|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-730 |
0e+00 |
|
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: 805.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 3 HYPVYTQLDRMDCGPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLvDDFPLPCI 82
Cdd:COG2274 3 KVPFVLQMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEEL-AELPLPAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 83 LHWNQQHFVVCYRIRKRrnkyKILIGDPAgTQTVTYNEEEFKRCWissrekgqdTGVALVLEPTPDFysmeEDRKEAKKK 162
Cdd:COG2274 82 LHWDGNHFVVLEGVDGD----KVTIADPA-TGRRKLSLEEFAESW---------TGVALLLEPTPEF----DKRGEKPFG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 163 LNFFFRYLSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHM 242
Cdd:COG2274 144 LRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 243 NIRINISLISDFLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLL 322
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 323 GNLLYVIWVLSFMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQV 402
Cdd:COG2274 304 LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLST 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 403 GSVFFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEIHQKEDEEETAVD 482
Cdd:COG2274 384 LSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 483 KVSFLPQDHTFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNIN 562
Cdd:COG2274 464 KLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 563 PHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIA 642
Cdd:COG2274 544 PASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIA 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 643 RAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIY 722
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
....*...
gi 496428897 723 YRLVKNQL 730
Cdd:COG2274 704 AELVQQQL 711
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
174-467 |
7.08e-173 |
|
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: 496.97 E-value: 7.08e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISIISD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLS 333
Cdd:cd18571 81 FLIKLMRLPISFFDTKMTGDILQRINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILWILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNI 413
Cdd:cd18571 161 FLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFINQLKNI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 496428897 414 LISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18571 241 LITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
156-731 |
3.85e-158 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 470.03 E-value: 3.85e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 156 RKEAKKKLNFFFRYLSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIR 235
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 236 SWLLLHMNIRINISLISDFLVKLMRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDL 314
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLtNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 315 SIFGLFLLGNLLYVIWVLSFMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGL 394
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 395 ALQQYQQVGSVFFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEIHQKE 474
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 475 DEEETAVDKVSFLPQDHTFTIENLCFSYDGSPdYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVG 554
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVSFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 555 DVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQG 634
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 635 QRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQE 714
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEE 560
|
570
....*....|....*..
gi 496428897 715 LTCLKGIYYRLVKNQLE 731
Cdd:COG1132 561 LLARGGLYARLYRLQFG 577
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
5-727 |
2.03e-122 |
|
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: 382.37 E-value: 2.03e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 5 PVYTQLDRMDCGPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLvDDFPLPCILH 84
Cdd:TIGR03796 3 PTVLQMEAVECGAASLAMILAYYGRYVPLEELREECGVSRDGSKASNLLKAARSYGLEAKGFRKELDAL-AELPLPYIVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 85 WNQQHFVVCYRIRKRRnkykILIGDPA-GTQTVTYneEEFKRCWissrekgqdTGVALVLEPTPDFysmeedRKEAKKK- 162
Cdd:TIGR03796 82 WNFNHFVVVEGFRGGR----VYLNDPAlGPRTVSL--EEFDESF---------TGVVLTFEPGPEF------QKGGRKPs 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 163 -LNFFFRYLSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLH 241
Cdd:TIGR03796 141 lLRALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIFVDEILVQGRQDWLRPLLLGMGLTALLQGVLTWLQLYYLRR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 242 MNIRINISLISDFLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLsIFGLFL 321
Cdd:TIGR03796 221 LEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYALLMLLYDP-VLTLIG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 322 LGNLLYVIWVLSFMKYRRELDLRRFSQastEQSTLYQI-ITGMQEIklnncETQKR--------WKWERIQVKLFKISVK 392
Cdd:TIGR03796 300 IAFAAINVLALQLVSRRRVDANRRLQQ---DAGKLTGVaISGLQSI-----ETLKAsglesdffSRWAGYQAKLLNAQQE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 393 GLALQQYQQVGSVFFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEIHQ 472
Cdd:TIGR03796 372 LGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 473 ----KEDEEETAVDKVSFLPQDHTFTIE--NLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTP 546
Cdd:TIGR03796 452 npvdPLLEEPEGSAATSEPPRRLSGYVElrNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQP 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 547 NKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGM 626
Cdd:TIGR03796 532 WSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAE 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 627 EGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNefYRGKTVVIVAHRLSTVQNADKIVVLDKGGI 706
Cdd:TIGR03796 612 GGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEIIVLERGKV 689
|
730 740
....*....|....*....|.
gi 496428897 707 VEEGTHQELTCLKGIYYRLVK 727
Cdd:TIGR03796 690 VQRGTHEELWAVGGAYARLIR 710
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-728 |
4.32e-117 |
|
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: 368.30 E-value: 4.32e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 9 QLDRMDCGPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLVD-DFPLPCILHWNQ 87
Cdd:TIGR01193 1 QVDEKDCGIAALSMILKKYGTEYSLAKLRQLAKTDLEGTTVLGLVKAAEYLNFEAKAIQADMSLFEDkNLPLPFIAHVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 88 Q----HFVVCYRIrkrrNKYKILIGDPAGTQTVT-YNEEEFKRCWissrekgqdTGVALVLEPTPDFYSMeedrKEAKKK 162
Cdd:TIGR01193 81 NgklpHYYVVYGV----TKNHLIIADPDPTVGITkISKEDFYEEW---------TGIAIFISPTPEYKPI----KEKENS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 163 LNFFFRYLSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHM 242
Cdd:TIGR01193 144 LLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 243 NIRINISLISDFLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLtGSSISTLFSFVNFIVF-GFVLAYYDLSIFGLFL 321
Cdd:TIGR01193 224 GQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDAL-ASTILSLFLDMWILVIvGLFLVRQNMLLFLLSL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 322 LGNLLYVIWVLSFMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQ 401
Cdd:TIGR01193 303 LSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 402 VGSVFFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEIHQKEDEEETAV 481
Cdd:TIGR01193 383 AIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 482 DKVSFLPQDHTFTIENLCFSYdGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNI 561
Cdd:TIGR01193 463 KRTELNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 562 NPHLWRSVTGSVMQDGFIFSETIAENIAIG-EEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRIL 640
Cdd:TIGR01193 542 DRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIA 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 641 IARAVYKNPDFLFFDEATNALDANNEREIMEHLnEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKG 720
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
....*...
gi 496428897 721 IYYRLVKN 728
Cdd:TIGR01193 701 FYASLIHN 708
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
16-731 |
1.15e-115 |
|
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: 364.06 E-value: 1.15e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 16 GPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLvDDFPLPCILHWNQQHFVVcyr 95
Cdd:TIGR01846 1 GLEALSLLAQVHNIAVTPSQLRHMLGHAGASLDDLEILLAAKQLGLKAKAVKVSIGRL-NKLPLPALIDGEGGWFVL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 96 IRKRRNKYkiLIGDPAGTQTVTYNEEEFKRCWissrekgqDTGVALVleptpdfysmeEDRKEAKKKLNFFFRYLSP--- 172
Cdd:TIGR01846 77 GKLTANGV--TIYDPPGDAPEVLSREVLEALW--------SGTVILL-----------ATRSVAGKALKFGFSWFIPaii 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 173 -HKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLI 251
Cdd:TIGR01846 136 rYRKQFREVLLISLALQLFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 252 SDFLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLY-VIW 330
Cdd:TIGR01846 216 ARLYRHLLGLPLGYFESRRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYaLLS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 331 VLSFMKYRRELDlRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKL----FKISVKGLALQQyqqvGSVF 406
Cdd:TIGR01846 296 VFVGPILRKRVE-DKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYvaasFRVTNLGNIAGQ----AIEL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 407 FNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEIhQKEDEEETAVDKVSF 486
Cdd:TIGR01846 371 IQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDI-LNSPTEPRSAGLAAL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 487 LPQDHTFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLW 566
Cdd:TIGR01846 450 PELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVY 646
Cdd:TIGR01846 530 RRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALV 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 647 KNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLV 726
Cdd:TIGR01846 610 GNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLW 689
|
....*
gi 496428897 727 KNQLE 731
Cdd:TIGR01846 690 QQQSG 694
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
494-725 |
2.87e-90 |
|
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: 282.20 E-value: 2.87e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRL 725
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
459-715 |
1.34e-89 |
|
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: 291.66 E-value: 1.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 459 DAKISLERLNEIHQKEDEEETAVDKVSFLPQDHTFTIENLCFSYDGSPDyVLNNVNLTIPRNKITAIVGASGSGKTTLIK 538
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 539 LLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPL 618
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPD 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 619 GYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKI 698
Cdd:COG4988 462 GLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRI 541
|
250
....*....|....*..
gi 496428897 699 VVLDKGGIVEEGTHQEL 715
Cdd:COG4988 542 LVLDDGRIVEQGTHEEL 558
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
494-729 |
2.72e-87 |
|
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: 274.42 E-value: 2.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDY-VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGS 572
Cdd:cd03249 2 EFKNVSFRYPSRPDVpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFL 652
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 653 FFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLVKNQ 729
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
166-730 |
1.68e-84 |
|
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: 278.52 E-value: 1.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 166 FFR---YLSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLlhm 242
Cdd:TIGR02203 2 FRRlwsYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 243 nIRINISLISDFLV----KLMRLPLHFFDTKMIGDIMQRIG-DHSRIESFLTGSsISTLFSFVNFIVFGF-VLAYYD--L 314
Cdd:TIGR02203 79 -SWVSNKVVRDIRVrmfeKLLGLPVSFFDRQPTGTLLSRITfDSEQVASAATDA-FIVLVRETLTVIGLFiVLLYYSwqL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 315 SIFGLFllgnllyVIWVLSFMKYRRELDLRRFS---QASTEQST--LYQIITGMQEIKLNNCETQKRWKWERIQVKL--- 386
Cdd:TIGR02203 157 TLIVVV-------MLPVLSILMRRVSKRLRRISkeiQNSMGQVTtvAEETLQGYRVVKLFGGQAYETRRFDAVSNRNrrl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 387 -FKISVKGLALQQYQQ-VGSVFFNqttniLISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISL 464
Cdd:TIGR02203 230 aMKMTSAGSISSPITQlIASLALA-----VVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 465 ERLNEIHQKEDEEET-------AVDKVSFlpqdhtftiENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLI 537
Cdd:TIGR02203 305 ESLFTLLDSPPEKDTgtraierARGDVEF---------RNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 538 KLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGE-EVIDKERLLKAAQIANIDQFIDSL 616
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 617 PLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNAD 696
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535
|
570 580 590
....*....|....*....|....*....|....
gi 496428897 697 KIVVLDKGGIVEEGTHQELTCLKGIYYRLVKNQL 730
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNGLYAQLHNMQF 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
496-729 |
6.85e-84 |
|
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: 265.63 E-value: 6.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 496 ENLCFSYDGSPDyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQ 575
Cdd:cd03253 4 ENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 576 DGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFD 655
Cdd:cd03253 83 DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 656 EATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLVKNQ 729
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
344-727 |
8.70e-84 |
|
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: 276.26 E-value: 8.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 344 RRFSQASTE-QSTLYQ----IITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNILISYI 418
Cdd:COG4987 181 RRAGRRLAAaRAALRArltdLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 419 AARAVVEGNMT---LGMM----MSLtyiigqlnspIEQFIGFARSFQ---DAKISLERLNEIHQKEDEEETAVDKVSfLP 488
Cdd:COG4987 261 AAPLVAAGALSgplLALLvlaaLAL----------FEALAPLPAAAQhlgRVRAAARRLNELLDAPPAVTEPAEPAP-AP 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 489 QDHTFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRS 568
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 569 VTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKN 648
Cdd:COG4987 410 RIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRD 489
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 649 PDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLVK 727
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
291-731 |
2.23e-83 |
|
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: 276.32 E-value: 2.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 291 SSISTLFSFVNF----------IVFGFVLAYYDLSIFGLFLLGNLLYVIWVLSF----MKYRRELdlrrfSQASTEQSTl 356
Cdd:COG5265 146 KGIEFLLRFLLFnilptlleiaLVAGILLVKYDWWFALITLVTVVLYIAFTVVVtewrTKFRREM-----NEADSEANT- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 357 yQIITGmqeikLNNCETQK---------------RWKWERIQVKlfkiSVKGLALQQYQQvgSVFFNQTTnILISYIAAR 421
Cdd:COG5265 220 -RAVDS-----LLNYETVKyfgnearearrydeaLARYERAAVK----SQTSLALLNFGQ--ALIIALGL-TAMMLMAAQ 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 422 AVVEGNMTLG-------MMMSLtYIigQLNspieqFIGFA-RSFQDAKISLERLNEIHQKEDEEETAVDKVSFLPQDHTF 493
Cdd:COG5265 287 GVVAGTMTVGdfvlvnaYLIQL-YI--PLN-----FLGFVyREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDgsPDY-VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGS 572
Cdd:COG5265 359 RFENVSFGYD--PERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFL 652
Cdd:COG5265 437 VPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPIL 516
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 653 FFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLVKNQLE 731
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQE 595
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
170-730 |
2.58e-81 |
|
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: 272.99 E-value: 2.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 170 LSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINIS 249
Cdd:TIGR03797 131 LRGARRDLLAILAMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDAS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 250 LISDFLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVnFIVFGFVLA-YYD--LSIFGLFLLGNLL 326
Cdd:TIGR03797 211 LQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGI-FALLNLGLMfYYSwkLALVAVALALVAI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 327 YVIWVLSFMKYRREldlRRFSQASTEQSTL-YQIITGMQEIKLNNCETQKRWKWERI---QVKLFkisvkgLALQQYQQV 402
Cdd:TIGR03797 290 AVTLVLGLLQVRKE---RRLLELSGKISGLtVQLINGISKLRVAGAENRAFARWAKLfsrQRKLE------LSAQRIENL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 403 GSVF---FNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEIHQKEDEeet 479
Cdd:TIGR03797 361 LTVFnavLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPE--- 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 480 aVDKVSFLPQDHTFTIE--NLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVY 557
Cdd:TIGR03797 438 -VDEAKTDPGKLSGAIEvdRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 558 LKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEeVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQ 637
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA-PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQ 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 638 RILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFyrGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTC 717
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
570
....*....|...
gi 496428897 718 LKGIYYRLVKNQL 730
Cdd:TIGR03797 674 REGLFAQLARRQL 686
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
168-730 |
7.38e-80 |
|
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: 266.18 E-value: 7.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 168 RYLSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFIT----LILVAQLIIFIArlsvDFIRSWLLLHMN 243
Cdd:TIGR02204 11 PFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNryfaFLLVVALVLALG----TAARFYLVTWLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 244 IRINISLISDFLVKLMRLPLHFFDTKMIGDIMQRI-GDHSRIESfLTGSSIS-TLFSFVNFIvfGFVLAYYDLSIFGLFL 321
Cdd:TIGR02204 87 ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLtTDTTLLQS-VIGSSLSmALRNALMCI--GGLIMMFITSPKLTSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 322 LGNLLYVIWVLSFMKYRRELDLRRFSQASTEQSTLY--QIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQY 399
Cdd:TIGR02204 164 VLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYagETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 400 QQVGSVFFNQTTNILISYIAARAVVEGNM---TLGMMMSLTYIIGQLNSPIEQFIGfarSFQDAKISLERLNEIHQKEDE 476
Cdd:TIGR02204 244 LTAIVIVLVFGAIVGVLWVGAHDVIAGKMsagTLGQFVFYAVMVAGSIGTLSEVWG---ELQRAAGAAERLIELLQAEPD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 477 EETAVDKVSfLPQDHTFTI--ENLCFSYDGSPDY-VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKV 553
Cdd:TIGR02204 321 IKAPAHPKT-LPVPLRGEIefEQVNFAYPARPDQpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 554 GDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQ 633
Cdd:TIGR02204 400 DGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 634 GQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQ 713
Cdd:TIGR02204 480 GQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHA 559
|
570
....*....|....*..
gi 496428897 714 ELTCLKGIYYRLVKNQL 730
Cdd:TIGR02204 560 ELIAKGGLYARLARLQF 576
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
494-729 |
3.47e-79 |
|
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: 253.18 E-value: 3.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:cd03252 2 TFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03252 82 LQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLVKNQ 729
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
495-720 |
9.25e-79 |
|
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: 251.76 E-value: 9.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYD-GSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:cd03254 5 FENVNFSYDeKKP--VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKG 720
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
494-704 |
2.06e-71 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 229.96 E-value: 2.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:cd03228 2 EFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSETIAENIaigeevidkerllkaaqianidqfidslplgyntkigmegsgISQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03228 82 PQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKG 704
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
157-714 |
5.97e-66 |
|
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: 228.48 E-value: 5.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 157 KEAKKKLNFFFRYLSPHKKALVQL-VLGMVIgSILQLIVPF---------LT-QSLVdvgirdnNLNFITLILVAqLIIF 225
Cdd:COG4618 2 SRASAGRSELRAALRACRRAFLSVgLFSFFI-NLLMLTPPLymlqvydrvLTsRSVD-------TLLMLTLLALG-LYAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 226 IARLsvDFIRSWLLLHMNIRINISLISDFLVKLMRLPLHFFDtkmiGDIMQRIGDHSRIESFLTGSSISTLFS---FVNF 302
Cdd:COG4618 73 MGLL--DAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGG----GAAAQALRDLDTLRQFLTGPGLFALFDlpwAPIF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 303 IVFGF----VLAYYDL--SIfglfllgnllyVIWVLSFMKyrreldlRRFSQASTEQSTLYQII-TGMQEIKLNNCET-- 373
Cdd:COG4618 147 LAVLFlfhpLLGLLALvgAL-----------VLVALALLN-------ERLTRKPLKEANEAAIRaNAFAEAALRNAEVie 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 374 --------QKRWkweriqvklFKISVKGLALQ-QYQQVGSV------FFNQTTNILISYIAARAVVEGNMTLGMMMSLTY 438
Cdd:COG4618 209 amgmlpalRRRW---------QRANARALALQaRASDRAGGfsalskFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 439 IIGQLNSPIEQFIGFARSFQDAKISLERLNEIHQKEDEEETAVDkvsfLPQ-DHTFTIENLCFSYDGSPDYVLNNVNLTI 517
Cdd:COG4618 280 LMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMP----LPRpKGRLSVENLTVVPPGSKRPILRGVSFSL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 518 PRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP-HLWRSVtGSVMQDGFIFSETIAENIA-IGEevI 595
Cdd:COG4618 356 EPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDReELGRHI-GYLPQDVELFDGTIAENIArFGD--A 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 596 DKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNE 675
Cdd:COG4618 433 DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA 512
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 496428897 676 F-YRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQE 714
Cdd:COG4618 513 LkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
493-710 |
1.84e-63 |
|
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: 210.91 E-value: 1.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSPDYVLNNVNLTI-PRNKItAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTG 571
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIrAGEKV-AIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDF 651
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 652 LFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEG 710
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
170-715 |
1.33e-62 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 218.76 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 170 LSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINIS 249
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 250 LISDFLVKLMRLPLhffdTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLayYDLSIFGLFLLGNLLYVI 329
Cdd:TIGR01842 81 LNQPIFAASFSATL----RRGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVC--FLLHPWIGILALGGAVVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 330 WVLSFMKyrreldlRRFSQASTEQSTLYQIITGMQ-EIKLNNCET----------QKRWKWERIQvklfKISVKGLALQQ 398
Cdd:TIGR01842 155 VGLALLN-------NRATKKPLKEATEASIRANNLaDSALRNAEVieamgmmgnlTKRWGRFHSK----YLSAQSAASDR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 399 YQQVGSV--FFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEIHqkedE 476
Cdd:TIGR01842 224 AGMLSNLskYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELL----A 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 477 EETAVDKVSFLPQ-DHTFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGD 555
Cdd:TIGR01842 300 NYPSRDPAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 556 VYLKNINPH-LWRSVtGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQG 634
Cdd:TIGR01842 380 ADLKQWDREtFGKHI-GYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 635 QRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQ 713
Cdd:TIGR01842 459 QRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERD 538
|
..
gi 496428897 714 EL 715
Cdd:TIGR01842 539 EV 540
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
474-731 |
2.81e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 216.25 E-value: 2.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 474 EDEEETAVDKVSFLPQDHTFTIE--NLC-FSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFyTPNKGN 550
Cdd:PRK11174 329 ETPLAHPQQGEKELASNDPVTIEaeDLEiLSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 551 IKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSG 630
Cdd:PRK11174 406 LKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 631 ISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEG 710
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
250 260
....*....|....*....|.
gi 496428897 711 THQELTCLKGIYYRLVKNQLE 731
Cdd:PRK11174 566 DYAELSQAGGLFATLLAHRQE 586
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
142-726 |
3.33e-61 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 218.44 E-value: 3.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 142 VLEPTPDFYSMEEDRKEAKKKLNF-FFRYLSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNL-NFITLILV 219
Cdd:TIGR00958 127 VLSSAGASEKEAEQGQSETADLLFrLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPpALASAIFF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 220 AQLIIFIARLSVdFIRSWLLLHMNIRINISLISDFLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESfltgSSISTLFS- 298
Cdd:TIGR00958 207 MCLLSIASSVSA-GLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMS----RSLSLNVNv 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 299 FVNFIVFGFVLAYYDLSIFGLFLLGNLLYV--IWVLS--FMKYRRELDLRrfSQASTEQST--LYQIITGMQEIKLNNCE 372
Cdd:TIGR00958 282 LLRNLVMLLGLLGFMLWLSPRLTMVTLINLplVFLAEkvFGKRYQLLSEE--LQEAVAKANqvAEEALSGMRTVRSFAAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 373 TQ--KRWKwERIQVKLFKISVKGLALQQYQQVGSVFFNqTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQF 450
Cdd:TIGR00958 360 EGeaSRFK-EALEETLQLNKRKALAYAGYLWTTSVLGM-LIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 451 IGFARSFQDAKISLERLNEIhqkedeeetaVDKVSFLPQDHTFTIENL---------CFSYDGSPDY-VLNNVNLTIPRN 520
Cdd:TIGR00958 438 SYVYSGMMQAVGASEKVFEY----------LDRKPNIPLTGTLAPLNLegliefqdvSFSYPNRPDVpVLKGLTFTLHPG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 521 KITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERL 600
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEI 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 601 LKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEhLNEFYrGK 680
Cdd:TIGR00958 588 MAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE-SRSRA-SR 665
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 496428897 681 TVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLV 726
Cdd:TIGR00958 666 TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
458-701 |
6.65e-61 |
|
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: 213.69 E-value: 6.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 458 QDAKISLERLNEIHQkEDEEETAVDKVSFLPQDHTFTIENLCFSYDGSpDYVLNNVNLTIPRNKITAIVGASGSGKTTLI 537
Cdd:TIGR02857 288 ADGVAAAEALFAVLD-AAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 538 KLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLP 617
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 618 LGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADK 697
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADR 525
|
....
gi 496428897 698 IVVL 701
Cdd:TIGR02857 526 IVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
169-730 |
6.19e-59 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 209.49 E-value: 6.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 169 YLSPHKKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLL------LHM 242
Cdd:PRK11176 19 TIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGITSFISSYCIswvsgkVVM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 243 NIRINIslisdfLVKLMRLPLHFFDTKMIGDIMQRIG-DHSRIESfltgSSISTLFSFVN---FIVFGFVLAYY---DLS 315
Cdd:PRK11176 99 TMRRRL------FGHMMGMPVSFFDKQSTGTLLSRITyDSEQVAS----SSSGALITVVRegaSIIGLFIMMFYyswQLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 316 IFGLFLLGNLLYVIWVLSfmkyRRELDLRRFSQASTEQ--STLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKG 393
Cdd:PRK11176 169 LILIVIAPIVSIAIRVVS----KRFRNISKNMQNTMGQvtTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 394 LALQQyqqvgsvffnqTTNILISYIAARAV-----------VEGNMTLGmmmSLTYIIGQ---LNSPIEQFIGFARSFQD 459
Cdd:PRK11176 245 VSASS-----------ISDPIIQLIASLALafvlyaasfpsVMDTLTAG---TITVVFSSmiaLMRPLKSLTNVNAQFQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 460 AKISLERLNEIHQKEDEEETAVDKVSFLPQDHTFtiENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKL 539
Cdd:PRK11176 311 GMAACQTLFAILDLEQEKDEGKRVIERAKGDIEF--RNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 540 LLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIG-EEVIDKERLLKAAQIANIDQFIDSLPL 618
Cdd:PRK11176 389 LTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDN 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 619 GYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKI 698
Cdd:PRK11176 469 GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEI 548
|
570 580 590
....*....|....*....|....*....|..
gi 496428897 699 VVLDKGGIVEEGTHQELTCLKGIYYRLVKNQL 730
Cdd:PRK11176 549 LVVEDGEIVERGTHAELLAQNGVYAQLHKMQF 580
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
423-729 |
1.55e-58 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 208.66 E-value: 1.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 423 VVEGNMTLG---MMMSL-TYIIGQLnspiEQFIGFARS-FQDAKisleRLNEIHQKED------EEETAVDkVSFLPQDH 491
Cdd:PRK13657 265 VQKGQLRVGevvAFVGFaTLLIGRL----DQVVAFINQvFMAAP----KLEEFFEVEDavpdvrDPPGAID-LGRVKGAV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 492 TFtiENLCFSYDGSPDYVlNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTG 571
Cdd:PRK13657 336 EF--DDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDF 651
Cdd:PRK13657 413 VVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 652 LFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLVKNQ 729
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
496-706 |
7.97e-54 |
|
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: 184.98 E-value: 7.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 496 ENLCFSYDGSPDY-VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVM 574
Cdd:cd03248 15 QNVTFAYPTRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFF 654
Cdd:cd03248 95 QEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496428897 655 DEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGI 706
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
174-467 |
1.38e-52 |
|
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: 183.92 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLS 333
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNI 413
Cdd:cd18568 161 SSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 496428897 414 LISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18568 241 AVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
181-731 |
1.18e-51 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 189.15 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDvGIRDNNLNFITLILVAQLIIFIArLSVDFIRS-W--LLLHMNIRINISLISDFLVK 257
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVD-GVTEQHMTTGQILMWIGTMVLIA-VVVYLLRYvWrvLLFGASYQLAVELREDFYRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 258 LMRLPLHFFDTKMIGDIMQR-IGDHSRIeSFLTGSSISTLfsfVNFIVFGF-VLAYYDLSIFglfllgnllyviWVLSFM 335
Cdd:PRK10789 79 LSRQHPEFYLRHRTGDLMARaTNDVDRV-VFAAGEGVLTL---VDSLVMGCaVLIVMSTQIS------------WQLTLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 336 -------------KYRRELDlRRFSQASTEQSTLyqiitgmqeiklNNcetqkrwkweRIQVKLFKIS-VKGLALQQYQq 401
Cdd:PRK10789 143 allpmpvmaimikRYGDQLH-ERFKLAQAAFSSL------------ND----------RTQESLTSIRmIKAFGLEDRQ- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 402 vgSVFFNQTT------NILISYIAAR----------------------AVVEGNMTLGMMMSLTYIIGQLNSPIeqfIGF 453
Cdd:PRK10789 199 --SALFAADAedtgkkNMRVARIDARfdptiyiaigmanllaigggswMVVNGSLTLGQLTSFVMYLGLMIWPM---LAL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 454 ARSFQDAKISLERLNEIHQKEDEEETAVDKVSFLPQDH-TFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSG 532
Cdd:PRK10789 274 AWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRgELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 533 KTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQF 612
Cdd:PRK10789 354 KSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDD 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 613 IDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTV 692
Cdd:PRK10789 434 ILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSAL 513
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 496428897 693 QNADKIVVLDKGGIVEEGTHQELTCLKGIY---YRLvkNQLE 731
Cdd:PRK10789 514 TEASEILVMQHGHIAQRGNHDQLAQQSGWYrdmYRY--QQLE 553
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
495-711 |
4.22e-51 |
|
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: 177.30 E-value: 4.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDYVLNNVNLTI-PRNKItAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:cd03244 5 FKNVSLRYRPNLPPVLKNISFSIkPGEKV-GIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSETIAENIAIGEEVIDkERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03244 84 PQDPVLFSGTIRSNLDPFGEYSD-EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGT 711
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
174-467 |
1.21e-50 |
|
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: 178.79 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLS 333
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNI 413
Cdd:cd18570 161 FNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 496428897 414 LISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18570 241 LILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| Peptidase_C39B |
cd02418 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
4-148 |
3.01e-50 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239099 [Multi-domain] Cd Length: 136 Bit Score: 172.01 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 4 YPVYTQLDRMDCGPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQ-LVDDFPLPCI 82
Cdd:cd02418 1 YPYVLQVDEMDCGAACLAMIAKYYGKNYSLAKLRELAGTDREGTSLLGLVKAAEKLGFETRAVKADMDLfELKDIPLPFI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 83 LH----WNQQHFVVCYRIRKRrnkyKILIGDPAGTQTvTYNEEEFKRCWissrekgqdTGVALVLEPTPD 148
Cdd:cd02418 81 AHvikeWKLNHYVVVYKIKKK----KILIADPAVGIT-KISKEEFEKEW---------TGVALFLEPTPN 136
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
463-725 |
8.80e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 180.79 E-value: 8.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 463 SLERLNEI-HQKED-----EEETAVDKVSFlpqdhtfTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTL 536
Cdd:PRK11160 310 SARRINEItEQKPEvtfptTSTAAADQVSL-------TLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 537 IKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIANIDQFIDSl 616
Cdd:PRK11160 383 LQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 617 PLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNAD 696
Cdd:PRK11160 462 DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541
|
250 260
....*....|....*....|....*....
