|
Name |
Accession |
Description |
Interval |
E-value |
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-1485 |
0e+00 |
|
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: 2311.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1 MQRSPVEDANCLSRYFFWWTNPIMRKGFKEKLRPSDVYQAPSQDAADILAERLEKEWDREVASGKKKPSLLRAMARCYIK 80
Cdd:TIGR01271 1 MQRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 81 PFLLFGFLLYIGEATKTVQPQLLGRIIASFDPAHEPERANGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSI 160
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 161 IYKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQAF 240
Cdd:TIGR01271 161 IYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 241 LSHKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSSAYFFSAIFVIV 320
Cdd:TIGR01271 241 LGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 321 AAVVPHALSRGINLRRIFTTLSYCMVLRMTVTRQLPGSIQMWYDTMRLIWKIEEFLSKEEYKLMEYDLSITELELQDVTA 400
Cdd:TIGR01271 321 LSVVPYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 401 SWDEGPGELLERIKQENKANGHHNGDAGLFFTN--LYVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSS 478
Cdd:TIGR01271 401 SWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNfsLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 479 GKIRHSGRISYSSQTAWIMPGTIRDNILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALA 558
Cdd:TIGR01271 481 GKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 559 RAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPD 638
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 639 FSSLLLGLEAYDNISAERRCSILTETLHRVSVDESA----GMQPERSAFRQVPPTkpmYIDERKASVIVNPLGVARKASF 714
Cdd:TIGR01271 641 FSSLLLGLEAFDNFSAERRNSILTETLRRVSIDGDStvfsGPETIKQSFKQPPPE---FAEKRKQSIILNPIASARKFSF 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 715 IQ--------VPEEEVRRTLPDRKFSLVPENELVDESFMGSDVYHnHGVHMAGQRRQSVLAFMTNA-QGQGRREHLQSSF 785
Cdd:TIGR01271 718 VQmgpqkaqaTTIEDAVREPSERKFSLVPEDEQGEESLPRGNQYH-HGLQHQAQRRQSVLQLMTHSnRGENRREQLQTSF 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 786 RRRLSVVPQSELASELDIYTRRLS-DSTYDMTGILEEENIEACLTdeiDEIEETFETTKWNTYVRYVSNNKSLLYVLIFI 864
Cdd:TIGR01271 797 RKKSSITQQNELASELDIYSRRLSkDSVYEISEEINEEDLKECFA---DERENVFETTTWNTYLRYITTNRNLVFVLIFC 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 865 LFIAAIEIAGSVAGIFLITDELWREEHQRSEpnmtkHSNASSSGQTYAITVTPTSSYYILYIYVATSESLLAMGFFRGLP 944
Cdd:TIGR01271 874 LVIFLAEVAASLLGLWLITDNPSAPNYVDQQ-----HANASSPDVQKPVIITPTSAYYIFYIYVGTADSVLALGFFRGLP 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 945 FVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFVQLTVVVVGCILVVSIVRPYIF 1024
Cdd:TIGR01271 949 LVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIF 1028
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1025 LAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQAYFEALFHKTLNTHTATWFLYLSTL 1104
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTL 1108
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1105 RWFLFRADILFVFFFTLAAWIAVGTNQDKPGEIGIIICLAMLILGTFQWCVATSIAVDGMMRSVDRVFKFIDLPSETPKP 1184
Cdd:TIGR01271 1109 RWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRP 1188
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1185 DKGKD-----SDLIIENVDAQadSSWPHRGQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL 1259
Cdd:TIGR01271 1189 SGGGGkyqlsTVLVIENPHAQ--KCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL 1266
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1260 KLVYTDGEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDFQ 1339
Cdd:TIGR01271 1267 RLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFV 1346
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1340 LEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDK 1419
Cdd:TIGR01271 1347 LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEG 1426
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 1420 GQVKTYDSIQKLLNETSHLKQAISPAERLKLFP--RRNSSMRTPQSKLSSvtqtLQEEAEDNIQDTRL 1485
Cdd:TIGR01271 1427 SSVKQYDSIQKLLNETSLFKQAMSAADRLKLFPlhRRNSSKRKPQPKITA----LREEAEEEVQNTRL 1490
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
842-1175 |
0e+00 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; 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: 350044 [Multi-domain] Cd Length: 324 Bit Score: 554.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 842 TKWNTYVRYVSNNKSLLYVLIFILFIAAIEIAGSVAGIFLITDELWREEHQRSEpnmtkhsnasSSGQTYAITVTPTSSY 921
Cdd:cd18600 1 TTWNTYLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPE----------SSSNTYAVIVTFTSSY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 922 YILYIYVATSESLLAMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFD 1001
Cdd:cd18600 71 YVFYIYVGVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1002 FVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQAY 1081
Cdd:cd18600 151 FIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1082 FEALFHKTLNTHTATWFLYLSTLRWFLFRADILFVFFFTLAAWIAVGTNQDKPGEIGIIICLAMLILGTFQWCVATSIAV 1161
Cdd:cd18600 231 FETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDV 310
|
330
....*....|....
gi 68390341 1162 DGMMRSVDRVFKFI 1175
Cdd:cd18600 311 DSLMRSVSRIFKFI 324
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
390-669 |
2.25e-180 |
|
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: 537.52 E-value: 2.25e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 390 ITELELQDVTASWDEGPGELLERIKQENKANGHHNGDAGLFFTN--LYVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLL 467
Cdd:cd03291 1 TTGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNlcLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 468 MTILGELVPSSGKIRHSGRISYSSQTAWIMPGTIRDNILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNL 547
Cdd:cd03291 81 MLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 548 SGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYG 627
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 68390341 628 TFPELQSERPDFSSLLLGLEAYDNISAERRCSILTETLHRVS 669
Cdd:cd03291 241 TFSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRRFS 282
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-1432 |
6.81e-175 |
|
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: 564.57 E-value: 6.81e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 5 PVEDANCLSRYFFWWTNPIMRKGFKEKLRPSDVYQAPSQDAADILAERLEKEWDRE----------VASGKK-------- 66
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKEckktrkqpvsAVYGKKdpskpkgs 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 67 ---------------------KPSLLRAMARCYIKPFLLFGFLLYIGEATKTVQPQLLGRIIASFDPAHEPErANGYFLA 125
Cdd:TIGR00957 283 sqldaneevealivksphkprKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPD-WQGYFYT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 126 fglGLLFTARFLllqpAMFGLHHL-------GMQIRIALFSIIYKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGM 198
Cdd:TIGR00957 362 ---GLLFVCACL----QTLILHQYfhicfvsGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATY 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 199 AHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQAFLSHKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGW 278
Cdd:TIGR00957 435 INMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAW 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 279 EEIMETLIKNIRQDEVKLTRKIGSLRYFYSSAYFFSAIFV--IVAAVVPHALSRGI-NLRRIFTTLSYCMVLRMTVTrQL 355
Cdd:TIGR00957 515 ELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLValITFAVYVTVDENNIlDAEKAFVSLALFNILRFPLN-IL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 356 PGSIQMWYDTMRLIWKIEEFLSKEEyklmeydLSITELELQDVTaswdegPGEllerikqeNKANGHHNGDaglFFTNLY 435
Cdd:TIGR00957 594 PMVISSIVQASVSLKRLRIFLSHEE-------LEPDSIERRTIK------PGE--------GNSITVHNAT---FTWARD 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 436 VAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAWIMPGTIRDNILFGLTYDEYR 515
Cdd:TIGR00957 650 LPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKY 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 YKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCK--L 593
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegV 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 594 MASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSLLlglEAYDNisaerrcsiltetlhrvsvDES 673
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL---RTYAP-------------------DEQ 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 674 AGMQPERSAFRQVPPTKpmyiderkasvivnplgvarkasfiqvpeeevrrtlpdrkfslvpENELVDESFMGSDVYHNH 753
Cdd:TIGR00957 868 QGHLEDSWTALVSGEGK---------------------------------------------EAKLIENGMLVTDVVGKQ 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 754 GvhmagQRRQSVLAfmTNAQGQGRreHLQSSFRrrlsvVPQSELASEldiytrrlsdstydmTGILEEENIEACLTDEId 833
Cdd:TIGR00957 903 L-----QRQLSASS--SDSGDQSR--HHGSSAE-----LQKAEAKEE---------------TWKLMEADKAQTGQVEL- 952
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 834 eieetfeTTKWNtYVRYVSNNKSLLYVLIFIlfiaAIEIAGSVAGIFLitdELWREEhqrsepnmtKHSNASSSGQTYAI 913
Cdd:TIGR00957 953 -------SVYWD-YMKAIGLFITFLSIFLFV----CNHVSALASNYWL---SLWTDD---------PMVNGTQNNTSLRL 1008
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 914 TVtptssyyilYIYVATSESLLAMGFfrGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDD 993
Cdd:TIGR00957 1009 SV---------YGALGILQGFAVFGY--SMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDS 1077
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 994 MLPLLMFDFVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTI 1073
Cdd:TIGR00957 1078 MIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVI 1157
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1074 RAFERQAYFEALFHKTLNTHTATWFLYLSTLRWFLFRADILFVFFFTLAAWIAV-GTNQDKPGEIGIIICLAMLILGTFQ 1152
Cdd:TIGR00957 1158 RAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAViSRHSLSAGLVGLSVSYSLQVTFYLN 1237
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1153 WCVATSIAVDGMMRSVDRVFKFIDLPSETPkpdkgkdsdLIIEnvDAQADSSWPHRGQIEVRNLTVKYTEAGHAVLKNLS 1232
Cdd:TIGR00957 1238 WLVRMSSEMETNIVAVERLKEYSETEKEAP---------WQIQ--ETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHIN 1306
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1233 FSAEGRQRVGILGRTGSGKSSLFNALLKLVYT-DGEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLDPYGCH 1311
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQY 1386
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1312 SDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:TIGR00957 1387 SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT 1466
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|.
