
|
250
....*....|...
gi 931518516 567 GTHQ--QLLRKHG 577
Cdd:CHL00131 234 GDAElaKELEKKG 246
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
367-562 |
5.94e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.48 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQ--VQKGEILIDG--INIEHItKESLRKHIGVVLQDVFLFSG-SV 441
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGspLKASNI-RDTERAGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIALTNSKITDAELIRAAKDVH-AHQFIEKLDRDYDEEVLERGsNFSTGQKQLISFARVLVYNPRILVLDEATSNI-D 519
Cdd:TIGR02633 96 AENIFLGNEITLPGGRMAYNAMYLrAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSSSLtE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 931518516 520 TETEILIQKALNRLMHKRTSVIIAHRLSTIKNV-ERIIVMHKGR 562
Cdd:TIGR02633 175 KETEILLDIIRDLKAHGVACVYISHKLNEVKAVcDTICVIRDGQ 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
367-561 |
6.40e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 70.35 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLT--RFYQVQKGEILIDGINIehitKESLRKHIGVVLQ-DVFLFSGSVRD 443
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPL----DKNFQRSTGYVEQqDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 444 NIaltnskitdaeliraakdvhahQFIEKLdrdydeevleRGsnFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETE 523
Cdd:cd03232 99 AL----------------------RFSALL----------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931518516 524 ILIQKALNRL-MHKRTSVIIAHRLS--TIKNVERIIVMHKG 561
Cdd:cd03232 145 YNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
34-325 |
7.10e-14 |
|
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: 72.54 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDG---LTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDirsQ 110
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSgyyLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHD---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 111 IFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVvtilgdillllgLATMMFVFD--AKLALIT-------LTI 181
Cdd:cd18580 78 LLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLAL------------LDFLQSLFSvlGSLIVIAivspyflIVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 182 MPLLFITAFIFK--IKARegfRSIRIL--IAK--INSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLrtiLYF 255
Cdd:cd18580 146 PPLLVVYYLLQRyyLRTS---RQLRRLesESRspLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFY---LLL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 256 SI-----FYpaVEVLSAVAITLIIWFGgldILTNNLTWGQLVGF-----IMAAQMFYRPIEDLSEkyniLQSAMASSERI 325
Cdd:cd18580 220 AVqrwlgLR--LDLLGALLALVVALLA---VLLRSSISAGLVGLaltyaLSLTGSLQWLVRQWTE----LETSMVSVERI 290
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
366-563 |
7.58e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHItkeslRKHIGVVLQDVFLFS-GSVRDN 444
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IALTnskitdaelIRAAKDVHAHQFIEKL---DRdydeeVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTE 521
Cdd:PRK11247 102 VGLG---------LKGQWRDAALQALAAVglaDR-----ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931518516 522 TEILIQKALNRL--MHKRTSVIIAHRLS-TIKNVERIIVMHKGRI 563
Cdd:PRK11247 168 TRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
33-305 |
7.65e-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: 72.55 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 33 QVIYAALLLvctSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVmyDIR--SQ 110
Cdd:cd18783 6 DVAIASLIL---HVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRI--DARlaLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 111 IFKHLQRLSLSFFDKTPIGRLvTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAF 190
Cdd:cd18783 81 TFDRLLSLPIDFFERTPAGVL-TKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 191 IF-KIKAREGFRSIRILIAKiNSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLrtilyfsifypAVEVLSAVA 269
Cdd:cd18783 160 AFlPPFRRRLQALYRAEGER-QAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARF-----------AVGRLSNWP 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 931518516 270 ITL-----------IIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPI 305
Cdd:cd18783 228 QTLtgpleklmtvgVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPL 274
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
362-561 |
9.28e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 362 DEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVlqdvflfsGSV 441
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRK--------GDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIA-LTNSKITDAELIRaakdvhahqfiekldRDYDEevlergsnFSTGQKQLISFARVLVYNPRILVLDEATSNIDT 520
Cdd:COG2401 113 KDAVElLNAVGLSDAVLWL---------------RRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931518516 521 ETEILIQKALNRLM--HKRTSVIIAHRLSTIK--NVERIIVMHKG 561
Cdd:COG2401 170 QTAKRVARNLQKLArrAGITLVVATHHYDVIDdlQPDLLIFVGYG 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
351-563 |
1.46e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.29 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKES---LRKHI 427
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQD-VFLFSGSVRDNIALTnSKITDAELIRAAKDVHAhqfieKLDRdydEEVLERGSNF----STGQKQLISFARVL 502
Cdd:PRK10908 82 GMIFQDhHLLMDRTVYDNVAIP-LIIAGASGDDIRRRVSA-----ALDK---VGLLDKAKNFpiqlSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 503 VYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIA-HRLSTI-KNVERIIVMHKGRI 563
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAtHDIGLIsRRSYRMLTLSDGHL 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
343-573 |
1.49e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 343 APAYVRGEiefkNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKES 422
Cdd:PRK10253 4 SVARLRGE----QLTLGYGKYT-VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 423 LRKHIGVVLQDvflfsgsvrdniALTNSKITDAELIraAKDVHAHQFIEKLDRDYDEEVLERG--------------SNF 488
Cdd:PRK10253 79 VARRIGLLAQN------------ATTPGDITVQELV--ARGRYPHQPLFTRWRKEDEEAVTKAmqatgithladqsvDTL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 489 STGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLS-TIKNVERIIVMHKGRIRE 565
Cdd:PRK10253 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVA 224
|
....*...
gi 931518516 566 EGTHQQLL 573
Cdd:PRK10253 225 QGAPKEIV 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
353-567 |
1.54e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 353 FKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHItkESLRKHIGVVLQ 432
Cdd:PRK11000 6 LRNVTKAYGDVV-ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 433 DVFLFSG-SVRDNIA--LTNSKITDAELIRAAKDVHA-HQFIEKLDRdydeevleRGSNFSTGQKQLISFARVLVYNPRI 508
Cdd:PRK11000 83 SYALYPHlSVAENMSfgLKLAGAKKEEINQRVNQVAEvLQLAHLLDR--------KPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 509 LVLDEATSNIDTETEILIQKALNRLmHKR---TSVIIAH-RLSTIKNVERIIVMHKGRIREEG 567
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRL-HKRlgrTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-544 |
1.84e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.64 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQ-----KGEILIDGINI--EHITKESL 423
Cdd:PRK14267 5 IETVNLRVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 424 RKHIGVVLQDVFLFSG-SVRDNIA-------LTNSKITDAELIRAAKDvHAHQFIEKLDRDYDeevleRGSNFSTGQKQL 495
Cdd:PRK14267 84 RREVGMVFQYPNPFPHlTIYDNVAigvklngLVKSKKELDERVEWALK-KAALWDEVKDRLND-----YPSNLSGGQRQR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931518516 496 ISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAH 544
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
351-562 |
2.19e-13 |
|
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: 67.47 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniehitkeslRKHIGVV 430
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQdvflFSGsvrdnialtnskitdaeliraakdvhahqfiekldrdydeevlergsnfstGQKQLISFARVLVYNPRILV 510
Cdd:cd03221 69 EQ----LSG---------------------------------------------------GEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518516 511 LDEATSNIDTETEILIQKALNRlmHKRTSVIIAHRLSTIKNV-ERIIVMHKGR 562
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE--YPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
351-573 |
2.32e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHI-TKESLRKHIGV 429
Cdd:PRK11614 6 LSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSG-SVRDNIALTNskitdaelIRAAKDvhahQFIEKLDRDYD------EEVLERGSNFSTGQKQLISFARVL 502
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGG--------FFAERD----QFQERIKWVYElfprlhERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 503 VYNPRILVLDEATSNIdteTEILIQKALNRLMHKR----TSVIIAHRLS-TIKNVERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQLReqgmTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
369-573 |
3.41e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.16 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 369 DISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQ-KGEILIDG--INIEHITKeSLRKHIGVVLQDV----FLFSGSV 441
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQ-AIRAGIAMVPEDRkrhgIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIALTN-SKITDAELIRAAKDVHA-HQFIEKLDRDYDEEVLERGSnFSTGQKQLISFARVLVYNPRILVLDEATSNID 519
Cdd:TIGR02633 357 GKNITLSVlKSFCFKMRIDAAAELQIiGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 520 TETEILIQKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGR-----IREEGTHQQLL 573
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIvVSSELAEVLGLsDRVLVIGEGKlkgdfVNHALTQEQVL 496
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-573 |
4.70e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESlRKHIGVV 430
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQ-DVFLFSGSVRDNIALTNSKI-TDAELIRAAkdVHAHQFIEKLDRDYDEEVLErgsnFSTGQKQLISFARVLVYNPRI 508
Cdd:PRK13537 86 PQfDNLDPDFTVRENLLVFGRYFgLSAAAARAL--VPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 509 LVLDEATSNIDTETEILIQKALNRLMHK-RTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
367-573 |
6.40e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIE-HITKESL----------RKHIGVVLqdvf 435
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLangivyisedRKRDGLVL---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 436 lfSGSVRDNIALT--NSKITDAELIRAAKDVHA-HQFIEKLD-----RDydeevlERGSNFSTGQKQLISFARVLVYNPR 507
Cdd:PRK10762 344 --GMSVKENMSLTalRYFSRAGGSLKHADEQQAvSDFIRLFNiktpsME------QAIGLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKRTSVIIAHrlSTIKNV----ERIIVMHKGRI-----REEGTHQQLL 573
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVS--SEMPEVlgmsDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
74-325 |
7.36e-13 |
|
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: 69.50 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 74 IAGLFIVIAGLNFifqyFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTI 153
Cdd:cd18574 48 LLGLYLLQSLLTF----AYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 154 LGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKN 233
Cdd:cd18574 124 LRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 234 YRQFERiNADHLKAyLRTILYFSI-FYPAVEVLSAVAITLI-IWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEK 311
Cdd:cd18574 204 LELYEE-EVEKAAK-LNEKLGLGIgIFQGLSNLALNGIVLGvLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVL 281
|
250
....*....|....