gi 496428897 697 KIVVLDKGGIVEEGTHQELTCLKGIYYRL 725
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
493-715 |
4.36e-48 |
|
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: 169.44 E-value: 4.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSPdYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGS 572
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQ--DGFIFSETIAENIAIG--------EEVidKERLLKAAQIANIDQFIDSLP--LgyntkigmegsgiSQGQRQRIL 640
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAFGpenlglprEEI--RERVEEALELVGLEHLADRPPheL-------------SGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 641 IARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
495-706 |
9.44e-48 |
|
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: 166.62 E-value: 9.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVM 574
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFIFSETIAENIaigeevidkerllkaaqianidqfidslplgyntkigmegsgISQGQRQRILIARAVYKNPDFLFF 654
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 655 DEATNALDANNEREIME---HLNEfyRGKTVVIVAHRLSTVQNADKIVVLDKGGI 706
Cdd:cd03246 121 DEPNSHLDVEGERALNQaiaALKA--AGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
174-467 |
2.58e-47 |
|
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: 169.61 E-value: 2.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLS 333
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNI 413
Cdd:cd18555 161 TRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 496428897 414 LISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18555 241 LILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
425-730 |
4.21e-47 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 176.45 E-value: 4.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 425 EGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEI----HQKEDEEETAVdkvsflpQDHTFTIENLCF 500
Cdd:PRK10790 276 SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELmdgpRQQYGNDDRPL-------QSGRIDIDNVSF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 501 SY-DGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFI 579
Cdd:PRK10790 349 AYrDDNL--VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVV 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSETIAENIAIGEEvIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:PRK10790 427 LADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 660 ALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLVKNQL 730
Cdd:PRK10790 506 NIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQL 576
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
495-704 |
7.95e-47 |
|
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: 164.95 E-value: 7.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDG---SPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGdvylkninphlwRSVtG 571
Cdd:cd03250 3 VEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP------------GSI-A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQDGFIFSETIAENIAIGEEvIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDF 651
Cdd:cd03250 70 YVSQEPWIQNGTIRENILFGKP-FDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 652 LFFDEATNALDANNEREIMEH--LNEFYRGKTVVIVAHRLSTVQNADKIVVLDKG 704
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
495-704 |
3.65e-45 |
|
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: 160.71 E-value: 3.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVM 574
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 Q--DGFIFSETIAENIAIG------EEVIDKERLLKAAQIANI----DQFIDSLplgyntkigmegSGisqGQRQRILIA 642
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLeglrDRSPFTL------------SG---GQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 643 RAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQN-ADKIVVLDKG 704
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
454-689 |
5.09e-44 |
|
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: 166.38 E-value: 5.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 454 ARSFQDAKISLERLNEI-----HQKEDEEETAVDKVSFLPqdhTFTIENLCFSYDGSPDyVLNNVNLTIPRNKITAIVGA 528
Cdd:TIGR02868 294 AQQLTRVRAAAERIVEVldaagPVAEGSAPAAGAVGLGKP---TLELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGP 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 529 SGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIAN 608
Cdd:TIGR02868 370 SGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 609 IDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHR 688
Cdd:TIGR02868 450 LADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
.
gi 496428897 689 L 689
Cdd:TIGR02868 530 L 530
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
494-731 |
2.24e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.98 E-value: 2.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDvylKNI--NPHLWRSVTG 571
Cdd:COG1131 2 EVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG---EDVarDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQDGFIFSE-TIAENIA-------IGEEVIDK--ERLLKAAQIAN-IDQFIDSLplgyntkigmegsgiSQGQRQRIL 640
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlygLPRKEAREriDELLELFGLTDaADRKVGTL---------------SGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 641 IARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQELT-- 716
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKar 221
|
250
....*....|....*
gi 496428897 717 CLKGIYYRLVKNQLE 731
Cdd:COG1131 222 LLEDVFLELTGEEAR 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
494-716 |
4.77e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 4.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVylkniNPHLWRSVTGSV 573
Cdd:COG1121 8 ELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQdgfifSETIAENIAI-GEEVI-----------------DKERLLKAAQIANIDQFIDslplgynTKIGmEGSGisqGQ 635
Cdd:COG1121 81 PQ-----RAEVDWDFPItVRDVVlmgrygrrglfrrpsraDREAVDEALERVGLEDLAD-------RPIG-ELSG---GQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 636 RQRILIARAVYKNPDFLFFDEATNALDANNEREIME---HLNEfyRGKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGT 711
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrELRR--EGKTILVVTHDLGAVrEYFDRVLLLNRGLVAHGPP 222
|
....*
gi 496428897 712 HQELT 716
Cdd:COG1121 223 EEVLT 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
494-710 |
7.50e-41 |
|
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: 147.58 E-value: 7.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHlwrsvtgsv 573
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 mqdgfifseTIAENIAIGEEVIDkerLLKAAQIAniDQFIDSLplgyntkigmegSGisqGQRQRILIARAVYKNPDFLF 653
Cdd:cd03214 70 ---------ELARKIAYVPQALE---LLGLAHLA--DRPFNEL------------SG---GERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 654 FDEATNALDANNEREIMEHLNEF--YRGKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEG 710
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
493-715 |
2.06e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 149.04 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP-HLWRSVtG 571
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELARRI-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQDGFI-FSETIAENIAIG---------------EEVIdkERLLKAAQIANI-DQFIDSLplgyntkigmegSGisqG 634
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgrpsaedREAV--EEALERTGLEHLaDRPVDEL------------SG---G 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 635 QRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF--YRGKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEGT 711
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
....
gi 496428897 712 HQEL 715
Cdd:COG1120 222 PEEV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
494-710 |
6.19e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 146.50 E-value: 6.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSY--DGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHL---WRS 568
Cdd:cd03257 3 EVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkiRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 569 VTGSVMQD-----------GFIFSETI-AENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLgyntkigmEGSGisqGQR 636
Cdd:cd03257 83 EIQMVFQDpmsslnprmtiGEQIAEPLrIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPH--------ELSG---GQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 637 QRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFY--RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG 710
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeeLGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
494-715 |
4.64e-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: 151.59 E-value: 4.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPN---KGNIKVGDVYLKNINPHLWRSVT 570
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 571 GSVMQDGF--IFSETIAENIAIGEEVID------KERLLKAAQIANIDQFIDSLPlgyntkigMEGSGisqGQRQRILIA 642
Cdd:COG1123 86 GMVFQDPMtqLNPVTVGDQIAEALENLGlsraeaRARVLELLEAVGLERRLDRYP--------HQLSG---GQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 643 RAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
494-732 |
7.46e-39 |
|
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: 144.23 E-value: 7.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVtgSV 573
Cdd:COG4555 3 EVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI--GV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSE--TIAENIAIGEEV--IDKERLLKAaqianIDQFIDSLPLG--YNTKIGmegsGISQGQRQRILIARAVYK 647
Cdd:COG4555 79 LPDERGLYDrlTVRENIRYFAELygLFDEELKKR-----IEELIELLGLEefLDRRVG----ELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 648 NPDFLFFDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL------TCLK 719
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELreeigeENLE 229
|
250
....*....|...
gi 496428897 720 GIYYRLVKNQLEL 732
Cdd:COG4555 230 DAFVALIGSEEGE 242
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
493-706 |
8.73e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 142.65 E-value: 8.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGS 572
Cdd:COG4619 1 LELEGLSFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQDGFIFSETIAENIA----IGEEVIDKERLLKAAQIANIDQFIdslpLGYNTkigmegSGISQGQRQRILIARAVYKN 648
Cdd:COG4619 79 VPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLPPDI----LDKPV------ERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 649 PDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAH------RLstvqnADKIVVLDKGGI 706
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
495-715 |
1.70e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 143.20 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSV---TG 571
Cdd:COG1127 8 VRNLTKSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQDGFIF-SETIAENIA--------IGEEVIDKERLLKAAQiANIDQFIDSLPlgyntkigmegSGISQGQRQRILIA 642
Cdd:COG1127 86 MLFQGGALFdSLTVFENVAfplrehtdLSEAEIRELVLEKLEL-VGLPGAADKMP-----------SELSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 643 RAVYKNPDFLFFDEATNALDANNEREIME---HLNEFYrGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDElirELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
495-709 |
3.29e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.72 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSY-DGSPDY-VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP----HLWRS 568
Cdd:COG1136 7 LRNLTKSYgTGEGEVtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelaRLRRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 569 VTGSVMQDGFIFSE-TIAENIAIG------EEVIDKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILI 641
Cdd:COG1136 87 HIGFVFQFFNLLPElTALENVALPlllagvSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 642 ARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQNADKIVVLDKGGIVEE 709
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
174-467 |
6.97e-38 |
|
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: 143.12 E-value: 6.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLS 333
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWER-----IQvKLFKISVKGLALQQYqqvgSVFFN 408
Cdd:cd18782 161 FGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNryarsLG-EGFKLTVLGTTSGSL----SQFLN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 409 QTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18782 236 KLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
174-467 |
8.01e-38 |
|
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: 142.99 E-value: 8.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLS 333
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNI 413
Cdd:cd18567 161 LYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 414 LISYIAARAVVEGNMTLGMMMS-LTYiIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18567 241 LVIYLGALLVLDGEFTVGMLFAfLAY-KDQFSSRASSLIDKLFELRMLRLHLERL 294
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
510-659 |
9.58e-38 |
|
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: 137.78 E-value: 9.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSE-TIAENI 588
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 589 AIGEEVidkERLLKAAQIANIDQFIDSLPLGY--NTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:pfam00005 81 RLGLLL---KGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
495-715 |
1.50e-37 |
|
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: 140.33 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSV---TG 571
Cdd:cd03261 3 LRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQDGFIF-SETIAENIA--------IGEEVIDKERLLKAAQiANIDQFIDSLPlgyntkigmegSGISQGQRQRILIA 642
Cdd:cd03261 81 MLFQSGALFdSLTVFENVAfplrehtrLSEEEIREIVLEKLEA-VGLRGAEDLYP-----------AELSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 643 RAVYKNPDFLFFDEATNALDANNEREIME---HLNEFYrGKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDlirSLKKEL-GLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
494-704 |
2.71e-37 |
|
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: 136.61 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQdgfifsetiaeniaigeevidkerllkaaqianidqfidslplgyntkigmegsgISQGQRQRILIARAVYKNPDFLF 653
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496428897 654 FDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQNA-DKIVVLDKG 704
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
494-715 |
3.65e-37 |
|
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: 146.20 E-value: 3.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPD---YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP----HLW 566
Cdd:COG1123 262 EVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslrELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVtGSVMQDGF--IF-SETIAENIAigeEVIDKERLLKAAQI-ANIDQFIDS--LPLGYNTKIGMEGSGisqGQRQRIL 640
Cdd:COG1123 342 RRV-QMVFQDPYssLNpRMTVGDIIA---EPLRLHGLLSRAERrERVAELLERvgLPPDLADRYPHELSG---GQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 641 IARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
488-711 |
9.10e-37 |
|
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: 137.16 E-value: 9.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 488 PQDHTFTIENLCFSYdgSPDY--VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHL 565
Cdd:cd03369 2 PEHGEIEVENLSVRY--APDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 WRSVTGSVMQDGFIFSETIAENIAIGEEVIDKErLLKAAQIANidqfidslplgyntkigmEGSGISQGQRQRILIARAV 645
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEE-IYGALRVSE------------------GGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 646 YKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGT 711
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
494-710 |
1.47e-36 |
|
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: 136.50 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVtGSV 573
Cdd:cd03259 2 ELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-RNI-GMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSE-TIAENIAIG-------EEVIdKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAV 645
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlklrgvpKAEI-RARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 646 YKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEG 710
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
495-710 |
1.83e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.72 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNIN----PHLWRSVt 570
Cdd:COG2884 4 FENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreiPYLRRRI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 571 GSVMQD-GFIFSETIAENIAIGEEVIDKERLLKAAQIA------NIDQFIDSLPlgyntkigMEGSGisqGQRQRILIAR 643
Cdd:COG2884 82 GVVFQDfRLLPDRTVYENVALPLRVTGKSRKEIRRRVRevldlvGLSDKAKALP--------HELSG---GEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 644 AVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQNADK-IVVLDKGGIVEEG 710
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
495-706 |
4.44e-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: 133.68 E-value: 4.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNiNPHLWRSVTGSVM 574
Cdd:cd03230 3 VRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFIFSE-TIAENIaigeevidkeRLlkaaqianidqfidslplgyntkigmegsgiSQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03230 80 EEPSLYENlTVRENL----------KL-------------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 654 FDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTVQN-ADKIVVLDKGGI 706
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
495-706 |
1.62e-35 |
|
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: 133.81 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVylkniNPHLWRSVTGSVM 574
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFI---FSETIAENIAIG----------EEVIDKERLLKAAQIANIDQFIDSlPLGyntkigmEGSGisqGQRQRILI 641
Cdd:cd03235 75 QRRSIdrdFPISVRDVVLMGlyghkglfrrLSKADKAKVDEALERVGLSELADR-QIG-------ELSG---GQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 642 ARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQN-ADKIVVLDKGGI 706
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
508-715 |
1.63e-35 |
|
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: 134.25 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 508 YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVmqdGFIF------- 580
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRI---GMIFqhfnlls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 581 SETIAENIAIGEEVidkERLLKAAQIANIDQFIDSLPLGynTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNA 660
Cdd:cd03258 96 SRTVFENVALPLEI---AGVPKAEIEERVLELLELVGLE--DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 661 LDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:cd03258 171 LDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
495-727 |
1.76e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 145.17 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDY-VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYT---------------------------- 545
Cdd:PTZ00265 1168 IMDVNFRYISRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdee 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 546 --------------------------PNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKER 599
Cdd:PTZ00265 1248 qnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATRED 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 600 LLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF--Y 677
Cdd:PTZ00265 1328 VKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdK 1407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 678 RGKTVVIVAHRLSTVQNADKIVVL---DKGG--IVEEGTHQELTCLK-GIYYRLVK 727
Cdd:PTZ00265 1408 ADKTIITIAHRIASIKRSDKIVVFnnpDRTGsfVQAHGTHEELLSVQdGVYKKYVK 1463
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
493-713 |
1.94e-35 |
|
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: 133.85 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGspDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLL-----LGFYTPNKGNIKVG--DVYLKNINPHL 565
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDgkDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 WRSVTGSVMQDGFIFSETIAENIAIG--------EEVIDkERLLKAAQIANI-DQFIDSLplgyntkigmEGSGISQGQR 636
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklKEELD-ERVEEALRKAALwDEVKDRL----------HALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 637 QRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG-THQ 713
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGpTEQ 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
495-715 |
3.39e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.73 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVM 574
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QD---GFIFSeTIAENIAIGEE--VID----KERLLKAAQIANIDQFIDSLPLgyntkigmegsGISQGQRQRILIARAV 645
Cdd:PRK13632 90 QNpdnQFIGA-TVEDDIAFGLEnkKVPpkkmKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 646 YKNPDFLFFDEATNALDANNEREIMEHLNEFY--RGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
363-728 |
3.61e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 143.96 E-value: 3.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 363 MQEIkLNNCETQKRWKWER-IQVKLFKISVKGLALQQYQQVGSVFFNQTTN------ILISYiAARAVVEGNMTLGMMMS 435
Cdd:PLN03232 482 INEI-LASMDTVKCYAWEKsFESRIQGIRNEELSWFRKAQLLSAFNSFILNsipvvvTLVSF-GVFVLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 436 LTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEIHQKEdeEETAVDKVSFLPQDHTFTIENLCFSYDG-SPDYVLNNVN 514
Cdd:PLN03232 560 SLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSE--ERILAQNPPLQPGAPAISIKNGYFSWDSkTSKPTLSDIN 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 515 LTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVgdvylkninphlWRSVTGSVMQDGFIFSETIAENIAIGEEv 594
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFGSD- 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 595 IDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEH-L 673
Cdd:PLN03232 705 FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScM 784
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 674 NEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLVKN 728
Cdd:PLN03232 785 KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMEN 839
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
174-467 |
3.63e-35 |
|
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: 135.32 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYV-IWVL 332
Cdd:cd18588 81 LFRHLLRLPLSYFESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYAlLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 333 SFMKYRRELDlRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTN 412
Cdd:cd18588 161 VTPILRRRLE-EKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 413 ILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18588 240 LAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
493-710 |
4.03e-35 |
|
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: 131.28 E-value: 4.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVTGS 572
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-SSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQDGFIFSETIAENIaigeevidkerllkaaqianidqfidslplgyntkigmeGSGISQGQRQRILIARAVYKNPDFL 652
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 653 FFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEG 710
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
459-728 |
5.41e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 143.34 E-value: 5.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 459 DAKISLERLNEIHQKEdeEETAVDKVSFLPQDHTFTIENLCFSYDGSPDY-VLNNVNLTIPRNKITAIVGASGSGKTTLI 537
Cdd:PLN03130 583 NANVSLKRLEELLLAE--ERVLLPNPPLEPGLPAISIKNGYFSWDSKAERpTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 538 KLLLGFYTPNKGnikvGDVYLkninphlwRSVTGSVMQDGFIFSETIAENIAIGEEvIDKERLLKAAQIANIDQFIDSLP 617
Cdd:PLN03130 661 SAMLGELPPRSD----ASVVI--------RGTVAYVPQVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLP 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 618 LGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEH-LNEFYRGKTVVIVAHRLSTVQNAD 696
Cdd:PLN03130 728 GGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVD 807
|
250 260 270
....*....|....*....|....*....|..
gi 496428897 697 KIVVLDKGGIVEEGTHQELTCLKGIYYRLVKN 728
Cdd:PLN03130 808 RIILVHEGMIKEEGTYEELSNNGPLFQKLMEN 839
|
|
| Peptidase_C39 |
pfam03412 |
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
3-148 |
7.19e-35 |
|
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family.
Pssm-ID: 367483 [Multi-domain] Cd Length: 133 Bit Score: 128.88 E-value: 7.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 3 HYPVYTQLDRMDCGPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLvDDFPLPCI 82
Cdd:pfam03412 1 KYKIVLQVDENDCGLACLAMILKYYGSNVSLEELRELAGTPAEGTSLLGLKKAAEKLGFKAKAIKADLSEL-KELPLPFI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 83 LHWNQQ--HFVVCYRIRKRrnkyKILIGDPA-GtqTVTYNEEEFKRCWissrekgqdTGVALVLEPTPD 148
Cdd:pfam03412 80 AHWDGNggHFVVVYGIKKN----KVLIADPAvG--KIKLSREEFEKEW---------TGVALLVAPKPS 133
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
495-715 |
1.71e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 131.85 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPD--YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGS 572
Cdd:COG1124 4 VRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQDG-------FIFSETIAENIAIGEEVIDKERLLKAAQIANID-QFIDSLP--LgyntkigmegSGisqGQRQRILIA 642
Cdd:COG1124 84 VFQDPyaslhprHTVDRILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRYPhqL----------SG---GQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 643 RAVYKNPDFLFFDEATNALDANNEREIMEHLNEF--YRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLreERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
177-467 |
2.18e-34 |
|
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: 133.06 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 177 LVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLV 256
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 257 KLMRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLSFM 335
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLtSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 336 KYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNILI 415
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 496428897 416 SYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
495-715 |
2.62e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 133.64 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDYV--LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPN---KGNIKVGDVYLKNINPHLWRSV 569
Cdd:COG0444 4 VRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 570 TGSVMQdgFIF-------------SETIAENIAI-----GEEVIDK-ERLLKAAQIANIDQFIDSLP--Lgyntkigmeg 628
Cdd:COG0444 84 RGREIQ--MIFqdpmtslnpvmtvGDQIAEPLRIhgglsKAEARERaIELLERVGLPDPERRLDRYPheL---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 629 SGisqGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTV-QNADKIVVLDKGG 705
Cdd:COG0444 152 SG---GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVaEIADRVAVMYAGR 228
|
250
....*....|
gi 496428897 706 IVEEGTHQEL 715
Cdd:COG0444 229 IVEEGPVEEL 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
495-704 |
5.15e-34 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 129.53 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPD--YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLW-----R 567
Cdd:cd03255 3 LKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 568 SVtgsvmqdGFIFSE-------TIAENIAIGEEVI------DKERLLKAAQIANIDQFIDSLPlgyntkigMEGSGisqG 634
Cdd:cd03255 83 HI-------GFVFQSfnllpdlTALENVELPLLLAgvpkkeRRERAEELLERVGLGDRLNHYP--------SELSG---G 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 635 QRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF--YRGKTVVIVAHRLSTVQNADKIVVLDKG 704
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
494-709 |
1.57e-33 |
|
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: 128.36 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDY--VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHlwrsvTG 571
Cdd:cd03293 2 EVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQDGFIFS-ETIAENIAIGEEVidkERLLKAAQIANIDQFIDslplgyntKIGMEGSG------ISQGQRQRILIARA 644
Cdd:cd03293 77 YVFQQDALLPwLTVLDNVALGLEL---QGVPKAEARERAEELLE--------LVGLSGFEnayphqLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 645 VYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLS-TVQNADKIVVLDK--GGIVEE 709
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
493-704 |
5.81e-33 |
|
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: 124.99 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSpdYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVG--DVYLKNINPHLWRSVT 570
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgeDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 571 GSVMQDGFIFSE-TIAENIAigeevidkerllkaaqianidqfidsLPLgyntkigmegSGisqGQRQRILIARAVYKNP 649
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIA--------------------------LGL----------SG---GQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 650 DFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKG 704
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
495-715 |
8.53e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.82 E-value: 8.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINphLW--RSVTGS 572
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET--VWdvRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQ--DGFIFSETIAENIAIG--------EEVIdkERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIA 642
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGlenigvprEEMV--ERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 643 RAVYKNPDFLFFDEATNALDANNEREIME---HLNEfYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLEtvrQLKE-QKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
487-729 |
1.52e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 135.93 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 487 LPQDHTFTIENLCFSYDGSPDY-VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVY-LKNINPH 564
Cdd:PTZ00265 377 LKDIKKIQFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 565 LWRSVTGSVMQDGFIFSETIAENI-----------AIGE----------------------------------------- 592
Cdd:PTZ00265 457 WWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleALSNyynedgndsqenknkrnscrakcagdlndmsnttdsnelie 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 593 -----EVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNER 667
Cdd:PTZ00265 537 mrknyQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 668 EIMEHLNEFY--RGKTVVIVAHRLSTVQNADKIVVL--------------------------------DKGG-------- 705
Cdd:PTZ00265 617 LVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkdDNNNnnnnnnnk 696
|
330 340 350
....*....|....*....|....*....|..
gi 496428897 706 -------IVEEGTHQELTCLK-GIYYRLVKNQ 729
Cdd:PTZ00265 697 innagsyIIEQGTHDALMKNKnGIYYTMINNQ 728
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
494-715 |
4.22e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 124.72 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL----KNINPHlwRSV 569
Cdd:COG1126 3 EIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINKL--RRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 570 TGSVMQDGFIFSE-TIAENIAIG---------EEVIDK-ERLLKAAQIAN-IDQFIDSLplgyntkigmegSGisqGQRQ 637
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLApikvkkmskAEAEERaMELLERVGLADkADAYPAQL------------SG---GQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 638 RILIARAVYKNPDFLFFDEATNALDANNERE---IMEHLNEfyRGKTVVIVAHRLS---TVqnADKIVVLDKGGIVEEGT 711
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEvldVMRDLAK--EGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGP 219
|
....
gi 496428897 712 HQEL 715
Cdd:COG1126 220 PEEF 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
494-715 |
6.32e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.19 E-value: 6.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGD-VYLKNINPHLwRSVtgs 572
Cdd:COG1118 4 EVRNISKRFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrDLFTNLPPRE-RRV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 vmqdGFIFSE-------TIAENIAIG-------EEVIDK--ERLLKAAQianIDQFIDSLPlgyntkigmegSGISQGQR 636
Cdd:COG1118 78 ----GFVFQHyalfphmTVAENIAFGlrvrppsKAEIRArvEELLELVQ---LEGLADRYP-----------SQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 637 QRILIARAVYKNPDFLFFDEATNALDANN----EREIMEHLNEFyrGKTVVIVAH------RLstvqnADKIVVLDKGGI 706
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVrkelRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRI 212
|
....*....
gi 496428897 707 VEEGTHQEL 715
Cdd:COG1118 213 EQVGTPDEV 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
412-728 |
3.15e-31 |
|
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: 131.61 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 412 NILISYIAARAVV-EGNMTLGMM-MSLTYIIgQLNSPIEQFIGFARSFQDAKISLERLNEIHQKEDE-----EETAvdKV 484
Cdd:TIGR00957 1200 NCIVLFAALFAVIsRHSLSAGLVgLSVSYSL-QVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEapwqiQETA--PP 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 485 SFLPQDHTFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPH 564
Cdd:TIGR00957 1277 SGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 565 LWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKErLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARA 644
Cdd:TIGR00957 1357 DLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEE-VWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARA 1435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 645 VYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKGIYYR 724
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
....
gi 496428897 725 LVKN 728
Cdd:TIGR00957 1516 MAKD 1519
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
494-709 |
8.32e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.74 E-value: 8.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDY--VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwrsvtg 571
Cdd:COG1116 9 ELRGVSKRFPTGGGGvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 svmqdGFIFSE-------TIAENIAIGEEVidkERLLKAAQIANIDQFIDslplgyntKIGMEGSG------ISQGQRQR 638
Cdd:COG1116 83 -----GVVFQEpallpwlTVLDNVALGLEL---RGVPKAERRERARELLE--------LVGLAGFEdayphqLSGGMRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 639 ILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAH------RLstvqnADKIVVLDK--GGIVE 708
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
.
gi 496428897 709 E 709
Cdd:COG1116 222 E 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
494-724 |
9.25e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 124.05 E-value: 9.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVtGSV 573
Cdd:COG3842 7 ELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RNV-GMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSE-TIAENIAIGeeviDKERLLKAAQIAN-IDQFIDslplgyntKIGMEG---------SGisqGQRQRILIA 642
Cdd:COG3842 83 FQDYALFPHlTVAENVAFG----LRMRGVPKAEIRArVAELLE--------LVGLEGladryphqlSG---GQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 643 RAVYKNPDFLFFDEATNALDANN----EREIMEHLNEFyrGKTVVIVAHRLS---TVqnADKIVVLDKGGIVEEGTHQEl 715
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLreemREELRRLQREL--GITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE- 222
|
....*....
gi 496428897 716 tclkgIYYR 724
Cdd:COG3842 223 -----IYER 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
494-715 |
1.38e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.64 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGspDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDvylKNIN----------- 562
Cdd:COG3839 5 ELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTdlppkdrniam 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 563 --------PHLwrsvtgsvmqdgfifseTIAENIAIG-------EEVIDKeRLLKAAQIANIDQFIDSLPlgyntkigme 627
Cdd:COG3839 80 vfqsyalyPHM-----------------TVYENIAFPlklrkvpKAEIDR-RVREAAELLGLEDLLDRKP---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 628 gSGISQGQRQRILIARAVYKNPDFLFFDEATNALDA----NNEREIMEHLNEFyrGKTVVIVAH------RLstvqnADK 697
Cdd:COG3839 132 -KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL--GTTTIYVTHdqveamTL-----ADR 203
|
250
....*....|....*...