gi 68390341 1392 SFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLL 1432
Cdd:TIGR00957 1467 QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1209-1485 |
1.94e-172 |
|
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: 516.33 E-value: 1.94e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1209 GQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTDGEISIDGVNWNKMPLQKWRKAFG 1288
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARIL 1368
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1369 LLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLLNETSHLKQAISPAERL 1448
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 68390341 1449 KLFPRRNSSMRTpqSKLSSVTQTLQEEAEDNIQDTRL 1485
Cdd:cd03289 241 KLFPRRNSSKSK--RKPRPQIQALQEETEEEVQDTRL 275
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-1458 |
1.16e-171 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 554.97 E-value: 1.16e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 5 PVEDANCLSRYFFWWTNPIMRKGFKEKLRPSDVYQAPSQDAADILAERLEKEWDREvaSGKKKPSLLRAMARCYIKPFLL 84
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE--SRRPKPWLLRALNNSLGGRFWL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 85 FGFLLYIGEATKTVQPQLLGRIIASF---DPAHEperanGYFLAF--GLGLLFTArflLLQPAMF-GLHHLGMQIRIALF 158
Cdd:PLN03232 306 GGIFKIGHDLSQFVGPVILSHLLQSMqegDPAWV-----GYVYAFliFFGVTFGV---LCESQYFqNVGRVGFRLRSTLV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 159 SIIYKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQ 238
Cdd:PLN03232 378 AAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 239 AFLSHKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSsaYFFSAIFV 318
Cdd:PLN03232 458 TLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNS--FILNSIPV 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 319 IVAAV---VPHALSRGINLRRIFTTLSYCMVLRMTVTrQLPGSIQMWYDTMRLIWKIEEFLSKEEYKLME---YDLSITE 392
Cdd:PLN03232 536 VVTLVsfgVFVLLGGDLTPARAFTSLSLFAVLRSPLN-MLPNLLSQVVNANVSLQRIEELLLSEERILAQnppLQPGAPA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 393 LELQDVTASWDegpgellerIKQENkanghhngdaglfftnlyvaPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILG 472
Cdd:PLN03232 615 ISIKNGYFSWD---------SKTSK--------------------PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 473 ELVP---SSGKIRhsGRISYSSQTAWIMPGTIRDNILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSG 549
Cdd:PLN03232 666 ELSHaetSSVVIR--GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISG 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 550 GQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTF 629
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTF 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 630 PELQSERPDFSSLLlgleaydnisaerrcsiltetlhrvsvdESAGMQPERsafrQVPPTKPMYIDERKASVIVNplgva 709
Cdd:PLN03232 824 AELSKSGSLFKKLM----------------------------ENAGKMDAT----QEVNTNDENILKLGPTVTID----- 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 710 rkasfiqvpeeevrrtlpdrkfslvpenelVDESFMGSDvyhnhgvhMAGQRRQSVLAfmtnaqGQGRREhlqssfrrrl 789
Cdd:PLN03232 867 ------------------------------VSERNLGST--------KQGKRGRSVLV------KQEERE---------- 892
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 790 svvpqselaseldiytrrlsdstydmTGILEeenieacltdeideieetfettkWNTYVRYVSNNKSLLYVLIFILFIAA 869
Cdd:PLN03232 893 --------------------------TGIIS-----------------------WNVLMRYNKAVGGLWVVMILLVCYLT 923
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 870 IEIAGSVAGIFLitdELWREEhqrsepnmtkhsnasSSGQTYaitvtpTSSYYIlYIYVATSESLLAMGFFRGLPFVHTT 949
Cdd:PLN03232 924 TEVLRVSSSTWL---SIWTDQ---------------STPKSY------SPGFYI-VVYALLGFGQVAVTFTNSFWLISSS 978
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 950 ITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFVQLTVVVVGCILVVSIVRPYIFLAATP 1029
Cdd:PLN03232 979 LHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMP 1058
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1030 LAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQAYFEALFHKTLNTHTATWFLYLSTLRWFLF 1109
Cdd:PLN03232 1059 LLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTI 1138
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1110 RADILFVFFFTLAAWIAVGTNQDKPGEIGIIICLAMLILGTFQwcvATSIaVDGMMR----------SVDRVFKFIDLPS 1179
Cdd:PLN03232 1139 RLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLN---ITTL-LSGVLRqaskaenslnSVERVGNYIDLPS 1214
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1180 ETPKpdkgkdsdlIIENvdAQADSSWPHRGQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL 1259
Cdd:PLN03232 1215 EATA---------IIEN--NRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF 1283
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1260 KLVYTD-GEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDF 1338
Cdd:PLN03232 1284 RIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDA 1363
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1339 QLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMD 1418
Cdd:PLN03232 1364 EVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLS 1443
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*...
gi 68390341 1419 KGQVKTYDSIQKLL-NETS---HLKQAISPAERLKL----FPRRNSSM 1458
Cdd:PLN03232 1444 SGQVLEYDSPQELLsRDTSaffRMVHSTGPANAQYLsnlvFERRENGM 1491
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-1436 |
8.23e-165 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 538.94 E-value: 8.23e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 5 PVEDANCLSRYFFWWTNPIMRKGFKEKLRPSDVYQAPSQDAADILAERLEKEWDREvaSGKKKPSLLRAMARCYIKPFLL 84
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEE--LKKPKPWLLRALNNSLGGRFWL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 85 FGFLLYIGEATKTVQPQLLGRIIASF---DPAHEperanGYFLAFG------LGLLFTARFLllQPAMfglhHLGMQIRI 155
Cdd:PLN03130 306 GGFFKIGNDLSQFVGPLLLNLLLESMqngEPAWI-----GYIYAFSifvgvvLGVLCEAQYF--QNVM----RVGFRLRS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 156 ALFSIIYKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLG 235
Cdd:PLN03130 375 TLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMF 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 236 VLQAFLSHKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSSAYFFSA 315
Cdd:PLN03130 455 PIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIP 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 316 IFVIVAAVVPHALSRG-INLRRIFTTLSYCMVLRMTVTrQLPGSIQMWYDTMRLIWKIEEFLSKEEYKLME---YDLSIT 391
Cdd:PLN03130 535 VLVTVVSFGVFTLLGGdLTPARAFTSLSLFAVLRFPLF-MLPNLITQAVNANVSLKRLEELLLAEERVLLPnppLEPGLP 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 392 ELELQDVTASWDegpgellerIKQENkanghhngdaglfftnlyvaPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTIL 471
Cdd:PLN03130 614 AISIKNGYFSWD---------SKAER--------------------PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 472 GELVPSSGK---IRhsGRISYSSQTAWIMPGTIRDNILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLS 548
Cdd:PLN03130 665 GELPPRSDAsvvIR--GTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNIS 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 549 GGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGT 628
Cdd:PLN03130 743 GGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGT 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 629 FPELQSERPDFSSLLlgleaydnisaerrcsiltetlhrvsvdESAGMQPERSafrqvpptkpmyiderkasvivnplgv 708
Cdd:PLN03130 823 YEELSNNGPLFQKLM----------------------------ENAGKMEEYV--------------------------- 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 709 arkasfiqvpEEEVRRTLPDRKFSLVPENElvdesfmGSDVYHNHGVHMAGQRRQSVLAfmtnaqGQGRREhlqssfrrr 788
Cdd:PLN03130 848 ----------EENGEEEDDQTSSKPVANGN-------ANNLKKDSSSKKKSKEGKSVLI------KQEERE--------- 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 789 lsvvpqselaseldiytrrlsdstydmTGILEeenieacltdeideieetfettkWNTYVRYVSNNKSLLYVLIFILFIA 868
Cdd:PLN03130 896 ---------------------------TGVVS-----------------------WKVLERYKNALGGAWVVMILFLCYV 925
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 869 AIEI--AGSVAGIFLITDELWREEHQRSEPNMTkhSNASSSGQtyaITVTPTSSYYILyiyvatSESLLAmgffrglpfv 946
Cdd:PLN03130 926 LTEVfrVSSSTWLSEWTDQGTPKTHGPLFYNLI--YALLSFGQ---VLVTLLNSYWLI------MSSLYA---------- 984
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 947 httitiSKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFVQLTVVVVGCILVVSIVRPYIFLA 1026
Cdd:PLN03130 985 ------AKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWA 1058
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1027 ATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAF---ERQAYFEAlfhKTLNTHTATWFLYLST 1103
Cdd:PLN03130 1059 IMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYkayDRMAEING---RSMDNNIRFTLVNMSS 1135
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1104 LRWFLFRADILFVFFFTLAAWIAVGTN------QDKPGEIGIIICLAMLILGTFQWCVATSIAVDGMMRSVDRVFKFIDL 1177
Cdd:PLN03130 1136 NRWLAIRLETLGGLMIWLTASFAVMQNgraenqAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDL 1215
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1178 PSETPkpdkgkdsdLIIENvdAQADSSWPHRGQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNA 1257
Cdd:PLN03130 1216 PSEAP---------LVIEN--NRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNA 1284
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1258 LLKLVYTD-GEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKL 1336
Cdd:PLN03130 1285 LFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGL 1364
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1337 DFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLM 1416
Cdd:PLN03130 1365 DAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILV 1444
|
1450 1460
....*....|....*....|.