gi 931518516 312 YNILQSAMASSERI 325
Cdd:cd18574 282 FGQYVKGKSAGARV 295
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
366-574 |
8.24e-13 |
|
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: 70.87 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKT----TVISLLTRFYQVQKGEILIDGINIEHITKESLRK----HIGVVLQD---- 433
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 434 ---VFlfsgSVRDNIALTnskitdAELIRAAKDVHAHQ-FIEKLDR-----------DYDEEvlergsnFSTGQKQLISF 498
Cdd:COG4172 105 lnpLH----TIGKQIAEV------LRLHRGLSGAAARArALELLERvgipdperrldAYPHQ-------LSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 499 ARVLVYNPRILVLDEATSNID--TETEILiqKALNRLMHKR-TSVI-IAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLL 573
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDvtVQAQIL--DLLKDLQRELgMALLlITHDLGVVRRFaDRVAVMRQGEIVEQGPTAELF 245
|
.
gi 931518516 574 R 574
Cdd:COG4172 246 A 246
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
351-568 |
1.14e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.49 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHItkESLRKHIGVV 430
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL--EPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSG-SVRDNIA--LTNSKITDAELIR----AAKDVHAHQFiekLDRdydeevleRGSNFSTGQKQLISFARVLV 503
Cdd:PRK11650 82 FQNYALYPHmSVRENMAygLKIRGMPKAEIEErvaeAARILELEPL---LDR--------KPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 504 YNPRILVLDEATSNIDTE------TEIliqkalnRLMHKR---TSVIIAHrlstiKNVE------RIIVMHKGRIREEGT 568
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKlrvqmrLEI-------QRLHRRlktTSLYVTH-----DQVEamtladRVVVMNGGVAEQIGT 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
361-567 |
1.37e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 361 KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITK---ESLRKHIGVVLQDVFlf 437
Cdd:PRK10261 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPY-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 438 sgsvrdniALTNSKITDAELIRAAKDVH--------AHQFIEKLDRD--YDEEVLERGSNFSTGQKQLISFARVLVYNPR 507
Cdd:PRK10261 412 --------ASLDPRQTVGDSIMEPLRVHgllpgkaaAARVAWLLERVglLPEHAWRYPHEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 508 ILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERIsHRVAVMYLGQIVEIG 546
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
359-543 |
3.74e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 359 AYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIeHITKESLRKH-IGvvLQDVFLF 437
Cdd:PRK13539 10 CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-DDPDVAEACHyLG--HRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 438 SGSVRDNIAL-TNSKITDAELIRAAKDVHAHQFIEKLdrdydeevleRGSNFSTGQKQLISFARVLVYNPRILVLDEATS 516
Cdd:PRK13539 87 ALTVAENLEFwAAFLGGEELDIAAALEAVGLAPLAHL----------PFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*..
gi 931518516 517 NIDTETEILIQKALNRLMHKRTSVIIA 543
Cdd:PRK13539 157 ALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
37-305 |
4.39e-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: 67.14 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFI--VIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKH 114
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLAygLARILSSLFNELRDALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 115 LQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFV-FDAKLALITLTIMpLLFITAFIFK 193
Cdd:cd18582 81 LHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYlYGWSYALITLVTV-ALYVAFTIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 194 IKAREGFRSIRILI-AKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITL 272
Cdd:cd18582 160 TEWRTKFRREMNEAdNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTA 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 931518516 273 IIWFGGLDILTNNLTWGQLV---GFIMaaqMFYRPI 305
Cdd:cd18582 240 IMLLAAQGVVAGTLTVGDFVlvnTYLL---QLYQPL 272
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
350-573 |
6.87e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.81 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 350 EIEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGV 429
Cdd:PRK11231 2 TLRTENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 430 VLQDVFLFSG-SVRDNIALTNS-------KITDAELIRAAKDVHAHQFIEKLDRdydeevleRGSNFSTGQKQLISFARV 501
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGRSpwlslwgRLSAEDNARVNQAMEQTRINHLADR--------RLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 502 LVYNPRILVLDEATSNIDteteILIQKALNRLMHK-----RTSVIIAHRLS-TIKNVERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLD----INHQVELMRLMRElntqgKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
367-570 |
8.28e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRF------YQVQkGEILIDGINI--EHITKESLRKHIGVVLQDVFLFS 438
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVE-GKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 439 GSVRDNIALtNSKITDAEliraakdVHAHQFIEKLDRD---YDE---EVLERGSNFSTGQKQLISFARVLVYNPRILVLD 512
Cdd:PRK14243 105 KSIYDNIAY-GARINGYK-------GDMDELVERSLRQaalWDEvkdKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 513 EATSNIDTETEILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQ 570
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRY 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
367-562 |
1.23e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIE-HITKESLRKHIGVVLQDVFLF-SGSVRDN 444
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IALTNSK-----ITDAELIRAAKDVhahqfIEKLDRDYDEEvlERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNId 519
Cdd:PRK10982 94 MWLGRYPtkgmfVDQDKMYRDTKAI-----FDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518516 520 TETEI-LIQKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGR 562
Cdd:PRK10982 166 TEKEVnHLFTIIRKLKERGCGIVyISHKMEEIFQLcDEITILRDGQ 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
357-573 |
2.01e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 357 WFAYKDEEWVlKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVfl 436
Cdd:PRK15112 20 WFRRQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 437 fSGSV--RDNIaltnSKITDAELiraakdvhahqfieKLDRDYDEEVLERGSN-------------------FSTGQKQL 495
Cdd:PRK15112 97 -STSLnpRQRI----SQILDFPL--------------RLNTDLEPEQREKQIIetlrqvgllpdhasyyphmLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 496 ISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQL 572
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADV 237
|
.