gi 496428897 698 IVVLDKGGIVEEGTHQEL 715
Cdd:COG3839 204 IAVMNDGRIQQVGTPEEL 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
495-715 |
3.66e-30 |
|
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: 118.88 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVtGSVM 574
Cdd:cd03300 3 LENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK-RPV-NTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFIFSE-TIAENIAIGEEVidkERLLKAAQIANIDQFIDslplgyntKIGMEG------SGISQGQRQRILIARAVYK 647
Cdd:cd03300 79 QNYALFPHlTVFENIAFGLRL---KKLPKAEIKERVAEALD--------LVQLEGyanrkpSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 648 NPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLS---TVqnADKIVVLDKGGIVEEGTHQEL 715
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
177-467 |
5.28e-30 |
|
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: 120.34 E-value: 5.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 177 LVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLV 256
Cdd:cd18779 4 LGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 257 KLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLSFMK 336
Cdd:cd18779 84 HLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 337 YRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNILIS 416
Cdd:cd18779 164 RVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 496428897 417 YIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18779 244 WVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
493-716 |
5.50e-30 |
|
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: 118.82 E-value: 5.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYdGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHL---WRSV 569
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 570 TGSVMQDGFIFSE-TIAENIAIGE--------------EVIDKERLLKAAQIANIDQFidslplgYNTKIGmEGSGisqG 634
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRlgrrstwrslfglfPKEEKQRALAALERVGLLDK-------AYQRAD-QLSG---G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 635 QRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGT 711
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGP 228
|
....*
gi 496428897 712 HQELT 716
Cdd:cd03256 229 PAELT 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
509-710 |
5.97e-30 |
|
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: 117.70 E-value: 5.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKV-GDVYLKNINPhlwRSVTGSVMQDGFIFSE-TIAE 586
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEA---LRRIGALIEAPGFYPNlTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 587 NIAIGEEVIDKERllkaaqiANIDQFIDSLPLGYNT--KIGmegsGISQGQRQRILIARAVYKNPDFLFFDEATNALDAN 664
Cdd:cd03268 92 NLRLLARLLGIRK-------KRIDEVLDVVGLKDSAkkKVK----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496428897 665 NEREIMEHL-NEFYRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG 710
Cdd:cd03268 161 GIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
510-704 |
1.82e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 116.35 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNIN----PHLWRSVtGSVMQDG-FIFSETI 584
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRRKI-GVVFQDFrLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AENIAIGEEVIDK------ERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAVYKNPDFLFFDEAT 658
Cdd:cd03292 96 YENVAFALEVTGVppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496428897 659 NALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQNADK-IVVLDKG 704
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINkAGTTVVVATHAKELVDTTRHrVIALERG 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
456-728 |
2.00e-29 |
|
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: 125.83 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 456 SFQDAKISLERLNEIHQKEDEEETAVDKVSFLP-QDHTFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKT 534
Cdd:TIGR00957 599 SIVQASVSLKRLRIFLSHEELEPDSIERRTIKPgEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKS 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 535 TLIKLLLGFYTPNKGNIkvgdvylkninpHLWRSVtGSVMQDGFIFSETIAENIAIGEEvIDKERLLKAAQIANIDQFID 614
Cdd:TIGR00957 679 SLLSALLAEMDKVEGHV------------HMKGSV-AYVPQQAWIQNDSLRENILFGKA-LNEKYYQQVLEACALLPDLE 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 615 SLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHL---NEFYRGKTVVIVAHRLST 691
Cdd:TIGR00957 745 ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISY 824
|
250 260 270
....*....|....*....|....*....|....*..
gi 496428897 692 VQNADKIVVLDKGGIVEEGTHQELTCLKGIYYRLVKN 728
Cdd:TIGR00957 825 LPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRT 861
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
494-715 |
8.35e-29 |
|
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: 115.48 E-value: 8.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDYVlNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:cd03295 2 EFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSE-TIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGisqGQRQRILIARAVYKNPDFL 652
Cdd:cd03295 81 IQQIGLFPHmTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSG---GQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 653 FFDEATNALDANNEREIMEhlnEFYR-----GKTVVIVAHRL-STVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:cd03295 158 LMDEPFGALDPITRDQLQE---EFKRlqqelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
494-710 |
1.13e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 114.27 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGspDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVtGSV 573
Cdd:cd03301 2 ELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI-AMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSE-TIAENIAIG-------EEVIDkERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAV 645
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGlklrkvpKDEID-ERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 646 YKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAH-RLSTVQNADKIVVLDKGGIVEEG 710
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
494-711 |
1.46e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 117.10 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLC--FSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTG 571
Cdd:COG1135 3 ELENLSktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVmqdGFIF-------SETIAENIAIGEEVIDKERllkaaqiANIDQFIDSLpLGYntkIGMEG---------SGisqGQ 635
Cdd:COG1135 83 KI---GMIFqhfnllsSRTVAENVALPLEIAGVPK-------AEIRKRVAEL-LEL---VGLSDkadaypsqlSG---GQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 636 RQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGT 711
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
495-707 |
1.53e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 112.14 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGdvylkninphlwrsvtgsvm 574
Cdd:cd03216 3 LRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 qdgfifsetiaeniaiGEEVidkerllkaaqiaNIDQFIDSLPLGyntkIGMegsgISQ---GQRQRILIARAVYKNPDF 651
Cdd:cd03216 61 ----------------GKEV-------------SFASPRDARRAG----IAM----VYQlsvGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 652 LFFDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIV 707
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
492-715 |
1.63e-28 |
|
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: 114.36 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 492 TFTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDvylkninphlwRSVTG 571
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG-----------EDATD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQD---GFIFSE-------TIAENIAIGEEVIDKERLLKAAQIA----------NIDQFIDSLPlgyntkigmegSGI 631
Cdd:cd03296 69 VPVQErnvGFVFQHyalfrhmTVFDNVAFGLRVKPRSERPPEAEIRakvhellklvQLDWLADRYP-----------AQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 632 SQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLS-TVQNADKIVVLDKGGIVE 708
Cdd:cd03296 138 SGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQ 217
|
....*..
gi 496428897 709 EGTHQEL 715
Cdd:cd03296 218 VGTPDEV 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
217-728 |
2.11e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 122.78 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 217 ILVAQLIIFiARLSVDFIRS-WLL---LHMNIRINISLISDFLvklmRLPLHFFDTKMIGDIMQR----IGDHSRIESFL 288
Cdd:PLN03232 953 IVVYALLGF-GQVAVTFTNSfWLIsssLHAAKRLHDAMLNSIL----RAPMLFFHTNPTGRVINRfskdIGDIDRNVANL 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 289 TGSSISTLFSFVN-FIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLSFMKYRReLDlrrfsqaSTEQSTLY----QIITGM 363
Cdd:PLN03232 1028 MNMFMNQLWQLLStFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRR-LD-------SVTRSPIYaqfgEALNGL 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 364 QEIKlnnceTQKRWKW----------ERIQVKLFKISVKGLALQQYQQVGSVffnqttniLISYIAARAVVE-GNM---- 428
Cdd:PLN03232 1100 SSIR-----AYKAYDRmakingksmdNNIRFTLANTSSNRWLTIRLETLGGV--------MIWLTATFAVLRnGNAenqa 1166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 429 ----TLGMMMSLTYIIGQLNSpieqfiGFARSFQDAKISLERLNEIHQKED--EEETAVDK----VSFLPQDHTFTIENL 498
Cdd:PLN03232 1167 gfasTMGLLLSYTLNITTLLS------GVLRQASKAENSLNSVERVGNYIDlpSEATAIIEnnrpVSGWPSRGSIKFEDV 1240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 499 CFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGF 578
Cdd:PLN03232 1241 HLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPV 1320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 579 IFSETIAENIAIGEEVIDKErLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEAT 658
Cdd:PLN03232 1321 LFSGTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 659 NALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLKG-IYYRLVKN 728
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHS 1470
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
490-710 |
2.53e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.83 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 490 DHTFTIENLCFSY-DGSpdYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRS 568
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGT--KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 569 VTGSVMQ--DGFIFSETIAENIAIG--------EEVidKERLLKAAQIANIDQFIDSLPlgYNtkigmegsgISQGQRQR 638
Cdd:PRK13647 80 KVGLVFQdpDDQVFSSTVWDDVAFGpvnmgldkDEV--ERRVEEALKAVRMWDFRDKPP--YH---------LSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 639 ILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEG 710
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
490-715 |
5.35e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.03 E-value: 5.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 490 DHTFTIENLCFSY----DGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINpHL 565
Cdd:PRK13633 2 NEMIKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE-NL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 W--RSVTGSVMQ--DGFIFSETIAENIAIGEEVID------KERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQ 635
Cdd:PRK13633 81 WdiRNKAGMVFQnpDNQIVATIVEEDVAFGPENLGippeeiRERVDESLKKVGMYEYRRHAP-----------HLLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 636 RQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQ 713
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
..
gi 496428897 714 EL 715
Cdd:PRK13633 230 EI 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
276-705 |
1.38e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 117.99 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 276 QRIGDHSR--IE---SFLTG--SSISTLFSFVnFI------VFGFVLAYYDLSIFGLFLLGNLLYVI-------WV---- 331
Cdd:COG4178 128 QRIAEDIRlfTEttlSLSLGllSSVVTLISFI-GIlwslsgSLTFTLGGYSITIPGYMVWAALIYAIigtllthLIgrpl 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 332 --LSFMKYRRELDLR----RFSQAStEQSTLYQiitgmqeiklnnCETQkrwkwERIQVK-LFKISVKGLALQQYQQVG- 403
Cdd:COG4178 207 irLNFEQQRREADFRfalvRVRENA-ESIALYR------------GEAA-----ERRRLRrRFDAVIANWRRLIRRQRNl 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 404 ---SVFFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERLNEIHQKEDEEETA 480
Cdd:COG4178 269 tffTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAADAL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 481 VDKVSFL--PQDHTFTIENLC-FSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVgdvy 557
Cdd:COG4178 349 PEAASRIetSEDGALALEDLTlRTPDGRP--LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---- 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 558 lkninPHLWRsvtgsVM---QDGFIFSETIAENIA--IGEEVIDKERLLKAAQIANIDQFIDSLPLGYN-TKIgmegsgI 631
Cdd:COG4178 423 -----PAGAR-----VLflpQRPYLPLGTLREALLypATAEAFSDAELREALEAVGLGHLAERLDEEADwDQV------L 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 632 SQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGG 705
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
494-727 |
1.80e-27 |
|
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: 111.92 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:cd03288 21 KIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSETIAENIAIGEEVIDkERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03288 101 LQDPILFSGSIRFNLDPECKCTD-DRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLK-GIYYRLVK 727
Cdd:cd03288 180 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVR 254
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
494-715 |
3.18e-27 |
|
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: 110.22 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPH-LWRSVTGS 572
Cdd:cd03224 2 EVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeRARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQDGFIFSE-TIAENIAIGEEVIDKERllKAAQIANI-------DQFIDSLplgyntkigmeGSGISQGQRQRILIARA 644
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGAYARRRAK--RKARLERVyelfprlKERRKQL-----------AGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 645 VYKNPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
492-715 |
3.64e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.00 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 492 TFTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL---KNINPH--LW 566
Cdd:PRK11264 3 AIEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQkgLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVTGSVmqdGFIFS-------ETIAENIAIGEEVIDKERllKAAQIANIDQFIdslplgynTKIGMEGSG------ISQ 633
Cdd:PRK11264 81 RQLRQHV---GFVFQnfnlfphRTVLENIIEGPVIVKGEP--KEEATARARELL--------AKVGLAGKEtsyprrLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 634 GQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGK-TVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGT 711
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGP 227
|
....
gi 496428897 712 HQEL 715
Cdd:PRK11264 228 AKAL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
509-716 |
3.72e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHlwrsvtgsvmqD------GFIFSE 582
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR-----------DaqaagiAIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 -------TIAENIAIGEE-----VIDKERLLKAAQianidQFIDSLPLGYN--TKIGmegsGISQGQRQRILIARAVYKN 648
Cdd:COG1129 88 lnlvpnlSVAENIFLGREprrggLIDWRAMRRRAR-----ELLARLGLDIDpdTPVG----DLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 649 PDFLFFDEATNALDAnNERE----IMEHLNEfyRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQELT 716
Cdd:COG1129 159 ARVLILDEPTASLTE-REVErlfrIIRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELT 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
491-715 |
4.69e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.43 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 491 HTFTIENLCFSYDGSPDyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVT 570
Cdd:PRK13652 2 HLIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 571 GSVMQ--DGFIFSETIAENIAIG-------EEVIdKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILI 641
Cdd:PRK13652 81 GLVFQnpDDQIFSPTVEQDIAFGpinlgldEETV-AHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 642 ARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
495-706 |
4.83e-27 |
|
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: 109.54 E-value: 4.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSpdYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGD--VYLKNINPHLWRSVTGS 572
Cdd:cd03262 3 IKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQDGFIFSE-TIAENIAIG---------EEVIDK-ERLLKAAQIANidqFIDSLPlgyntkigmegSGISQGQRQRILI 641
Cdd:cd03262 81 VFQQFNLFPHlTVLENITLApikvkgmskAEAEERaLELLEKVGLAD---KADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 642 ARAVYKNPDFLFFDEATNALDANNERE---IMEHLNEfyRGKTVVIVAHRLSTVQN-ADKIVVLDKGGI 706
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEvldVMKDLAE--EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
502-710 |
8.56e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.57 E-value: 8.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 502 YDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIkvgdvylkninphlW--RSVtGSVMQDGFI 579
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WaeRSI-AYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSETIAENIAIGEEViDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:PTZ00243 733 MNATVRGNILFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496428897 660 ALDAN-NEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEG 710
Cdd:PTZ00243 812 ALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
500-704 |
1.07e-26 |
|
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: 108.57 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 500 FSYdGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGfytpnKGNIKVGDVYLKNINPHLW---------RSVT 570
Cdd:cd03290 8 FSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG-----EMQTLEGKVHWSNKNESEPsfeatrsrnRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 571 GSVMQDGFIFSETIAENIAIGEEvIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPD 650
Cdd:cd03290 82 AYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 651 FLFFDEATNALDANNEREIM-EHLNEFYRG--KTVVIVAHRLSTVQNADKIVVLDKG 704
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMqEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
495-716 |
1.15e-26 |
|
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: 108.36 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNiNPHLWRSVTGSVM 574
Cdd:cd03263 3 IRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFIFSE-TIAENIAI-----GEEvidkerllKAAQIANIDQFIDSLPLG--YNTKIGMegsgISQGQRQRILIARAVY 646
Cdd:cd03263 82 QFDALFDElTVREHLRFyarlkGLP--------KSEIKEEVELLLRVLGLTdkANKRART----LSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 647 KNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQELT 716
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQELK 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
488-710 |
2.16e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.97 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 488 PQDHTFTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLL-----LgfyTPN---KGNIKVG--DVY 557
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndL---IPGarvEGEILLDgeDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 558 LKNINPHLWRSVTGSVMQDGFIFSETIAENIAIG--------EEVIDK--ERLLKAAQIanIDQFIDSLplgyntkiGME 627
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSELDEivEESLRKAAL--WDEVKDRL--------KKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 628 GSGISQGQRQRILIARAVYKNPDFLFFDEATNALD----ANNErEIMEHLNEFYrgkTVVIVAH------RLStvqnaDK 697
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIE-ELILELKKDY---TIVIVTHnmqqaaRVS-----DY 222
|
250
....*....|...
gi 496428897 698 IVVLDKGGIVEEG 710
Cdd:COG1117 223 TAFFYLGELVEFG 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
164-716 |
2.27e-26 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 114.12 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 164 NFFFRYLSPHKKALVQLVLGMVIGSILQ-LIVPFLTQSLVdvGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHM 242
Cdd:COG4615 2 NLLRLLLRESRWLLLLALLLGLLSGLANaGLIALINQALN--ATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 243 NIRINISLISdflvKLMRLPLHFFdtkmigdimQRIGDHsRIESFLTG--SSISTLFS-----FVNFIVFGFVLAY--Yd 313
Cdd:COG4615 80 VARLRLRLSR----RILAAPLERL---------ERIGAA-RLLAALTEdvRTISQAFVrlpelLQSVALVLGCLAYlaW- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 314 LSIFGLFLLgnllyVIW-VLSFMKYRRELD--LRRFSQASTEQSTLYQ----IITGMQEIKLNncetqkrwkWERIQVkL 386
Cdd:COG4615 145 LSPPLFLLT-----LVLlGLGVAGYRLLVRraRRHLRRAREAEDRLFKhfraLLEGFKELKLN---------RRRRRA-F 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 387 FKISVKGLA--LQQYQQVGSVFFNQTTN-------ILISYIAARAVVEGNMTLGMM----MSLTYIIGqlnsPIEQFIGF 453
Cdd:COG4615 210 FDEDLQPTAerYRDLRIRADTIFALANNwgnllffALIGLILFLLPALGWADPAVLsgfvLVLLFLRG----PLSQLVGA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 454 ARSFQDAKISLERLNEIHQKEDEEETAVDKVSFLPQDHTF-TIE--NLCFSY---DGSPDYVLNNVNLTIPRNKITAIVG 527
Cdd:COG4615 286 LPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFqTLElrGVTYRYpgeDGDEGFTLGPIDLTIRRGELVFIVG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 528 ASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDkeRLLKAAQIA 607
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLLGLDGEADPARAR--ELLERLELD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 608 NIDQFID---SlplgyNTKigmegsgISQGQRQRI-LIArAVYKNPDFLFFDEAtnALDANNE-REImehlneFY----- 677
Cdd:COG4615 444 HKVSVEDgrfS-----TTD-------LSQGQRKRLaLLV-ALLEDRPILVFDEW--AADQDPEfRRV------FYtellp 502
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 496428897 678 ----RGKTVVIVAH-----RLstvqnADKIVVLDKGGIVEEGTHQELT 716
Cdd:COG4615 503 elkaRGKTVIAISHddryfDL-----ADRVLKMDYGKLVELTGPAALA 545
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
495-714 |
2.46e-26 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 108.19 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDgspDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVtGSVM 574
Cdd:cd03299 3 VENLSKDWK---EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-RDI-SYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFIFSE-TIAENIAIG------EEVIDKERLLKAAQIANIDQFIDSLPLgyntkigmegsGISQGQRQRILIARAVYK 647
Cdd:cd03299 78 QNYALFPHmTVYKNIAYGlkkrkvDKKEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 648 NPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQE 714
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
494-722 |
2.86e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 108.25 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNI-NPHLWRSVtgS 572
Cdd:COG4604 3 EIKNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTpSRELAKRL--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VM-QDGFIFSE-TIAENIAIG-------------EEVIDKE-RLLKAAQIAniDQFIDSLplgyntkigmegSGisqGQR 636
Cdd:COG4604 79 ILrQENHINSRlTVRELVAFGrfpyskgrltaedREIIDEAiAYLDLEDLA--DRYLDEL------------SG---GQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 637 QRILIARAVYKNPDFLFFDEATNALDANNEREIMEHL----NEFyrGKTVVIVAHRLstvqN-----ADKIVVLDKGGIV 707
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLrrlaDEL--GKTVVIVLHDI----NfascyADHIVAMKDGRVV 215
|
250
....*....|....*...
gi 496428897 708 EEGTHQEL---TCLKGIY 722
Cdd:COG4604 216 AQGTPEEIitpEVLSDIY 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
491-702 |
2.95e-26 |
|
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: 106.79 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 491 HTFTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVT 570
Cdd:COG4133 1 MMLEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 571 GSVMQDGFIFSETIAENI----AIGEEVIDKERLLKAAQIANIDQFIDsLPLGYntkigmegsgISQGQRQRILIARAVY 646
Cdd:COG4133 79 YLGHADGLKPELTVRENLrfwaALYGLRADREAIDEALEAVGLAGLAD-LPVRQ----------LSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 647 KNPDFLFFDEATNALDANN----EREIMEHLNefyRGKTVVIVAHRLSTVQNADKIVVLD 702
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGvallAELIAAHLA---RGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
494-715 |
6.78e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.18 E-value: 6.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYD-GSP--DYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL------KNINPh 564
Cdd:PRK13634 4 TFQKVEHRYQyKTPfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKKLKP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 565 lWRSVTGSVMQdgF----IFSETIAENIAIGEE---VIDKERLLKAAQIANidqfIDSLPLGYNTKIGMEGSGisqGQRQ 637
Cdd:PRK13634 83 -LRKKVGIVFQ--FpehqLFEETVEKDICFGPMnfgVSEEDAKQKAREMIE----LVGLPEELLARSPFELSG---GQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 638 RILIARAVYKNPDFLFFDEATNALDANNEREIMEHlneFYR-----GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGT 711
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEM---FYKlhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....
gi 496428897 712 HQEL 715
Cdd:PRK13634 230 PREI 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
490-715 |
9.57e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.14 E-value: 9.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 490 DHTFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSV 569
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 570 TGSVMQ---DGFIFSeTIAENIAIGEE---VIDKERLLKAAQIANIDQFIDslplgyntKIGMEGSGISQGQRQRILIAR 643
Cdd:PRK13648 85 IGIVFQnpdNQFVGS-IVKYDVAFGLEnhaVPYDEMHRRVSEALKQVDMLE--------RADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 644 AVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVA--HRLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
494-716 |
1.02e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyvlNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVTgSV 573
Cdd:COG3840 3 RLDDLTYRYGDFP----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RPVS-ML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSE-TIAENIAIG--------EEviDKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIARA 644
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGlrpglkltAE--QRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 645 VYKNPDFLFFDEATNALDANNEREIMEHLNEFY--RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQELT 716
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCreRGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
495-714 |
1.02e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.83 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSY-DGSP--DYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL--KNINPHLWRSV 569
Cdd:PRK13637 5 IENLTHIYmEGTPfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 570 TGSVMQ--DGFIFSETIAENIAIG--------EEVidKERLLKAAQIANIDQfidslpLGYNTKIGMEGSGisqGQRQRI 639
Cdd:PRK13637 85 VGLVFQypEYQLFEETIEKDIAFGpinlglseEEI--ENRVKRAMNIVGLDY------EDYKDKSPFELSG---GQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 640 LIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGK--TVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQE 714
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
492-710 |
1.06e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 104.94 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 492 TFTIENLCFSYDGSPDY----VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGfYTPNKGniKVGDVYLKNIN--PHL 565
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKsgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG-RRTGLG--VSGEVLINGRPldKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 WRSVTGSVMQDGFIFSE-TIAENIAIgeevidkerllkAAQIanidqfidslplgyntkigmegSGISQGQRQRILIARA 644
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMF------------AAKL----------------------RGLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 645 VYKNPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLST--VQNADKIVVLDKGGIVEEG 710
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| Peptidase_C39C |
cd02419 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
5-145 |
1.72e-25 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239100 [Multi-domain] Cd Length: 127 Bit Score: 101.95 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 5 PVYTQLDRMDCGPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLvDDFPLPCILH 84
Cdd:cd02419 2 PVILQTEAAECGLACLAMIASYHGHHVDLASLRQRFPVSLKGATLADLIDIAQQLGLSTRALRLDLEEL-GQLKLPCILH 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 85 WNQQHFVVCYRIRKRRnkykILIGDPA-GTQTVTYneEEFKRCWissrekgqdTGVALVLEP 145
Cdd:cd02419 81 WDMNHFVVLKKVSRRR----IVIHDPAlGKRKLSL--EEASRHF---------TGVALELWP 127
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
495-714 |
2.70e-25 |
|
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: 105.21 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVTGSVM 574
Cdd:cd03219 3 VRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 --QDGFIFSE-TIAENIAIGEEVIDKERLL-------KAAQIANIDQFIDSLPLGynTKIGMEGSGISQGQRQRILIARA 644
Cdd:cd03219 80 tfQIPRLFPElTVLENVMVAAQARTGSGLLlararreEREARERAEELLERVGLA--DLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 645 VYKNPDFLFFDEAT---NALDANNEREIMEHLNEfyRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQE 714
Cdd:cd03219 158 LATDPKLLLLDEPAaglNPEETEELAELIRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
500-719 |
3.83e-25 |
|
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: 106.09 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 500 FSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKvgdvylkninpHLWRSVTGSvmQDGFI 579
Cdd:cd03291 45 LCLVGAP--VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------HSGRISFSS--QFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSETIAENIAIGEEViDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:cd03291 110 MPGTIKENIIFGVSY-DEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 660 ALDANNEREIMEH-LNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLK 719
Cdd:cd03291 189 YLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
174-467 |
4.76e-25 |
|
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: 106.02 E-value: 4.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIwVLS 333
Cdd:cd18569 81 FFWHVLRLPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLL-VLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FMKYRRELDLRRFSQ-----ASTEQSTLYQIITgmqeIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFN 408
Cdd:cd18569 160 LVSRKRVDLNRRLLQdsgklTGTTMSGLQMIET----LKASGAESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 409 QTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18569 236 ALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
515-710 |
1.09e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 102.57 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 515 LTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVTgSVMQDGFIFSE-TIAENIAIGE- 592
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-RPVS-MLFQENNLFAHlTVEQNVGLGLs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 593 -----EVIDKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNER 667
Cdd:cd03298 97 pglklTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496428897 668 EIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG 710
Cdd:cd03298 166 EMLDLVLDLHAetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
495-711 |
1.31e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.30 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSY-DGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKV-----GDVY-LKNInphlwR 567
Cdd:PRK13644 4 LENVSYSYpDGTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGDFSkLQGI-----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 568 SVTGSVMQD---GFIfSETIAENIAIGEEVIdkerLLKAAQIAN-IDQFIDSLPLG-YNTKigmEGSGISQGQRQRILIA 642
Cdd:PRK13644 77 KLVGIVFQNpetQFV-GRTVEEDLAFGPENL----CLPPIEIRKrVDRALAEIGLEkYRHR---SPKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 643 RAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGT 711
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
494-710 |
2.01e-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: 102.06 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYD--GSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVgDVYLKNINPHLWRSVTG 571
Cdd:cd03266 3 TADALTKRFRdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 sVMQDGFIFSE--TIAENIaigEEVIDKERLLKAAQIANIDQFIDSLplGYNTKIGMEGSGISQGQRQRILIARAVYKNP 649
Cdd:cd03266 82 -FVSDSTGLYDrlTARENL---EYFAGLYGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 650 DFLFFDEATNALD---ANNEREIMEHLNEfyRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG 710
Cdd:cd03266 156 PVLLLDEPTTGLDvmaTRALREFIRQLRA--LGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
487-715 |
3.01e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.16 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 487 LPQDHTFTIENLCFSYD---GSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYlknINP 563
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIY---IGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 564 HLW-------------------RSVTGSVMQ--DGFIFSETIAENIAIGeEVIDKERLLKAAQIANIdqFIDSLPLGYNT 622
Cdd:PRK13631 93 KKNnhelitnpyskkiknfkelRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKF--YLNKMGLDDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 623 kigMEGS--GISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEH-LNEFYRGKTVVIVAHRLSTV-QNADKI 698
Cdd:PRK13631 170 ---LERSpfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLiLDAKANNKTVFVITHTMEHVlEVADEV 246
|
250
....*....|....*..
gi 496428897 699 VVLDKGGIVEEGTHQEL 715
Cdd:PRK13631 247 IVMDKGKILKTGTPYEI 263
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
174-467 |
3.02e-24 |
|
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: 103.37 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGI---RDNNLNFITLILVAqLIIFIARLSvdFIRSWLLLHMNIRINISL 250
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLvhqSYSTLYVLTIGVVI-ALLFEGILG--YLRRYLLLVATTRIDARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 251 ISDFLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIW 330
Cdd:cd18783 78 ALRTFDRLLSLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 331 VLSFMK-YRRELDlrRFSQASTE-QSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFN 408
Cdd:cd18783 158 ILAFLPpFRRRLQ--ALYRAEGErQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 409 QTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18783 236 KLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVRML 294
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
494-711 |
3.75e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.50 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDYV--LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP----HLWR 567
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 568 SVtgsvmqdGFIF-------SETIAENIAIGEEVIDKERllkaaqiANIDQFIDSL-PLgyntkIGMEG------SGISQ 633
Cdd:PRK11153 83 QI-------GMIFqhfnllsSRTVFDNVALPLELAGTPK-------AEIKARVTELlEL-----VGLSDkadrypAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 634 GQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEG 710
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQG 223
|
.