gi 68390341 1417 MDKGQVKTYDSIQKLL-NETS 1436
Cdd:PLN03130 1445 LDAGRVVEFDTPENLLsNEGS 1465
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
84-373 |
6.39e-128 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 398.54 E-value: 6.39e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 84 LFGFLLYIGEATKTVQPQLLGRIIASFDPAHEPERANGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSIIYK 163
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 164 KTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQAFLSH 243
Cdd:cd18594 81 KTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 244 KMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSSAYFFSAIFVIVAAV 323
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 324 VPHALSRGI-NLRRIFTTLSYCMVLRMTVTRQLPGSIQMWYDTMRLIWKIE 373
Cdd:cd18594 241 VPYVLTGNTlTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| CFTR_R |
pfam14396 |
Cystic fibrosis TM conductance regulator (CFTR), regulator domain; |
638-847 |
4.22e-107 |
|
Cystic fibrosis TM conductance regulator (CFTR), regulator domain;
Pssm-ID: 464164 Cd Length: 213 Bit Score: 338.63 E-value: 4.22e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 638 DFSSLLLGLEAYDNISAERRCSILTETLHRVSVDESAGMQ---PERSAFRQVpptkPMYIDERKASVIVNPLGVARKASF 714
Cdd:pfam14396 1 DFSSLLMGLEAFDNFSAERRNSILTETLRRFSVDEDAGGSrnePKKQSFKQT----DDFNEKRKNSVILNPLAASRKFSI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 715 IQVP------EEEVRRTLPDRKFSLVPENELVDESFMGSDVYHnHGVHMAGQRRQSVLAFMTN--AQGQGRREHLQSSFr 786
Cdd:pfam14396 77 IQKSqlqmngIEEGLSELPERRLSLVPESEQGEAALPRSNVLN-TGPTLQGQRRQSVLALMTNtvAQGQGRREKGQSSF- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 787 RRLSVVPQSELASELDIYTRRLS-DSTYDMTGILEEENIEACLTdeiDEIEETFETTKWNTY 847
Cdd:pfam14396 155 RKMSVVPQSNLASELDIYARRLSkDSVLDITEEINEEDLKECFA---DDIENVFETTTWNTY 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
125-1422 |
6.82e-107 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 374.12 E-value: 6.82e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 125 AFGLGLLFTarFLLLQPAMFGLHH--------LGMQIRIALFSIIYKKTLKLSSRVLDK--ISTGQLVSLMSANLGKFDQ 194
Cdd:PTZ00243 282 GRGLGLVLT--LFLTQLIQSVCLHrfyyisirCGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 195 SLGMAHFIWISPLQCILCTGLIWELIdvnSFCALAAISLLGV---LQAFLS-HKMgpyKAQKVLL--TNKRLALTSEIME 268
Cdd:PTZ00243 360 FMQYCMYLWSSPMVLLLSILLLSRLV---GWCALMAVAVLLVtlpLNGAIMkHQM---AARRKIAkaADARVKATNEFFS 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 269 NLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSSAYFFSAIFVIVAA-VVPHALSRGINLRRIFTTLSYCMVL 347
Cdd:PTZ00243 434 GIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVfTVYYLLGHELTPEVVFPTIALLGVL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 348 RMTVtRQLPGSIQMWYDTMRLIWKIEEFLS-----------KEEYKLMEYDLSITE-----LELQDVTA----------- 400
Cdd:PTZ00243 514 RMPF-FMIPWVFTTVLQFLVSIKRISTFLEcdnatcstvqdMEEYWREQREHSTACqlaavLENVDVTAfvpvklprapk 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 401 --------------------------------SWDEG-PGELLERIKQENKANGHHNGDA-----------GLFFTNLYV 436
Cdd:PTZ00243 593 vktsllsralrmlcceqcrptkrhpspsvvveDTDYGsPSSASRHIVEGGTGGGHEATPTsersaktpkmkTDDFFELEP 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAWIMPGTIRDNILFGLTYDEYRY 516
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARL 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 517 KSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCKLMAS 596
Cdd:PTZ00243 753 ADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAG 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 597 KTRILVTNKIEHLKRADKILLLHNGESFFYGtfpelqsERPDF--SSLLLGLEAYDNISAERRCSILTETLHRVSVDESA 674
Cdd:PTZ00243 833 KTRVLATHQVHVVPRADYVVALGDGRVEFSG-------SSADFmrTSLYATLAAELKENKDSKEGDADAEVAEVDAAPGG 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 675 GMQPERSAFRQvpptkpmyidERKASvivnplgvarkasfiqvPEEEVRRTLPDRKFSLVPENelvdesfmgsdvyhnhg 754
Cdd:PTZ00243 906 AVDHEPPVAKQ----------EGNAE-----------------GGDGAALDAAAGRLMTREEK----------------- 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 755 vhmagqrrqsvlafmtnAQGQgrrehlqssfrrrlsvVPqselaseldiytrrlsdstydmtgileeenieacltdeide 834
Cdd:PTZ00243 942 -----------------ASGS----------------VP----------------------------------------- 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 835 ieetfettkWNTYVRYVSNNKSLLYVLIFILFIAAIEIAGSVAGIFLitdELWreehqrsEPNMTKHSNASSSGQTYAIT 914
Cdd:PTZ00243 948 ---------WSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWL---SMW-------STRSFKLSAATYLYVYLGIV 1008
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 915 VTPTSSYYILYIyvaTSESLLAMGffrglpfvhttitiSKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDM 994
Cdd:PTZ00243 1009 LLGTFSVPLRFF---LSYEAMRRG--------------SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNT 1071
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 995 LPLLMFDFVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIR 1074
Cdd:PTZ00243 1072 LPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATIT 1151
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1075 AFERQAYF--EALfhKTLNTHTATWFLYLSTLRWFLFRADILFVFFFTLAAWIAVGT-----NQDKPGEIGIIICLAMLI 1147
Cdd:PTZ00243 1152 AYGKAHLVmqEAL--RRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGtmlraTSQEIGLVSLSLTMAMQT 1229
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1148 LGTFQWCVATSIAVDGMMRSVDRVFKFID-LPSE-TPKPDKGKD-------------SDLIIEnvDAQADSSWPH---RG 1209
Cdd:PTZ00243 1230 TATLNWLVRQVATVEADMNSVERLLYYTDeVPHEdMPELDEEVDalerrtgmaadvtGTVVIE--PASPTSAAPHpvqAG 1307
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1210 QIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYT-DGEISIDGVNWNKMPLQKWRKAFG 1288
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFS 1387
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILS-GARI 1367
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGF 1467
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1368 LLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:PTZ00243 1468 ILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
393-622 |
1.97e-94 |
|
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: 302.85 E-value: 1.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 393 LELQDVTASWDEGPGELlerikqenkanghhngdaglfftnlyvAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILG 472
Cdd:cd03250 1 ISVEDASFTWDSGEQET---------------------------SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 473 ELVPSSGKIRHSGRISYSSQTAWIMPGTIRDNILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQK 552
Cdd:cd03250 54 ELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 553 ARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCK-LMASKTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGlLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1209-1427 |
2.85e-87 |
|
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: 283.23 E-value: 2.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1209 GQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKWRKAF 1287
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVElSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKVFIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARI 1367
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1368 LLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDS 1427
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
860-1171 |
3.54e-74 |
|
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: 249.93 E-value: 3.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 860 VLIFILFIAAieiagsvAGIFLITDeLWREEHQRSEPNMTKHSNASSSGQTYAITVTPTSSYYILYIYVATSESLLAMGF 939
Cdd:cd18601 6 ILLVLLNIAA-------QVLYVLSD-WWLSYWANLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 940 FRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFVQLTVVVVGCILVVSIV 1019
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1020 RPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQAYFEALFHKTLNTHTATWFL 1099
Cdd:cd18601 158 NPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1100 YLSTLRWFLFRADILFVFFFTLAAWIAVGTNQD-KPGEIGIIICLAMLILGTFQWCVATSIAVDGMMRSVDRV 1171
Cdd:cd18601 238 FLATSRWLAVRLDALCALFVTVVAFGSLFLAESlDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
916-1175 |
1.50e-71 |
|
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: 241.64 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 916 TPTSSYYILYIYVATSESLLAMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDML 995
Cdd:cd18580 34 NSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 996 PLLMFDFVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRA 1075
Cdd:cd18580 114 PLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1076 FERQAYFEALFHKTLNTHTATWFLYLSTLRWFLFRADILFVFFFTLAAWIAVGTNQDK-PGEIGIIICLAMLILGTFQWC 1154
Cdd:cd18580 194 FGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSSIsAGLVGLALTYALSLTGSLQWL 273
|
250 260
....*....|....*....|.
gi 68390341 1155 VATSIAVDGMMRSVDRVFKFI 1175
Cdd:cd18580 274 VRQWTELETSMVSVERILEYT 294
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
936-1422 |
1.80e-69 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 245.46 E-value: 1.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 936 AMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFVQltvvvvgcilv 1015
Cdd:COG1132 76 LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVR----------- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1016 vSIVRP-----YIF--------LAATPLAIIFIVMRkYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQAYF 1082
Cdd:COG1132 145 -SVVTLigalvVLFvidwrlalIVLLVLPLLLLVLR-LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1083 EALFHKTLNTHTATWFLYLSTLRWFLFRADILFVFFFTLAAWIA---VGTNQDKPGEIGIIICLAMLILGTFQWCVATSI 1159
Cdd:COG1132 223 LERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGgllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1160 AVDGMMRSVDRVFKFIDLPSETPKPDKGKDSDliienvdaqadsswPHRGQIEVRNLTVKYtEAGHAVLKNLSFSAEGRQ 1239
Cdd:COG1132 303 QLQRALASAERIFELLDEPPEIPDPPGAVPLP--------------PVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1240 RVGILGRTGSGKSSLFNALLKLvY--TDGEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLDpYGC--HSDEE 1315
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRF-YdpTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGRpdATDEE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1316 LWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFST 1395
Cdd:COG1132 446 VEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKG 525
|
490 500
....*....|....*....|....*..