gi 931518516 573 L 573
Cdd:PRK15112 238 L 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
351-567 |
2.05e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHI--- 427
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVpqs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 -------GVVLQDVFLFS-----GSVRDNIAlTNSKITDAELIRAAKDVHAHQFIEKLdrdydeevlergsnfSTGQKQL 495
Cdd:PRK15056 87 eevdwsfPVLVEDVVMMGryghmGWLRRAKK-RDRQIVTAALARVDMVEFRHRQIGEL---------------SGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518516 496 ISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHK-RTSVIIAHRLSTIKNVERIIVMHKGRIREEG 567
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
331-572 |
2.88e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 331 KVDEIPDKPDAiapayVRGEI--EFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEI 408
Cdd:COG3845 241 EVLLRVEKAPA-----EPGEVvlEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 409 LIDGINIEHITKESLRK----HI-------GVVLqdvflfSGSVRDNIALTNSK--------ITDAELIRAakdvHAHQF 469
Cdd:COG3845 316 RLDGEDITGLSPRERRRlgvaYIpedrlgrGLVP------DMSVAENLILGRYRrppfsrggFLDRKAIRA----FAEEL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 470 IEKLD---RDYDEEVlergSNFSTG--QKQLIsfARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSV---- 540
Cdd:COG3845 386 IEEFDvrtPGPDTPA----RSLSGGnqQKVIL--ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVllis 459
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 931518516 541 -----IIAhrLSTiknveRIIVMHKGRI-----REEGTHQQL 572
Cdd:COG3845 460 edldeILA--LSD-----RIAVMYEGRIvgevpAAEATREEI 494
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-574 |
7.22e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 350 EIEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKT-TVISLLTRFYQVQ-KGEILIDG-----------IN-- 414
Cdd:NF040905 259 EVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGkevdvstvsdaIDag 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 415 IEHITKEslRKHIGVVLQDvflfsgSVRDNIALTN-SKITDAELIRAAKDVH-AHQFIEKLdRDYDEEVLERGSNFSTGQ 492
Cdd:NF040905 339 LAYVTED--RKGYGLNLID------DIKRNITLANlGKVSRRGVIDENEEIKvAEEYRKKM-NIKTPSVFQKVGNLSGGN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 493 KQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGRI-----RE 565
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIvISSELPELLGMcDRIYVMNEGRItgelpRE 489
|
....*....
gi 931518516 566 EGTHQQLLR 574
Cdd:NF040905 490 EASQERIMR 498
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
107-323 |
7.68e-11 |
|
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: 63.13 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 107 IRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLF 186
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 187 ITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLS 266
Cdd:cd18590 151 IAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQ 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 267 AVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKY-NILQSAMASSE 323
Cdd:cd18590 231 LGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYgDMLSNVGAAAK 288
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
351-572 |
9.96e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESL---RKHI 427
Cdd:PRK11831 8 VDMRGVSFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDVFLFSG-SVRDNIALTNSKITD--AELIRAAkdvhahqFIEKLdrdydEEVLERG------SNFSTGQKQLISF 498
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPLREHTQlpAPLLHST-------VMMKL-----EAVGLRGaaklmpSELSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 499 ARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKR--TSVIIAHRLS---TIKNVERIIVMHKgrIREEGTHQQL 572
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPevlSIADHAYIVADKK--IVAHGSAQAL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
367-563 |
1.01e-10 |
|
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: 61.51 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTT---VISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFlfsgsvrd 443
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVH-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 444 nialtNSKITDAELIRAAKDVHAHQFIekldrdydeevleRGsnFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETE 523
Cdd:cd03233 95 -----FPTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 931518516 524 ILIQKALNRLMH--KRTSVIIAHRLS--TIKNVERIIVMHKGRI 563
Cdd:cd03233 155 LEILKCIRTMADvlKTTTFVSLYQASdeIYDLFDKVLVLYEGRQ 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
366-566 |
1.12e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.72 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKE---SLR-KHIGVVLQDVFLfsgsV 441
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFML----I 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIALTNSKItdAELIRAAKD----VHAHQFIEKLDrdYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSN 517
Cdd:PRK10584 101 PTLNALENVEL--PALLRGESSrqsrNGAKALLEQLG--LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 518 IDTETEILIQK---ALNRlMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREE 566
Cdd:PRK10584 177 LDRQTGDKIADllfSLNR-EHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
71-301 |
3.08e-10 |
|
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: 61.91 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 71 LTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGV 150
Cdd:cd18558 58 MTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 151 VTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIF-KIKAREGFRSIRILiAKINSFLQENITGMKIVQLFNR 229
Cdd:cd18558 138 GVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWaKILSGFTDKEKKAY-AKAGAVAEEVLEAFRTVIAFGG 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518516 230 EDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMF 301
Cdd:cd18558 217 QQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIG 288
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
361-561 |
3.19e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 361 KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQ---VQKGEILIDGINIEhitkESLRKHIGVVLQ-DVFL 436
Cdd:TIGR00956 773 KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD----SSFQRSIGYVQQqDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 437 FSGSVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLD-RDYDEEVL-ERGSNFSTGQKQLISFARVLVYNPRILV-LDE 513
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEmESYADAVVgVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 931518516 514 ATSNIDTETEILIQKALNRLM-HKRTSVIIAHRLSTI--KNVERIIVMHKG 561
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
363-562 |
4.81e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 363 EEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQ--KGEILIDGiniEHITKESLRKhIGVVLQDVFLFSG- 439
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANN---RKPTKQILKR-TGFVTQDDILYPHl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 440 SVRDNIA------LTNSkITDAELIRAAKDVHAHQFIEKLDRDYDEEVLERGsnFSTGQKQLISFARVLVYNPRILVLDE 513
Cdd:PLN03211 156 TVRETLVfcsllrLPKS-LTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 514 ATSNIDTETEILIQKALNRLMHK-RTSVIIAHRLST--IKNVERIIVMHKGR 562
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKgKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
107-325 |
1.83e-09 |
|
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: 59.02 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 107 IRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLF 186
Cdd:cd18589 71 LQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 187 ITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNRED---KNYR----QFERINADHLKAYLRTILYFSify 259
Cdd:cd18589 151 LVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEgeaQRYRqrlqKTYRLNKKEAAAYAVSMWTSS--- 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 260 pavevLSAVAITL-IIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18589 228 -----FSGLALKVgILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
352-566 |
3.88e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 352 EFKNVwfAYKDEEWVlKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITK-ESLRKHIGVV 430
Cdd:PRK09700 267 EVRNV--TSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDV----FLFSGSVRDNIALTNSkITDAELIRAAKDVHAHQfiEKLDRDYDEEVL--------ERGSNFSTGQKQLISF 498
Cdd:PRK09700 344 TESRrdngFFPNFSIAQNMAISRS-LKDGGYKGAMGLFHEVD--EQRTAENQRELLalkchsvnQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 499 ARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGRIREE 566
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILmVSSELPEIITVcDRIAVFCEGRLTQI 490
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
376-568 |
4.25e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.03 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 376 EGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEhITKESLRKHIGVVLQDVFLFSgsvrdNIALTNSKITDA 455
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFH-----HLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 456 ELIRAAKDvHAHQFIEKL--DRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRL 533
Cdd:TIGR01257 1029 QLKGRSWE-EAQLEMEAMleDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*.