gi 496428897 711 T 711
Cdd:PRK11153 224 T 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
510-715 |
6.31e-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: 101.95 E-value: 6.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP----HLWRSVTGSVMQD-GFIFSETI 584
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrELRRKKISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AENIAIGEEV------IDKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAVYKNPDFLFFDEAT 658
Cdd:cd03294 120 LENVAFGLEVqgvpraEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 659 NALDANNEREIMEHLNEFYR--GKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
506-710 |
1.37e-23 |
|
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: 99.29 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 506 PDYVLNnVNLTIPRNkITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL----KNIN--PHlwRSVTGSVMQDGFI 579
Cdd:cd03297 11 PDFTLK-IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINlpPQ--QRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSE-TIAENIAIGEEVI-DKERLLKAAQIA---NIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAVYKNPDFLFF 654
Cdd:cd03297 87 FPHlNVRENLAFGLKRKrNREDRISVDELLdllGLDHLLNRYP-----------AQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 655 DEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG 710
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
447-714 |
1.90e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 447 IEQFIGFARSFQDAKISLERLNEIHQKEDEEETAVDKVSFLPQDHT----FTIENLCFSYDGSPdyVLNNVNLTIPRNKI 522
Cdd:COG0488 266 IRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLgkkvLELEGLSKSYGDKT--LLDDLSLRIDRGDR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 523 TAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGD----VYLkninphlwrsvtgSVMQDGFIFSETIAENIAigeEVIDKE 598
Cdd:COG0488 344 IGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvkiGYF-------------DQHQEELDPDKTVLDELR---DGAPGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 599 RLLKAAQI--------ANIDQFIDSLplgyntkigmegSGisqGQRQRILIARAVYKNPDFLFFDEATNALDANNeREIM 670
Cdd:COG0488 408 TEQEVRGYlgrflfsgDDAFKPVGVL------------SG---GEKARLALAKLLLSPPNVLLLDEPTNHLDIET-LEAL 471
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 496428897 671 EH-LNEFyRGkTVVIVAH-R--LSTVqnADKIVVLDKGGIVE-EGTHQE 714
Cdd:COG0488 472 EEaLDDF-PG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDD 516
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
494-714 |
3.13e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.70 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP-HLWRSVTGS 572
Cdd:PRK11231 4 RTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQdgfifsETIAENIAIGEEVI----------------DKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQR 636
Cdd:PRK11231 82 PQH------HLTPEGITVRELVAygrspwlslwgrlsaeDNARVNQAMEQTRINHLADRRL-----------TDLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 637 QRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQE 714
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
494-711 |
4.34e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.82 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYD-GSP--DYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL----KNINPHLW 566
Cdd:PRK13649 4 NLQNVSYTYQaGTPfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVTGSVMQ--DGFIFSETIAENIAIGEE-----VIDKERLL--KAAQIANIDQFIDSLPLgyntkigmEGSGisqGQRQ 637
Cdd:PRK13649 84 RKKVGLVFQfpESQLFEETVLKDVAFGPQnfgvsQEEAEALAreKLALVGISESLFEKNPF--------ELSG---GQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 638 RILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGT 711
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
488-715 |
4.86e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 4.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 488 PQDHTFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTP---NKGNIKVGDVYLKNINph 564
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 565 LW--RSVTGSVMQ--DGFIFSETIAENIAIGEE--VIDKERLLKAAQ--IANID--QFIDSLPlgyntkigmegSGISQG 634
Cdd:PRK13640 79 VWdiREKVGIVFQnpDNQFVGATVGDDVAFGLEnrAVPRPEMIKIVRdvLADVGmlDYIDSEP-----------ANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 635 QRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGK--TVVIVAHRLSTVQNADKIVVLDKGGIVEEGTH 712
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
...
gi 496428897 713 QEL 715
Cdd:PRK13640 228 VEI 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
509-715 |
5.72e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 5.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVG--DVYLKNINPHLWRSVTGSVMQDGFIFSETIA- 585
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglKVNDPKVDERLIRQEAGMVFQQFYLFPHLTAl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 586 ENIAIGeevidKERLLKAAQIANIDQFIDSLplgynTKIGMEG------SGISQGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:PRK09493 96 ENVMFG-----PLRVRGASKEEAEKQARELL-----AKVGLAErahhypSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 660 ALDANNERE---IMEHLNEfyRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK09493 166 ALDPELRHEvlkVMQDLAE--EGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVL 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
495-712 |
6.08e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL---KNINPHLWRSVTG 571
Cdd:COG4161 5 LKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVmqdGFIFSE-------TIAENI------AIG---EEVIDK-ERLLKAAQIANidqFIDSLPLGyntkigmegsgISQG 634
Cdd:COG4161 83 KV---GMVFQQynlwphlTVMENLieapckVLGlskEQAREKaMKLLARLRLTD---KADRFPLH-----------LSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 635 QRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTH 712
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
495-715 |
7.90e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.07 E-value: 7.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVTgSVM 574
Cdd:PRK11607 22 IRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ-RPIN-MMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFIFSE-TIAENIAIGeevIDKERLLKAAQIANIDQFIDSLPLGYNTKigMEGSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:PRK11607 98 QSYALFPHmTVEQNIAFG---LKQDKLPKAEIASRVNEMLGLVHMQEFAK--RKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 654 FDEATNALDAN-NEREIMEHLNEFYR-GKTVVIVAH-RLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK11607 173 LDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
495-710 |
8.47e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 97.26 E-value: 8.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSpdYVLNNVNLTIPrNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNiNPHLWRSVTGSVM 574
Cdd:cd03264 3 LENLTKRYGKK--RALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QD-GFIFSETIAE---NIAIGEEVIDKErllkaaQIANIDQFIDSLPLG--YNTKIGmegsGISQGQRQRILIARAVYKN 648
Cdd:cd03264 79 QEfGVYPNFTVREfldYIAWLKGIPSKE------VKARVDEVLELVNLGdrAKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 649 PDFLFFDEATNALDAnNERE-IMEHLNEFYRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG 710
Cdd:cd03264 149 PSILIVDEPTAGLDP-EERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
510-689 |
1.17e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.32 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIK-------LLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSE 582
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 TIAENIAIGEEV------IDK--ERLLKaaQIANIDQFIDslplgyntKIGMEGSGISQGQRQRILIARAVYKNPDFLFF 654
Cdd:PRK14243 106 SIYDNIAYGARIngykgdMDElvERSLR--QAALWDEVKD--------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190
....*....|....*....|....*....|....*
gi 496428897 655 DEATNALDANNEREIMEHLNEFYRGKTVVIVAHRL 689
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
489-714 |
1.35e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.41 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 489 QDHTFTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRS 568
Cdd:PRK09452 11 LSPLVELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 569 VTgSVMQDGFIFSE-TIAENIAIG--------EEVidKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRI 639
Cdd:PRK09452 88 VN-TVFQSYALFPHmTVFENVAFGlrmqktpaAEI--TPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 640 LIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAH----RLSTvqnADKIVVLDKGGIVEEGTHQ 713
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPR 230
|
.
gi 496428897 714 E 714
Cdd:PRK09452 231 E 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
495-715 |
1.88e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.16 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDY---VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGD----VYLKNIN--PHL 565
Cdd:PRK13645 9 LDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKevKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 WRSVtGSVMQ--DGFIFSETIAENIAIGEEVI--DKERLLKaaqiaNIDQFID--SLPLGYNTKIGMEGSGisqGQRQRI 639
Cdd:PRK13645 89 RKEI-GLVFQfpEYQLFQETIEKDIAFGPVNLgeNKQEAYK-----KVPELLKlvQLPEDYVKRSPFELSG---GQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 640 LIARAVYKNPDFLFFDEATNALDANNEREIM---EHLNEFYrGKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFInlfERLNKEY-KKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEI 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
500-719 |
1.96e-22 |
|
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: 103.45 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 500 FSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKvgdvylkninpHLWRSVTGSvmQDGFI 579
Cdd:TIGR01271 434 FSLYVTP--VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----------HSGRISFSP--QTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSETIAENIAIGEEViDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:TIGR01271 499 MPGTIKDNIIFGLSY-DEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 660 ALDANNEREIMEH-LNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQELTCLK 719
Cdd:TIGR01271 578 HLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
495-710 |
2.06e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 97.08 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGN-IKV-----GDVYLKNINPHLwrS 568
Cdd:COG1119 6 LRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerrGGEDVWELRKRI--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 569 VTGSVMQDGFIFSETIAENIA------IG------EEVIDK-ERLLKAAQIANI-DQFIDSLplgyntkigmegsgiSQG 634
Cdd:COG1119 82 LVSPALQLRFPRDETVLDVVLsgffdsIGlyreptDEQRERaRELLELLGLAHLaDRPFGTL---------------SQG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 635 QRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQNA-DKIVVLDKGGIVEEG 710
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
494-687 |
3.37e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKniNPHLWRSVtgsV 573
Cdd:PRK11248 3 QISHLYADYGGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAERGV---V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQ-DGFIFSETIAENIAIGEE---VIDKERLLKAAQIANidqfidslplgyntKIGMEGSG------ISQGQRQRILIAR 643
Cdd:PRK11248 76 FQnEGLLPWRNVQDNVAFGLQlagVEKMQRLEIAHQMLK--------------KVGLEGAEkryiwqLSGGQRQRVGIAR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496428897 644 AVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAH 687
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
512-715 |
4.37e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 98.63 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 512 NVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL----KNIN--PHLwRSVtGSVMQDGFIFSE-TI 584
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIFlpPHR-RRI-GYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AENIAIG-------------EEVIDkerLLkaaQIANI-DQFIDSLplgyntkigmegSGisqGQRQRILIARAVYKNPD 650
Cdd:COG4148 95 RGNLLYGrkrapraerrisfDEVVE---LL---GIGHLlDRRPATL------------SG---GERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 651 FLFFDEATNALDANNEREIMEHLnEFYRGKT---VVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYL-ERLRDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
498-710 |
4.57e-22 |
|
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: 95.42 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 498 LCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGfYTPNKGNIKvGDVYLKN--INPHLWRSVTGSVMQ 575
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTS-GQILFNGqpRKPDQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 576 DGFIFSE-TIAENIAIgEEVIDKERLLKAAQIANIDQFIDSLPLGyNTKIG-MEGSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03234 89 DDILLPGlTVRETLTY-TAILRLPRKSSDAIRKKRVEDVLLRDLA-LTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYRGKTVVIVA-H--RLSTVQNADKIVVLDKGGIVEEG 710
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
174-467 |
5.48e-22 |
|
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: 96.88 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIW-VL 332
Cdd:cd18566 81 AFEHLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVaIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 333 SFMKYRRELDlRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVK----LFKISVKGLALQQYQQVgsvfFN 408
Cdd:cd18566 161 LGPILRRALK-ERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANaayaGFKVAKINAVAQTLGQL----FS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 409 QTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18566 236 QVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| Peptidase_C39F |
cd02425 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
9-125 |
1.04e-21 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239105 [Multi-domain] Cd Length: 126 Bit Score: 91.17 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 9 QLDRMDCGPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLVDDFPLPCILHWNQQ 88
Cdd:cd02425 6 QNNQTECGLACYAMILNYFGYKVSLNELREKYELGRDGLSLSYLKQLLEEYGFKCKVYKISFKKNLYPLKLPVIIFWNNN 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 496428897 89 HFVVCYRIRKRrnkyKILIGDPAgTQTVTYNEEEFKR 125
Cdd:cd02425 86 HFVVLEKIKKN----KVTIVDPA-IGRIKISIDEFLE 117
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
509-717 |
2.41e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.31 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIK-----VGDVYLKNinphlwRSVtGSVMQDGFIFSE- 582
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdVSRLHARD------RKV-GFVFQHYALFRHm 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 TIAENIAIGEEVIDK-ERLLKAAQIANIDQFIDSLPLGYNTkiGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNAL 661
Cdd:PRK10851 90 TVFDNIAFGLTVLPRrERPNAAAIKAKVTQLLEMVQLAHLA--DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 662 DANNEREIMEHLNEFYR--GKTVVIVAH-RLSTVQNADKIVVLDKGGIVEEGTHQELTC 717
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
510-715 |
2.76e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.85 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL------KNINPhlWRSVTGSVMQ--DGFIFS 581
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRP--VRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 582 ETIAENIAIG--------EEVIDKE-RLLkaaqianidqfidsLPLGYNTKIgMEGS--GISQGQRQRILIARAVYKNPD 650
Cdd:PRK13646 101 DTVEREIIFGpknfkmnlDEVKNYAhRLL--------------MDLGFSRDV-MSQSpfQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 651 FLFFDEATNALDANNEREIMEHLNEFY--RGKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
492-687 |
3.91e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.77 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 492 TFTIENLCFSYDGS--PDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDvylkninphlwRSV 569
Cdd:COG4525 3 MLTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-----------VPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 570 TGSVMQDGFIFSE-------TIAENIAIG---EEVIDKERLLKAAQianidqfidslplgYNTKIGMEGSG------ISQ 633
Cdd:COG4525 72 TGPGADRGVVFQKdallpwlNVLDNVAFGlrlRGVPKAERRARAEE--------------LLALVGLADFArrriwqLSG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 634 GQRQRILIARAVYKNPDFLFFDEATNALDANNeREIM-EHLNEFYR--GKTVVIVAH 687
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALT-REQMqELLLDVWQrtGKGVFLITH 193
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
510-720 |
4.80e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.03 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL------KNINPhlWRSVTGSVMQ--DGFIFS 581
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstskqKEIKP--VRKKVGVVFQfpESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 582 ETIAENIAIGEEV--IDKErllKAAQIANIDQFIDSLPLGYNTKIGMEGSGisqGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:PRK13643 100 ETVLKDVAFGPQNfgIPKE---KAEKIAAEKLEMVGLADEFWEKSPFELSG---GQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 660 ALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGT----HQELTCLKG 720
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTpsdvFQEVDFLKA 240
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
512-710 |
8.42e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 94.56 E-value: 8.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 512 NVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL----KNIN--PHLWRsvTGSVMQDGFIFSE-TI 584
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGIClpPEKRR--IGYVFQDARLFPHyKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AENIAIGEEVIDKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAVYKNPDFLFFDEATNALDAN 664
Cdd:PRK11144 94 RGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496428897 665 NEREIMEHLNEFyrGKTVVI----VAHRLSTV-QNADKIVVLDKGGIVEEG 710
Cdd:PRK11144 163 RKRELLPYLERL--AREINIpilyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
509-711 |
9.08e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 92.41 E-value: 9.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPH------LWRSvtgsvmqdgF---- 578
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriarlgIART---------Fqnpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 579 IFSE-TIAENIAIGEEVIDKERLLKA------------AQIANIDQFIDSLPLGynTKIGMEGSGISQGQRQRILIARAV 645
Cdd:COG0411 90 LFPElTVLENVLVAAHARLGRGLLAAllrlprarreerEARERAEELLERVGLA--DRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 646 YKNPDFLFFDEATNALDANNEREIMEHLNEF--YRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGT 711
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
509-715 |
9.44e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.89 E-value: 9.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTI-PRNKItAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAEN 587
Cdd:PLN03130 1254 VLHGLSFEIsPSEKV-GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 588 IAIGEEVIDKErLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNER 667
Cdd:PLN03130 1333 LDPFNEHNDAD-LWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496428897 668 EIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
494-731 |
1.24e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYD-GSPDY--VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNI-------------KVGDVY 557
Cdd:PRK13651 4 KVKNIVKIFNkKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktKEKEKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 558 -------------LKNINpHLWRSVtGSVMQdgF----IFSETIAENIAIGEEV--IDKERLLKAAqiANIDQFIDsLPL 618
Cdd:PRK13651 84 leklviqktrfkkIKKIK-EIRRRV-GVVFQ--FaeyqLFEQTIEKDIIFGPVSmgVSKEEAKKRA--AKYIELVG-LDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 619 GYNTKIGMEGSGisqGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTV-QNAD 696
Cdd:PRK13651 157 SYLQRSPFELSG---GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVlEWTK 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 496428897 697 KIVVLDKGGIVEEG-THQELTCLKgiyyRLVKNQLE 731
Cdd:PRK13651 234 RTIFFKDGKIIKDGdTYDILSDNK----FLIENNME 265
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
489-715 |
1.28e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.02 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 489 QDHTFTIENLCFSYdGSpDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVG--DVYLKNINPhlw 566
Cdd:PRK11432 3 QKNFVVLKNITKRF-GS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgeDVTHRSIQQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVTgSVMQDGFIFSE-TIAENIAIG--------EEVidKERLLKAAQIANI----DQFIDSlplgyntkigmegsgISQ 633
Cdd:PRK11432 78 RDIC-MVFQSYALFPHmSLGENVGYGlkmlgvpkEER--KQRVKEALELVDLagfeDRYVDQ---------------ISG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 634 GQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEG 710
Cdd:PRK11432 140 GQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIG 219
|
....*
gi 496428897 711 THQEL 715
Cdd:PRK11432 220 SPQEL 224
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
9-127 |
1.38e-20 |
|
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families.
Pssm-ID: 239073 [Multi-domain] Cd Length: 122 Bit Score: 87.82 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 9 QLDRMDCGPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLVdDFPLPCILHWNQQ 88
Cdd:cd02259 1 GGGPLDCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALS-RLQLPALLLWKQG 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 496428897 89 HFVVCYRIRKRrnkyKILIGDPAGTQTVTYNEEEFKRCW 127
Cdd:cd02259 80 HFVILYGADKG----QVLIADPLEEGPVTLSESELEERW 114
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
508-711 |
1.67e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 508 YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVgdvylkninphlwrsvTGSV-----MQDGFIFSE 582
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV----------------NGRVsalleLGAGFHPEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 TIAENIAIG--------EEVidKERLLKAAQIANIDQFIDsLPLG-YntkigmegsgiSQGQRQRILIARAVYKNPDFLF 653
Cdd:COG1134 104 TGRENIYLNgrllglsrKEI--DEKFDEIVEFAELGDFID-QPVKtY-----------SSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 654 FDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGT 711
Cdd:COG1134 170 VDEVLAVGDAAFQKKCLARIRELReSGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
180-466 |
2.01e-20 |
|
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: 92.19 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 180 LVLGMVIGSILQLIVPFLTQSLVD----VGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFL 255
Cdd:cd18563 4 GFLLMLLGTALGLVPPYLTKILIDdvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 256 VKLMRLPLHFFDTKMIGDIMQRIG-DHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLSF 334
Cdd:cd18563 84 EHLQRLSLSFFDKRQTGSLMSRVTsDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 335 MKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKglALQQYQQVGSV--FFNQTTN 412
Cdd:cd18563 164 WKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR--AEKLWATFFPLltFLTSLGT 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 496428897 413 ILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLER 466
Cdd:cd18563 242 LIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
495-715 |
2.21e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.69 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDY-VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:PRK13642 7 VENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQ--DGFIFSETIAENIAIGEEvidKERLLKAAQIANIDQFIDSLP-LGYNTKigmEGSGISQGQRQRILIARAVYKNPD 650
Cdd:PRK13642 87 FQnpDNQFVGATVEDDVAFGME---NQGIPREEMIKRVDEALLAVNmLDFKTR---EPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 651 FLFFDEATNALDANNEREIMEHLNEFyRGK---TVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
509-718 |
2.43e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 91.67 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGS---VMQD---GFIFSE 582
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDiqmVFQDsisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 TIAEniAIGEEVIDKERLLKAAQIANIDQFIDS--LPLGYNTKIGMEGSGisqGQRQRILIARAVYKNPDFLFFDEATNA 660
Cdd:PRK10419 107 TVRE--IIREPLRHLLSLDKAERLARASEMLRAvdLDDSVLDKRPPQLSG---GQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 661 LDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQELTCL 718
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTF 242
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
497-715 |
2.48e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.68 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 497 NLCFSY-DGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLW--RSVTGSV 573
Cdd:PRK13639 6 DLKYSYpDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQ--DGFIFSETIAENIAIG--------EEVidKERLLKAAQianidqfidslplgyntKIGMEGSG------ISQGQRQ 637
Cdd:PRK13639 84 FQnpDDQLFAPTVEEDVAFGplnlglskEEV--EKRVKEALK-----------------AVGMEGFEnkpphhLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 638 RILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQ-NADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
494-710 |
3.33e-20 |
|
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: 90.47 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYD---------GS------PDY----VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVG 554
Cdd:cd03267 2 EVSNLSKSYRvyskepgliGSlkslfkRKYreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 555 DvylknINPhlWRSVTGSVMQDGFIFS--ETIAENIAigeeVIDKERLLKAA-QI------ANIDQFIDSLPLGYNTKIG 625
Cdd:cd03267 82 G-----LVP--WKRRKKFLRRIGVVFGqkTQLWWDLP----VIDSFYLLAAIyDLpparfkKRLDELSELLDLEELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 626 MEgsGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFY--RGKTVVIVAHRLSTVQN-ADKIVVLD 702
Cdd:cd03267 151 VR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNreRGTTVLLTSHYMKDIEAlARRVLVID 228
|
....*...
gi 496428897 703 KGGIVEEG 710
Cdd:cd03267 229 KGRLLYDG 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
508-710 |
9.27e-20 |
|
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: 88.74 E-value: 9.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 508 YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVgdvylkninphlwrsvTGSV-----MQDGFIFSE 582
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV----------------RGRVssllgLGGGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 TIAENIAI--------GEEVIDKERLLkaAQIANIDQFIDsLPLG-YntkigmegsgiSQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03220 100 TGRENIYLngrllglsRKEIDEKIDEI--IEFSELGDFID-LPVKtY-----------SSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 654 FDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEG 710
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLkQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
181-467 |
9.59e-20 |
|
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: 90.17 E-value: 9.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLVKLMR 260
Cdd:cd18552 5 ILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 261 LPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYD--LSIFGLFLLGNLLYVIWVLSfmky 337
Cdd:cd18552 85 LPLSFFDRNSSGDLISRItNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDwkLTLIALVVLPLAALPIRRIG---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 338 RReldLRRFSQASTEQ-----STLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQY-----QQVGSVFF 407
Cdd:cd18552 161 KR---LRKISRRSQESmgdltSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALssplmELLGAIAI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 408 nqttnILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18552 238 -----ALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
510-731 |
1.79e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 88.68 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLL--LGFYTPN---KGNIKVG--DVYLKNINPHLWRSVTGSVMQDGFIFSE 582
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNghNIYSPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 TIAENIAIG--------EEVIDK--ERLLKAAQIAniDQFIDSLplgYNTKIGMEGsgisqGQRQRILIARAVYKNPDFL 652
Cdd:PRK14239 101 SIYENVVYGlrlkgikdKQVLDEavEKSLKGASIW--DEVKDRL---HDSALGLSG-----GQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 653 FFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLstvQNADKIVvlDKGGIVEEGTHQELTCLKGIYYRLVKNQLE 731
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM---QQASRIS--DRTGFFLDGDLIEYNDTKQMFMNPKHKETE 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
495-706 |
1.94e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTI-PRNKItAIVGASGSGKTTLIKLLLGFYTPNKGNIkvgdvylkNINPHLwrsVTGSV 573
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSInPGDRI-GLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGL---RIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSE-TIAENIAIG-EEVIDKERLLKAAQIANIDQFIDSLPLG-------------YNTKIG--MEGSGISQ--- 633
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGdAELRALEAELEELEAKLAEPDEDLERLAelqeefealggweAEARAEeiLSGLGFPEedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 634 ---------GQRQRILIARAVYKNPDFLFFDEATNALDANNereIM---EHLNEfYRGkTVVIVAH-R--LSTVqnADKI 698
Cdd:COG0488 147 drpvselsgGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwleEFLKN-YPG-TVLVVSHdRyfLDRV--ATRI 219
|
....*...
gi 496428897 699 VVLDKGGI 706
Cdd:COG0488 220 LELDRGKL 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
494-705 |
2.18e-19 |
|
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: 85.19 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGdvylkninphlwrsvtgsv 573
Cdd:cd03221 2 ELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 mqdgfifsetiaeniaigeevidkerllKAAQIANIDQFidslplgyntkigmegsgiSQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03221 61 ----------------------------STVKIGYFEQL-------------------SGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYRgkTVVIVAH-R--LSTVqnADKIVVLDKGG 705
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPG--TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
492-716 |
2.71e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.29 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 492 TFTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVTG 571
Cdd:PRK13548 2 MLEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVM-QD---GFIFseTIAENIAIG-----EEVIDKERLLKAA-QIANIDQFIDSLplgYNTkigmegsgISQGQRQRILI 641
Cdd:PRK13548 79 AVLpQHsslSFPF--TVEEVVAMGraphgLSRAEDDALVAAAlAQVDLAHLAGRD---YPQ--------LSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 642 ARA------VYKNPDFLFFDEATNALDANNEREIMEHLNEF--YRGKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEGTH 712
Cdd:PRK13548 146 ARVlaqlwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTP 225
|
....*
gi 496428897 713 QE-LT 716
Cdd:PRK13548 226 AEvLT 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
495-713 |
3.89e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.38 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYdGSpDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL---KNINP-------- 563
Cdd:PRK11124 5 LNGINCFY-GA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDkairelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 564 ---------HLWRSVTgsVMQDgFI--------FSETIAENIAigEEVIDKERLlkaaqianiDQFIDSLPLGyntkigm 626
Cdd:PRK11124 83 nvgmvfqqyNLWPHLT--VQQN-LIeapcrvlgLSKDQALARA--EKLLERLRL---------KPYADRFPLH------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 627 egsgISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQN-ADKIVVLDKG 704
Cdd:PRK11124 142 ----LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENG 217
|
....*....
gi 496428897 705 GIVEEGTHQ 713
Cdd:PRK11124 218 HIVEQGDAS 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
510-716 |
3.94e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDvylkninphlwRSVT------------GSVMQ-- 575
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-----------KPVRirsprdaialgiGMVHQhf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 576 ---DGFifseTIAENIAIGEE-----VIDKERLlkAAQIANI-DQFidSLPLGYNTKIGmegsGISQGQRQRILIARAVY 646
Cdd:COG3845 90 mlvPNL----TVAENIVLGLEptkggRLDRKAA--RARIRELsERY--GLDVDPDAKVE----DLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 647 KNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQELT 716
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAeGKSIIFITHKLREVmAIADRVTVLRRGKVVGTVDTAETS 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
494-715 |
8.39e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.09 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPD-YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINphLW--RSVT 570
Cdd:PRK13650 6 EVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN--VWdiRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 571 GSVMQ--DGFIFSETIAENIAIGEE------VIDKERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIA 642
Cdd:PRK13650 84 GMVFQnpDNQFVGATVEDDVAFGLEnkgiphEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 643 RAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-715 |
8.79e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKL---LLGFYTPNKGNikvGDVYL------KNINPHLWRSVTGSVMQDGFI 579
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARVS---GEVYLdgqdifKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSETIAENIAIGEEVidkERLLKAAQ--IANIDQFIDSLPLGYNTK--IGMEGSGISQGQRQRILIARAVYKNPDFLFFD 655
Cdd:PRK14247 95 PNLSIFENVALGLKL---NRLVKSKKelQERVRWALEKAQLWDEVKdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 656 EATNALDANNEREIMEHLNEFYRGKTVVIVAH------RLStvqnaDKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREV 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
510-715 |
1.22e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.49 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLlGFYTPnKGNIKVGDVYL--KNINPHLWRSVTGSVMQDG-FIFSETIAE 586
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSP-KGVKGSGSVLLngMPIDAKEMRAISAYVQQDDlFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 587 NIAIGEEVIDKERLLKAAQIANIDQFIDSLPLG--YNTKIGMEGS--GISQGQRQRILIARAVYKNPDFLFFDEATNALD 662
Cdd:TIGR00955 119 HLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 663 ---ANNEREIMEHLNEfyRGKTVVIVAHRLST--VQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:TIGR00955 199 sfmAYSVVQVLKGLAQ--KGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
489-725 |
1.42e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 489 QDHTFTIENLCFSY-DGSpdYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVG----DVYLKNINP 563
Cdd:PRK13636 2 EDYILKVEELNYNYsDGT--HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpiDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 564 hlWRSVTGSVMQ--DGFIFSETIAENIAIG--------EEVidKERLLKAAQIANIDQFIDSlplgyntkigmEGSGISQ 633
Cdd:PRK13636 80 --LRESVGMVFQdpDNQLFSASVYQDVSFGavnlklpeDEV--RKRVDNALKRTGIEHLKDK-----------PTHCLSF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 634 GQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQ-NADKIVVLDKGGIVEEG 710
Cdd:PRK13636 145 GQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224
|
250
....*....|....*....