gi 68390341 1396 CTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:COG1132 526 RTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
84-366 |
6.14e-65 |
|
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: 222.36 E-value: 6.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 84 LFGFLLYIGEATKTVQPQLLGRIIASFDPAHEPERANGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSIIYK 163
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 164 KTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQAFLSH 243
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 244 KMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSSAYFFSAIFVIVAAV 323
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 68390341 324 VPHALSRG-INLRRIFTTLSYCMVLRMtVTRQLPGSIQMWYDTM 366
Cdd:cd18579 241 ATYVLLGNpLTAAKVFTALSLFNLLRF-PLLMLPQAISSLIEAL 283
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
935-1422 |
2.72e-61 |
|
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: 224.33 E-value: 2.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 935 LAMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFtKDMATIDDMLP----LLMFDFVQLtvvvv 1010
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgsllTALLDLLFV----- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1011 gcilvvsIVrpYI--------FLAATPLAII--FIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAF---- 1076
Cdd:COG2274 284 -------LI--FLivlffyspPLALVVLLLIplYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALgaes 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1077 ERQAYFEALFHKTLNTHtatwflylstlrwflFRADILFVFFFTLAAWIAVGTNqdkpgeIGIIICLAMLI------LGT 1150
Cdd:COG2274 355 RFRRRWENLLAKYLNAR---------------FKLRRLSNLLSTLSGLLQQLAT------VALLWLGAYLVidgqltLGQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1151 FqwcVATSIAVDGMM-----------------RSVDRVFKFIDLPSETPKPDKGKDSDLIienvdaqadsswphRGQIEV 1213
Cdd:COG2274 414 L---IAFNILSGRFLapvaqligllqrfqdakIALERLDDILDLPPEREEGRSKLSLPRL--------------KGDIEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1214 RNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLvY--TDGEISIDGVNWNKMPLQKWRKAFGVVP 1291
Cdd:COG2274 477 ENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL-YepTSGRILIDGIDLRQIDPASLRRQIGVVL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1292 QKVFIFTGPLRMNL---DPYgcHSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARIL 1368
Cdd:COG2274 556 QDVFLFSGTIRENItlgDPD--ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRIL 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1369 LLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
65-632 |
1.47e-59 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 216.18 E-value: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 65 KKKPSLLRAMARcYIKPF---LLFGFLLYIGEA-TKTVQPQLLGRIIASFDPAHEPERAngYFLAFGLGLLFTARFLLLQ 140
Cdd:COG1132 3 KSPRKLLRRLLR-YLRPYrglLILALLLLLLSAlLELLLPLLLGRIIDALLAGGDLSAL--LLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 141 PAMFGLHHLGMQIRIALFSIIYKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMA-HFIWISPLQCILCTGLI--- 216
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGlPQLVRSVVTLIGALVVLfvi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 217 -WELidvnSFCALAAISLLGVLQAFLSHKMGPYKAQkvlLTNKRLALTSEIMENLHS---VKAYGWEEIMETLIKNIRQD 292
Cdd:COG1132 160 dWRL----ALIVLLVLPLLLLVLRLFGRRLRKLFRR---VQEALAELNGRLQESLSGirvVKAFGREERELERFREANEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 293 EVKLTRKIGSLRYFYSSAYFF--SAIFVIVAAVVPHALSRG-INLRRIFTTLSYCMVLRMTVtRQLPGSIQMWYDTMRLI 369
Cdd:COG1132 233 LRRANLRAARLSALFFPLMELlgNLGLALVLLVGGLLVLSGsLTVGDLVAFILYLLRLFGPL-RQLANVLNQLQRALASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 370 WKIEEFLS-----KEEYKLMEYDLSITELELQDVTASWDEGPgellerikqenkanghhngdaglfftnlyvaPVLKDIS 444
Cdd:COG1132 312 ERIFELLDeppeiPDPPGAVPLPPVRGEIEFENVSFSYPGDR-------------------------------PVLKDIS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 445 LKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDNILFG-LT 510
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGrPD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 511 YDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKcL 590
Cdd:COG1132 441 ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-L 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 68390341 591 CKLMASKTRILVTNKIEHLKRADKILLLHNG---ESffyGTFPEL 632
Cdd:COG1132 520 ERLMKGRTTIVIAHRLSTIRNADRILVLDDGrivEQ---GTHEEL 561
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1205-1427 |
5.65e-59 |
|
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: 201.87 E-value: 5.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1205 WPHRGQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKW 1283
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKAFGVVPQKVFIFTGPLRMNLDPYGCHSDEELW---RVAEevglktvieqfpdkldfqleyGGYVLSNGHKQLICLARS 1360
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYgalRVSE---------------------GGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1361 ILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDS 1427
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
84-361 |
1.43e-56 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) 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: 350037 [Multi-domain] Cd Length: 291 Bit Score: 198.21 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 84 LFGFLLYIGEATKTVQPQLLGRIIASFDPAHEP-ERANGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSIIY 162
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSiSLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 163 KKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQAFLS 242
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 243 HKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSSAYFFSAIFVIVAA 322
Cdd:cd18593 161 KLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 68390341 323 VVPHALSRG-INLRRIFTTLSYCMVLRMTVTRQLPGSIQM 361
Cdd:cd18593 241 FLAYILLGNiLTAERVFVTMALYNAVRLTMTLFFPFAIQF 280
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1023-1422 |
4.48e-55 |
|
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: 202.30 E-value: 4.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1023 IFLAATPLAIIFIVM---------RKYFlrtgQQLKQLetearspiFSHLIMSLKGLWTIRAFER-QAYFEALFHKTLNT 1092
Cdd:COG4988 163 ILLVTAPLIPLFMILvgkgaakasRRQW----RALARL--------SGHFLDRLRGLTTLKLFGRaKAEAERIAEASEDF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1093 HTATwflyLSTLRW-FLfradILFV--FFFTLA-AWIAVGT-----NqdkpGEIGIIICLAMLIL-----------GTFQ 1152
Cdd:COG4988 231 RKRT----MKVLRVaFL----SSAVleFFASLSiALVAVYIgfrllG----GSLTLFAALFVLLLapefflplrdlGSFY 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1153 WCVATSIAVdgmmrsVDRVFKFIDLPSETPKPdkgkdsdliienvdAQADSSWPHRGQIEVRNLTVKYtEAGHAVLKNLS 1232
Cdd:COG4988 299 HARANGIAA------AEKIFALLDAPEPAAPA--------------GTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1233 FSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLDPYG-C 1310
Cdd:COG4988 358 LTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpD 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1311 HSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLR 1390
Cdd:COG4988 438 ASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALR 517
|
410 420 430
....*....|....*....|....*....|..
gi 68390341 1391 QSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:COG4988 518 RLAKGRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
971-1441 |
1.86e-54 |
|
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: 200.76 E-value: 1.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 971 VLNTMKTGRIMNRFTKDMATIDD-----MLPLLmfdfVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTG 1045
Cdd:COG4987 105 GLARLRSGDLLNRLVADVDALDNlylrvLLPLL----VALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1046 QQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQAYFEAlfhkTLNTHTATWFLYLSTLRWFLFRADILFVFFFTLAAW- 1124
Cdd:COG4987 181 RRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALA----RLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1125 -IAVGTNQDKPGEIGIIIcLAMLILGT---FQWCVATSIAV---DGMMRSVDRVFKFIDLPSETPKPDKGKDSdliienv 1197
Cdd:COG4987 257 vLWLAAPLVAAGALSGPL-LALLVLAAlalFEALAPLPAAAqhlGRVRAAARRLNELLDAPPAVTEPAEPAPA------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1198 daqadsswPHRGQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWN 1276
Cdd:COG4987 329 --------PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdPQSGSITLGGVDLR 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1277 KMPLQKWRKAFGVVPQKVFIFTGPLRMNL---DPYGchSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQ 1353
Cdd:COG4987 401 DLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRPDA--TDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1354 LICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLLN 1433
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
....*...
gi 68390341 1434 ETSHLKQA 1441
Cdd:COG4987 559 QNGRYRQL 566
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
122-642 |
7.72e-53 |
|
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: 198.90 E-value: 7.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 122 YFLAFGLGLLFTARFLL--LQpaMFGLHHLGMQIRIALFSIIYKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMA 199
Cdd:COG2274 196 WVLAIGLLLALLFEGLLrlLR--SYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIREFLTGSL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 200 HFIWISPLQCILCTGLIWeLIDVN-SFCALAAISLLGVLQAFLSHKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGW 278
Cdd:COG2274 274 LTALLDLLFVLIFLIVLF-FYSPPlALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 279 EEIMETLIKNIRQDEVKLTRKIGSLR-YFYSSAYFFSAIF--VIVAAVVPHALSRGINLrrifTTLSYCMVLRMTVTR-- 353
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFKLRRLSnLLSTLSGLLQQLAtvALLWLGAYLVIDGQLTL----GQLIAFNILSGRFLApv 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 354 -QLPGSIQMWYDTMRLIWKIEEFLSKE-----EYKLMEYDLSITELELQDVTASWDEGPgellerikqenkanghhngda 427
Cdd:COG2274 429 aQLIGLLQRFQDAKIALERLDDILDLPpereeGRSKLSLPRLKGDIELENVSFRYPGDS--------------------- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 428 glfftnlyvAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTA 494
Cdd:COG2274 488 ---------PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 495 WIMPGTIRDNILFG---LTYDEyryksVVKACQ---LEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLY 568
Cdd:COG2274 559 FLFSGTIRENITLGdpdATDEE-----IIEAARlagLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRIL 633
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 569 LLDAPFTHLDIATEKEIFDKcLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSL 642
Cdd:COG2274 634 ILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
904-1171 |
9.13e-53 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 187.67 E-value: 9.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 904 ASSSGQTYAITVTPTSSYYILYIYVATSESLLAMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNR 983
Cdd:cd18604 26 ASAYETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 984 FTKDMATIDDMLPLLMFDFVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHL 1063
Cdd:cd18604 106 FSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1064 IMSLKGLWTIRAFERQAYFEALFHKTLNTHTATWFLYLSTLRWFLFRADILFVFFFTLAAWIAVGTNQDKPGEIGIIICL 1143
Cdd:cd18604 186 GETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPGIDAGLAGFSLSF 265
|
250 260
....*....|....*....|....*...