gi 931518516 534 MHKRTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGT 568
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
351-550 |
5.02e-09 |
|
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: 58.99 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniehitkeslRKHIGVV 430
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYV 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSGSVRDNIALTNSK-------ITDAELIRAAKDVHAHQFIEK---LD--RDYDEEVlergsnfSTGQKQLISF 498
Cdd:TIGR00954 521 PQRPYMTLGTLRDQIIYPDSSedmkrrgLSDKDLEQILDNVQLTHILEReggWSavQDWMDVL-------SGGEKQRIAM 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518516 499 ARVLVYNPRILVLDEATSNIDTETEiliQKALNRLMHKRTSVI-IAHRLSTIK 550
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVE---GYMYRLCREFGITLFsVSHRKSLWK 643
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
361-530 |
5.30e-09 |
|
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: 56.35 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 361 KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFLFSGS 440
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 441 VRDNIALTNSKITDAELIRAAKDVHAHQFiekldrdydeEVLERGSnFSTGQKQLISFARVLVYNPRILVLDEATSNIDT 520
Cdd:cd03231 90 VLENLRFWHADHSDEQVEEALARVGLNGF----------EDRPVAQ-LSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|
gi 931518516 521 ETEILIQKAL 530
Cdd:cd03231 159 AGVARFAEAM 168
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
367-549 |
5.47e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHIT----KESLRKHIGVVLQDVFLFSG-SV 441
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTfngpKSSQEAGIGIIHQELNLIPQlTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIALTNSKITDAELIRAAK-DVHAHQFIEKLDRDYDEEVLErgSNFSTGQKQLISFARVLVYNPRILVLDEATSNI-D 519
Cdd:PRK10762 97 AENIFLGREFVNRFGRIDWKKmYAEADKLLARLNLRFSSDKLV--GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtD 174
|
170 180 190
....*....|....*....|....*....|.
gi 931518516 520 TETEILIqKALNRLM-HKRTSVIIAHRLSTI 549
Cdd:PRK10762 175 TETESLF-RVIRELKsQGRGIVYISHRLKEI 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
36-325 |
5.67e-09 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 57.50 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 36 YAALLLVCTSIFTLARPLLTQYAIdNYVMPGD----FDGLTIIAGLFIVIAGLNFIFQYFhFYLMYMTGQKVMYDIRSQI 111
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLI-SYLSSYPdeplSEGYLLALALFLVSLLQSLLLHQY-FFLSFRLGMRVRSALSSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 112 FKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTS-----------GVVTilgdillllglaTMMFVFDAKLALITLT 180
Cdd:cd18579 79 YRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFlhylwsaplqiIVAL------------YLLYRLLGWAALAGLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 181 IMPLLF-ITAFIFKIkaregFRSIRILIAKIN----SFLQENITGMKIVQLFNREDKNYRQFERINADHLKAyLRTILYF 255
Cdd:cd18579 147 VLLLLIpLQAFLAKL-----ISKLRKKLMKATdervKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKA-LRKFGYL 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 256 SIFYPAVEVLSAVAITLIIwFGGLDILTNNLTwgqlvgfimAAQMFY---------RPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18579 221 RALNSFLFFSTPVLVSLAT-FATYVLLGNPLT---------AAKVFTalslfnllrFPLLMLPQAISSLIEALVSLKRI 289
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
369-573 |
6.13e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 369 DISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILI---DGINIEHIT-KESLRKHI-----GVVLQDVflfsg 439
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYAlSEAERRRLlrtewGFVHQHP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 440 svRDNIALTNS---KItdAELIRAAKDVH-------AHQFIEKLDRDYDEeVLERGSNFSTGQKQLISFARVLVYNPRIL 509
Cdd:PRK11701 99 --RDGLRMQVSaggNI--GERLMAVGARHygdiratAGDWLERVEIDAAR-IDDLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 510 VLDEATSNIDteteILIQKALNRLMHKRTS------VIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK11701 174 FMDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHDLAVARLLaHRLLVMKQGRVVESGLTDQVL 240
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
32-296 |
6.51e-09 |
|
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: 57.45 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 32 MQVIYAALLLvctSIFTLARPLLTQYAIDNyVMPGD-FDGLTIIA-GLFIVIaGLNFIFQYFHFYLMYMTGQKVMYDIRS 109
Cdd:cd18587 5 RDVLLAALLI---NLFALASPLFVMNVYDR-VVPNNaIETLWVLAiGVLIAL-LFDFILKLLRAYFIDVAGKRADVILSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 110 QIFKHLQRLSLSfFDKTPIGRLVTRLtTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITA 189
Cdd:cd18587 80 RLFERVLGLRLE-ARPASVGSFANNL-REFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVAIPLVLLYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 190 FIFKIK----AREGFR--SIRiliakiNSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRT------ILYFSI 257
Cdd:cd18587 158 LLLQKPlrrlVEESMResAQK------NALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSrllsssATNFAQ 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 931518516 258 FypaveVLSAVAITLIIWfGGLDILTNNLTWGQLVGFIM 296
Cdd:cd18587 232 F-----VQQLVTVAIVIV-GVYLISDGELTMGGLIACVI 264
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-574 |
8.06e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 354 KNVWFAYKDEEW---VLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDG----------INIEHITK 420
Cdd:PRK10261 16 ENLNIAFMQEQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 421 ESLRK----HIGVVLQD-------VFLFSGSVRDNIALtNSKITDAELIRAAKdvhahQFIEKLDRDYDEEVLER-GSNF 488
Cdd:PRK10261 96 AQMRHvrgaDMAMIFQEpmtslnpVFTVGEQIAESIRL-HQGASREEAMVEAK-----RMLDQVRIPEAQTILSRyPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 489 STGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTS--VIIAHRLSTIKNV-ERIIVMHKGRIRE 565
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEIaDRVLVMYQGEAVE 249
|
....*....
gi 931518516 566 EGTHQQLLR 574
Cdd:PRK10261 250 TGSVEQIFH 258
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
367-562 |
1.08e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQ--VQKGEILIDG--INIEHItKESLRKHIGVVLQDVFLFSG-SV 441
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDGevCRFKDI-RDSEALGIVIIHQELALIPYlSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNIALTNSKITDAELIRAAKDVHAHQFIEK--LDRDYDEEVlergSNFSTGQKQLISFARVLVYNPRILVLDEATSNI- 518
Cdd:NF040905 96 AENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALn 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931518516 519 DTETEILiqkaLNRLMHKR----TSVIIAHRLSTIKNV-ERIIVMHKGR 562
Cdd:NF040905 172 EEDSAAL----LDLLLELKaqgiTSIIISHKLNEIRRVaDSITVLRDGR 216
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
37-325 |
2.55e-08 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; 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: 350028 [Multi-domain] Cd Length: 290 Bit Score: 55.49 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 37 AALLLVCTSIFTLARPLLTQYAIDNYVMPG-DFDGLTIIAGLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHL 115
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGaGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 116 QRLSLSFFDKTPIGRLVTRLTTDVDALNE--------MFTSGVVTilgdilllLGLATMMFVFD---AKLALITLTIMPL 184
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGyfarylpqLVLAAIVP--------LLILVAVFPLDwvsALILLVTAPLIPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 185 LFI----TAfifKIKAREGFRSIRILiakiNSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRT--ILYFSIF 258
Cdd:cd18584 153 FMIligkAA---QAASRRQWAALSRL----SGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVlrVAFLSSA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 259 ypAVEVLSAVAITLIIWFGGLDILTNNLTWGQlvGF---IMAAQmFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18584 226 --VLEFFATLSIALVAVYIGFRLLGGSLTLFT--ALfvlLLAPE-FYLPLRQLGAAYHARADGLAAAERL 290
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
374-557 |
2.56e-08 |
|