gi 496428897 711 THQEL----TCLKGIYYRL 725
Cdd:PRK13636 225 NPKEVfaekEMLRKVNLRL 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
508-709 |
1.56e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.01 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 508 YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFY--TPNKGNIKVGDVylkninpHLWRSVtgsvmqdgfifseTIA 585
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDN-------QFGREA-------------SLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 586 ENIAIGEEVIDKERLLKAAqianidqfidslplGYNTKIGMEG--SGISQGQRQRILIARAVYKNPDFLFFDEATNALDA 663
Cdd:COG2401 104 DAIGRKGDFKDAVELLNAV--------------GLSDAVLWLRrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496428897 664 NNEREIMEHLNEFYR--GKTVVIVAHRlSTVQNA---DKIVVLDKGGIVEE 709
Cdd:COG2401 170 QTAKRVARNLQKLARraGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPEE 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
494-715 |
2.43e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.39 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVtGSV 573
Cdd:PRK11000 5 TLRNVTKAYGDVV--ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-RGV-GMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSE-TIAENIAIG-------EEVIDKeRLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAV 645
Cdd:PRK11000 81 FQSYALYPHlSVAENMSFGlklagakKEEINQ-RVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 646 YKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAH-RLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
185-447 |
2.83e-18 |
|
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: 85.39 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 185 VIGSILQLIVPFLTQSLVDVGIRDNNLNF--ITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLVKLMRLP 262
Cdd:pfam00664 9 ILSGAISPAFPLVLGRILDVLLPDGDPETqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 263 LHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLSFMKYRREL 341
Cdd:pfam00664 89 MSFFDTNSVGELLSRLtNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 342 DLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNILISYIAAR 421
Cdd:pfam00664 169 SRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAY 248
|
250 260
....*....|....*....|....*.
gi 496428897 422 AVVEGNMTLGMMMSLTYIIGQLNSPI 447
Cdd:pfam00664 249 LVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
489-722 |
3.16e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.22 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 489 QDHTFTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLW-R 567
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 568 SVTGSVMQDGFIFSETIAENIAIGE----------EVIDKERLLKAAQIANIDQF----IDSLplgyntkigmegsgiSQ 633
Cdd:PRK10575 86 KVAYLPQQLPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLahrlVDSL---------------SG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 634 GQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF--YRGKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEG 710
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQG 230
|
250
....*....|....*
gi 496428897 711 THQELTC---LKGIY 722
Cdd:PRK10575 231 TPAELMRgetLEQIY 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
494-715 |
3.25e-18 |
|
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: 88.59 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDY--VLNNVNLTIPRNKITAIVGASGSGKT----TLIKLLlgfytPNKGNIKVGDVYLK-----NIN 562
Cdd:COG4172 8 SVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLL-----PDPAAHPSGSILFDgqdllGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 563 PHLWRSVTGSVMqdGFIFSE---------TIAENIAigeEVID----------KER---LLKAAQIANIDQFIDSLPlgy 620
Cdd:COG4172 83 ERELRRIRGNRI--AMIFQEpmtslnplhTIGKQIA---EVLRlhrglsgaaaRARaleLLERVGIPDPERRLDAYP--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 621 ntkigMEGSGisqGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADK 697
Cdd:COG4172 155 -----HQLSG---GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRfADR 226
|
250
....*....|....*...
gi 496428897 698 IVVLDKGGIVEEGTHQEL 715
Cdd:COG4172 227 VAVMRQGEIVEQGPTAEL 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
495-715 |
3.64e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 83.96 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSpdYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVgdvylkniNPHLWRSVTGSVM 574
Cdd:cd03265 3 VENLVKKYGDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV--------AGHDVVREPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QD-GFIFSETIAENIAIG-EEVIDKERL--LKAAQIAN-IDQFIDSLPLG-YNTKIGMEGSGisqGQRQRILIARAVYKN 648
Cdd:cd03265 73 RRiGIVFQDLSVDDELTGwENLYIHARLygVPGAERRErIDELLDFVGLLeAADRLVKTYSG---GMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 649 PDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
509-715 |
5.42e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.16 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVgdvylkninphlwrsvtgsvmqDGFIFSETIAENI 588
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW----------------------DGEPLDPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 589 A-------------IGEEVIDKERL--LKAAQI-ANIDQFIDSLPLG--YNTKIgmegSGISQGQRQRILIARAVYKNPD 650
Cdd:COG4152 74 GylpeerglypkmkVGEQLVYLARLkgLSKAEAkRRADEWLERLGLGdrANKKV----EELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 651 FLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELaAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
509-710 |
6.65e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 82.71 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDvylkninphlwRSVTGSVMQD-GFIFSET-IAE 586
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----------KPLDIAARNRiGYLPEERgLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 587 NIAIGEEVIDKERL--LKAAQIA-NIDQFIDSLPLGYNTKIGMEGsgISQGQRQRILIARAVYKNPDFLFFDEATNALDA 663
Cdd:cd03269 84 KMKVIDQLVYLAQLkgLKKEEARrRIDEWLERLELSEYANKRVEE--LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496428897 664 NNEREIMEHLNEFYR-GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG 710
Cdd:cd03269 162 VNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
509-707 |
7.03e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.86 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP----HLWRSVTGSVMQDGFIFSE-T 583
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaQLRREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 584 IAENI---AIGEEVIDKERLLKAAQIAnidqfidsLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNA 660
Cdd:PRK10535 103 AAQNVevpAVYAGLERKQRLLRAQELL--------QRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496428897 661 LDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQNADKIVVLDKGGIV 707
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
493-715 |
8.21e-18 |
|
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: 83.36 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVTGS 572
Cdd:cd03218 1 LRAENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VM--QDGFIFSE-TIAENIAIGEEVIdkeRLLKAAQIANIDQFIDSLPLGYNTKigMEGSGISQGQRQRILIARAVYKNP 649
Cdd:cd03218 78 GYlpQEASIFRKlTVEENILAVLEIR---GLSKKEREEKLEELLEEFHITHLRK--SKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 650 DFLFFDEATNALDANNEREIME---HLNEfyRGKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKiikILKD--RGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| Peptidase_C39D |
cd02420 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
5-143 |
9.87e-18 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239101 [Multi-domain] Cd Length: 125 Bit Score: 79.78 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 5 PVYTQLDRMDCGPTCLRMIAKYYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLvDDFPLPCILH 84
Cdd:cd02420 2 PTVLQMEATECGAASLAIILAYYGRYVPLSELRIACGVSRDGSNASNLLKAAREYGLTAKGYKKDLEAL-REVSLPAIVF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 85 WNQQHFVVCYRIRKRrnkyKILIGDPA-GTQTVTynEEEFKRCWissrekgqdTGVALVL 143
Cdd:cd02420 81 WNFNHFLVVEGFDKR----KVFLNDPAtGRRTVS--LEEFDQSF---------TGVVLTM 125
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
495-713 |
1.18e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVM 574
Cdd:PRK10247 10 LQNVGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFIFSETIAENIAIGEEvIDKERLLKAAQIANIDQFidSLPLGYNTKIGMEGSGisqGQRQRILIARAVYKNPDFLFF 654
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPWQ-IRNQQPDPAIFLDDLERF--ALPDTILTKNIAELSG---GEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 655 DEATNALDANNEREIMEHLNEFYRGKTVVI--VAHRLSTVQNADKIVVLD-KGGIVEEGTHQ 713
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
493-715 |
1.33e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.97 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPN-----KGNIKV--GDVYLKNINPHL 565
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLfgRNIYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 WRSVTGSVMQDGFIFSE-TIAENIAIG---------EEVIDKE---RLLKAAQIANIDQFIDSLPlgyntkigmegSGIS 632
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNVAIGvklnglvksKKELDERvewALKKAALWDEVKDRLNDYP-----------SNLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 633 QGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHrlSTVQNA---DKIVVLDKGGIVEE 709
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEV 229
|
....*.
gi 496428897 710 GTHQEL 715
Cdd:PRK14267 230 GPTRKV 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
503-715 |
1.65e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 87.53 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 503 DGSPdYVLNNVNLTI-PRNKItAIVGASGSGKTTLIKLLLGFYTPNKGNIKV-----GDVYLKNInphlwRSVTGSVMQD 576
Cdd:PTZ00243 1320 EGLP-LVLRGVSFRIaPREKV-GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVngreiGAYGLREL-----RRQFSMIPQD 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 577 GFIFSETIAENI-----AIGEEVidkerlLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYK-NPD 650
Cdd:PTZ00243 1393 PVLFDGTVRQNVdpfleASSAEV------WAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSG 1466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 651 FLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PTZ00243 1467 FILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
509-706 |
1.68e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNInphlwRSVTGSVMQDGFIFS-ETIAEN 587
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 588 IAIGeevidkerlLKAAQIANIDQFIDSlpLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNER 667
Cdd:PRK11247 102 VGLG---------LKGQWRDAALQALAA--VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496428897 668 EiMEHLNE-FYR--GKTVVIVAHRLS-TVQNADKIVVLDKGGI 706
Cdd:PRK11247 171 E-MQDLIEsLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
506-715 |
2.25e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 85.89 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 506 PDYV--LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFyTPNKGNIKVGDVYLKNINPHLWRS------VtgsVMQDG 577
Cdd:COG4172 296 VGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRPlrrrmqV---VFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 578 F--------IfSETIAENIAI-GEEVIDKERLLKAAQIanidqfidslpLgynTKIGM----------EGSGisqGQRQR 638
Cdd:COG4172 372 FgslsprmtV-GQIIAEGLRVhGPGLSAAERRARVAEA-----------L---EEVGLdpaarhryphEFSG---GQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 639 ILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQV 513
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
510-715 |
2.40e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.01 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSvMQdgFIF--------- 580
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRR-MQ--MVFqdpyaslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 581 ----SETIAENIAIGEEVIDKERLLKAAQIanIDQ------FIDSLPlgyntkigMEGSGisqGQRQRILIARAVYKNPD 650
Cdd:COG4608 111 rmtvGDIIAEPLRIHGLASKAERRERVAEL--LELvglrpeHADRYP--------HEFSG---GQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 651 FLFFDEATNALDANNEREI---MEHL-NEFyrGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVlnlLEDLqDEL--GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
497-711 |
2.97e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.79 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 497 NLCFSY-DGS-PDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKgnikvGDVYLKNINPHLWRSVTGSVM 574
Cdd:PRK11629 10 NLCKRYqEGSvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS-----GDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QD---GFIFS-------ETIAENIA----IG----EEVIDKERLLKAAqianidqfidslpLGYNTKIGMEGSGISQGQR 636
Cdd:PRK11629 85 RNqklGFIYQfhhllpdFTALENVAmpllIGkkkpAEINSRALEMLAA-------------VGLEHRANHRPSELSGGER 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 637 QRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGT 711
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlqGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
509-715 |
3.52e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP-------------HLWRSVTGSVMQ 575
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 576 DGFIFSE-TIAENIAigEEVIDKERLLKAAQIANIDQFIDslplgyntKIGMEGSG-------ISQGQRQRILIARAVYK 647
Cdd:PRK10619 100 HFNLWSHmTVLENVM--EAPIQVLGLSKQEARERAVKYLA--------KVGIDERAqgkypvhLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 648 NPDFLFFDEATNALDANNERE---IMEHLNEfyRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEvlrIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
504-707 |
5.85e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 504 GSPD--YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVT-GSVMQD---G 577
Cdd:COG1101 14 GTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKYiGRVFQDpmmG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 578 FIFSETIAENIAI----GEevidKERLLKAAQIANIDQFID---SLPLGY----NTKIGMegsgISQGQRQRILIARAVY 646
Cdd:COG1101 93 TAPSMTIEENLALayrrGK----RRGLRRGLTKKRRELFREllaTLGLGLenrlDTKVGL----LSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 647 KNPDFLFFDEATNALDANNEREIMEHLNEFYRGK--TVVIVAHRLstvQNA----DKIVVLDKGGIV 707
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNM---EQAldygNRLIMMHEGRII 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
494-717 |
6.92e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.40 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyvlNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIkvgdvYLKNIN----PHLWRSV 569
Cdd:PRK10771 3 KLTDITWLYHHLP----MRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-----TLNGQDhtttPPSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 570 TgSVMQDGFIFSE-TIAENIAIGeevID---------KERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRI 639
Cdd:PRK10771 74 S-MLFQENNLFSHlTVAQNIGLG---LNpglklnaaqREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 640 LIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGK--TVVIVAHRLS-TVQNADKIVVLDKGGIVEEGTHQELT 716
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
.
gi 496428897 717 C 717
Cdd:PRK10771 219 S 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
494-715 |
7.52e-17 |
|
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: 81.44 E-value: 7.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTpNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:cd03289 4 TVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSETIAENIAIGEEVIDKErLLKAAQIANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWSDEE-IWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| C39G |
COG3271 |
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ... |
15-127 |
8.16e-17 |
|
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442502 [Multi-domain] Cd Length: 179 Bit Score: 78.88 E-value: 8.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 15 CGPTCLRMIAKY-YGRVYSLQTLRDKAF----ISRSGVSLLGISEAAESIGFRTTGVKITFEQLVdDFPLPCILHWNQQ- 88
Cdd:COG3271 54 CGAAALATLLNYhYGRPVSEAEVLEGMLthgdQRRRGFSLLDMKRYLEALGLRADGYRLTLDDLA-QLGIPAIVLINLGg 132
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 496428897 89 --HFVVCYRIRKRRnkykILIGDPA-GtqTVTYNEEEFKRCW 127
Cdd:COG3271 133 ykHFVVVKGVDDGR----VLLADPAlG--NRSLSREEFEKMW 168
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
495-715 |
1.57e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.49 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPDYV--LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYtpnKGNIKV-------GDVYLKNINPHL 565
Cdd:COG4170 6 IRNLTIEIDTPQGRVkaVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGIT---KDNWHVtadrfrwNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 WRSVTGSVMqdGFIF---------SETIAENIaigEEVIDKE------------------RLLKAAQIANIDQFIDSLPL 618
Cdd:COG4170 83 RRKIIGREI--AMIFqepsscldpSAKIGDQL---IEAIPSWtfkgkwwqrfkwrkkraiELLHRVGIKDHKDIMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 619 gyntkigmegsGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREI---MEHLNEFyRGKTVVIVAHRLSTV-QN 694
Cdd:COG4170 158 -----------ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIfrlLARLNQL-QGTSILLISHDLESIsQW 225
|
250 260
....*....|....*....|.
gi 496428897 695 ADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG4170 226 ADTITVLYCGQTVESGPTEQI 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
510-715 |
3.13e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.87 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLK----NINPHLWRSVTGSVMQ--DGFIFSET 583
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 584 IAENIAIGEE---VIDKERLLKA----AQIANIDQFIDSLPLgyntkigmEGSGisqGQRQRILIARAVYKNPDFLFFDE 656
Cdd:PRK13641 103 VLKDVEFGPKnfgFSEDEAKEKAlkwlKKVGLSEDLISKSPF--------ELSG---GQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 657 ATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
443-708 |
3.18e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 82.33 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 443 LNSPIEQFIGFARSFQDAKISLERLNEIHQKEDEEETAVDKVsfLPQDHTFTIENLCFSYdGSPDYVLNNVNLTIPRNKI 522
Cdd:PRK10522 275 LRTPLLSAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQA--FPDWQTLELRNVTFAY-QDNGFSVGPINLTIKRGEL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 523 TAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIA-ENIAIGEEVIDK--ER 599
Cdd:PRK10522 352 LFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGpEGKPANPALVEKwlER 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 600 LLKAAQIANIDQFIDSLPLgyntkigmegsgiSQGQRQRILIARAVYKNPDFLFFDEATNALDANNEReimehlnEFYR- 678
Cdd:PRK10522 432 LKMAHKLELEDGRISNLKL-------------SKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR-------EFYQv 491
|
250 260 270
....*....|....*....|....*....|....*...
gi 496428897 679 --------GKTVVIVAHRLSTVQNADKIVVLDKGGIVE 708
Cdd:PRK10522 492 llpllqemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
495-715 |
3.82e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.93 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKlLLGFYTPNKGNIKV--------GDVYLKNINPHLW 566
Cdd:PRK14258 10 VNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVegrveffnQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVTGSVMQDGFIFSETIAENIAIGEEVIDKERLLKAAQIanIDQFIDSLPLGYNTKIGMEGSG--ISQGQRQRILIARA 644
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDI--VESALKDADLWDEIKHKIHKSAldLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 645 VYKNPDFLFFDEATNALDANNEREImEHL--NEFYRGK-TVVIVAHRLSTVQNADKIVVLDKGG------IVEEGTHQEL 715
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKV-ESLiqSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGNenrigqLVEFGLTKKI 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
492-710 |
4.64e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 492 TFTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTG 571
Cdd:PRK09536 3 MIDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQD---GFIFS-ETIAE--------NIAIGEEVIDK--ERLLKAAQIAN-IDQFIDSLplgyntkigmegsgiSQGQR 636
Cdd:PRK09536 81 SVPQDtslSFEFDvRQVVEmgrtphrsRFDTWTETDRAavERAMERTGVAQfADRPVTSL---------------SGGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 637 QRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEG 710
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
510-716 |
6.03e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVylkninPHLWRSVTGSVMQD-GFIFSE------ 582
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRFASTTAALAAGvAIIYQElhlvpe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 -TIAENIAIGE-----EVIDKERLLKAA--QIANIDQFID-SLPLGYntkigmegsgISQGQRQRILIARAVYKNPDFLF 653
Cdd:PRK11288 94 mTVAENLYLGQlphkgGIVNRRLLNYEAreQLEHLGVDIDpDTPLKY----------LSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 654 FDEATNALDAnneREImEHLNEFYR-----GKTVVIVAHRLSTV-QNADKIVVLDKGGIVEegTHQELT 716
Cdd:PRK11288 164 FDEPTSSLSA---REI-EQLFRVIRelraeGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDMA 226
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
503-694 |
8.14e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.09 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 503 DGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKV-GDVYLKNINPHLWRSVTG--SVMQDGFI 579
Cdd:PRK13545 33 DGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISSGLNGQLTGieNIELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSETIAENIAIGEEVIDkerllkaaqIANIDQFIDSLPLGYntkigmegsgiSQGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:PRK13545 113 MGLTKEKIKEIIPEIIE---------FADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 496428897 660 ALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN 694
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKS 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
510-715 |
9.28e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 9.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNIN--PHLWRSVTGSVMQDGFIFSE----- 582
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQreGRLARDIRKSRANTGYIFQQfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 --TIAENIAIGE--------------EVIDKERLLKAAqianidqfidslplgynTKIGMEG------SGISQGQRQRIL 640
Cdd:PRK09984 100 rlSVLENVLIGAlgstpfwrtcfswfTREQKQRALQAL-----------------TRVGMVHfahqrvSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 641 IARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
181-466 |
1.82e-15 |
|
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: 77.51 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLVKLMR 260
Cdd:cd18545 6 LLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 261 LPLHFFDTKMIGDIMQR-IGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLSFMKYRR 339
Cdd:cd18545 86 LSFSFFDSRPVGKILSRvINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 340 eldlRRFSQASTEQSTLY----QIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNILI 415
Cdd:cd18545 166 ----KAWQRVRKKISNLNaylhESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 496428897 416 SYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLER 466
Cdd:cd18545 242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAER 292
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
494-710 |
1.93e-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: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGF--YTPNKGNIKVGDVYLKNINPHLwRSVTG 571
Cdd:cd03217 2 EIKDLHVSVGGKE--ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMqdGFIFSETIAEniaigeevidkerllkaaqIANIDqFIDSLplgyntkigmeGSGISQGQRQRILIARAVYKNPDF 651
Cdd:cd03217 79 IFL--AFQYPPEIPG-------------------VKNAD-FLRYV-----------NEGFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 652 LFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAH--RLSTVQNADKIVVLDKGGIVEEG 710
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
510-715 |
2.15e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.92 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSV----TGSVMQDGFIFSE-TI 584
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AENIAIGEEVID------KERLLKAAQIANIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAVYKNPDFLFFDEAT 658
Cdd:PRK10070 124 LDNTAFGMELAGinaeerREKALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 659 NALDANNEREIMEHLNEFY--RGKTVVIVAHRL-STVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
509-715 |
3.39e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.34 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKV-GDvylkNInPHLWRSVTGSV-------MQDGFIF 580
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGE----NI-PAMSRSRLYTVrkrmsmlFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 581 SE-TIAENIA--IGEEVIDKERLLKAAQIANIDqfidslplgyntKIGMEG------SGISQGQRQRILIARAVYKNPDF 651
Cdd:PRK11831 97 TDmNVFDNVAypLREHTQLPAPLLHSTVMMKLE------------AVGLRGaaklmpSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 652 LFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
508-715 |
4.14e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 76.03 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 508 YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYL---------KNI-----------NPHLwr 567
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeygdykyrcKHIrmifqdpntslNPRL-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 568 svtgsvmQDGFIFSETIAENIAIGEEvidkERllkAAQIANIDQFIDSLPLGYNTKIGMegsgISQGQRQRILIARAVYK 647
Cdd:COG4167 105 -------NIGQILEEPLRLNTDLTAE----ER---EERIFATLRLVGLLPEHANFYPHM----LSSGQKQRVALARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496428897 648 NPDFLFFDEATNALDANNEREI---MEHLNEFYrGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:COG4167 167 QPKIIIADEALAALDMSVRSQIinlMLELQEKL-GISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEV 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
494-715 |
5.13e-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: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGF--YTPNKGNI-----------------KVG 554
Cdd:TIGR03269 2 EVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpsKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 555 -------------DVYLKNINPHLWRSVTGSV---MQDGFIF--SETIAENIAIGEEVID---KERLLKAAQIanidqfI 613
Cdd:TIGR03269 80 epcpvcggtlepeEVDFWNLSDKLRRRIRKRIaimLQRTFALygDDTVLDNVLEALEEIGyegKEAVGRAVDL------I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 614 DSLPLGYN-TKIGMEGSGisqGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLS 690
Cdd:TIGR03269 154 EMVQLSHRiTHIARDLSG---GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 496428897 691 TVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:TIGR03269 231 VIEDlSDKAIWLENGEIKEEGTPDEV 256
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
509-711 |
5.58e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 74.78 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPH---LWRSvtGSVmqdGFIF----- 580
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDaraRLRA--RHV---GFVFqsfql 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 581 --SETIAENIAIG-EEVIDKErllkAAQIA-------NIDQFIDSLPlgyntkigmegSGISQGQRQRILIARAVYKNPD 650
Cdd:COG4181 102 lpTLTALENVMLPlELAGRRD----ARARArallervGLGHRLDHYP-----------AQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 651 FLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQNADKIVVLDKGGIVEEGT 711
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
493-705 |
7.77e-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: 72.57 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSydgSPDY--VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKV---GDVYLkninphlwr 567
Cdd:cd03223 1 IELENLSLA---TPDGrvLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpegEDLLF--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 568 svtgsVMQDGFIFSETIAENIAigeevidkerllkaaqianidqfidsLPLGyntkigMEGSGisqGQRQRILIARAVYK 647
Cdd:cd03223 69 -----LPQRPYLPLGTLREQLI--------------------------YPWD------DVLSG---GEQQRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 648 NPDFLFFDEATNALDANNEREIMEHLNEfyRGKTVVIVAHRLSTVQNADKIVVLDKGG 705
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
501-715 |
9.60e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 501 SYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNiNPHLWRSVTGSVMQ-DGFI 579
Cdd:PRK13536 50 SYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSETIAENIAI-GEEVIDKERLLKAAqIANIDQFIdSLPLGYNTKIgmegSGISQGQRQRILIARAVYKNPDFLFFDEAT 658
Cdd:PRK13536 127 LEFTVRENLLVfGRYFGMSTREIEAV-IPSLLEFA-RLESKADARV----SDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 659 NALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHAL 259
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
128-715 |
1.00e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.41 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 128 ISSREKGQDTGVALVLEPTpdfysmEEDRKE----------AKKKLNFFFRYLSPHKKALVQLVLGMVI------GSILQ 191
Cdd:TIGR01271 814 IYSRRLSKDSVYEISEEIN------EEDLKEcfaderenvfETTTWNTYLRYITTNRNLVFVLIFCLVIflaevaASLLG 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 192 LIVpfLTQSLVDVGIRDNN-------LNFITLILV---AQLIIFI------ARLSVDFIRSWLLLHMNIRINISLISDFL 255
Cdd:TIGR01271 888 LWL--ITDNPSAPNYVDQQhanasspDVQKPVIITptsAYYIFYIyvgtadSVLALGFFRGLPLVHTLLTVSKRLHEQML 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 256 VKLMRLPLHFFDTKMIGDIMQR-IGDHSRIESFLTgssiSTLFSFVNF--IVFG--FVLAYYDLSIFGLFLLGNLLYVIW 330
Cdd:TIGR01271 966 HSVLQAPMAVLNTMKAGRILNRfTKDMAIIDDMLP----LTLFDFIQLtlIVLGaiFVVSVLQPYIFIAAIPVAVIFIML 1041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 331 VLSFMKYRRELD-----------------------LRRFSQASTEQSTLYQIITGMQEIKLNNCETQkRWKWERIQV--K 385
Cdd:TIGR01271 1042 RAYFLRTSQQLKqlesearspifshlitslkglwtIRAFGRQSYFETLFHKALNLHTANWFLYLSTL-RWFQMRIDIifV 1120
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 386 LFKISVKGLALQQYQ----QVGSVFfnqTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEqfiGFARSFQDAK 461
Cdd:TIGR01271 1121 FFFIAVTFIAIGTNQdgegEVGIIL---TLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQE---EPRPSGGGGK 1194
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 462 ISLERLNEIHQKEDEEEtavdkvsfLPQDHTFTIENLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLL 541
Cdd:TIGR01271 1195 YQLSTVLVIENPHAQKC--------WPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL 1266
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 542 GFYTpNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENIAIGEEVIDKErLLKAAQIANIDQFIDSLPLGYN 621
Cdd:TIGR01271 1267 RLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDKLD 1344
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 622 TKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVL 701
Cdd:TIGR01271 1345 FVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVI 1424
|
650
....*....|....
gi 496428897 702 DKGGIVEEGTHQEL 715
Cdd:TIGR01271 1425 EGSSVKQYDSIQKL 1438
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-715 |
1.01e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLK------NINPHLWRSVTGSVMQDGFIFSE 582
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 -TIAENIA--IGEEVIDKERLLKAAQIANIDQFidSLPLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:PRK14246 105 lSIYDNIAypLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 660 ALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
497-715 |
1.19e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 497 NLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLlgfytpNKGNIKV------GDVYLKNINPHLWRSV- 569
Cdd:PRK14271 26 NLTLGFAGKT--VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL------NRMNDKVsgyrysGDVLLGGRSIFNYRDVl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 570 -----TGSVMQDGFIFSETIAENIAIGeevIDKERLLKAAQIANIDQF-IDSLPLGYNTKIGMEGSG--ISQGQRQRILI 641
Cdd:PRK14271 98 efrrrVGMLFQRPNPFPMSIMDNVLAG---VRAHKLVPRKEFRGVAQArLTEVGLWDAVKDRLSDSPfrLSGGQQQLLCL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 642 ARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
492-715 |
1.98e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.39 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 492 TFTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVG--DVYLKNINPHLWRSV 569
Cdd:PRK10895 3 TLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 570 tGSVMQDGFIFSE-TIAENI----AIGEEVIDKERLLKAAQIA---NIDQFIDSLplgyntkigmeGSGISQGQRQRILI 641
Cdd:PRK10895 81 -GYLPQEASIFRRlSVYDNLmavlQIRDDLSAEQREDRANELMeefHIEHLRDSM-----------GQSLSGGERRRVEI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 642 ARAVYKNPDFLFFDEATNALD---ANNEREIMEHLNEfyRGKTVVIVAHRL-STVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRD--SGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
463-727 |
2.05e-14 |
|
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: 77.75 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 463 SLERLNEIHQK-EDEEETAVDKVSFLPQDHTFTIENLC-------FSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKT 534
Cdd:TIGR01257 893 ALEKTEPLTEEmEDPEHPEGINDSFFERELPGLVPGVCvknlvkiFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKT 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 535 TLIKLLLGFYTPNKGNIKVGDvylKNINPHL--WRSVTGSVMQDGFIFSE-TIAENIAIGEEVidKERLLKAAQIANIDQ 611
Cdd:TIGR01257 971 TTLSILTGLLPPTSGTVLVGG---KDIETNLdaVRQSLGMCPQHNILFHHlTVAEHILFYAQL--KGRSWEEAQLEMEAM 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 612 FIDSlplGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVAHRLST 691
Cdd:TIGR01257 1046 LEDT---GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE 1122
|
250 260 270
....*....|....*....|....*....|....*....
gi 496428897 692 VQN-ADKIVVLDKGGIVEEGTHQEL-TCL-KGIYYRLVK 727
Cdd:TIGR01257 1123 ADLlGDRIAIISQGRLYCSGTPLFLkNCFgTGFYLTLVR 1161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
509-715 |
2.08e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.84 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLwRSVTGSVMQ-DGFIFSETIAEN 587
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVPQfDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 588 IaigeEVIDKERLLKAAQI-ANIDQFIDSLPLgyNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNE 666
Cdd:PRK13537 101 L----LVFGRYFGLSAAAArALVPPLLEFAKL--ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496428897 667 REIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13537 175 HLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
180-467 |
4.07e-14 |
|
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: 73.62 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 180 LVLGmVIGSILQLIVPFLTQSLVDvGIRDNNLNFITLILVAqlIIFIARLSVDFIRSWLLLHM------NIRinISLISd 253
Cdd:cd18551 5 LLLS-LLGTAASLAQPLLVKNLID-ALSAGGSSGGLLALLV--ALFLLQAVLSALSSYLLGRTgervvlDLR--RRLWR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 flvKLMRLPLHFFDTKMIGDIMQRIG-DHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYD--LSIFGLFLLGNLLYVIW 330
Cdd:cd18551 78 ---RLLRLPVSFFDRRRSGDLVSRVTnDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDwvLTLVTLAVVPLAFLIIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 331 VLSfmkyRReldLRRFSQASTEQ-----STLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQ-VGS 404
Cdd:cd18551 155 PLG----RR---IRKASKRAQDAlgelsAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGpLMG 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 405 VFFNQTTNILISYIAARaVVEGNMTLGMMMS-LTYIIgQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18551 228 LAVQLALLVVLGVGGAR-VASGALTVGTLVAfLLYLF-QLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
491-705 |
4.10e-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: 71.51 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 491 HTFTIENLCFSYD--GSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTpnKGNIKvGDVYL--KNINPHLW 566
Cdd:cd03232 2 SVLTWKNLNYTVPvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVIT-GEILIngRPLDKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSvTGSVMQ-DGFIFSETIaeniaigeevidKERLLKAAQIanidqfidslplgyntkigmegSGISQGQRQRILIARAV 645
Cdd:cd03232 79 RS-TGYVEQqDVHSPNLTV------------REALRFSALL----------------------RGLSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 646 YKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTV--QNADKIVVLDKGG 705
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADsGQAILCTIHQPSASifEKFDRLLLLKRGG 186
|
|
| Peptidase_C39G |
cd02423 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
15-127 |
5.83e-14 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature.