gi 68390341 1144 AMLILGTFQWCVATSIAVDGMMRSVDRV 1171
Cdd:cd18604 266 ALGFSSAILWLVRSYNELELDMNSVERI 293
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
860-1175 |
2.40e-52 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 187.00 E-value: 2.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 860 VLIFILFIAAIEIAGSVAGIFLITdeLWREEHqRSEPNMTKHSNASSSGQtyaITVTPTSSYYILyIYVATSESLLAMGF 939
Cdd:cd18599 4 VFLFVLLLFILSVGSTVFSDWWLS--YWLKQG-SGNTTNNVDNSTVDSGN---ISDNPDLNFYQL-VYGGSILVILLLSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 940 FRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFVQLTVVVVGCILVVSIV 1019
Cdd:cd18599 77 IRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1020 RPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQAYFEALFHKTLNTHTATWFL 1099
Cdd:cd18599 157 FPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1100 YLSTLRWFLFRADILFVFFFTLAAWIAVGT-NQDKPGEIGIIICLAMLILGTFQWCVATSIAVDGMMRSVDRVFKFI 1175
Cdd:cd18599 237 FNCAMRWLAVRLDILAVLITLITALLVVLLkGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
84-635 |
3.95e-50 |
|
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: 187.66 E-value: 3.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 84 LFGFLLYIGEATktvqpqLLGRIIAS-FDPAHEPERANGYFLAFGLGLLFTARFLLLQPAMfgLHHLGMQIRIALFSIIY 162
Cdd:COG4988 27 LLSGLLIIAQAW------LLASLLAGlIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERA--AFRAAARVKRRLRRRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 163 KKTLKLSSRVLDKISTGQLVSLMSANLGKFD--------QSLGMAhfiwISPLqCILCtgLIWeLIDVNSFCALAA-ISL 233
Cdd:COG4988 99 EKLLALGPAWLRGKSTGELATLLTEGVEALDgyfarylpQLFLAA----LVPL-LILV--AVF-PLDWLSGLILLVtAPL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 234 LGVLQAFLShkmgpYKAQKVlltNKR--LALTS------EIMENLHSVKAYGWEEIMetlIKNIRQ--DEVkltRKI--G 301
Cdd:COG4988 171 IPLFMILVG-----KGAAKA---SRRqwRALARlsghflDRLRGLTTLKLFGRAKAE---AERIAEasEDF---RKRtmK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 302 SLRY-FYSSAY--FFSAIFVIVAAVV--PHALSRGINLrriFTTLsycMVLRMTV-----TRQLpGSiqMWYDTMRLIW- 370
Cdd:COG4988 237 VLRVaFLSSAVleFFASLSIALVAVYigFRLLGGSLTL---FAAL---FVLLLAPefflpLRDL-GS--FYHARANGIAa 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 371 --KIEEFLSKEEYKLMEYDLSIT-----ELELQDVTASWDEGPgellerikqenkanghhngdaglfftnlyvaPVLKDI 443
Cdd:COG4988 308 aeKIFALLDAPEPAAPAGTAPLPaagppSIELEDVSFSYPGGR-------------------------------PALDGL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 444 SLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDNILFGLT 510
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRP 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 511 -YDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKc 589
Cdd:COG4988 437 dASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA- 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 68390341 590 LCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSE 635
Cdd:COG4988 516 LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1211-1421 |
8.85e-48 |
|
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: 168.33 E-value: 8.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTGPLRMNLdpygchsdeelwrvaeevglktvieqfpdkldfqleyggyvLSNGHKQLICLARSILSGARILL 1369
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1370 LDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQ 1421
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
393-643 |
1.25e-45 |
|
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: 174.57 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 393 LELQDVTASWDEGPgellerikqenkanghhngdaglfftnlyvAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILG 472
Cdd:COG4987 334 LELEDVSFRYPGAG------------------------------RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 473 ELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDNILFG---LTYDEYRykSVVKACQLEEDLAALPEKD 536
Cdd:COG4987 384 FLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLArpdATDEELW--AALERVGLGDWLAALPDGL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 537 KTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKcLCKLMASKTRILVTNKIEHLKRADKIL 616
Cdd:COG4987 462 DTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRIL 540
|
250 260
....*....|....*....|....*..
gi 68390341 617 LLHNGESFFYGTFPELQSERPDFSSLL 643
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
902-1171 |
8.42e-45 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 164.70 E-value: 8.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 902 SNASSSGQTYAITVTPTS------SYYILyIYVATSESLLAMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTM 975
Cdd:cd18602 26 TEANHDVASVVFNITSSSleddevSYYIS-VYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 976 KTGRIMNRFTKDMATIDDMLPLLMFDFVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEA 1055
Cdd:cd18602 105 PIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNIT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1056 RSPIFSHLIMSLKGLWTIRAFERQAYFEALFHKTLNTHTATWFLYLSTLRWFLFRADIL---FVFFFTLAAWIAVGTNQD 1132
Cdd:cd18602 185 KSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLgavIVFLAALSSLTAALAGYI 264
|
250 260 270
....*....|....*....|....*....|....*....
gi 68390341 1133 KPGEIGIIICLAMLILGTFQWCVATSIAVDGMMRSVDRV 1171
Cdd:cd18602 265 SPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERV 303
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1209-1422 |
2.03e-44 |
|
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: 160.83 E-value: 2.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1209 GQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLvY--TDGEISIDGVNWNKMPLQKWRKA 1286
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL-YkpTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQKVFIFTGPLRMNL---DPYgcHSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILS 1363
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 1364 GARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
437-622 |
3.54e-44 |
|
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: 157.93 E-value: 3.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRD 503
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSGTIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILfgltydeyryksvvkacqleedlaalpekdktpmaegglnlSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:cd03228 95 NIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 68390341 584 EIFDKcLCKLMASKTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:cd03228 134 LILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1209-1432 |
4.98e-43 |
|
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: 158.15 E-value: 4.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1209 GQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKWRKAF 1287
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVdIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKVFIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARI 1367
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1368 LLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLL 1432
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
430-621 |
8.58e-43 |
|
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: 155.95 E-value: 8.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 430 FFTNLYVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI-----------------RHSGRISYSSQ 492
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 493 TAWIMPGTIRDNILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:cd03290 87 KPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 573 PFTHLDIATEKEIFDKCLCKLMA--SKTRILVTNKIEHLKRADKILLLHNG 621
Cdd:cd03290 167 PFSALDIHLSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
856-1171 |
2.31e-42 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 157.26 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 856 SLLYVLIFILFIAAieiagSVAGIFLITDelWREEHQRSepnmtkhSNASSSGQTYAITVtptssyYILY-----IYVAT 930
Cdd:cd18603 1 SLLILLLYLLSQAF-----SVGSNIWLSE--WSDDPALN-------GTQDTEQRDYRLGV------YGALglgqaIFVFL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 931 SESLLAMGFFRGlpfvhttitiSKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFVQLTVVVV 1010
Cdd:cd18603 61 GSLALALGCVRA----------SRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1011 GCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQAYFEALFHKTL 1090
Cdd:cd18603 131 STLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1091 NTHTATWFLYLSTLRWFLFRADIL--FVFFFtlAAWIAV-GTNQDKPGEIGIIICLAMLILGTFQWCVATSIAVDGMMRS 1167
Cdd:cd18603 211 DENQRAYYPSIVSNRWLAVRLEFLgnLIVLF--AALFAVlSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVS 288
|
....
gi 68390341 1168 VDRV 1171
Cdd:cd18603 289 VERI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
861-1151 |
4.83e-42 |
|
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: 155.88 E-value: 4.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 861 LIFILFIAAIEIAGSVAGIFLITdelwreehqrsepNMTKHSNASSSGQTYAITVtptssYYILYIYVATSESLLAMGFF 940
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLG-------------RILDVLLPDGDPETQALNV-----YSLALLLLGLAQFILSFLQS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 941 RGlpFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFVQLTVVVVGCILVVSIVR 1020
Cdd:pfam00664 63 YL--LNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1021 PYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQAYFEALFHKTLNTHTATWFLY 1100
Cdd:pfam00664 141 WKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKK 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1101 LSTLRWFLFRADILFVFFFTLAAWIA---VGTNQDKPGEIGIIICLAMLILGTF 1151
Cdd:pfam00664 221 AVANGLSFGITQFIGYLSYALALWFGaylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
86-364 |
1.11e-41 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 155.30 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 86 GFLLYIGEATKTVQPQLLGRII----ASFDPAHEPERANGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSII 161
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLInfveDAYLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 162 YKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLiweLIdVN---SfcALAAISLL---G 235
Cdd:cd18597 83 YRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL---LI-VNlgpS--ALVGIGVLilsI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 236 VLQAFLSHKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYF-YSSAYFFS 314
Cdd:cd18597 157 PLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSIlTAVAFSLP 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 68390341 315 AIFVIVAAVVPHALSRGINLRRIFTTLSYCMVLRMTVTrQLPGSIQMWYD 364
Cdd:cd18597 237 VLASMLSFITYYATGHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLAD 285
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1209-1432 |
3.44e-41 |
|
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: 151.61 E-value: 3.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1209 GQIEVRNLTVKYTEaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLvY--TDGEISIDGVNWNKMPLQKWRKA 1286
Cdd:cd03254 1 GEIEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF-YdpQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQKVFIFTGPLRMNLDPYGCHSDEELW-RVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGA 1365
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1366 RILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLL 1432
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
918-1171 |
2.47e-40 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 151.47 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 918 TSSYYILyIYVATSESLLAMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPL 997
Cdd:cd18606 33 SQGFYIG-IYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 998 LMFDFVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFE 1077
Cdd:cd18606 112 SLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1078 RQAYFEALFHKTLNTHTATWFLYLSTLRWFLFRADI---LFVFFFTLAAwiAVGTNQDKPGEIGIIICLAMLILGTFQWC 1154
Cdd:cd18606 192 AQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLlgsLLVLIVALLC--VTRRFSISPSSTGLVLSYVLQITQVLSWL 269
|
250
....*....|....*..
gi 68390341 1155 VATSIAVDGMMRSVDRV 1171
Cdd:cd18606 270 VRQFAEVENNMNSVERL 286
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
98-361 |
3.74e-40 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 150.70 E-value: 3.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 98 VQPQLLGRIIASFDPAHEPErANGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSIIYKKTLKLSSRVLDKIS 177
Cdd:cd18595 15 ASPQLLKLLINFVEDPDEPL-WKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLSNSARKKST 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 178 TGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQAFLSHKMGPYKAQKVLLTN 257
Cdd:cd18595 94 VGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 258 KRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSSAYFFSAIFVIVAAVVPHALSRGINL--- 334
Cdd:cd18595 174 ERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNVlda 253
|
250 260
....*....|....*....|....*..
gi 68390341 335 RRIFTTLSYCMVLRMTVTrQLPGSIQM 361
Cdd:cd18595 254 EKAFVSLSLFNILRFPLS-MLPMVISN 279
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
431-618 |
3.03e-38 |
|
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: 151.67 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 431 FTNLYVA-----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQ 492
Cdd:TIGR02857 324 FSGVSVAypgrrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 493 TAWIMPGTIRDNILFGLTY-DEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLD 571
Cdd:TIGR02857 404 HPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68390341 572 APFTHLDIATEKEIFDKCLCkLMASKTRILVTNKIEHLKRADKILLL 618
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1200-1417 |
2.77e-37 |
|
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: 148.59 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1200 QADSSWPHRGQIEVRNLTVKYtEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKM 1278
Cdd:TIGR02857 311 KAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1279 PLQKWRKAFGVVPQKVFIFTGPLRMNL---DPYGchSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLI 1355
Cdd:TIGR02857 390 DADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1356 CLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMM 1417
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
82-351 |
4.19e-36 |
|
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: 138.54 E-value: 4.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 82 FLLFGFLLYIGEATKTVQPQLLGRIIASFDP--AHEPERANGYFLAFGLGLLFTARFLLLQPamFGLHHLGMQIRIALFS 159
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPdgDPETQALNVYSLALLLLGLAQFILSFLQS--YLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 160 IIYKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVN-SFCALAAISLLGVLQ 238
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 239 AFLSHKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSS-AYFFSAIF 317
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGiTQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 68390341 318 VIVAAVVPHAL--SRGINLRRIFTTLSYCMVLRMTV 351
Cdd:pfam00664 239 YALALWFGAYLviSGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
918-1175 |
7.18e-36 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 138.82 E-value: 7.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 918 TSSYYILYIYVATSESLLAmgFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPL 997
Cdd:cd18605 41 FNFFLTVYGFLAGLNSLFT--LLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 998 LMFDFVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFE 1077
Cdd:cd18605 119 ILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1078 RQAYFEALFHKTLNTHTATWFLYLSTLRWFLFRADIL--FVFFF--TLAAWIAVGTNQDKPGEIGIIICLAMLILGTFQW 1153
Cdd:cd18605 199 KQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLgvLIVTFvaLTAVVQHFFGLSIDAGLIGLALSYALPITGLLSG 278
|
250 260
....*....|....*....|..