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: 55.11 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 374 VKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLRKhigvvlqdvflFSGSVRDniaLTNSKIt 453
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD-----------YEGTVRD---LLSSIT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 454 daeliraaKDVHAHQFIE-------KLDRDYDEEVLErgsnFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILI 526
Cdd:cd03237 87 --------KDFYTHPYFKteiakplQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 931518516 527 QKALNRLM--HKRTSVIIAHRLSTIKNV-ERIIV 557
Cdd:cd03237 155 SKVIRRFAenNEKTAFVVEHDIIMIDYLaDRLIV 188
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
354-583 |
3.55e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.44 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 354 KNVWFAYKDEE--WVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDG----INIEHITKESLRKHI 427
Cdd:PRK13545 25 KDLFFRSKDGEyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsaalIAISSGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 428 GVVLQDvfLFSGSVRDNIALTNSKITDAELIraakdvhaHQFIEKLDRDYdeevlergsnfSTGQKQLISFARVLVYNPR 507
Cdd:PRK13545 105 NIELKG--LMMGLTKEKIKEIIPEIIEFADI--------GKFIYQPVKTY-----------SSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 508 ILVLDEATSNID-TETEILIQKaLNRLMHK-RTSVIIAHRLSTIKN-VERIIVMHKGRIREEGTHQQLLRKHGIYYKLY 583
Cdd:PRK13545 164 ILVIDEALSVGDqTFTKKCLDK-MNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKY 241
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
370-574 |
7.41e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 370 ISFKVKEGEKVAVVGATGAGKT----TVISLLTRFYQVQKGEILIDGINIEHITKESLRKHIGVVLQDVFlfsgsvRDNI 445
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIF------QDPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 446 ALTNSKITDAELIRAAKDVHA--------HQFIEKLDRDYDEEVLERGSNF----STGQKQLISFARVLVYNPRILVLDE 513
Cdd:PRK11022 100 TSLNPCYTVGFQIMEAIKVHQggnkktrrQRAIDLLNQVGIPDPASRLDVYphqlSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 514 ATSNIDTETEILIQKALNRLMHKRTS--VIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLLR 574
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEAaHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
310-537 |
7.58e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 310 EKYNILQSA----MASSERIFKL-LDKVDEIPDKPdAIAPAYVRgeIEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVG 384
Cdd:PRK10938 218 EREEILQQAlvaqLAHSEQLEGVqLPEPDEPSARH-ALPANEPR--IVLNNGVVSYNDRP-ILHNLSWQVNPGEHWQIVG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 385 ATGAGKTTVISL------------LTRF-YQVQKGEILIDginiehitkesLRKHIGVVLQDVFL---FSGSVRDNIAlt 448
Cdd:PRK10938 294 PNGAGKSTLLSLitgdhpqgysndLTLFgRRRGSGETIWD-----------IKKHIGYVSSSLHLdyrVSTSVRNVIL-- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 449 nSKITDA-ELIRAAKDVHAHQFIEKLDR-DYDEEVLErgSNF---STGQKQLISFARVLVYNPRILVLDEATSNIDTete 523
Cdd:PRK10938 361 -SGFFDSiGIYQAVSDRQQKLAQQWLDIlGIDKRTAD--APFhslSWGQQRLALIVRALVKHPTLLILDEPLQGLDP--- 434
|
250
....*....|....
gi 931518516 524 iliqkaLNRLMHKR 537
Cdd:PRK10938 435 ------LNRQLVRR 442
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
327-578 |
1.35e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 327 KLLDKV--DEIpdKPDAIAPAYVRGE---------IEFKNVWFAYkDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVIS 395
Cdd:PRK15064 287 KQIDKIklEEV--KPSSRQNPFIRFEqdkklhrnaLEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 396 LLTRFYQVQKGEIlidginiehitKESLRKHIGVVLQDvflfsgsvrdnialtnskitdaeliraakdvHAHQFIEKLD- 474
Cdd:PRK15064 364 TLVGELEPDSGTV-----------KWSENANIGYYAQD-------------------------------HAYDFENDLTl 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 475 --------RDYDEEVLERG----------------SNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKAL 530
Cdd:PRK15064 402 fdwmsqwrQEGDDEQAVRGtlgrllfsqddikksvKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMAL 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 531 NrlMHKRTSVIIAH------RLSTiknveRII-VMHKGRIREEGTHQQLLRKHGI 578
Cdd:PRK15064 482 E--KYEGTLIFVSHdrefvsSLAT-----RIIeITPDGVVDFSGTYEEYLRSQGI 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
370-573 |
1.41e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 370 ISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIE-HITKESLRKhiGVVL------QDVFLFSGSVR 442
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRA--GIMLcpedrkAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 443 DNIALT--NSKITDAELIRAAKDV-HAHQFIEKLD---RDYDEEVLergsNFSTGQKQLISFARVLVYNPRILVLDEATS 516
Cdd:PRK11288 350 DNINISarRHHLRAGCLINNRWEAeNADRFIRSLNiktPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 517 NID--TETEI--LIQKALNRlmhKRTSVIIAHRLSTIKNV-ERIIVMHKGRI-----REEGTHQQLL 573
Cdd:PRK11288 426 GIDvgAKHEIynVIYELAAQ---GVAVLFVSSDLPEVLGVaDRIVVMREGRIagelaREQATERQAL 489
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
351-536 |
2.49e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.04 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVIslltrfyQVQKGEILIDGINIEHitKESLRkhIGVV 430
Cdd:PRK09544 5 VSLENVSVSFGQRR-VLSDVSLELKPGKILTLLGPNGAGKSTLV-------RVVLGLVAPDEGVIKR--NGKLR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDVFLFSgsvrdNIALTNSK-------ITDAELIRAAKDVHAHQFIE----KLdrdydeevlergsnfSTGQKQLISFA 499
Cdd:PRK09544 73 PQKLYLDT-----TLPLTVNRflrlrpgTKKEDILPALKRVQAGHLIDapmqKL---------------SGGETQRVLLA 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 931518516 500 RVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHK 536
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
366-573 |
3.29e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKT-TVISLL----TRFYQVQKGEILIDGINIEHITKESLRK----HIGVVLQD--- 433
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEpmv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 434 --------------VFLFSGSVRDNIAltnskitDAELIRAAKDVHAHQFIEKLdRDYDEEVlergsnfSTGQKQLISFA 499
Cdd:PRK15134 104 slnplhtlekqlyeVLSLHRGMRREAA-------RGEILNCLDRVGIRQAAKRL-TDYPHQL-------SGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 500 RVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHK--RTSVIIAHRLSTIKNV-ERIIVMHKGRIREEGTHQQLL 573
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLF 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
93-580 |
4.79e-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: 53.09 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 93 FYLMYMTGQKVMYDIRSQI--FKHLQRLSlsffDKTPIGRLVTRLTTDVdaLNEMFTSGVVTILGDILLLLGLATM--MF 168
Cdd:TIGR01257 1688 FAMSFVPASFVLYLIQERVnkAKHLQFIS----GVSPTTYWLTNFLWDI--MNYAVSAGLVVGIFIGFQKKAYTSPenLP 1761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 169 VFDAKLALITLTIMPLLFITAFIFKIKAregfrSIRILIAKINSFLQENITGMK-IVQLFnredKNYRQFERINAdHLKA 247
Cdd:TIGR01257 1762 ALVALLMLYGWAVIPMMYPASFLFDVPS-----TAYVALSCANLFIGINSSAITfVLELF----ENNRTLLRFNA-MLRK 1831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 248 YLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLTWgQLVG---FIMAAQMFYRPIEDLSEKYNILQSAMASSER 324
Cdd:TIGR01257 1832 LLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQW-DLIGknlVAMAVEGVVYFLLTLLIQHHFFLSRWIAEPA 1910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 325 IFKLLDKVDEIPDKPDAIAPAYVRGEI----EFKNVWFAYKDEewVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRF 400
Cdd:TIGR01257 1911 KEPIFDEDDDVAEERQRIISGGNKTDIlrlnELTKVYSGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD 1988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 401 YQVQKGEILIDGINIehITKES-LRKHIGVVLQ-DVF--LFSGsvRDNIAL-TNSKITDAELIRAAkdvhAHQFIEKLDR 475
Cdd:TIGR01257 1989 TTVTSGDATVAGKSI--LTNISdVHQNMGYCPQfDAIddLLTG--REHLYLyARLRGVPAEEIEKV----ANWSIQSLGL 2060
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 476 DYDEEVLerGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHK-RTSVIIAHRLSTIKNV-E 553
Cdd:TIGR01257 2061 SLYADRL--AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSMEECEALcT 2138
|
490 500
....*....|....*....|....*..