Pssm-ID: 239103 [Multi-domain] Cd Length: 129 Bit Score: 69.22 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 15 CGPTCLRMIAKYYGRV-YSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQLVdDFPLPCI-LHWNQQ--HF 90
Cdd:cd02423 12 CGPAALATLLRYYGGInITEQEVLKLMLIRSEGFSMLDLKRYAEALGLKANGYRLNLDKLN-ALQIPVIvLVNNGGygHF 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 496428897 91 VVCYRIRKRRnkykILIGDPA-GtqTVTYNEEEFKRCW 127
Cdd:cd02423 91 VVIKGIDGDR----VLVGDPAlG--NISMSREEFERIW 122
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
176-466 |
1.19e-13 |
|
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: 72.18 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 176 ALVQLVLgMVIGSILQLIVPFLTQSLVD-VGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDF 254
Cdd:cd18778 1 LILTLLC-ALLSTLLGLVPPWLIRELVDlVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 255 LVKLMRLPLHFFDTKMIGDIMQR-IGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLS 333
Cdd:cd18778 80 YDKLQRLSLRYFDDRQTGDLMSRvINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FMKYRRELdLRRFSQASTEQSTLYQ-IITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTN 412
Cdd:cd18778 160 YSKKVRPR-YRKVREALGELNALLQdNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 496428897 413 ILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLER 466
Cdd:cd18778 239 VLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAER 292
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
505-716 |
1.33e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 505 SPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSV-TGSVMQDGFIFSE- 582
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDEl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 TIAENIAIGE---------EVIDKERLLKAAQIANIdqfIDSLPLGYNTKIGmegsGISQGQRQRILIARAVYKNPDFLF 653
Cdd:PRK09700 96 TVLENLYIGRhltkkvcgvNIIDWREMRVRAAMMLL---RVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 654 FDEATNALdANNERE----IMEHLNEfyRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQELT 716
Cdd:PRK09700 169 MDEPTSSL-TNKEVDylflIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVS 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
493-687 |
1.52e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSPdyVLNNVNLTIPR-NKItAIVGASGSGKTTLIKLLLGFYTPNKGNIKVG--------DVYLKNINP 563
Cdd:PRK11147 320 FEMENVNYQIDGKQ--LVKDFSAQVQRgDKI-ALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtklevayfDQHRAELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 564 hlwrsvtgsvmqdgfifSETIAENIAIGEEVIdkerllkaaQIANIDQFIdslpLGY------NTKIGMEG-SGISQGQR 636
Cdd:PRK11147 397 -----------------EKTVMDNLAEGKQEV---------MVNGRPRHV----LGYlqdflfHPKRAMTPvKALSGGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496428897 637 QRILIARAVYKNPDFLFFDEATNALDANNeREIMEHLNEFYRGkTVVIVAH 687
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDVET-LELLEELLDSYQG-TVLLVSH 495
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
510-711 |
1.72e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 72.30 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINP---HLWRSVTGSVMQDGF-------I 579
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPYgslnprkK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSETIAENIAIGEEVIDKERLLKAAQIAnidqfidslplgynTKIGM--EGSG-----ISQGQRQRILIARAVYKNPDFL 652
Cdd:PRK11308 111 VGQILEEPLLINTSLSAAERREKALAMM--------------AKVGLrpEHYDryphmFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 653 FFDEATNALDANNEREI----MEHLNEFyrGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGT 711
Cdd:PRK11308 177 VADEPVSALDVSVQAQVlnlmMDLQQEL--GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
510-704 |
2.28e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVG--DVY-LKNINPHLWRSVTGSVMQDG-FIFSETIA 585
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDITrLKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 586 ENIAI-----GEEVIDKERLLKAAqianIDQfIDSLPLGYNTKIGMEGsgisqGQRQRILIARAVYKNPDFLFFDEATNA 660
Cdd:PRK10908 98 DNVAIpliiaGASGDDIRRRVSAA----LDK-VGLLDKAKNFPIQLSG-----GEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496428897 661 LDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQNAD-KIVVLDKG 704
Cdd:PRK10908 168 LDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
182-440 |
2.31e-13 |
|
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: 71.05 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 182 LGMVIGSILQLIVPFLTQSLVDVGIRD---NNLNFITLILvaqLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLVKL 258
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTIIKGgdlDVLNELALIL---LAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 259 MRLPLHFFDTKMIGDIMQRIG-DHSRIESFLTGSSISTLFSFVNFIVFGFVLAY--YDLSIFGLFLLGNLLYVIWVLSfm 335
Cdd:cd18557 80 LRQEIAFFDKHKTGELTSRLSsDTSVLQSAVTDNLSQLLRNILQVIGGLIILFIlsWKLTLVLLLVIPLLLIASKIYG-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 336 KYRRELdLRRFSQASTEQSTLYQ-IITGMQEIKLNNCETQKRWKWERIQVKLFKISVK-GLALQQYQQVGSVFFNQTTnI 413
Cdd:cd18557 158 RYIRKL-SKEVQDALAKAGQVAEeSLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKkALANALFQGITSLLIYLSL-L 235
|
250 260
....*....|....*....|....*..
gi 496428897 414 LISYIAARAVVEGNMTLGMMMSltYII 440
Cdd:cd18557 236 LVLWYGGYLVLSGQLTVGELTS--FIL 260
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
493-716 |
2.90e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLcfsydgSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPH-------- 564
Cdd:COG1129 257 LEVEGL------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagia 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 565 LwrsVTGSVMQDGFIFSETIAENIAI---------GeeVIDKERLLKAAQ---------IANIDQFIDSLplgyntkigm 626
Cdd:COG1129 331 Y---VPEDRKGEGLVLDLSIRENITLasldrlsrgG--LLDRRRERALAEeyikrlrikTPSPEQPVGNL---------- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 627 egSGisqGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVahrlST-----VQNADKIVV 700
Cdd:COG1129 396 --SG---GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVI----SSelpelLGLSDRILV 466
|
250
....*....|....*.
gi 496428897 701 LDKGGIVEEGTHQELT 716
Cdd:COG1129 467 MREGRIVGELDREEAT 482
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
174-467 |
4.23e-13 |
|
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: 70.32 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNN---LNFITLILVAqLIIFIARLSVdfIRSWLLLHMNIRINISL 250
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSlstLLGLTLGMVV-LLAFDGLLRQ--VRSRILQRVGLRLDVEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 251 ISDFLVKLMRLPLhffDTKMIGDIMQRIGDHSRIESFLTGSSISTLFSFVNFIVFGFVLayYDLSIFGLFLLGNLLYVIW 330
Cdd:cd18586 78 GRRVFRAVLELPL---ESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVI--FLIHPPLGWVALVGAPVLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 331 VLSFMKYRREldlRRFSQ-ASTEQSTLYQIITGMqeikLNNCETQK--------RWKWERIQVKLFKISVKGLALQQYQQ 401
Cdd:cd18586 153 GLAWLNHRAT---RKPLGeANEAQAARDALAAET----LRNAETIKalgmlgnlRRRWEARHAETLELQIRASDLAGAIS 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 402 VGSVFFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18586 226 AIGKTLRMALQSLILGVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYERL 291
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
509-715 |
4.73e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.02 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSE-TIAEN 587
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 588 IAIGE----------EVIDKERLLKAAQIANI----DQFIDSLplgyntkigmegsgiSQGQRQRILIARAVYKNPDFLF 653
Cdd:PRK10253 102 VARGRyphqplftrwRKEDEEAVTKAMQATGIthlaDQSVDTL---------------SGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 654 FDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNRekGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEI 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
494-715 |
6.84e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.18 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDgsPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNI--KVGDVYLKNINP-------H 564
Cdd:PRK11701 8 SVRGLTKLYG--PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyRMRDGQLRDLYAlseaerrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 565 LWRSVTGSVMQ---DGFIFSETIAENI-----AIG---------------EEV-IDKERllkaaqianidqfIDSLPLGY 620
Cdd:PRK11701 86 LLRTEWGFVHQhprDGLRMQVSAGGNIgerlmAVGarhygdiratagdwlERVeIDAAR-------------IDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 621 ntkigmegsgiSQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADK 697
Cdd:PRK11701 153 -----------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLlAHR 221
|
250
....*....|....*....
gi 496428897 698 IVVLDKGGIVEEG-THQEL 715
Cdd:PRK11701 222 LLVMKQGRVVESGlTDQVL 240
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
181-466 |
9.68e-13 |
|
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: 69.35 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVD------VGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDF 254
Cdd:cd18547 5 IILAIISTLLSVLGPYLLGKAIDliieglGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 255 LVKLMRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYD--LSIFGLFLLGNLLYVIWV 331
Cdd:cd18547 85 FEKLQRLPLSYFDTHSHGDIMSRVtNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISplLTLIVLVTVPLSLLVTKF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 332 LsfMKYRReldlRRFSQASTEQSTLY----QIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGlalqqyQQVGSV-- 405
Cdd:cd18547 165 I--AKRSQ----KYFRKQQKALGELNgyieEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKA------QFYSGLlm 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 406 ----FFNQTTNILISYIAARAVVEGNMTLGMMMS-LTYiIGQLNSPIEQFIGFARSFQDAKISLER 466
Cdd:cd18547 233 pimnFINNLGYVLVAVVGGLLVINGALTVGVIQAfLQY-SRQFSQPINQISQQINSLQSALAGAER 297
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
497-716 |
1.05e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 497 NLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVtGS--VM 574
Cdd:PRK15439 16 SISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL-GIylVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 QDGFIF-SETIAENIAIG--EEVIDKERLlkAAQIANidqfidslpLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDF 651
Cdd:PRK15439 93 QEPLLFpNLSVKENILFGlpKRQASMQKM--KQLLAA---------LGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 652 LFFDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQELT 716
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLaQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADLS 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
495-715 |
1.72e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.19 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSpdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFyTPNKGNIKVGDVYL--KNINPHLWRSVT-G 571
Cdd:PRK10418 7 LRNIALQAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGI-LPAGVRQTAGRVLLdgKPVAPCALRGRKiA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 572 SVMQD---GFIFSETIAENIaigeevidKERLLKAAQIANIDQFIDSLplgynTKIGMEGSG---------ISQGQRQRI 639
Cdd:PRK10418 83 TIMQNprsAFNPLHTMHTHA--------RETCLALGKPADDATLTAAL-----EAVGLENAArvlklypfeMSGGMLQRM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 640 LIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFY--RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVqkRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
510-715 |
1.85e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKG--NIKVGD--VYLKNINPHLWRSVTGSVmqdGFIFSE--- 582
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDewVDMTKPGPDGRGRAKRYI---GILHQEydl 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 ----TIAENI--AIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEgsgISQGQRQRILIARAVYKNPDFLFFDE 656
Cdd:TIGR03269 377 yphrTVLDNLteAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDE---LSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 657 ATNALDANNERE----IMEHLNEFyrGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:TIGR03269 454 PTGTMDPITKVDvthsILKAREEM--EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
222-467 |
2.03e-12 |
|
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: 68.62 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 222 LIIFIARLSVDFIRSWLLLHMNIRINISLISDFLVKLMRLPLHFfDTKMIGDIMQRIGDHSRIESFLTGSSISTL----F 297
Cdd:cd18587 49 LIALLFDFILKLLRAYFIDVAGKRADVILSSRLFERVLGLRLEA-RPASVGSFANNLREFESVRDFFTSATLTALidlpF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 298 SFVNFIVFGFV---LAYYDLSIFGlfllgnllyVIWVLSFMKYRReldLRRFSQASTE-----QSTLYQIITGMQEIKLN 369
Cdd:cd18587 128 VLLFLAVIALIggpLALVPLVAIP---------LVLLYGLLLQKP---LRRLVEESMResaqkNALLVESLSGLETIKAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 370 NCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQ 449
Cdd:cd18587 196 GAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQ 275
|
250
....*....|....*...
gi 496428897 450 FIGFARSFQDAKISLERL 467
Cdd:cd18587 276 IAGLLTRYQQARTALKSL 293
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
495-691 |
2.28e-12 |
|
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: 69.96 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDgspDYVL-NNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGD-VYLkninphlwrsvtGS 572
Cdd:TIGR03719 325 AENLTKAFG---DKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtVKL------------AY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQ--DGFIFSETIAENIAIGEEVID--KERLLKAAQIANI-----DQfidslplgyNTKIGMegsgISQGQRQRILIAR 643
Cdd:TIGR03719 390 VDQsrDALDPNKTVWEEISGGLDIIKlgKREIPSRAYVGRFnfkgsDQ---------QKKVGQ----LSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496428897 644 AVYKNPDFLFFDEATNALDANNEREIMEHLNEFyrGKTVVIVAH------RLST 691
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
177-467 |
2.37e-12 |
|
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: 68.28 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 177 LVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLllhmNIRINISLISDFLV 256
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYL----SARIGQGVMYDLRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 257 K----LMRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYD-----LSIFGLFLlgnll 326
Cdd:cd18550 77 QlyahLQRMSLAFFTRTRTGEIQSRLnNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDwrlalLSLVLLPL----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 327 yVIWVLSFM-KYRRELDLRRFSQASTEQSTLYQI--ITGMQEIKLNNCETQKRWKWERIQVKLFKISVK-GLALQQYQQV 402
Cdd:cd18550 152 -FVLPTRRVgRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRqALAGRWFFAA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 403 GSVFFNQTTnILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18550 231 LGLFTAIGP-ALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
181-467 |
3.13e-12 |
|
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: 67.84 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLL------LHMNIRinisliSDF 254
Cdd:cd18542 5 ILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAekasqkVAYDLR------NDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 255 LVKLMRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLsifglfllgnlLYVIWVLS 333
Cdd:cd18542 79 YDHLQRLSFSFHDKARTGDLMSRCtSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINW-----------KLTLISLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FM--------KYRRELDlRRFSQASTEQSTLYQI----ITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQ 401
Cdd:cd18542 148 IIpfialfsyVFFKKVR-PAFEEIREQEGELNTVlqenLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYW 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 402 VGSVFFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQfIGFARS-FQDAKISLERL 467
Cdd:cd18542 227 PLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQ-LGRLINdMSRASASAERI 292
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
509-704 |
6.15e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.92 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKV----GDVYLKNINPH----LWRSVTGSVMQdgfiF 580
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPReilaLRRRTIGYVSQ----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 581 ---------SETIAEN-IAIGEEviDKERLLKAAQIA---NIDQFIDSLPLgyNTkigmegsgISQGQRQRILIARAVYK 647
Cdd:COG4778 102 lrviprvsaLDVVAEPlLERGVD--REEARARARELLarlNLPERLWDLPP--AT--------FSGGEQQRVNIARGFIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 648 NPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTVQN-ADKIVVLDKG 704
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
511-715 |
6.26e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 511 NNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTgSVMQdgFIFSE-------- 582
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQ--MIFQDplaslnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 -TIAENIA----------IGEEVID--KERLLKAAQIANIdqfIDSLPlgyntkigMEGSGisqGQRQRILIARAVYKNP 649
Cdd:PRK15079 115 mTIGEIIAeplrtyhpklSRQEVKDrvKAMMLKVGLLPNL---INRYP--------HEFSG---GQCQRIGIARALILEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 650 DFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
514-701 |
7.37e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 7.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 514 NLTIPRN-KITAIVGASGSGKTTLIKLLLGFYTPNKGNikvgdvYLKNINphlWRSV----TGSVMQDGFifsETIAEN- 587
Cdd:PRK13409 92 GLPIPKEgKVTGILGPNGIGKTTAVKILSGELIPNLGD------YEEEPS---WDEVlkrfRGTELQNYF---KKLYNGe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 588 --IAIGEEVID----------KERLLKAAQIANIDQFIDSLPLG--YNTKIgmegSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:PRK13409 160 ikVVHKPQYVDlipkvfkgkvRELLKKVDERGKLDEVVERLGLEniLDRDI----SELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 654 FDEATNALDannereIMEHLN------EFYRGKTVVIVAHRLSTVQN-ADKIVVL 701
Cdd:PRK13409 236 FDEPTSYLD------IRQRLNvarlirELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
510-710 |
9.10e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKvgdVYLKNINPHLWRSVTGSVMQD---GFIFSETIAE 586
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS---ILGQPTRQALQKNLVAYVPQSeevDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 587 NIAIG--------EEVIDKERLLKAAQIANIDQfidslpLGYNTKIGMEGSGisqGQRQRILIARAVYKNPDFLFFDEAT 658
Cdd:PRK15056 100 VVMMGryghmgwlRRAKKRDRQIVTAALARVDM------VEFRHRQIGELSG---GQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496428897 659 NALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQNADKIVVLDKGGIVEEG 710
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
514-701 |
1.07e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.89 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 514 NLTIPR-NKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKvgdvylkniNPHLWRSV----TGSVMQDGFifsETIAEN- 587
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYD---------EEPSWDEVlkrfRGTELQDYF---KKLANGe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 588 --IAIGEEVID----------KERLLKAAQIANIDQFIDSLPLG--YNTKIgmegSGISQGQRQRILIARAVYKNPDFLF 653
Cdd:COG1245 160 ikVAHKPQYVDlipkvfkgtvRELLEKVDERGKLDELAEKLGLEniLDRDI----SELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496428897 654 FDEATNALD----ANNEREIMEHLNEfyrGKTVVIVAHRLSTVQN-ADKIVVL 701
Cdd:COG1245 236 FDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAILDYlADYVHIL 285
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
509-710 |
1.23e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYtpnKGNIKVGDVYLKNINPH---LWRsvTGSVMQDGFIFSE-TI 584
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI---QGNNFTGTILANNRKPTkqiLKR--TGFVTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGY--NTKIGMEG-SGISQGQRQRILIARAVYKNPDFLFFDEATNAL 661
Cdd:PLN03211 158 RETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKceNTIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496428897 662 DANNEREIMEHLNEF-YRGKTVVIVAHRLST--VQNADKIVVLDKGGIVEEG 710
Cdd:PLN03211 238 DATAAYRLVLTLGSLaQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
494-715 |
2.07e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENL--CFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKT-TLIKLLLGFYTPN----KGNIKV-GDVYLKNINPHL 565
Cdd:PRK15134 7 AIENLsvAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFhGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 wRSVTGSVMqdGFIFSE---------TIAENIAigeEVIDKER-LLKAAQIANIDQFIDslplgyntKIGMEGSG----- 630
Cdd:PRK15134 87 -RGVRGNKI--AMIFQEpmvslnplhTLEKQLY---EVLSLHRgMRREAARGEILNCLD--------RVGIRQAAkrltd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 631 ----ISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTV-QNADKIVVLDK 703
Cdd:PRK15134 153 yphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQN 232
|
250
....*....|..
gi 496428897 704 GGIVEEGTHQEL 715
Cdd:PRK15134 233 GRCVEQNRAATL 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
497-715 |
2.38e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 497 NLCFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHL----------W 566
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVielseqsaaqM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVTGSVMqdGFIFSE---------TIAENIAIG----------EEVIDKERLLKAAQIANIDQFIDSLPlgyntkigme 627
Cdd:PRK10261 99 RHVRGADM--AMIFQEpmtslnpvfTVGEQIAESirlhqgasreEAMVEAKRMLDQVRIPEAQTILSRYP---------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 628 gSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLN----EFYRGktVVIVAHRLSTVQN-ADKIVVLD 702
Cdd:PRK10261 167 -HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMG--VIFITHDMGVVAEiADRVLVMY 243
|
250
....*....|...
gi 496428897 703 KGGIVEEGTHQEL 715
Cdd:PRK10261 244 QGEAVETGSVEQI 256
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
519-693 |
2.79e-11 |
|
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: 62.01 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 519 RNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVgdvylknINPHLWRSVTGSVMQdgfifsetiaeniaigeevidke 598
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLL----------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 599 rllkaaqianidqfidslplgyNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF-- 676
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRll 108
|
170 180
....*....|....*....|..
gi 496428897 677 -----YRGKTVVIVAHRLSTVQ 693
Cdd:smart00382 109 lllksEKNLTVILTTNDEKDLG 130
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
494-711 |
3.22e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.63 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGsPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDvylKNIN----------- 562
Cdd:PRK11650 5 KLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG---RVVNelepadrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 563 --------PHLwrsvtgsvmqdgfifseTIAENIAIG-------EEVIDkERLLKAAQIANIDQFIDSLPlgyntkigME 627
Cdd:PRK11650 81 vfqnyalyPHM-----------------SVRENMAYGlkirgmpKAEIE-ERVAEAARILELEPLLDRKP--------RE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 628 GSGisqGQRQRILIARAVYKNPDFLFFDEATNALDA---NNER-EIMehlnEFYR--GKTVVIVAH-RLSTVQNADKIVV 700
Cdd:PRK11650 135 LSG---GQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrVQMRlEIQ----RLHRrlKTTSLYVTHdQVEAMTLADRVVV 207
|
250
....*....|.
gi 496428897 701 LDKGGIVEEGT 711
Cdd:PRK11650 208 MNGGVAEQIGT 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
509-704 |
3.24e-11 |
|
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: 63.28 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETIAENI 588
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 589 AIGEEVIDKERLLKAAQIANIDQFIDsLPLGYntkigmegsgISQGQRQRILIARAVYKNPDFLFFDEATNALDANNERE 668
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNGFED-RPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 496428897 669 IMEHLNEFYRGKTVVIVAHRLSTVQNADKIVVLDKG 704
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
508-710 |
3.78e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.11 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 508 YVLNNVNLT-IPRNKItAIVGASGSGKTTLIKLLLGFYTPNKG------NIKVGdvYLKNiNPHL--WRSVTGSVM---- 574
Cdd:TIGR03719 19 EILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKDFNGearpqpGIKVG--YLPQ-EPQLdpTKTVRENVEegva 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 -----QDGF-----IFSETIAENIAIGEEVIDKERLLKAAQIANIDQFID------SLPLGyNTKIgmegSGISQGQRQR 638
Cdd:TIGR03719 95 eikdaLDRFneisaKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEiamdalRCPPW-DADV----TKLSGGERRR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 639 ILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEfYRGkTVVIVAHRLSTVQN-ADKIVVLDKG-GIVEEG 710
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTHDRYFLDNvAGWILELDRGrGIPWEG 241
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
510-710 |
4.06e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 62.34 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLikLLLGFYTPNKGNIKVgdvylkninphlwrsvtgsvmqdgfiFSETIAENIA 589
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLIS--------------------------FLPKFSRNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 590 IgeeVIDKERLLkaaqianIDQFIDSLPLGYNTkigmegSGISQGQRQRILIARAVYKNP-DFLF-FDEATNALDANNER 667
Cdd:cd03238 63 I---FIDQLQFL-------IDVGLGYLTLGQKL------STLSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496428897 668 EIMEHLNEFY-RGKTVVIVAHRLSTVQNADKIVVLDKGG------IVEEG 710
Cdd:cd03238 127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPGSgksggkVVFSG 176
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
181-312 |
4.15e-11 |
|
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: 64.43 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLVKLMR 260
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 496428897 261 LPLHFFDTKMIGDIMQRI-GDHSRIESFLTgSSISTLFSFVNFIVFGFVLAYY 312
Cdd:cd18576 82 LPLSFFHERRVGELTSRLsNDVTQIQDTLT-TTLAEFLRQILTLIGGVVLLFF 133
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
507-687 |
4.87e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 507 DYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVylKNINPHLWRSVTGSVMQDGFIFSETIAE 586
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG--DIDDPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 587 NIAIGEEVIDKERLLKAAQIANID-QFIDSLPLGYntkigmegsgISQGQRQRILIAR-AVYKNPDFLfFDEATNALDAN 664
Cdd:PRK13539 93 NLEFWAAFLGGEELDIAAALEAVGlAPLAHLPFGY----------LSAGQKRRVALARlLVSNRPIWI-LDEPTAALDAA 161
|
170 180
....*....|....*....|....*..