gi 68390341 1154 CVATSIAVDGMMRSVDRVFKFI 1175
Cdd:cd18605 279 LLNSFTETEKEMVSVERVRQYF 300
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
438-621 |
1.89e-35 |
|
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: 135.02 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDN 504
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGLTY-DEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:cd03245 98 ITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 68390341 584 EIFDKcLCKLMASKTRILVTNKIEHLKRADKILLLHNG 621
Cdd:cd03245 178 RLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
438-632 |
9.12e-35 |
|
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: 133.12 E-value: 9.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI-----------RHSGR--ISYSSQTAWIMPGTIRDN 504
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRsmIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFG-LTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:cd03254 97 IRLGrPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 68390341 584 EIfDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPEL 632
Cdd:cd03254 177 LI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1211-1422 |
3.53e-34 |
|
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: 131.97 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYtEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLvY--TDGEISIDGVNWNKMPLQKWRKAFG 1288
Cdd:cd03253 1 IEFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF-YdvSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTGPLRMNLDpYGC--HSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGAR 1366
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIR-YGRpdATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 1367 ILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
431-635 |
4.58e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 431 FTNLYVA----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG--------RISYSSQTA---W 495
Cdd:COG1121 9 LENLTVSyggrPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRAevdW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 496 IMPGTIRDNILFGLT--------YDEYRYKSVVKAcqLE----EDLAalpekdKTPMAEgglnLSGGQKARVALARAVYR 563
Cdd:COG1121 89 DFPITVRDVVLMGRYgrrglfrrPSRADREAVDEA--LErvglEDLA------DRPIGE----LSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 564 DADLYLLDAPFTHLDIATEKEIFDkCLCKL-MASKTRILVTNKIEHLKR-ADKILLLhNGESFFYGTFPELQSE 635
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYE-LLRELrREGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVLTP 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1211-1440 |
5.00e-34 |
|
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: 130.92 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLF---NALLKlvYTDGEISIDGVNWNKMPLQKWRKAF 1287
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLrllNGLLK--PTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQ---------KVF---IFtGPLRMNLDPygchsdEELWRVAEEVgLKTV-IEQFPDKLDFQLeyggyvlSNGHKQL 1354
Cdd:COG1122 78 GLVFQnpddqlfapTVEedvAF-GPENLGLPR------EEIRERVEEA-LELVgLEHLADRPPHEL-------SGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1355 ICLArSILS-GARILLLDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQKL 1431
Cdd:COG1122 143 VAIA-GVLAmEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
....*....
gi 68390341 1432 LNETSHLKQ 1440
Cdd:COG1122 222 FSDYELLEE 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
437-622 |
7.47e-34 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 128.49 E-value: 7.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR-------------HSGRISYSSQTAWIMPGTIRD 503
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwdpneLGDHVGYLPQDDELFSGSIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILfgltydeyryksvvkacqleedlaalpekdktpmaegglnlSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:cd03246 95 NIL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 68390341 584 EIFDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGR 172
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
975-1403 |
1.32e-33 |
|
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: 137.49 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 975 MKTGRIMNRFTKDMATIDDMLPLLMFD-FVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLET 1053
Cdd:TIGR02868 107 LRRGDLLGRLGADVDALQDLYVRVIVPaGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1054 EARSPIFSHLIMSLKGLWTIRAFERQAYFEALFHKTLNTHTA-----TWFLYLSTlrwflfrADILFVFFFTLAAWIAVG 1128
Cdd:TIGR02868 187 RLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRaerraAAATALGA-------ALTLLAAGLAVLGALWAG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1129 TNQDKPGEIG--IIICLAMLILGTFQWCVATSIAVDGMMR---SVDRVFKFIDLPSETPKPdkgkdsdliienVDAQADS 1203
Cdd:TIGR02868 260 GPAVADGRLApvTLAVLVLLPLAAFEAFAALPAAAQQLTRvraAAERIVEVLDAAGPVAEG------------SAPAAGA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1204 SWPHRGQIEVRNLTVKYtEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYT-DGEISIDGVNWNKMPLQK 1282
Cdd:TIGR02868 328 VGLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPlQGEVTLDGVPVSSLDQDE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVPQKVFIFTGPLRMNLDpYGCH--SDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARS 1360
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDTTVRENLR-LARPdaTDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARA 485
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 68390341 1361 ILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEH 1403
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1211-1422 |
6.77e-33 |
|
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: 128.12 E-value: 6.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTGPLRMNLdPYGCH--SDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARI 1367
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1368 LLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
431-627 |
2.08e-32 |
|
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: 125.72 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 431 FTNLYVA----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG--------RISYSSQTA---W 495
Cdd:cd03235 2 VEDLTVSygghPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRsidR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 496 IMPGTIRDNILFGLTYD---EYRYKSVVKACqLEEDLAA--LPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLL 570
Cdd:cd03235 82 DFPISVRDVVLMGLYGHkglFRRLSKADKAK-VDEALERvgLSELADRQIGE----LSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 571 DAPFTHLDIATEKEIFD--KCLCKLmaSKTRILVTNKIEHLKR-ADKILLLhNGESFFYG 627
Cdd:cd03235 157 DEPFAGVDPKTQEDIYEllRELRRE--GMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
393-603 |
3.09e-32 |
|
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: 133.64 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 393 LELQDVTASWDEGPgellerikqenkanghhngdaglfftnlyvaPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILG 472
Cdd:TIGR02868 335 LELRDLSAGYPGAP-------------------------------PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 473 ELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDNILFG---LTYDEYRykSVVKACQLEEDLAALPEKD 536
Cdd:TIGR02868 384 LLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLArpdATDEELW--AALERVGLADWLRALPDGL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 537 KTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKcLCKLMASKTRILVT 603
Cdd:TIGR02868 462 DTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLIT 527
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1211-1422 |
1.00e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 132.66 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLK-LVYTdGEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:PRK11174 350 IEAEDLEILSPD-GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPYQ-GSLKINGIELRELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTGPLRMNL---DPYGchSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGAR 1366
Cdd:PRK11174 428 VGQNPQLPHGTLRDNVllgNPDA--SDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 1367 ILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
438-628 |
1.05e-31 |
|
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: 124.14 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDN 504
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 I-LFGLTYDEYRYkSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:cd03244 98 LdPFGEYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 584 EIFdKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGT 628
Cdd:cd03244 177 LIQ-KTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
440-575 |
1.14e-31 |
|
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: 121.60 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR-------------HSGRISYSSQTAWIMPG-TIRDNI 505
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 506 LFGLtyDEYRYKSVVKACQLEEDLAALPEKD--KTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFT 575
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1212-1421 |
1.16e-31 |
|
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: 123.73 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1212 EVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKWRKAFGVV 1290
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGpTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1291 PQ---------KVF--IFTGPLRMNLDPYgcHSDEELWRVAEEVGLKTVIEQFPdkldfqleyggYVLSNGHKQLICLAr 1359
Cdd:cd03225 81 FQnpddqffgpTVEeeVAFGLENLGLPEE--EIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIA- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1360 SILS-GARILLLDEPSAHLDPVTIKVLKKTLRQSFSTC-TILLSEHKVEPLLE-CQSFLMMDKGQ 1421
Cdd:cd03225 147 GVLAmDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
438-632 |
2.71e-31 |
|
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: 123.49 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-------------ISYSSQTAWIMPGTIRDN 504
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGL---TYDEYRykSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:cd03251 96 IAYGRpgaTREEVE--EAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 582 EKEIfDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPEL 632
Cdd:cd03251 174 ERLV-QAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
431-642 |
2.83e-31 |
|
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: 123.49 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 431 FTNLYVA-----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR-----------HSGR--ISYSSQ 492
Cdd:cd03253 3 FENVTFAydpgrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRraIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 493 TAWIMPGTIRDNILFG-LTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLD 571
Cdd:cd03253 83 DTVLFNDTIGYNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 572 APFTHLDIATEKEIFdKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSL 642
Cdd:cd03253 163 EATSALDTHTEREIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1197-1432 |
6.68e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 129.94 E-value: 6.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1197 VDAQADSSWPH-------RGQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNaLLKLVY--TDGE 1267
Cdd:PRK11160 318 TEQKPEVTFPTtstaaadQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ-LLTRAWdpQQGE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1268 ISIDGVnwnkmPLQKW-----RKAFGVVPQKVFIFTGPLRMNL---DPYGchSDEELWRVAEEVGLKTVIEQfPDKLDFQ 1339
Cdd:PRK11160 397 ILLNGQ-----PIADYseaalRQAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEKLLED-DKGLNAW 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1340 LEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDK 1419
Cdd:PRK11160 469 LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDN 548
|
250
....*....|...