gi 931518516 554 RIIVMHKGRIREEGTHQQLLRKHGIYY 580
Cdd:TIGR01257 2139 RLAIMVKGAFQCLGTIQHLKSKFGDGY 2165
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
368-572 |
5.70e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 368 KDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEHI-TKESLRKHIGVVLQD-----VFLFSgSV 441
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGLVYLPEDrqssgLYLDA-PL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 442 RDNI-ALTnskitdaeliraakdVHAHQFIekLDRDYDEEVLER-----GSNF----------STGQKQLISFARVLVYN 505
Cdd:PRK15439 359 AWNVcALT---------------HNRRGFW--IKPARENAVLERyrralNIKFnhaeqaartlSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518516 506 PRILVLDEATSNIDTETEILIQKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGRIREEGTHQQL 572
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQMaDRVLVMHQGEISGALTGAAI 490
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
361-535 |
5.98e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 361 KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGiniEHITKESLRKHIGVVLQdvflFSGS 440
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRFMAYLGH----LPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 441 VRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDRDYdEEVLERgsNFSTGQKQLISFARVLVYNPRILVLDEATSNIDT 520
Cdd:PRK13543 94 KADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGY-EDTLVR--QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
170
....*....|....*
gi 931518516 521 ETEILIQKALNRLMH 535
Cdd:PRK13543 171 EGITLVNRMISAHLR 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
351-563 |
6.22e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTrfyqvqkGEILIDG--INIEhitkeslrkhig 428
Cdd:PRK11147 4 ISIHGAWLSFSDAP-LLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDgrIIYE------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 429 vvlQDVFL----------FSGSVRDNIALTNSKItdAELIRAAkdvhaHQFIEKLDRDYDEEVLERG------------- 485
Cdd:PRK11147 64 ---QDLIVarlqqdpprnVEGTVYDFVAEGIEEQ--AEYLKRY-----HDISHLVETDPSEKNLNELaklqeqldhhnlw 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 486 ---------------------SNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETeilIQKALNRLMHKRTSVI-IA 543
Cdd:PRK11147 134 qlenrinevlaqlgldpdaalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQGSIIfIS 210
|
250 260
....*....|....*....|.
gi 931518516 544 HRLSTIKNV-ERIIVMHKGRI 563
Cdd:PRK11147 211 HDRSFIRNMaTRIVDLDRGKL 231
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
31-325 |
1.45e-06 |
|
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: 50.13 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 31 KMQVIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTII--AGLFIVI--AGLNFIFQYFhfyLMYMtGQKVMYD 106
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLIliAQLVLFLgsTSIEFIRSWI---LLHI-SSRINIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 107 IRSQIFKHLQRLSLSFFDKTPIGRLVTRLTtDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITL--TIMPL 184
Cdd:cd18571 77 IISDFLIKLMRLPISFFDTKMTGDILQRIN-DHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLigSVLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 185 LFITAFIFKIKA--REGFRsiriLIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAV 262
Cdd:cd18571 156 LWILLFLKKRKKldYKRFD----LSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 263 EVLSAVAITLIIWFGGLDILTNNLTWGQL--VGFIMaAQMfYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18571 232 LFINQLKNILITFLAAKLVIDGEITLGMMlaIQYII-GQL-NSPIEQLIGFIQSLQDAKISLERL 294
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
370-574 |
1.46e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.93 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 370 ISFKVKEGEKVAVVGATGAGKTTVIS----LLTrfyqvQKGEILIDGINIEHITKESLRKHIG-VVLQDVFLFSGSVRDN 444
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArmagLLP-----GSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 445 IALTNSKITDAELIRAAKDVHAHQFieKLDrdydeEVLERGSN-FSTGQKQLISFARVL-----VYNP--RILVLDEATS 516
Cdd:PRK03695 90 LTLHQPDKTRTEAVASALNEVAEAL--GLD-----DKLGRSVNqLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 517 NIDteteILIQKALNRLMHK-----RTSVIIAHRLS-TIKNVERIIVMHKGRIREEGTHQQLLR 574
Cdd:PRK03695 163 SLD----VAQQAALDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
78-253 |
1.53e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 50.22 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 78 FIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDA--------LNEMFTSG 149
Cdd:cd18605 48 YGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTiddslpfiLNILLAQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 150 VVTilgdillLLGLATMMFVFdaklALITLTIMPLLFITAFIFKiKAREGFRSIRILIA----KINSFLQENITGMKIVQ 225
Cdd:cd18605 128 FGL-------LGYLVVICYQL----PWLLLLLLPLAFIYYRIQR-YYRATSRELKRLNSvnlsPLYTHFSETLKGLVTIR 195
|
170 180
....*....|....*....|....*...
gi 931518516 226 LFNREDknyrQFERINADHLKAYLRTIL 253
Cdd:cd18605 196 AFRKQE----RFLKEYLEKLENNQRAQL 219
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
355-545 |
1.58e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 355 NVWFAYKDEEwVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIehitKESLRKHigvvlQDV 434
Cdd:PRK13540 6 ELDFDYHDQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTY-----QKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 435 FLFSG---SVRDNIALTNSKITDAELIRAAKDVHAHQFIEKLDR--DYDEEVLergsnfSTGQKQLISFARVLVYNPRIL 509
Cdd:PRK13540 76 LCFVGhrsGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHliDYPCGLL------SSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 931518516 510 VLDEATSNIDteteiliQKALNRLMHKrtsvIIAHR 545
Cdd:PRK13540 150 LLDEPLVALD-------ELSLLTIITK----IQEHR 174
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
34-325 |
3.44e-06 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 49.01 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 34 VIYAALLLVCTSIFTLARPLLTQYAIDNYVMPGDFDGLTIIAGLFIVIAGLNFIFQYF-HFYLMYMTGqKVMYDIRSQIF 112
Cdd:cd18569 4 LLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLqQYYLLRLET-KLALSSSSRFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 113 KHLQRLSLSFFDKTPIGRLVTRLTTDvDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIF 192
Cdd:cd18569 83 WHVLRLPVEFFSQRYAGDIASRVQSN-DRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 193 KIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKA---YLRTILYFSIFyPAveVLSAVA 269
Cdd:cd18569 162 SRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESDFFSRWAGYQAKVLNAqqeLGRTNQLLGAL-PT--LLSALT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 270 ITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18569 239 NAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
71-248 |
8.12e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, 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: 350047 [Multi-domain] Cd Length: 296 Bit Score: 47.86 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 71 LTIIAGLFIVIAGLNFIFQYFhFYLMYMTGQKVMYDirsQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFtsgv 150
Cdd:cd18603 44 LGVYGALGLGQAIFVFLGSLA-LALGCVRASRNLHN---KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTL---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 151 vtilgdilLLLGLATMMFVFD--AKLALITLT-------IMPLLFITAFI--FKIKAregFRSIRILIAK----INSFLQ 215
Cdd:cd18603 116 --------PQNIRSFLNCLFQviSTLVVISIStpiflvvIIPLAILYFFIqrFYVAT---SRQLKRLESVsrspIYSHFS 184
|
170 180 190
....*....|....*....|....*....|...