gi 496428897 665 NER----EIMEHLNefyRGKTVVIVAH 687
Cdd:PRK13539 162 AVAlfaeLIRAHLA---QGGIVIAATH 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
497-715 |
9.79e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.10 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 497 NLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNI----------KVGDVYLkninphlw 566
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldysKRGLLAL-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVTGSVMQD--GFIFSETIAENIA-------IGEEVIDKeRLLKAAQIANIDQFIDSlPLgyntkigmegSGISQGQRQ 637
Cdd:PRK13638 76 RQQVATVFQDpeQQIFYTDIDSDIAfslrnlgVPEAEITR-RVDEALTLVDAQHFRHQ-PI----------QCLSHGQKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 638 RILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEV 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
510-708 |
1.03e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYtpnkgnikvgdvylkninPHlwRSVTGSVMQDGFI--F-----SE 582
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY------------------PH--GSYEGEILFDGEVcrFkdirdSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 -----------------TIAENIAIGEE-----VIDKERLLKAAQianidQFIDSLPLGYN-----TKIGMegsgisqGQ 635
Cdd:NF040905 77 algiviihqelalipylSIAENIFLGNErakrgVIDWNETNRRAR-----ELLAKVGLDESpdtlvTDIGV-------GK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 636 RQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTV-QNADKIVVLDKGGIVE 708
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
181-466 |
1.04e-10 |
|
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: 63.18 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNF--ITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLVKL 258
Cdd:cd18544 5 LLLLLLATALELLGPLLIKRAIDDYIVPGQGDLqgLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 259 MRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWVLSFMKY 337
Cdd:cd18544 85 QRLPLSFFDRTPVGRLVTRVtNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 338 rreldLRRFSQASTEQ-----STLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLalqqyqQVGSVFFN---- 408
Cdd:cd18544 165 -----SRKAYREVREKlsrlnAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSI------KLFALFRPlvel 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 409 --QTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLER 466
Cdd:cd18544 234 lsSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAER 293
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
509-715 |
1.12e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDvylKNINPhlWRsvTGSVMQDGF--------IF 580
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG---KDITD--WQ--TAKIMREAVaivpegrrVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 581 SE-TIAENIAIGEEVIDKERLLKaaqiaNIDQFIDSLPLGYNTKIGMEGSgISQGQRQRILIARAVYKNPDFLFFDEATN 659
Cdd:PRK11614 93 SRmTVEENLAMGGFFAERDQFQE-----RIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 660 ALDANNEREIMEHLNEFY-RGKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLReQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
481-716 |
1.26e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.28 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 481 VDKVSFLPQDHTFTIENLCFSyDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKN 560
Cdd:COG3845 246 VEKAPAEPGEVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 561 INPH-LWRSVTGSV----MQDGFIFSETIAENIAIGEE---------VIDKERLLKAAQ---------IANIDQFIDSLp 617
Cdd:COG3845 325 LSPReRRRLGVAYIpedrLGRGLVPDMSVAENLILGRYrrppfsrggFLDRKAIRAFAEelieefdvrTPGPDTPARSL- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 618 lgyntkigmegSGisqGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTVQN-A 695
Cdd:COG3845 404 -----------SG---GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrDAGAAVLLISEDLDEILAlS 469
|
250 260
....*....|....*....|.
gi 496428897 696 DKIVVLDKGGIVEEGTHQELT 716
Cdd:COG3845 470 DRIAVMYEGRIVGEVPAAEAT 490
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
493-711 |
1.75e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGF--YTPNKGNIKVGDVYLKNINPHLwRSVT 570
Cdd:CHL00131 8 LEIKNLHASVNENE--ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE-RAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 571 GSVMqdGFIFSETIAeniaiGEEVIDKERL-LKAAQIANIDQFIDslPLGY----NTK---IGMEGS--------GISQG 634
Cdd:CHL00131 85 GIFL--AFQYPIEIP-----GVSNADFLRLaYNSKRKFQGLPELD--PLEFleiiNEKlklVGMDPSflsrnvneGFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 635 QRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAH--RLSTVQNADKIVVLDKGGIVEEGT 711
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
511-715 |
1.90e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.93 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 511 NNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWrSVTGSV--MQDGFIFSE-TIAEN 587
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVrtFQHVRLFREmTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 588 IAIGEEVIDKERLL---------KAAQIANIDQFIDSLplgynTKIGM------EGSGISQGQRQRILIARAVYKNPDFL 652
Cdd:PRK11300 101 LLVAQHQQLKTGLFsgllktpafRRAESEALDRAATWL-----ERVGLlehanrQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 653 FFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
510-710 |
2.03e-10 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 61.50 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTL-------------IKLLLGFYTPNKGNIKVGDV-YLKNINP----------HL 565
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMDKPDVdSIEGLSPaiaidqkttsRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 WRSVTGSVMqdgfifsetiaeniaigeEVIDKERLLKA-AQIANIDQFIDSLPLGYNTkIGMEGSGISQGQRQRILIARA 644
Cdd:cd03270 91 PRSTVGTVT------------------EIYDYLRLLFArVGIRERLGFLVDVGLGYLT-LSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 645 VYKNPDFLF--FDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQNADKIVVL-----DKGG-IVEEG 710
Cdd:cd03270 152 IGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVIDIgpgagVHGGeIVAQG 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
510-704 |
3.16e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYtpnkgnikvgdvylkninPHlwRSVTGSVMQDG------------ 577
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY------------------PH--GTYEGEIIFEGeelqasnirdte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 578 -----FIFSE-------TIAENIAIGEEVIDKERLLKAAQIANIDQFIDSLPLGYN--TKIGMEGSGisqgQRQRILIAR 643
Cdd:PRK13549 81 ragiaIIHQElalvkelSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGNLGLG----QQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 644 AVYKNPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTVQN-ADKIVVLDKG 704
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLkAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
477-705 |
5.13e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 477 EETAVDKVSFLPQD---HTFTIENLCFS--YDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTpnKGNI 551
Cdd:TIGR00956 741 ESDDVNDEKDMEKEsgeDIFHWRNLTYEvkIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVI 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 552 KVGDVyLKNINP---HLWRSvTGSVMQ-----------DGFIFSE--------TIAENIAIGEEVIDkerllkaaqIANI 609
Cdd:TIGR00956 819 TGGDR-LVNGRPldsSFQRS-IGYVQQqdlhlptstvrESLRFSAylrqpksvSKSEKMEYVEEVIK---------LLEM 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 610 DQFIDSLplgyntkIGMEGSGISQGQRQRILIARAVYKNPDFL-FFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAH 687
Cdd:TIGR00956 888 ESYADAV-------VGVPGEGLNVEQRKRLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIH 960
|
250 260
....*....|....*....|
gi 496428897 688 RLSTV--QNADKIVVLDKGG 705
Cdd:TIGR00956 961 QPSAIlfEEFDRLLLLQKGG 980
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
496-687 |
5.25e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 496 ENLCFSYDgspDYVL-NNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGD-VYLkninphlwrsvtGSV 573
Cdd:PRK11819 328 ENLSKSFG---DRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtVKL------------AYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQ--DGFIFSETIAENIAIGEEVIdkerllkaaQIANI----------------DQfidslplgyNTKIGMegsgISQGQ 635
Cdd:PRK11819 393 DQsrDALDPNKTVWEEISGGLDII---------KVGNReipsrayvgrfnfkggDQ---------QKKVGV----LSGGE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496428897 636 RQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFyrGKTVVIVAH 687
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF--PGCAVVISH 500
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
511-724 |
5.70e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.28 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 511 NNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNkGNIkvgdvylkninphlwrsvTGSVMQDGfifsetiAENIAI 590
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRI------------------GGSATFNG-------REILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 591 GEEVIDKerlLKAAQIANI---------------DQFIDSLPL--GYNTK---------------------IGMEGSGIS 632
Cdd:PRK09473 87 PEKELNK---LRAEQISMIfqdpmtslnpymrvgEQLMEVLMLhkGMSKAeafeesvrmldavkmpearkrMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 633 QGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEE 709
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 243
|
250
....*....|....*
gi 496428897 710 GTHQEltclkgIYYR 724
Cdd:PRK09473 244 GNARD------VFYQ 252
|
|
| Peptidase_C39E |
cd02424 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
9-127 |
1.05e-09 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family, which contains Colicin V perocessing peptidase.
Pssm-ID: 239104 [Multi-domain] Cd Length: 129 Bit Score: 56.96 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 9 QLDRMDCGPTCLRMIAK-YYGRVYSLQTLRDKAFISRSGVSLLGISEAAESIGFRTTGVKITFEQL--VDDFPLPCILHW 85
Cdd:cd02424 6 QTDLNDCGIAVIQMLYNhYYKKKYDLNELKIKANLKKNGLSIYDLENLAKKFGLETESYQGSFLEFleLKNKFIILLKSN 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 496428897 86 NQQHFVVCyrirKRRNKYKILIGDPA-GTQTVTYneEEFKRCW 127
Cdd:cd02424 86 GLNHFVIV----KKIKKNKFIVLDPKkGKYKITY--KEFEKIF 122
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
185-466 |
1.08e-09 |
|
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: 60.16 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 185 VIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLVKLMRLPLH 264
Cdd:cd18549 12 VLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 265 FFDTKMIGDIMQRI-GDHSRI--------ESFLTgSSISTLFSFVNFIVFGFVLAYYDLSIfglfllgnllyVIWVLSFM 335
Cdd:cd18549 92 FFDNNKTGQLMSRItNDLFDIselahhgpEDLFI-SIITIIGSFIILLTINVPLTLIVFAL-----------LPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 336 KYRReldlRRFSQASTEQ--------STLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFF 407
Cdd:cd18549 160 IYFN----KKMKKAFRRVrekigeinAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFF 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 408 NQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLER 466
Cdd:cd18549 236 TNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
493-715 |
1.20e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.53 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 493 FTIENLC--FSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYT-PNK---GNIKVGDVYLKNINPHLW 566
Cdd:PRK11022 4 LNVDKLSvhFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVTGS----VMQD-----------GFifseTIAENIAI---GEEVIDKER---LLKAAQIANIDQFIDSLPlgyntkig 625
Cdd:PRK11022 84 RNLVGAevamIFQDpmtslnpcytvGF----QIMEAIKVhqgGNKKTRRQRaidLLNQVGIPDPASRLDVYP-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 626 megSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYRGK--TVVIVAHRLSTV-QNADKIVVLD 702
Cdd:PRK11022 152 ---HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMY 228
|
250
....*....|...
gi 496428897 703 KGGIVEEGTHQEL 715
Cdd:PRK11022 229 AGQVVETGKAHDI 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
508-715 |
1.25e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 508 YVLNNVNLTIPRNKITAIVGASGSGKTT----LIKLLlgfytPNKGNIKVGDVYLKNINPHL---WRSVTGSVMQDGFif 580
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPN-- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 581 SE-----TIAENIAIGEEVidKERLLKAAQIAniDQFIDSLplgynTKIGMEG-------SGISQGQRQRILIARAVYKN 648
Cdd:PRK15134 373 SSlnprlNVLQIIEEGLRV--HQPTLSAAQRE--QQVIAVM-----EEVGLDPetrhrypAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 649 PDFLFFDEATNALDANNEREIME---HLNEFYRGKTVVIvAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILAllkSLQQKHQLAYLFI-SHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
494-715 |
1.45e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIEnlcFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFytpNKGNIKV-------GDVYLKNINPHLW 566
Cdd:PRK15093 10 TIE---FKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVtadrmrfDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 567 RSVTGSVMQdgFIFSE---TIAENIAIGEEVID------------------KER---LLKAAQIANIDQFIDSLPlgYNt 622
Cdd:PRK15093 84 RKLVGHNVS--MIFQEpqsCLDPSERVGRQLMQnipgwtykgrwwqrfgwrKRRaieLLHRVGIKDHKDAMRSFP--YE- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 623 kigmegsgISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTV-QNADKIV 699
Cdd:PRK15093 159 --------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKIN 230
|
250
....*....|....*.
gi 496428897 700 VLDKGGIVEEGTHQEL 715
Cdd:PRK15093 231 VLYCGQTVETAPSKEL 246
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
498-707 |
1.60e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 498 LCFSYdgSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKV-GDVYLKNINPHLWRSVTGSVmqd 576
Cdd:PRK11147 11 LSFSD--AP--LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLQQDPPRNVEGTV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 577 gFIFsetIAENIA-IGE------------EVIDKERLL-KAAQI-------------ANIDQFIDSLPLGYNTKIgmegS 629
Cdd:PRK11147 84 -YDF---VAEGIEeQAEylkryhdishlvETDPSEKNLnELAKLqeqldhhnlwqleNRINEVLAQLGLDPDAAL----S 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 630 GISQGQRQRILIARAVYKNPDFLFFDEATNALDAnnerEIMEHLNEF---YRGkTVVIVAHRLSTVQN-ADKIVVLDKGG 705
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFlktFQG-SIIFISHDRSFIRNmATRIVDLDRGK 230
|
..
gi 496428897 706 IV 707
Cdd:PRK11147 231 LV 232
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
180-310 |
1.64e-09 |
|
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: 59.80 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 180 LVLGMV---IGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLV 256
Cdd:cd18543 1 LILALLaalLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 257 KLMRLPLHFFDTKMIGDIMQR-IGDHSRIESFLTGSsistLFSFVNFIVFGFVLA 310
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRaTSDLSLVQRFLAFG----PFLLGNLLTLVVGLV 131
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
494-714 |
1.64e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKvgdvylkninphlWrsvtgsv 573
Cdd:PRK15064 321 EVENLTKGFDNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-------------W------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 mqdgfifsetiAENIAIG------EEVIDKERLL-----KAAQIANIDQFIDSLpLGY----NTKIGMEGSGISQGQRQR 638
Cdd:PRK15064 379 -----------SENANIGyyaqdhAYDFENDLTLfdwmsQWRQEGDDEQAVRGT-LGRllfsQDDIKKSVKVLSGGEKGR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 639 ILIARAVYKNPDFLFFDEATNALDAnnerEIMEHLN---EFYRGkTVVIVAHRLSTVQN-ADKIVVLDKGGIVE-EGTHQ 713
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDM----ESIESLNmalEKYEG-TLIFVSHDREFVSSlATRIIEITPDGVVDfSGTYE 521
|
.
gi 496428897 714 E 714
Cdd:PRK15064 522 E 522
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
509-692 |
1.73e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIK------VGDVYLK-NINPHLWRSVTGSVMQDGFIFS 581
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKrngklrIGYVPQKlYLDTTLPLTVNRFLRLRPGTKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 582 ETIAEniaigeevidkerLLKAAQIANIDQFidslPLgyntkigmegSGISQGQRQRILIARAVYKNPDFLFFDEATNAL 661
Cdd:PRK09544 99 EDILP-------------ALKRVQAGHLIDA----PM----------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190
....*....|....*....|....*....|...
gi 496428897 662 DANNEREIMEHLNEFYR--GKTVVIVAHRLSTV 692
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
515-690 |
1.90e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 515 LTIPR-NKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKvgdvylkniNPHLWRSVT----GSVMQDGF--IFSETIaeN 587
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD---------DPPDWDEILdefrGSELQNYFtkLLEGDV--K 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 588 IAIGEEVIDK----------ERLLKAAQIANIDQFIDSLPLgyNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEA 657
Cdd:cd03236 89 VIVKPQYVDLipkavkgkvgELLKKKDERGKLDELVDQLEL--RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496428897 658 TNALD-------ANNEREIMEHlnefyrGKTVVIVAHRLS 690
Cdd:cd03236 167 SSYLDikqrlnaARLIRELAED------DNYVLVVEHDLA 200
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
512-715 |
3.19e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.65 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 512 NVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLkNINPHLWRSvtgsvMQDGFIFSetiaeniaig 591
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRS-----QRIRMIFQ---------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 592 eeviDKERLLKAAQiaNIDQFIDsLPLGYNTKIGMEGSG-----------------------ISQGQRQRILIARAVYKN 648
Cdd:PRK15112 95 ----DPSTSLNPRQ--RISQILD-FPLRLNTDLEPEQREkqiietlrqvgllpdhasyyphmLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 649 PDFLFFDEATNALDANNEREI---MEHLNEFYrGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLinlMLELQEKQ-GISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADV 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
494-715 |
3.49e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 57.37 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 494 TIENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV 573
Cdd:TIGR01189 2 AARNLACSRGERM--LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 574 MQDGFIFSETIAENIAIGEEVIDKERL--LKAAQIANIDQFIDsLPLGYntkigmegsgISQGQRQRILIARAVYKNPDF 651
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIHGGAQRtiEDALAAVGLTGFED-LPAAQ----------LSAGQQRRLALARLWLSRRPL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 652 LFFDEATNALDANNEREIMEHLNefyrgktvvivAHrlstvqnadkivvLDKGGIVEEGTHQEL 715
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLR-----------AH-------------LARGGIVLLTTHQDL 188
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
522-707 |
4.58e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.24 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 522 ITAIVGASGSGKTTLIKLLLGFYTpnkGNIKVGDVYLKNI--NPHLWRSVTGSVMQDGfIFSE--TIAENIA------IG 591
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISGFpkKQETFARISGYCEQND-IHSPqvTVRESLIysaflrLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 592 EEVIDKERLLKAAQIANIDQfIDSLPlgyNTKIGMEG-SGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIM 670
Cdd:PLN03140 984 KEVSKEEKMMFVDEVMELVE-LDNLK---DAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496428897 671 EHL-NEFYRGKTVVIVAHRLS--TVQNADKIVVLDKGGIV 707
Cdd:PLN03140 1060 RTVrNTVDTGRTVVCTIHQPSidIFEAFDELLLMKRGGQV 1099
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
497-696 |
5.16e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 497 NLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIK-------------------VGdvY 557
Cdd:PRK13540 6 ELDFDYHDQP--LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqsikkdlctyqkqlcfVG--H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 558 LKNINPHLwrsvtgSVMQDGFIFSETIAENIAIGEEVidkerllkaaQIANIDQFIDsLPLGYntkigmegsgISQGQRQ 637
Cdd:PRK13540 82 RSGINPYL------TLRENCLYDIHFSPGAVGITELC----------RLFSLEHLID-YPCGL----------LSSGQKR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 638 RILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQNAD 696
Cdd:PRK13540 135 QVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
482-714 |
5.62e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 482 DKVSFLPQDHTFTIENLCfSYDGSPdyvLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFytpnkGNIKVGDVYL--K 559
Cdd:PRK09700 255 ENVSNLAHETVFEVRNVT-SRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-----DKRAGGEIRLngK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 560 NINPhlwRS-----------VTGSVMQDGFIFSETIAENIAIG--------------------EEVIDKERLLKAAQIAN 608
Cdd:PRK09700 326 DISP---RSpldavkkgmayITESRRDNGFFPNFSIAQNMAISrslkdggykgamglfhevdeQRTAENQRELLALKCHS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 609 IDQFIDSLplgyntkigmegsgiSQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREI---MEHLNEfyRGKTVVIV 685
Cdd:PRK09700 403 VNQNITEL---------------SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIykvMRQLAD--DGKVILMV 465
|
250 260 270
....*....|....*....|....*....|
gi 496428897 686 AHRLSTVQNA-DKIVVLDKGGIVEEGTHQE 714
Cdd:PRK09700 466 SSELPEIITVcDRIAVFCEGRLTQILTNRD 495
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
509-709 |
7.10e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.71 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPH----LWRSVTGSVMQDgFIFSETI 584
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarakLRAKHVGFVFQS-FMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 A--ENIAI-----GEevidKERLLKAAQIANIDQfidslpLGYNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEA 657
Cdd:PRK10584 104 NalENVELpallrGE----SSRQSRNGAKALLEQ------LGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496428897 658 TNALDANNEREIMEHLNEFYR--GKTVVIVAHRLSTVQNADKIVVLDKGGIVEE 709
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
510-711 |
7.31e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 57.24 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKgnikvgdVYLKNINPHLWRSVTGS--------VMQDGF--- 578
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARR-------LHLKKEQPGNHDRIEGLehidkvivIDQSPIgrt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 579 ----------IF-----------------SETIA-----ENIAigeEVID------KERLLKAAQIANIDQFIDSLPLGY 620
Cdd:cd03271 84 prsnpatytgVFdeirelfcevckgkrynRETLEvrykgKSIA---DVLDmtveeaLEFFENIPKIARKLQTLCDVGLGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 621 nTKIGMEGSGISQGQRQRILIARAVYK---NPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTVQNAD 696
Cdd:cd03271 161 -IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNLDVIKCAD 239
|
250 260
....*....|....*....|.
gi 496428897 697 KIVVL-----DKGG-IVEEGT 711
Cdd:cd03271 240 WIIDLgpeggDGGGqVVASGT 260
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
510-716 |
1.03e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPH--LwrsVTGSVM------QDGFIFS 581
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdgL---ANGIVYisedrkRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 582 ETIAENI---AIGEEVIDKERLLKAAQIANIDQFIDSlplgYNTK-------IGMegsgISQGQRQRILIARAVYKNPDF 651
Cdd:PRK10762 345 MSVKENMsltALRYFSRAGGSLKHADEQQAVSDFIRL----FNIKtpsmeqaIGL----LSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 652 LFFDEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQELT 716
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRISGEFTREQAT 483
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
181-467 |
1.34e-08 |
|
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: 57.14 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVD---------------VGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIR 245
Cdd:cd18564 5 LLALLLETALRLLEPWPLKVVIDdvlgdkplpgllglaPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 246 INISLISDFLVKLMRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYD--LSIFGLFLL 322
Cdd:cd18564 85 VVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLtGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDwqLALIALAVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 323 GNLLYVIWVLSfmkyrreldlRRFSQASTEQ--------STLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGL 394
Cdd:cd18564 165 PLLLLAARRFS----------RRIKEASREQrrregalaSVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 395 ALQqyqqvgsVFFNQTTNILIS-------YIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18564 235 RLQ-------ALLSPVVDVLVAvgtalvlWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
177-467 |
1.58e-08 |
|
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: 56.73 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 177 LVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSW--------LLLHMNIRIni 248
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRltgrtgerLLYDLRLRV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 249 slisdFlVKLMRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLly 327
Cdd:cd18546 79 -----F-AHLQRLSLDFHERETSGRIMTRMtSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALP-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 328 VIWVLSfMKYRRELDlRRFSQASTEQS----TLYQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVG 403
Cdd:cd18546 151 PLALAT-RWFRRRSS-RAYRRARERIAavnaDLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 404 SVFFNQTTNILISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18546 229 VELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
510-716 |
1.83e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIkvgdVYLKninphlwRSVTGSVMQD------GFIFSE- 582
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI----LYLG-------KEVTFNGPKSsqeagiGIIHQEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 583 ------TIAENIAIGEEV------IDKERLLKAAqianiDQFIDSLPLGYNTKIGMegSGISQGQRQRILIARAVYKNPD 650
Cdd:PRK10762 89 nlipqlTIAENIFLGREFvnrfgrIDWKKMYAEA-----DKLLARLNLRFSSDKLV--GELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 651 FLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTV-QNADKIVVLDKGGIVEEGTHQELT 716
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELkSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADLT 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
490-716 |
4.05e-08 |
|
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: 56.37 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 490 DHTFTIENL-CFSYDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYtPNKGNikvGDVYLK----NINPH 564
Cdd:TIGR02633 255 DVILEARNLtCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKFE---GNVFINgkpvDIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 565 LWRSVTGSVM------QDGFIFSETIAENIAIG--EEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIgMEGSGISQGQR 636
Cdd:TIGR02633 331 AQAIRAGIAMvpedrkRHGIVPILGVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF-LPIGRLSGGNQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 637 QRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEF-YRGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQE 714
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHA 489
|
..
gi 496428897 715 LT 716
Cdd:TIGR02633 490 LT 491
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
509-710 |
4.06e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLT-IPRNKItAIVGASGSGKTTLIKLLLGFYTPNKG------NIKVGdvYLKNiNPHL--WRSVTGSVM----- 574
Cdd:PRK11819 22 ILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGearpapGIKVG--YLPQ-EPQLdpEKTVRENVEegvae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 575 ----QDGF-----IFSETIAENIAIGEEVIDKERLLKAAQIANIDQFID------SLPLGyNTKIgmegSGISQGQRQRI 639
Cdd:PRK11819 98 vkaaLDRFneiyaAYAEPDADFDALAAEQGELQEIIDAADAWDLDSQLEiamdalRCPPW-DAKV----TKLSGGERRRV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 640 LIARAVYKNPDFLFFDEATNALDANN----EReimeHLNEfYRGkTVVIVAH-R--LSTVqnADKIVVLDKG-GIVEEG 710
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAESvawlEQ----FLHD-YPG-TVVAVTHdRyfLDNV--AGWILELDRGrGIPWEG 243
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
508-707 |
4.07e-08 |
|
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: 54.19 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 508 YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLL---LGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETI 584
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AEniaigeevidkerLLKAAQIANIDQFIdslplgyntkigmegSGISQGQRQRILIARAVYKNPDFLFFDEATNALDAN 664
Cdd:cd03233 101 RE-------------TLDFALRCKGNEFV---------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496428897 665 NEREI---MEHLNEFYRGKTVVIV-AHRLSTVQNADKIVVLDKGGIV 707
Cdd:cd03233 153 TALEIlkcIRTMADVLKTTTFVSLyQASDEIYDLFDKVLVLYEGRQI 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
509-714 |
6.13e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLL----GFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMQDGFIFSETI 584
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AENI-------AIGEEVIDKERLLKAAQIANIDQFIDSLPLGYNTKIGMEG-SGISQGQRQRILIARAVYKNPDFLFFDE 656
Cdd:TIGR00956 156 GETLdfaarckTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFvRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 657 ATNALDANNEREIMEHLNEFYR-GKTVVIVAhRLSTVQNA----DKIVVLDKGGIVEEGTHQE 714
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANiLDTTPLVA-IYQCSQDAyelfDKVIVLYEGYQIYFGPADK 297
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
524-710 |
7.05e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 524 AIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSVMqdgFIFSETIAE---NIAIGEEVIDKER- 599
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQ---FIFQDPYASldpRQTVGDSIMEPLRv 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 600 --LLK----AAQIANIDQFIDSLPlGYNTKIGMEGSGisqGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHL 673
Cdd:PRK10261 431 hgLLPgkaaAARVAWLLERVGLLP-EHAWRYPHEFSG---GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496428897 674 NEFYR--GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG 710
Cdd:PRK10261 507 LDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
180-467 |
9.84e-08 |
|
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: 54.35 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 180 LVLGMVIGSIlQLIVPFLTQSLVDVGIRDNNL-------NFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLIS 252
Cdd:cd18554 5 IVIGLVRFGI-PLLLPLILKYIVDDVIQGSSLtldekvyKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 253 DFLVKLMRLPLHFFDTKMIGDIMQR-IGDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYDLSIFGLFLLGNLLYVIWV 331
Cdd:cd18554 84 DLFDHLQKLSLRYYANNRSGEIISRvINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 332 LSFMKYRRELDLRRFSQASTEQSTLYQIITGMQEIKLNNCETQKRWKWERiqvKLFKISVKGLALQQYQQVGSVFFNQTT 411
Cdd:cd18554 164 KYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDK---RNGHFLTRALKHTRWNAKTFSAVNTIT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 412 NI---LISYIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18554 241 DLaplLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
495-704 |
1.25e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 495 IENLCFSYDGSPdyVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNI--KVGDVYLKNINPHLWRSVTGS 572
Cdd:PRK10982 1 MSNISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfQGKEIDFKSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 573 VMQDGFIFSETIAENIAIGEE-----VIDKERLLKAAQIANIDQFIDSLPlgyNTKIGMegsgISQGQRQRILIARAVYK 647
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYptkgmFVDQDKMYRDTKAIFDELDIDIDP---RAKVAT----LSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 648 NPDFLFFDEATNAL---DANNEREIMEHLNEfyRGKTVVIVAHRLSTV-QNADKIVVLDKG 704
Cdd:PRK10982 152 NAKIVIMDEPTSSLtekEVNHLFTIIRKLKE--RGCGIVYISHKMEEIfQLCDEITILRDG 210
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
181-467 |
2.39e-07 |
|
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: 53.18 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDvGIRDNNLNFITLILVAQLIIFIARLS--VDFIRSWLLLHMNIRINISLISDFLVKL 258
Cdd:cd18541 5 ILFLILVDLLQLLIPRIIGRAID-ALTAGTLTASQLLRYALLILLLALLIgiFRFLWRYLIFGASRRIEYDLRNDLFAHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 259 MRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTG---SSISTLFSFVNFIVFGFV----LAYYDLSIfglfllgnllYVIW 330
Cdd:cd18541 84 LTLSPSFYQKNRTGDLMARAtNDLNAVRMALGPgilYLVDALFLGVLVLVMMFTispkLTLIALLP----------LPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 331 VLSFMKYRRELDlRRFSQASTEQSTLY----QIITGMQEIKLNNCETQKRWKWERIQVKLFKisvKGLALQQYQqvgsVF 406
Cdd:cd18541 154 ALLVYRLGKKIH-KRFRKVQEAFSDLSdrvqESFSGIRVIKAFVQEEAEIERFDKLNEEYVE---KNLRLARVD----AL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 407 FNQTTNILIS-------YIAARAVVEGNMTLGMMMSLTYIIGQLNSPIEQfIGFARS-FQDAKISLERL 467
Cdd:cd18541 226 FFPLIGLLIGlsflivlWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMA-LGWVINlIQRGAASLKRI 293
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
509-711 |
3.23e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.52 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYT----PN----KGNIKVGDVYLKNINPH---LWRSVTGSVMQDG 577
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaPRgarvTGDVTLNGEPLAAIDAPrlaRLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 578 FIFSetIAENIAIGEevidKERLLKAAQIANIDQFIDSLPL---GYNTKIGMEGSGISQGQRQRILIARAVYK------- 647
Cdd:PRK13547 96 FAFS--AREIVLLGR----YPHARRAGALTHRDGEIAWQALalaGATALVGRDVTTLSGGELARVQFARVLAQlwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 648 --NPDFLFFDEATNALDANNEREIMEHLNEFYR--GKTVVIVAHRLS-TVQNADKIVVLDKGGIVEEGT 711
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
488-722 |
3.59e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 488 PQDHTFTIENLCFSYDGSpdyvLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHlwr 567
Cdd:PRK10982 246 PGEVILEVRNLTSLRQPS----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAN--- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 568 svtgSVMQDGFIF------SETIAENIAIG--------EEVIDKERLLKAAQIANIDQF-IDSLPL---GYNTKIGmegs 629
Cdd:PRK10982 319 ----EAINHGFALvteerrSTGIYAYLDIGfnslisniRNYKNKVGLLDNSRMKSDTQWvIDSMRVktpGHRTQIG---- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 630 GISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKG--- 704
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTDRILVMSNGlva 470
|
250 260
....*....|....*....|
gi 496428897 705 GIVE--EGTHQELTCLKGIY 722
Cdd:PRK10982 471 GIVDtkTTTQNEILRLASLH 490
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
508-710 |
3.97e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 508 YVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNI-KVGDVYLKNINPHLWRSVTGsvmqdgfifsetiAE 586
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAISAGLSGQLTG-------------IE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 587 NIAIG--------EEVidKERLLKAAQIANIDQFIDSLPLGYntkigmegsgiSQGQRQRILIARAVYKNPDFLFFDEAT 658
Cdd:PRK13546 105 NIEFKmlcmgfkrKEI--KAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496428897 659 NALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEG 710
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYG 225
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
526-687 |
4.08e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 526 VGASGSGKTTLIKLLLGFYTPNKGNIkvgdvylkNINPHLwrsVTGSVMQDGFIFSE-TIAENIAIGEE---VIDKER-- 599
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNV--------SLDPNE---RLGKLRQDQFAFEEfTVLDTVIMGHTelwEVKQERdr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 600 -----------LLKAA----QIANIDqfidslplGYNTK-----------IGMEG-----SGISQGQRQRILIARAVYKN 648
Cdd:PRK15064 102 iyalpemseedGMKVAdlevKFAEMD--------GYTAEaragelllgvgIPEEQhyglmSEVAPGWKLRVLLAQALFSN 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 496428897 649 PDFLFFDEATNALDANNEREIMEHLNEfyRGKTVVIVAH 687
Cdd:PRK15064 174 PDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
180-467 |
4.93e-07 |
|
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: 52.10 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 180 LVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAqLIIFIARLSVDFIRS---WLLLHMNIRINISLISdfLV 256
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLA-LALFLVSLLQSLLLHqyfFLSFRLGMRVRSALSS--LI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 257 --KLMRLPLHFFDTKMIGDIMQRIG-DHSRIESFLTgsSISTLFSFVNFIVFGFVLAYYDLSIfglfllgnllYVIWVLS 333
Cdd:cd18579 79 yrKALRLSSSARQETSTGEIVNLMSvDVQRIEDFFL--FLHYLWSAPLQIIVALYLLYRLLGW----------AALAGLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FM---------------KYRREL----DLRrfSQASTEqstlyqIITGMQEIKLNNcetqkrwkWERIQVKlfKIS---- 390
Cdd:cd18579 147 VLllliplqaflaklisKLRKKLmkatDER--VKLTNE------ILSGIKVIKLYA--------WEKPFLK--RIEelrk 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 391 --VKGLALQQYQQVGSVFFNQTTNILISYI--AARAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLER 466
Cdd:cd18579 209 keLKALRKFGYLRALNSFLFFSTPVLVSLAtfATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKR 288
|
.