gi 68390341 1420 GQVKTYDSIQKLL 1432
Cdd:PRK11160 549 GQIIEQGTHQELL 561
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
437-621 |
9.48e-31 |
|
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: 129.48 E-value: 9.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-------------ISYSSQTAWIMPGTIRD 503
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NI-LFGLTYDEyrykSVVKACQL---EEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:COG4618 425 NIaRFGDADPE----KVVAAAKLagvHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 580 ATEKeifdkclcKLMAS--------KTRILVTNKIEHLKRADKILLLHNG 621
Cdd:COG4618 501 EGEA--------ALAAAiralkargATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
438-636 |
1.39e-30 |
|
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: 121.49 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI-------------RHSGRISYSSQTAWIMPGTIRDN 504
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGLTYDEYryKSVVKACQL---EEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:cd03249 97 IRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 582 EKEIFDKcLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSER 636
Cdd:cd03249 175 EKLVQEA-LDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
437-643 |
2.45e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 128.42 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELvPSSGKIRHSG-------RISYSSQTAWI------MPGTIRD 503
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldPESWRKHLSWVgqnpqlPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFG-LTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATE 582
Cdd:PRK11174 442 NVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 583 KEIFdKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSLL 643
Cdd:PRK11174 522 QLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1228-1375 |
4.68e-30 |
|
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: 116.98 E-value: 4.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1228 LKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTG-----PL 1301
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTeGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRltvreNL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1302 RMNLDPYGC---HSDEELWRVAEEVGLktvieqfPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSA 1375
Cdd:pfam00005 81 RLGLLLKGLskrEKDARAEEALEKLGL-------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1211-1422 |
7.46e-30 |
|
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: 117.11 E-value: 7.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLqKWRKAFGV 1289
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIKVLGKDIKKEPE-EVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFtgplrmnldpygchsdEELwrvaeevglkTVIEQFpdkldfqleyggyVLSNGHKQLICLARSILSGARILL 1369
Cdd:cd03230 78 LPEEPSLY----------------ENL----------TVRENL-------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1370 LDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVEPLLE-CQSFLMMDKGQV 1422
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1211-1435 |
1.50e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 118.24 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPlQKWRKAFGV 1289
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLGEDVARDP-AEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFI---FTGplRMNLDPYGC---HSDEELWRVAEEVgLKTV-IEQFPDKLdfqleYGGYvlSNGHKQLICLARSIL 1362
Cdd:COG1131 78 VPQEPALypdLTV--RENLRFFARlygLPRKEARERIDEL-LELFgLTDAADRK-----VGTL--SGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 1363 SGARILLLDEPSAHLDPVTIKVLKKTLRQSFST-CTILLSEHkvepLLE-----CQSFLMMDKGQVKTYDSIQKLLNET 1435
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTH----YLEeaerlCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1212-1421 |
1.61e-29 |
|
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: 115.42 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1212 EVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKWRKAFGVV 1290
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1291 PQkvfiftgplrmnldpygchsdeelwrvaeevglktvieqfpdkldfqleyggyvLSNGHKQLICLARSILSGARILLL 1370
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1371 DEPSAHLDPVTIKVLKKTLRQSFST-CTILLSEHKVEPLLE-CQSFLMMDKGQ 1421
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1211-1437 |
2.41e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 118.04 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPLqKWRKAFGV 1289
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsGSILIDGEDVRKEPR-EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTGP-LRMNLDPYGchsdeELWRVAEEVgLKTVIEQFPDKLDFQLEYGGYV--LSNGHKQLICLARSILSGAR 1366
Cdd:COG4555 79 LPDERGLYDRLtVRENIRYFA-----ELYGLFDEE-LKKRIEELIELLGLEEFLDRRVgeLSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1367 ILLLDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQKLLNETSH 1437
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1211-1422 |
5.74e-29 |
|
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: 116.87 E-value: 5.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKY-TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLvY--TDGEISIDGVNWNKMPLQKWRKAF 1287
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-YdpTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKVFIFTGPLRMNLDpYGCHS--DEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGA 1365
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIR-YGKPDatDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1366 RILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
438-622 |
2.10e-28 |
|
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: 112.34 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRisyssQTAWIMPGTIRDNILFgltydeyryk 517
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIGY---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 518 svvkacqleedlaaLPEkdktpmaegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKcLCKLMAS- 596
Cdd:cd00267 78 --------------VPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL-LRELAEEg 130
|
170 180
....*....|....*....|....*..
gi 68390341 597 KTRILVTNKIEHLKRA-DKILLLHNGE 622
Cdd:cd00267 131 RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
433-627 |
1.85e-27 |
|
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: 110.60 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 433 NLYVA----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRhsgrisyssqtawimpgtirdniLFG 508
Cdd:cd03214 4 NLSVGyggrTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-----------------------LDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 509 LTYDEYRYKSVVKAC----QLEEDLAALPEKDKtPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKE 584
Cdd:cd03214 61 KDLASLSPKELARKIayvpQALELLGLAHLADR-PFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 68390341 585 IFDKcLCKLMAS--KTRILVTNKIEH-LKRADKILLLHNGESFFYG 627
Cdd:cd03214 136 LLEL-LRRLARErgKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
438-642 |
1.88e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 119.16 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-------------ISYSSQTAWIMPGTIRDN 504
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGL-TYDEYRYKSVVKacQLEedLAALPEKDK---TPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:PRK11160 434 LLLAApNASDEALIEVLQ--QVG--LEKLLEDDKglnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 581 TEKEIFDkCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSL 642
Cdd:PRK11160 510 TERQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
98-366 |
2.35e-27 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 114.13 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 98 VQPQLLGRIIASFDPAHEPERANGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSIIYKKTLKL--------- 168
Cdd:cd18596 15 APPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssks 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 169 ----------SSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQ 238
Cdd:cd18596 95 seskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 239 AFLSHKMgpYKAQKVLL--TNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSSAYFFSAI 316
Cdd:cd18596 175 GYLAKRY--SRAQKELMkaRDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPI 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 317 FVIVAAVVPHALSRGINLR--RIFTTLSYCMVLRMTVtRQLPGSIQMWYDTM 366
Cdd:cd18596 253 LVTVVTFATYTLVMGQELTasVAFTSLALFNMLRGPL-NVLPELITQLLQAK 303
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
78-342 |
2.65e-27 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 113.87 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 78 YIKPFLLFGFLLYIGEATktvQPQLLGRIIASFDPAHEPE-RANGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIA 156
Cdd:cd18591 14 FVGPLCISGIVDYVEENT---YSSSNSTDKLSVSYVTVEEfFSNGYVLAVILFLALLLQATFSQASYHIVIREGIRLKTA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 157 LFSIIYKKTLKLSSRVLD--KISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLL 234
Cdd:cd18591 91 LQAMIYEKALRLSSWNLSsgSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 235 GVLQAFLSHKMGpyKAQKVLL--TNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIgslrYFYSSAYF 312
Cdd:cd18591 171 TPLQYLIARKLS--KNQKSTLeySDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKD----AVYWSLMT 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 68390341 313 F----SAIFVIVAAVVPHALSRGINLR--RIFTTLS 342
Cdd:cd18591 245 FltqaSPILVTLVTFGLYPYLEGEPLTaaKAFSSLA 280
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
438-622 |
2.91e-27 |
|
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: 111.02 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAW---------------IMPgTI 501
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdLTKLSLKELrrkvglvfqnpddqfFGP-TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGL---TYDEYRYKSVVKACQLEEDLAALpeKDKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:cd03225 94 EEEVAFGLenlGLPEEEIEERVEEALELVGLEGL--RDRSP-----FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 68390341 579 IATEKEIFDKcLCKLMAS-KTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:cd03225 167 PAGRRELLEL-LKKLKAEgKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
438-622 |
4.77e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.29 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDN 504
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGLTYDEYRYKSVvkacQLEEDLAA--LPEKD-KTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:COG4619 94 LPFPFQLRERKFDRE----RALELLERlgLPPDIlDKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68390341 582 eKEIFDKCLCKLMASKTR--ILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:COG4619 166 -TRRVEELLREYLAEEGRavLWVSHDPEQIERvADRVLTLEAGR 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
438-644 |
7.77e-27 |
|
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: 110.72 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAW-----IMPG--------TIRDN 504
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqigVLPDerglydrlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 I-LFGLTYD------EYRYKSVVKACQLEEDLaalpeKDKTpmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:COG4555 95 IrYFAELYGlfdeelKKRIEELIELLGLEEFL-----DRRV------GELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 578 DIATeKEIFDKCLCKLMASKTRILVT----NKIEHLkrADKILLLHNGESFFYGTFPELQSE--RPDFSSLLL 644
Cdd:COG4555 164 DVMA-RRLLREILRALKKEGKTVLFSshimQEVEAL--CDRVVILHKGKVVAQGSLDELREEigEENLEDAFV 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
438-628 |
1.27e-26 |
|
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: 110.52 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAwIMPG--TIR 502
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEP-PAPFglTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 503 DNILFGLT--------YDEYRYKSVVKAcqLEE-DLAALPEKdktPMAEgglnLSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:COG1120 94 ELVALGRYphlglfgrPSAEDREAVEEA--LERtGLEHLADR---PVDE----LSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 574 FTHLDIATEKEIFDkcLCKLMAS---KTRILVTNKIEHLKR-ADKILLLHNGESFFYGT 628
Cdd:COG1120 165 TSHLDLAHQLEVLE--LLRRLARergRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1211-1422 |
2.08e-26 |
|
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: 107.30 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTGPLRMNldpygchsdeelwrvaeevglktvieqfpdkldfqleyggyVLSNGHKQLICLARSILSGARILL 1369
Cdd:cd03246 81 LPQDDELFSGSIAEN-----------------------------------------ILSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1370 LDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
84-342 |
3.45e-26 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 110.33 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 84 LFGFLLYIGEATKTVQPQLLGRIIASFDPAHEPERaNGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSIIYK 163
Cdd:cd18598 1 PLGLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLS-DGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 164 KTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQAFLSH 243
Cdd:cd18598 80 KALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 244 KMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLR----YFYSSA-YFFSAIFV 318
Cdd:cd18598 160 RIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDalcvYFWATTpVLISILTF 239
|
250 260
....*....|....*....|....