gi 931518516 216 ENITGMKIVQLFNREDKNYRQFERINADHLKAY 248
Cdd:cd18603 185 ETLQGASTIRAYGVQERFIRESDRRVDENQRAY 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
351-548 |
8.30e-06 |
|
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: 48.78 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVWFAYKDEeWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDginiehitkESLrkHIGVV 430
Cdd:TIGR03719 323 IEAENLTKAFGDK-LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETV--KLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 431 LQDvflfsgsvRDniALTNSK-----ITD-AELIRAAK-DVHAHQFIEKLD-RDYDEEvlERGSNFSTGQKQLISFARVL 502
Cdd:TIGR03719 391 DQS--------RD--ALDPNKtvweeISGgLDIIKLGKrEIPSRAYVGRFNfKGSDQQ--KKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 503 VYNPRILVLDEATSNIDTETEILIQKALnrLMHKRTSVIIAH------RLST 548
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEAL--LNFAGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
76-145 |
8.32e-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: 47.85 E-value: 8.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 76 GLFIVIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDAL-NEM 145
Cdd:cd18606 39 GIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLdNEL 109
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
384-553 |
1.43e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 384 GATGAGKTTVISLLTRFYQVQKGEILIDGINIEHITKESLrKHIGVVLQdvFLFSGSVRDNIALTNSKITDAELIRAAkd 463
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIGHNLG--LKLEMTVFENLKFWSEIYNSAETLYAA-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 464 VHAHQFIEKLDrdydeevlERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALnrLMHKRTSVII- 542
Cdd:PRK13541 108 IHYFKLHDLLD--------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI--VMKANSGGIVl 177
|
170
....*....|...
gi 931518516 543 --AHRLSTIKNVE 553
Cdd:PRK13541 178 lsSHLESSIKSAQ 190
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
381-519 |
1.79e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 381 AVVGATGAGKTTVISLLTRFYQVQKGEI------LIDGINIEHITKEslRKHIGVVLQDVFLFSG-SVRDNialtnskit 453
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDAEKGICLPPE--KRRIGYVFQDARLFPHyKVRGN--------- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 454 daeLIRAAKDVHAHQF--------IEKLdrdydeevLER-GSNFSTGQKQLISFARVLVYNPRILVLDEATSNID 519
Cdd:PRK11144 97 ---LRYGMAKSMVAQFdkivallgIEPL--------LDRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
366-563 |
1.87e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVI-SLLTRFYQVQK---GEILIDGIniehiTKESLRKHI-GVVL----QDVFL 436
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGFHIgveGVITYDGI-----TPEEIKKHYrGDVVynaeTDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 437 FSGSVRDNIALTNSKITDA-------ELIRAAKDVHAHQFIEKLDRDYDEEVlerGSNF----STGQKQLISFARVLVYN 505
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTPQnrpdgvsREEYAKHIADVYMATYGLSHTRNTKV---GNDFvrgvSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 506 PRILVLDEATSNIDTETEILIQKALnrlmhkRTSVIIAHRLSTI----------KNVERIIVMHKGRI 563
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRAL------KTSANILDTTPLVaiyqcsqdayELFDKVIVLYEGYQ 289
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
369-577 |
2.44e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 369 DISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEIL-----IDGINIEhitkesLRKHIGVVLQDVFLFSG-SVR 442
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIA------TRRRVGYMSQAFSLYGElTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 443 DNIALtnskitDAELIRAAKDvHAHQFIEKLDRDYD-EEVLE-RGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDT 520
Cdd:NF033858 358 QNLEL------HARLFHLPAA-EIAARVAEMLERFDlADVADaLPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 521 ET-----EILIQkaLNRlmhkRTSVII---------AHRlstiknVERIIVMHKGRIREEGTHQQLLRKHG 577
Cdd:NF033858 431 VArdmfwRLLIE--LSR----EDGVTIfisthfmneAER------CDRISLMHAGRVLASDTPAALVAARG 489
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
368-567 |
2.55e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.23 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 368 KDISFKVKEGEKVAVVGATGAGKT----TVISLLTRFYQVQKGEILIDGINIEhitKESLR-KHIGVVLQD-------VF 435
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRgRKIATIMQNprsafnpLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 436 LFSGSVRDNIALTNSKITDAELIRAAKDVHahqfIEKLDRdydeeVLERGS-NFSTGQKQLISFARVLVYNPRILVLDEA 514
Cdd:PRK10418 97 TMHTHARETCLALGKPADDATLTAALEAVG----LENAAR-----VLKLYPfEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518516 515 TSNIDTETEILIQKALNRLMHKRTS--VIIAHRLSTIKNV-ERIIVMHKGRIREEG 567
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
76-325 |
2.55e-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: 46.31 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 76 GLFIVIAGLNFIFQYFHFYLMYMTGqkvmydIRS--QIFKHL-QRL---SLSFFDKTPIGRLVTRLTTDVDALNEMFTSG 149
Cdd:cd18604 47 GIYALISLLSVLLGTLRYLLFFFGS------LRAsrKLHERLlHSVlraPLRWLDTTPVGRILNRFSKDIETIDSELADS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 150 VVTILGDillllglaTMMFVFdaKLALITLTIMPLLFITAFIFKIKAREGF------RSIRIL--IAK--INSFLQENIT 219
Cdd:cd18604 121 LSSLLES--------TLSLLV--ILIAIVVVSPAFLLPAVVLAALYVYIGRlylrasRELKRLesVARspILSHFGETLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 220 GMKIVQLFNREDknyrQFERINADHLKAYLRTILYFSI------FYpaVEVLSAVAIT----LIIWFGGLDiltnnltwG 289
Cdd:cd18604 191 GLVTIRAFGAEE----RFIEEMLRRIDRYSRAFRYLWNlnrwlsVR--IDLLGALFSFataaLLVYGPGID--------A 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 931518516 290 QLVGFIMA-AQMFYRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18604 257 GLAGFSLSfALGFSSAILWLVRSYNELELDMNSVERI 293
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
352-525 |
2.87e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 352 EFKNVWFAYKDEEWVlKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEI----------------------- 408
Cdd:PRK11147 321 EMENVNYQIDGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevayfdqhraeldpekt 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 409 ----LIDGinIEHITKESLRKHIGVVLQDvFLFSGSvrdnialtnskitdaeliRAAKDVHAhqfiekldrdydeevler 484
Cdd:PRK11147 400 vmdnLAEG--KQEVMVNGRPRHVLGYLQD-FLFHPK------------------RAMTPVKA------------------ 440
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931518516 485 gsnFSTGQKQLISFARVLVYNPRILVLDEATSNIDTET-EIL 525
Cdd:PRK11147 441 ---LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETlELL 479
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
106-326 |
4.87e-05 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 45.55 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 106 DIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPL- 184
Cdd:cd18585 69 NLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLa 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 185 LFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLR--TILYFSIFypAV 262
Cdd:cd18585 149 GVVIPLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRlaRLSGLSQA--LM 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518516 263 EVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSERIF 326
Cdd:cd18585 227 ILLSGLTVWLVLWLGAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRLF 290
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
70-325 |
6.08e-05 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 45.28 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 70 GLTIIAGLFIvIAGLNFIFQYFHFYLMYMTGQKVMYDIRSQIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSg 149
Cdd:cd18559 37 GQVYLSVLGA-LAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQ- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 150 VVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNR 229
Cdd:cd18559 115 VIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEW 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 230 EDKNYRQFERINADHLKaYLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMA-AQMFYRPIEDL 308
Cdd:cd18559 195 EEAFIRQVDAKRDNELA-YLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLAlTTYLNWPLNMS 273
|
250
....*....|....*..