gi 496428897 467 L 467
Cdd:cd18579 289 I 289
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
513-716 |
5.07e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 513 VNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKVGDVYLKNINPHlwRSVTGSVM-------QDGFIFSETIA 585
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPR--DAIRAGIMlcpedrkAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 586 ENIAI--------GEEVIDKERllkaaQIANIDQFIDSLPL---GYNTKIGMegsgISQGQRQRILIARAVYKNPDFLFF 654
Cdd:PRK11288 350 DNINIsarrhhlrAGCLINNRW-----EAENADRFIRSLNIktpSREQLIMN----LSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496428897 655 DEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQELT 716
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQAT 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
509-716 |
5.84e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYtPNKgniKVGDVYLKN----INPHLWRSVTGSVM------QDGF 578
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGR---WEGEIFIDGkpvkIRNPQQAIAQGIAMvpedrkRDGI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 579 IFSETIAENIAIGeeVIDK----ERLLKAAQIANIDQFIDSLPLGYNT---KIGmegsGISQGQRQRILIARAVYKNPDF 651
Cdd:PRK13549 353 VPVMGVGKNITLA--ALDRftggSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 652 LFFDEATNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQELT 716
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVqQGVAIIVISSELPEVLGlSDRVLVMHEGKLKGDLINHNLT 493
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
514-715 |
6.86e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 514 NLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIK-----------------VGDVYLKNINPHLwrsvtgSVMQD 576
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqfshitrlsfeqlqklVSDEWQRNNTDML------SPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 577 GFifSETIAEniAIGEEVIDKERLLKAAQIANIDQFIDSlPLGYntkigmegsgISQGQRQRILIARAVYKNPDFLFFDE 656
Cdd:PRK10938 97 DT--GRTTAE--IIQDEVKDPARCEQLAQQFGITALLDR-RFKY----------LSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 657 ATNALDANNEREIMEHLNEFYRGK-TVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQSGiTLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
174-466 |
1.09e-06 |
|
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: 50.94 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 174 KKALVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISD 253
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRI-GDHSRIESFLTGSSISTLFSFVNFIVFGFVLAYYD-------LSIFGlfllgnl 325
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVtSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNwklalivLAVVP------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 326 lyVIWVLSfMKYRRELdLRRFSQASTEQStlyQI-------ITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQq 398
Cdd:cd18540 154 --VLAVVS-IYFQKKI-LKAYRKVRKINS---RItgafnegITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLS- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 399 yqqvgSVFFnqTTNILISYIAA--------RAVVEGNMTLGMMMSLTYIIGQLNSPIEQFIGFARSFQDAKISLER 466
Cdd:cd18540 226 -----ALFL--PIVLFLGSIATalvlwyggILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
181-467 |
2.45e-06 |
|
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: 49.80 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVD-VGIRDNNLNFITLILVAQ--LIIFIARLSVDfIRSWLLLHMNIRINISLISDFLVK 257
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDaLSAPASALLAVPLLLLLAygLARILSSLFNE-LRDALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 258 LMRLPLHFFDTKMIGDImQRIGDHSriesfltGSSISTLFSFVNF----------IVFGFVLAYYDLSIFGLFLLGNLLY 327
Cdd:cd18582 81 LHSLSLRFHLSRKTGAL-SRAIERG-------TRGIEFLLRFLLFnilptilellLVCGILWYLYGWSYALITLVTVALY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 328 VIWVLSFMKYRRELdLRRFSQASTEQSTLyqIITGmqeikLNNCETqkrwkweriqVKLF---KISVKGL--ALQQYQ-- 400
Cdd:cd18582 153 VAFTIKVTEWRTKF-RREMNEADNEANAK--AVDS-----LLNYET----------VKYFnneEYEAERYdkALAKYEka 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 401 ----QVGSVFFNQTTNILIS-------YIAARAVVEGNMTLG--MMMSlTYIIgQLNSPIeQFIGFA-RSFQDAKISLER 466
Cdd:cd18582 215 avksQTSLALLNIGQALIISlgltaimLLAAQGVVAGTLTVGdfVLVN-TYLL-QLYQPL-NFLGFVyREIRQSLIDMEK 291
|
.
gi 496428897 467 L 467
Cdd:cd18582 292 L 292
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
510-715 |
2.45e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.17 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLI----------KLLLGFYTPNKGNIKVGDVYLKNI--------------NPHL 565
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIndtlypalanRLNGAKTVPGRYTSIEGLEHLDKVihidqspigrtprsNPAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 566 WRSVTGSVMQ--------------------------------DGFI-----F-----------------SETIA-----E 586
Cdd:TIGR00630 704 YTGVFDEIRElfaetpeakvrgytpgrfsfnvkggrceacqgDGVIkiemhFlpdvyvpcevckgkrynRETLEvkykgK 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 587 NIAigeEVID------KERLLKAAQIANIDQFIDSLPLGYnTKIGMEGSGISQGQRQRILIARAVYK---NPDFLFFDEA 657
Cdd:TIGR00630 784 NIA---DVLDmtveeaYEFFEAVPSISRKLQTLCDVGLGY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEP 859
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496428897 658 TNALDANNEREIMEHLNEFY-RGKTVVIVAHRLSTVQNADKIVVL-----DKGG-IVEEGTHQEL 715
Cdd:TIGR00630 860 TTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLDVIKTADYIIDLgpeggDGGGtVVASGTPEEV 924
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
184-467 |
5.16e-06 |
|
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: 49.06 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 184 MVIGSILQLIVPFLTQSLVDVGIRDNnlnfiTLILVAQLIIFIA-RL-----SVDFIRSWLLLH--MNIRINISLIsdFL 255
Cdd:cd18583 5 LLAERVLNVLVPRQLGIIVDSLSGGS-----GKSPWKEIGLYVLlRFlqsggGLGLLRSWLWIPveQYSYRALSTA--AF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 256 VKLMRLPLHFFDTKMIGDIMQRIGDhsriesfltGSSISTLFSFVNF----------IVFGFVLAYYDLSIFGLFLLGNL 325
Cdd:cd18583 78 NHVMNLSMDFHDSKKSGEVLKAIEQ---------GSSINDLLEQILFqivpmiidlvIAIVYLYYLFDPYMGLIVAVVMV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 326 LYVIWVLSFMKYRRELDlRRFSQASTEQ-STLYQIITGMQEIKLNNcetqkrwkweRIQvklFKISVKGLALQQYQQVgS 404
Cdd:cd18583 149 LYVWSTIKLTSWRTKLR-RDMIDADREErSILTESLLNWETVKYFN----------REP---YEKERYREAVKNYQKA-E 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496428897 405 VFFNQTTNIL--------------ISYIAARAVVEGNMTLGM-MMSLTYIiGQLNSPIEQFIGFARSFQDAKISLERL 467
Cdd:cd18583 214 RKYLFSLNLLnavqsliltlgllaGCFLAAYQVSQGQATVGDfVTLLTYW-AQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
180-311 |
5.93e-06 |
|
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: 48.65 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 180 LVLGMVIGSILQLIVPFL----TQSLVDVGIRDNNLNFI--TLILVAQLIIFIarlsvdFIRSWLLLHMNIRINISLISD 253
Cdd:cd18580 4 LLLLLLLLAFLSQFSNIWldwwSSDWSSSPNSSSGYYLGvyAALLVLASVLLV------LLRWLLFVLAGLRASRRLHDK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 254 FLVKLMRLPLHFFDTKMIGDIMQRIG-DHSRIESFLTGSSISTLFSFVNFIVFGFVLAY 311
Cdd:cd18580 78 LLRSVLRAPMSFFDTTPSGRILNRFSkDIGLIDEELPLALLDFLQSLFSVLGSLIVIAI 136
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
177-312 |
8.24e-06 |
|
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: 48.24 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 177 LVQLVLGMVIGSILQLIVPFLTQSLVDVGIRDNnLNFITLILVaqlIIFIARLSVDFIRSWLLLHMNIRINISLISDFLV 256
Cdd:cd18577 13 AALPLMTIVFGDLFDAFTDFGSGESSPDEFLDD-VNKYALYFV---YLGIGSFVLSYIQTACWTITGERQARRIRKRYLK 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 496428897 257 KLMRLPLHFFDTKMIGDIMQRIGDHSR-IESFlTGSSISTLFSFVNFIVFGFVLAYY 312
Cdd:cd18577 89 ALLRQDIAWFDKNGAGELTSRLTSDTNlIQDG-IGEKLGLLIQSLSTFIAGFIIAFI 144
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
509-702 |
9.17e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 509 VLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIkvgdvYLKNIN----PHLWRSVTGSvmQDGFIFSETI 584
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI-----YYKNCNinniAKPYCTYIGH--NLGLKLEMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AENIAIGEEVIDKERLLKAA-QIANIDQFIDSlplgyntkigmEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDA 663
Cdd:PRK13541 88 FENLKFWSEIYNSAETLYAAiHYFKLHDLLDE-----------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496428897 664 NNeREIMEHLNEFY--RGKTVVIVAHRLSTVQNAdKIVVLD 702
Cdd:PRK13541 157 EN-RDLLNNLIVMKanSGGIVLLSSHLESSIKSA-QILQLD 195
|
|
| Peptidase_C39A |
cd02549 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
15-127 |
9.28e-06 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.
Pssm-ID: 239109 [Multi-domain] Cd Length: 141 Bit Score: 45.86 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 15 CGPTCLRMIAKYYGRVYSLQTLRDKAFI-----SRSGVSLLGISE-AAESIGFR---TTGVKITFEQLVDDFPL-----P 80
Cdd:cd02549 7 CGPTSLAMVLSYLGVKVTKPQLAAEGNTydfakDGYGTYPKPIVSaAARKYGLVvrpLTGLLALLRQLAAGHPVivsvnL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 496428897 81 CILHWNQQHFVVCYRIRKRRNkykILIGDPAGTQTVTYNEEEFKRCW 127
Cdd:cd02549 87 GVSITPSGHAMVVIGYDRKGN---VYVNDPGGGRRLVVSFDEFEKAW 130
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
181-440 |
1.51e-05 |
|
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: 47.39 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDVGIRDNNLNFIT-----LILVA--QLI------IFIARLSVDFIRswlllhmNIRin 247
Cdd:cd18548 5 PLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILrtgllMLLLAllGLIagilagYFAAKASQGFGR-------DLR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 248 isliSDFLVKLMRLPLHFFD--------TKMIGDIMQrigdhsrIESFLTGSSISTLFSFVNFIvFGFVLAYY---DLSI 316
Cdd:cd18548 76 ----KDLFEKIQSFSFAEIDkfgtssliTRLTNDVTQ-------VQNFVMMLLRMLVRAPIMLI-GAIIMAFRinpKLAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 317 FGLFLLGNLLYVIWVLS------FMKYRRELDlrRFSQASTEQstlyqiITGMQEIKLNNCETQKRWKWERIQVKLFKIS 390
Cdd:cd18548 144 ILLVAIPILALVVFLIMkkaiplFKKVQKKLD--RLNRVVREN------LTGIRVIRAFNREDYEEERFDKANDDLTDTS 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 496428897 391 VKGLALQQYQQVGSVFFNQTTNILISYIAARAVVEGNMTLGMMMSL-TYII 440
Cdd:cd18548 216 LKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFiNYLM 266
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
516-702 |
3.20e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 516 TIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKvGDV-------YLKNINP----HLWRSVTGSVMQDGFIFSEtI 584
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLkisykpqYISPDYDgtveEFLRSANTDDFGSSYYKTE-I 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 585 AENIAIgeevidkERLLkaaqianiDQFIDSLplgyntkigmegSGisqGQRQRILIARAVYKNPDFLFFDEATNALDAN 664
Cdd:COG1245 440 IKPLGL-------EKLL--------DKNVKDL------------SG---GELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496428897 665 NE-------REIMEHlnefyRGKTVVIVAHRLsTVQN--ADKIVVLD 702
Cdd:COG1245 490 QRlavakaiRRFAEN-----RGKTAMVVDHDI-YLIDyiSDRLMVFE 530
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
607-715 |
3.25e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 607 ANIDQFIDSLPLgyNTKIGMEGSGISQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFYR-GKTVVIV 685
Cdd:NF000106 123 ARADELLERFSL--TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLT 200
|
90 100 110
....*....|....*....|....*....|.
gi 496428897 686 AHRLSTV-QNADKIVVLDKGGIVEEGTHQEL 715
Cdd:NF000106 201 TQYMEEAeQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
185-431 |
3.34e-05 |
|
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: 46.32 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 185 VIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAqLIIFIARLSV-DFIRSWLLLHMNIRINISLISDFLVKLMRLPL 263
Cdd:cd18575 6 LIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLL-LLAVALVLALaSALRFYLVSWLGERVVADLRKAVFAHLLRLSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 264 HFFDTKMIGDIMQRI-GDHSRIESFLtGSSISTLFSfvNFIVF--GFVLAYY---DLSIFGLFLLGNLLYVIWVLSfmky 337
Cdd:cd18575 85 SFFETTRTGEVLSRLtTDTTLIQTVV-GSSLSIALR--NLLLLigGLVMLFItspKLTLLVLLVIPLVVLPIILFG---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 338 RReldLRRFSQASteQSTLYQI-------ITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVFFNQT 410
Cdd:cd18575 158 RR---VRRLSRAS--QDRLADLsafaeetLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFG 232
|
250 260
....*....|....*....|.
gi 496428897 411 TNILISYIAARAVVEGNMTLG 431
Cdd:cd18575 233 AIVFVLWLGAHDVLAGRMSAG 253
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
510-536 |
5.36e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 5.36e-05
10 20
....*....|....*....|....*..
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTL 536
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
510-704 |
7.08e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLikLLLGFYTPNKGNIKVGDVYLKN----------------------INPHLwR 567
Cdd:PRK00635 1506 IQNLNVSAPLHSLVAISGVSGSGKTSL--LLEGFYKQACALIEKGPSVFSEiifldshpqissqrsdistyfdIAPSL-R 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 568 SVTGSVMQ------DGFIFSETIAEN-----IAIGEEVIDKE--------------------------------RLLKAA 604
Cdd:PRK00635 1583 NFYASLTQakalniSASMFSTNTKQGqcsdcWGLGYQWIDRAfyalekrpcptcsgfriqplaqevvyegkhfgQLLQTP 1662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 605 --QIANIDQFIDSLP----------LGYnTKIGMEGSGISQGQRQRILIARAVY---KNPDFLFFDEATNALDANNEREI 669
Cdd:PRK00635 1663 ieEVAETFPFLKKIQkplqalidngLGY-LPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSAL 1741
|
250 260 270
....*....|....*....|....*....|....*.
gi 496428897 670 MEHLNEFY-RGKTVVIVAHRLSTVQNADKIVVLDKG 704
Cdd:PRK00635 1742 LVQLRTLVsLGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
510-536 |
7.95e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.22 E-value: 7.95e-05
10 20
....*....|....*....|....*..
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTL 536
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
184-455 |
9.35e-05 |
|
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: 44.84 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 184 MVIGSILQLIVPFLTQSLVDVGIRDNNLNFITLILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFLVKLMRLPL 263
Cdd:cd18572 5 LVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 264 HFFDTKMIGDIMQRIG-DHSRIesfltGSSISTLFSFV--NFIVFGFVLAY-----YDLSIFGLFLLGnllyVIWVLS-- 333
Cdd:cd18572 85 AFFDATKTGELTSRLTsDCQKV-----SDPLSTNLNVFlrNLVQLVGGLAFmfslsWRLTLLAFITVP----VIALITkv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 334 FMKYRRELdlrrfsqASTEQSTL-------YQIITGMQEIKLNNCETQKRWKWERIQVKLFKISVKGLALQQYQQVGSVF 406
Cdd:cd18572 156 YGRYYRKL-------SKEIQDALaeanqvaEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 407 FNQTTNILISYIAARAVVEGNMTLG----------MMMSLTYIIGQLNSPIEQFIGFAR 455
Cdd:cd18572 229 LQNGTQVLVLFYGGHLVLSGRMSAGqlvtfmlyqqQLGEAFQSLGDVFSSLMQAVGAAE 287
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
507-690 |
1.09e-04 |
|
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: 45.51 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 507 DYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGF--------YTPNKGNIkvgdVYLKNiNPHLwrsvTGSVMQDGF 578
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKL----FYVPQ-RPYM----TLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 579 IFSETIAENIAIGeeVIDKErllkaaqianIDQFIDSLPLGYNTKIGMEGSGI-------SQGQRQRILIARAVYKNPDF 651
Cdd:TIGR00954 536 IYPDSSEDMKRRG--LSDKD----------LEQILDNVQLTHILEREGGWSAVqdwmdvlSGGEKQRIAMARLFYHKPQF 603
|
170 180 190
....*....|....*....|....*....|....*....
gi 496428897 652 LFFDEATNALDANNEREIMEHLNEFyrGKTVVIVAHRLS 690
Cdd:TIGR00954 604 AILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
514-711 |
1.41e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.61 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 514 NLTIP-RNKITAIVGASGSGKTTLIKLLLGFYTPNKGN-IKVGDVYLKNINPHLWRSVT---GSVMQD--GFIFSETIAE 586
Cdd:COG3593 16 DLSIElSDDLTVLVGENNSGKSSILEALRLLLGPSSSRkFDEEDFYLGDDPDLPEIEIEltfGSLLSRllRLLLKEEDKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 587 NIAIGEEVIDKE--RLLKAAQ---------------------IANIDQFIDSLPLGYNTKIGMEGSGISQGQRQRILIAR 643
Cdd:COG3593 96 ELEEALEELNEElkEALKALNellseylkelldgldlelelsLDELEDLLKSLSLRIEDGKELPLDRLGSGFQRLILLAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496428897 644 AVY-------KNPDFLFFDEATNALDANNEREIMEHLNEFYRGKTVVIVA----HRLSTVqNADKIVVLDKGGIVEEGT 711
Cdd:COG3593 176 LSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITthspHLLSEV-PLENIRRLRRDSGGTTST 253
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
515-699 |
2.07e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 515 LTIPRNKITAIVGASGSGKTTLIKlllgfytpnkgnikvgdvylkninphlwrsvtgsvmQDGFIFsetIAENIAIGEEV 594
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILD------------------------------------AIGLAL---GGAQSATRRRS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 595 IDKERLLKAAQIANIDQFIDslplgyntkigmegsGISQGQRQRI----LIARAVYKNPDFLFFDEATNALDANNEREIM 670
Cdd:cd03227 57 GVKAGCIVAAVSAELIFTRL---------------QLSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|
gi 496428897 671 EHLNEFYRGKTVVIVA-HRLSTVQNADKIV 699
Cdd:cd03227 122 EAILEHLVKGAQVIVItHLPELAELADKLI 151
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
517-702 |
2.08e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 517 IPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKvgdvylkninphlWRSVTGSVMQdgfifsetiaeniaigeevid 596
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-------------WDGITPVYKP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 597 kerllkaaqianidQFIDslplgyntkigmegsgISQGQRQRILIARAVYKNPDFLFFDEATNALDAN---NEREIMEHL 673
Cdd:cd03222 68 --------------QYID----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|
gi 496428897 674 NEfYRGKTVVIVAHRLSTVQN-ADKIVVLD 702
Cdd:cd03222 118 SE-EGKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
510-538 |
2.73e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 2.73e-04
10 20
....*....|....*....|....*....
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLIK 538
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
510-537 |
3.39e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 3.39e-04
10 20
....*....|....*....|....*...
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTLI 537
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
502-715 |
8.17e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.08 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 502 YDGSPDYVLNNVNLTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNKGNIKV-GDVYLKNINphlwrsvtgSVMQD-GFI 579
Cdd:TIGR01257 1947 YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNIS---------DVHQNmGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 580 FSETIAENIAIGEE---VIDKERLLKAAQIANIDQF-IDSLPLG-YNTKIGMEGSGisqGQRQRILIARAVYKNPDFLFF 654
Cdd:TIGR01257 2018 PQFDAIDDLLTGREhlyLYARLRGVPAEEIEKVANWsIQSLGLSlYADRLAGTYSG---GNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 655 DEATNALDANNEREIMEHLNEFYR-GKTVVIVAHRLSTVQN-ADKIVVLDKGGIVEEGTHQEL 715
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
632-687 |
1.21e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 496428897 632 SQGQRQRILIARAVYKNPDFLFFDEATNALDANNEREIMEHLNEFyrGKTVVIVAH 687
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
510-536 |
2.12e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 2.12e-03
10 20
....*....|....*....|....*..
gi 496428897 510 LNNVNLTIPRNKITAIVGASGSGKTTL 536
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
519-556 |
2.77e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 2.77e-03
10 20 30
....*....|....*....|....*....|....*...
gi 496428897 519 RNKITAIVGASGSGKTTLIKLLLGfytpnKGNIKVGDV 556
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP-----ELVLATGEI 116
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
181-295 |
2.88e-03 |
|
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: 40.19 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDV---GIRDNNLNFITL--ILVAQLIIFIARLSVDFIRSWLLLHMNIRINISLISDFL 255
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLIDVaskESGDIEIFGLSLktFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLF 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 496428897 256 VKLMRLPLHFFDTKMIGDIMQRIGdhsrIESFLTGSSIST 295
Cdd:cd18573 82 KSILRQDAAFFDKNKTGELVSRLS----SDTSVVGKSLTQ 117
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
181-312 |
3.92e-03 |
|
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: 39.93 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVDVGIRD---------NNLNFITLILVaqLIIFIARLSVdFIRSWLLlhmniriniSLI 251
Cdd:cd18780 2 TIALLVSSGTNLALPYFFGQVIDAVTNHsgsggeealRALNQAVLILL--GVVLIGSIAT-FLRSWLF---------TLA 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496428897 252 SDFLVKLMRLPLH---------FFDTKMIGDIMQRIGDHSR-IESFLTgSSISTLFSFVNFIVFGFVLAYY 312
Cdd:cd18780 70 GERVVARLRKRLFsaiiaqeiaFFDVTRTGELLNRLSSDTQvLQNAVT-VNLSMLLRYLVQIIGGLVFMFT 139
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
198-277 |
4.40e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 40.00 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 198 TQSLVDVGIRDNNLNFITL-ILVAQLIIFiarlsvDFIRSWLLLHMNIRINISLISDFLVKLMRLPLHFFDTKMIGDIMQ 276
Cdd:cd18601 47 NSTNVDIEDLDRDFNLGIYaGLTAATFVF------GFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILN 120
|
.
gi 496428897 277 R 277
Cdd:cd18601 121 R 121
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
181-467 |
6.14e-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: 39.13 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 181 VLGMVIGSILQLIVPFLTQSLVD-VGIRDNNLNFITLILVaqLIIFIARLSVDFIRS-----WLLLHMNIRINISLisDF 254
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNaLTLAKVKDLESAVTLI--LLYALLRFSSKLLKElrsllYRRVQQNAYRELSL--KT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 255 LVKLMRLPLHFFDTKMIGDIMqRIGDHSriesfltGSSISTLFSFVNF----------IVFGFVLAYYDLSIFGLFLLGN 324
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVV-RIMDRG-------TESANTLLSYLVFylvptlleliVVSVVFAFHFGAWLALIVFLSV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 325 LLYVIWVLSFMKYRReldlrRFSQASTEQSTLYQIITGMQeikLNNCETQKRWKWERIQVKLFKISVKGLALQQYQ---- 400
Cdd:cd18560 150 LLYGVFTIKVTEWRT-----KFRRAANKKDNEAHDIAVDS---LLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKvqas 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496428897 401 ----QVGSVFFNQTTNILISYIAARAVVEGNMTLG-MMMSLTYIIgQLNSPIeQFIGFA-RSFQDAKISLERL 467
Cdd:cd18560 222 lsllNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGdFVAVNTYIF-QLFQPL-NFLGTIyRMIIQSLTDMENL 292
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
514-616 |
6.45e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496428897 514 NLTI-PRNKITAIVGASGSGKTTL---IKLLLGFYTPNKGNIKVGDVYLKNINPHLWRSVTGSV-----MQDG---FIFS 581
Cdd:pfam13476 11 DQTIdFSKGLTLITGPNGSGKTTIldaIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVeitfeNNDGrytYAIE 90
|
90 100 110
....*....|....*....|....*....|....*
gi 496428897 582 ETIAENIAIGEEVIDKERLLKAaqIANIDQFIDSL 616
Cdd:pfam13476 91 RSRELSKKKGKTKKKEILEILE--IDELQQFISEL 123
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
515-548 |
6.79e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 6.79e-03
10 20 30
....*....|....*....|....*....|....
gi 496428897 515 LTIPRNKITAIVGASGSGKTTLIKLLLGFYTPNK 548
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| |