gi 931518516 309 SEKYNILQSAMASSERI 325
Cdd:cd18559 274 PEVITNIVAAEVSLERS 290
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
377-556 |
6.61e-05 |
|
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: 43.52 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 377 GEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIdgINIEHItkeslrkhigvvlqdvflfsgsvrdnialtnskitdae 456
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDI-------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 457 liraakdvhahqFIEKLDRDYDEEVLERGSNFSTGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHK 536
Cdd:smart00382 42 ------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
170 180
....*....|....*....|
gi 931518516 537 RTSVIIAHRLSTIKNVERII 556
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDL 129
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
351-573 |
7.34e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 351 IEFKNVwfaykdEEWV--LKDISFKVKEGEKVAVVGATGAGKTTV---ISLLTR-FYQVQKGEILIDGINIEHITKESLR 424
Cdd:PRK15093 11 IEFKTS------DGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIakaICGVTKdNWRVTADRMRFDDIDLLRLSPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 425 KHIGVVLQDVFLFSGSvrdniALTNSKITDAELIRAA-----KDVHAHQF-------IEKLDR----DYDEEVLERGSNF 488
Cdd:PRK15093 85 KLVGHNVSMIFQEPQS-----CLDPSERVGRQLMQNIpgwtyKGRWWQRFgwrkrraIELLHRvgikDHKDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 489 STGQKQLISFARVLVYNPRILVLDEATSNIDTETEILIQKALNRLMHKRTSVI--IAHRLSTI-KNVERIIVMHKGRIRE 565
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLsQWADKINVLYCGQTVE 239
|
....*...
gi 931518516 566 EGTHQQLL 573
Cdd:PRK15093 240 TAPSKELV 247
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
168-324 |
1.20e-04 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 44.44 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 168 FVFDAKLALITLTIMPLLFITAFIFKIKAREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKA 247
Cdd:cd18583 133 YLFDPYMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKA 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 248 YLRTILYFSIFYPAVEVLSAVAITLIIWFGGLDILTNNLTWGQLVGFIMAAQMFYRPIEDLSEKYNILQSAMASSER 324
Cdd:cd18583 213 ERKYLFSLNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAER 289
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
311-527 |
1.70e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 311 KYNILQSAMASSeRIfKLLDK---VDEIPDKPDAI----APAYVRGE--IEFKNVWFAYKDEEWVLKDISFKVKEGEKVA 381
Cdd:PLN03073 462 RYNAKRASLVQS-RI-KALDRlghVDAVVNDPDYKfefpTPDDRPGPpiISFSDASFGYPGGPLLFKNLNFGIDLDSRIA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 382 VVGATGAGKTTVISLLTRFYQVQKGEIL--------------IDGINIEH------------ITKESLRKHIGvvlqdvf 435
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSnpllymmrcfpgVPEQKLRAHLG------- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 436 lfSGSVRDNIALtnskitdaeliraakdvhahQFIEKLdrdydeevlergsnfSTGQKQLISFARVLVYNPRILVLDEAT 515
Cdd:PLN03073 613 --SFGVTGNLAL--------------------QPMYTL---------------SGGQKSRVAFAKITFKKPHILLLDEPS 655
|
250
....*....|...
gi 931518516 516 SNIDTE-TEILIQ 527
Cdd:PLN03073 656 NHLDLDaVEALIQ 668
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
366-574 |
3.03e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 366 VLKDISFKVKEGEKVAVVGATGAGKTTVI---------SLLTRFYQVqKGEILIDGINIEHITKESLRKHIGVVLQD--- 433
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLkalagdltgGGAPRGARV-TGDVTLNGEPLAAIDAPRLARLRAVLPQAaqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 434 VFLFsgSVRDNIALtnSKITDAEliRAAKDVHAhqfieklDRDYDEEVLERG----------SNFSTGQKQLISFARVL- 502
Cdd:PRK13547 95 AFAF--SAREIVLL--GRYPHAR--RAGALTHR-------DGEIAWQALALAgatalvgrdvTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 503 --------VYNPRILVLDEATSNIDTETE---ILIQKALNRLMHKRTSVIIAHRLSTIKNVERIIVMHKGRIREEGTHQQ 571
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQhrlLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
...
gi 931518516 572 LLR 574
Cdd:PRK13547 242 VLT 244
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-410 |
3.30e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 3.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518516 351 IEFKNVWFAYKDEewVL-KDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILI 410
Cdd:PRK11819 325 IEAENLSKSFGDR--LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
361-417 |
4.61e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.71 E-value: 4.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518516 361 KDEEWVLKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEH 417
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR 67
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
39-325 |
6.85e-04 |
|
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: 41.82 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 39 LLLVCTSIFTLA--RPLLTQYAIDNYVMpgdfdgLTIIA-GLFIVIaglnFIFQYFHFYLMYMTGQKVMYDIRSQIFKHL 115
Cdd:cd18586 16 LLALAPPIFMLQvyDRVLPSGSLSTLLG------LTLGMvVLLAFD----GLLRQVRSRILQRVGLRLDVELGRRVFRAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 116 QRLSLsffDKTPIGRLVTRLTtDVDALNEMFTSGVVTILGDILLLLGLATMMFVFDAKLALITLTIMPLLFITAFIFKIK 195
Cdd:cd18586 86 LELPL---ESRPSGYWQQLLR-DLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 196 AREGFRSIRILIAKINSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAITLIIW 275
Cdd:cd18586 162 TRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 931518516 276 FGGLDILTNNLTwgqlVGFIMAAQMF----YRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18586 242 VGAYLVIDGELT----IGALIAASILsgraLAPIDQLVGAWKQLSAARQAYERL 291
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
367-563 |
4.97e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 367 LKDISFKVKEGEKVAVVGATGAGKTTVISLLTRFYQVQKGEILIDGINIEH-------------ITKEslRKHIGVVLQD 433
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgfalVTEE--RRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 434 VFLFSgSVRDNIALTNSKITDAELIRAAKDVHahQFIEKLDRDYDEEVLERGSnFSTGQKQLISFARVLVYNPRILVLDE 513
Cdd:PRK10982 342 DIGFN-SLISNIRNYKNKVGLLDNSRMKSDTQ--WVIDSMRVKTPGHRTQIGS-LSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931518516 514 ATSNIDTETEILIQKALNRLMHKRTSVI-IAHRLSTIKNV-ERIIVMHKGRI 563
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKKDKGIIiISSEMPELLGItDRILVMSNGLV 469
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
39-325 |
6.97e-03 |
|
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: 38.74 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 39 LLLVCTSIFTLARPLLTQYAIDNYVMP--GDFDGLTIIAGLFIVIAGLNFIFQYFHfYLMYMTGQKVMY-DIRSQIFKHL 115
Cdd:cd18560 3 LLLILGKACNVLAPLFLGRAVNALTLAkvKDLESAVTLILLYALLRFSSKLLKELR-SLLYRRVQQNAYrELSLKTFAHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 116 QRLSLSFFDKTPIGRLVTRLTTDVDALNEMFTSGVVTIL-GDILLLLGLATMMFVFDAKLALITLTIMpLLFItafIFKI 194
Cdd:cd18560 82 HSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVpTLLELIVVSVVFAFHFGAWLALIVFLSV-LLYG---VFTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 195 KAREGFRSIRILIAKINSFLQ----ENITGMKIVQLFNREDKNYRQFERINADHLKAYLRTILYFSIFYPAVEVLSAVAI 270
Cdd:cd18560 158 KVTEWRTKFRRAANKKDNEAHdiavDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518516 271 TLIIWFGGLDILTNNLTWGQLVG---FIMaaQMFyRPIEDLSEKYNILQSAMASSERI 325
Cdd:cd18560 238 TLGLLLAGYRVVDGGLSVGDFVAvntYIF--QLF-QPLNFLGTIYRMIIQSLTDMENL 292
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
110-249 |
8.49e-03 |
|
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: 38.70 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518516 110 QIFKHLQRLSLSFFDKTPIGRLVTRLTTDVDALN-------EMFTSGVVTilgdilLLLGLATMMFVFdaklALITLTIM 182
Cdd:cd18599 96 KLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDvrlpftlENFLQNVLL------VVFSLIIIAIVF----PWFLIALI 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518516 183 PLLFITAFIFKIkaregFR-SIRIL-----IAK--INSFLQENITGMKIVQLFNREDKNYRQFERINADHLKAYL 249
Cdd:cd18599 166 PLAIIFVFLSKI-----FRrAIRELkrlenISRspLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFF 235
|
|
| |