gi 68390341 319 IVAAVVPHALSRGinlrRIFTTLS 342
Cdd:cd18598 240 ATYVLMGNTLTAA----KVFTSLA 259
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
437-621 |
3.53e-26 |
|
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: 107.99 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDN 504
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQDYALFPHlTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKE 584
Cdd:cd03259 93 IAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 68390341 585 IFDKcLCKLMAS--KTRILVT-NKIEHLKRADKILLLHNG 621
Cdd:cd03259 169 LREE-LKELQRElgITTIYVThDQEEALALADRIAVMNEG 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1212-1422 |
5.53e-26 |
|
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: 106.37 E-value: 5.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1212 EVRNLTVKYTeaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKWRKAFGVV 1290
Cdd:cd03214 1 EVENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1291 PQkvfiftgplrmnldpygchsdeelwrVAEEVGlktvIEQFPDKlDFQleyggyVLSNGHKQLICLARSILSGARILLL 1370
Cdd:cd03214 79 PQ--------------------------ALELLG----LAHLADR-PFN------ELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 1371 DEPSAHLDPV-TIKVLK--KTLRQSFStCTILLSEHKVEP-LLECQSFLMMDKGQV 1422
Cdd:cd03214 122 DEPTSHLDIAhQIELLEllRRLARERG-KTVVMVLHDLNLaARYADRVILLKDGRI 176
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
438-632 |
8.27e-26 |
|
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: 107.42 E-value: 8.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRiSYSSQTAW-----------------IMPgT 500
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK-DITKKNLRelrrkvglvfqnpddqlFAP-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFGLT---YDEYRYKSVVKACqLEE-DLAALpeKDKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTH 576
Cdd:COG1122 93 VEEDVAFGPEnlgLPREEIRERVEEA-LELvGLEHL--ADRPP-----HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 577 LDIATEKEIFDkCLCKLMAS-KTRILVTNKIEHL-KRADKILLLHNGESFFYGTFPEL 632
Cdd:COG1122 165 LDPRGRRELLE-LLKRLNKEgKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
936-1432 |
1.13e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 114.04 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 936 AMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMlpllmfdFVQLTVVVVGCILV 1015
Cdd:PRK10790 80 GLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDL-------YVTVVATVLRSAAL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1016 VSIVRPYIF-----LAATPLAI---IFIVMRKYflrtgQQLKqletearSPI--------------FSHLImslKGLWTI 1073
Cdd:PRK10790 153 IGAMLVAMFsldwrMALVAIMIfpaVLVVMVIY-----QRYS-------TPIvrrvrayladindgFNEVI---NGMSVI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1074 RAFERQAYFEAlfhKTLNTHTATWFLYLSTLRW--FLFR-----------ADILFVFFFTLAAWIAVGT---------NQ 1131
Cdd:PRK10790 218 QQFRQQARFGE---RMGEASRSHYMARMQTLRLdgFLLRpllslfsalilCGLLMLFGFSASGTIEVGVlyafisylgRL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1132 DKPgeigiiiclamLILGTFQWCVATSIAVDGmmrsvDRVFKFIDlpseTPKPDKGKDSdliienvdaQADSSwphrGQI 1211
Cdd:PRK10790 295 NEP-----------LIELTTQQSMLQQAVVAG-----ERVFELMD----GPRQQYGNDD---------RPLQS----GRI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1212 EVRNLTVKYTEaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLK-LVYTDGEISIDGVNWNKMPLQKWRKAFGVV 1290
Cdd:PRK10790 342 DIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGyYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1291 PQKVFIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLL 1370
Cdd:PRK10790 421 QQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1371 DEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLL 1432
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
438-627 |
2.16e-25 |
|
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: 104.32 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG------------RISYSSQTAWIMPGTIRDNI 505
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLRNNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 lfgltydeyryksvvkacqleedlaalpekdktpmaegGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEI 585
Cdd:cd03247 96 --------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68390341 586 FdKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYG 627
Cdd:cd03247 138 L-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
438-622 |
2.33e-25 |
|
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: 105.65 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAWI----------------MPG- 499
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdISKLSEKELAafrrrhigfvfqsfnlLPDl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIRDNILFGLTY-------DEYRYKSVVKACQLEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:cd03255 98 TALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPSE-----------LSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 573 PFTHLDIATEKEIFDKcLCKL--MASKTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:cd03255 167 PTGNLDSETGKEVMEL-LRELnkEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1212-1420 |
2.70e-25 |
|
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: 105.31 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1212 EVRNLTVKYTeaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGvnwnkMPLQKWRKAFGVV 1290
Cdd:cd03235 1 EVEDLTVSYG--GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1291 PQK-VFIFTGPLR------MNLDPYGCHS---DEELWRVAEEVgLKTV-IEQFPDKldfQL-EyggyvLSNGHKQLICLA 1358
Cdd:cd03235 74 PQRrSIDRDFPISvrdvvlMGLYGHKGLFrrlSKADKAKVDEA-LERVgLSELADR---QIgE-----LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1359 RSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVEPLLE-CQSFLMMDKG 1420
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
439-642 |
3.10e-25 |
|
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: 106.03 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDNI 505
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 lfGLTYDEYRYKSVVKACQL---EEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATE 582
Cdd:cd03252 97 --ALADPGMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 583 KEIFDKcLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSL 642
Cdd:cd03252 175 HAIMRN-MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1211-1422 |
7.36e-25 |
|
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: 104.51 E-value: 7.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAV--LKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMP---LQKWR 1284
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1285 KAFGVVPQKVF-----------IFTGPLRMNLDPygcHSDEELWRVA----EEVGLKtviEQFPDKLDFQleyggyvLSN 1349
Cdd:cd03257 82 KEIQMVFQDPMsslnprmtigeQIAEPLRIHGKL---SKKEARKEAVllllVGVGLP---EEVLNRYPHE-------LSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 1350 GHKQLICLARSILSGARILLLDEPSAHLDPVT----IKVLKKtLRQSFSTcTILLSEHKVEPLLE-CQSFLMMDKGQV 1422
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKK-LQEELGL-TLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1211-1422 |
7.80e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.17 E-value: 7.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGvnwnkMPLQKWRKAFGV 1289
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLpPTSGTVRLFG-----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFI---FtgPLR------MNLDPYG---CHSDEELWRVAEEVgLKTV-IEQFPDKLdfqleYGGyvLSNGHKQLIC 1356
Cdd:COG1121 80 VPQRAEVdwdF--PITvrdvvlMGRYGRRglfRRPSRADREAVDEA-LERVgLEDLADRP-----IGE--LSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 1357 LARSILSGARILLLDEPSAHLDPVT----IKVLKKtLRQsfSTCTILLSEHKVEPLLE-CQSFLMMDKGQV 1422
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATeealYELLRE-LRR--EGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
918-1440 |
1.49e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 110.97 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 918 TSSYYILYIYVATSeSLLAmgFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPL 997
Cdd:TIGR00958 201 ASAIFFMCLLSIAS-SVSA--GLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 998 LMFDFVQLTVVVVGCILVVSIVRPYI-FLAATPLAIIFIVMRKYFLRTGQQLKQL-ETEARSPIFSHLIMSlkGLWTIRA 1075
Cdd:TIGR00958 278 NVNVLLRNLVMLLGLLGFMLWLSPRLtMVTLINLPLVFLAEKVFGKRYQLLSEELqEAVAKANQVAEEALS--GMRTVRS 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1076 F-----ERQAYFEALFH-KTLNTHTA-TWFLYLSTLRwflfradILFVFFFTLAAWIAVGTNQDKPGEIGIIICLAMLIL 1148
Cdd:TIGR00958 356 FaaeegEASRFKEALEEtLQLNKRKAlAYAGYLWTTS-------VLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1149 GTFQWCVATSIAVDGMMRSV---DRVFKFIDLPSETPKPDKGKDSDLiienvdaqadsswphRGQIEVRNLTVKY-TEAG 1224
Cdd:TIGR00958 429 QLGEAVRVLSYVYSGMMQAVgasEKVFEYLDRKPNIPLTGTLAPLNL---------------EGLIEFQDVSFSYpNRPD 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1225 HAVLKNLSFSAEGRQRVGILGRTGSGKSSLFnALLKLVY--TDGEISIDGVnwnkmPLQKW-----RKAFGVVPQKVFIF 1297
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVA-ALLQNLYqpTGGQVLLDGV-----PLVQYdhhylHRQVALVGQEPVLF 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1298 TGPLRMNLdPYGCHS--DEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSA 1375
Cdd:TIGR00958 568 SGSVRENI-AYGLTDtpDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1376 HLDpVTIKVLKKTLRqSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLLNETSHLKQ 1440
Cdd:TIGR00958 647 ALD-AECEQLLQESR-SRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
437-622 |
1.74e-24 |
|
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: 101.88 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG---------------RISYSSQTAWIMPG-T 500
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFGLtydeyryksvvkacqleedlaalpekdktpmaegglnlSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:cd03229 93 VLENIALGL--------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 581 TEKEIFD--KCLCKlMASKTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:cd03229 135 TRREVRAllKSLQA-QLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
431-622 |
2.66e-24 |
|
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: 103.03 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 431 FTNLYVAP----VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTI-----LGELVPSSGKIRHSGRISYSS---------- 491
Cdd:cd03260 3 LRDLNVYYgdkhALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLdvdvlelrrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 492 -----QTAWIMPGTIRDNILFGLTYDEYRYKSVVKAcqLEEDL---AALPE--KDKTpmaeGGLNLSGGQKARVALARAV 561
Cdd:cd03260 83 vgmvfQKPNPFPGSIYDNVAYGLRLHGIKLKEELDE--RVEEAlrkAALWDevKDRL----HALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 562 YRDADLYLLDAPFTHLD-IATEKeiFDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:cd03260 157 ANEPEVLLLDEPTSALDpISTAK--IEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1211-1422 |
2.71e-24 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 103.35 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKM---PLQKWRKA 1286
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDISGLseaELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQKVFIFTG---------PLRMNLDpygcHSDEELWRVAEE----VGLKTVIEQFPDKLdfqleyggyvlSNGHKQ 1353
Cdd:cd03261 79 MGMLFQSGALFDSltvfenvafPLREHTR----LSEEEIREIVLEkleaVGLRGAEDLYPAEL-----------SGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1354 LICLARSILSGARILLLDEPSAHLDPVTIKV---LKKTLRQSFSTCTILLSeHKVEPLLE-CQSFLMMDKGQV 1422
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGViddLIRSLKKELGLTSIMVT-HDLDTAFAiADRIAVLYDGKI 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
437-618 |
2.93e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.54 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG--RISYSSQ---TAWIMPGTIRDNILFG--- 508
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQrseVPDSLPLTVRDLVAMGrwa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 509 -------LTYDEYRyksVVKACQLEEDLAALpekDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:NF040873 85 rrglwrrLTRDDRA---AVDDALERVGLADL---AGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68390341 582 EKEIFDkclckLMASKTR-----ILVTNKIEHLKRADKILLL 618
Cdd:NF040873 155 RERIIA-----LLAEEHArgatvVVVTHDLELVRRADPCVLL 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
438-580 |
4.47e-24 |
|
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: 101.79 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG------RISYSSQTAWIMPG-------TIRDN 504
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHAdglkpelTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILF-----GLTYDEYRYKSVVKACQLeEDLAALPEKdktpmaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:COG4133 96 LRFwaalyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
.
gi 68390341 580 A 580
Cdd:COG4133 165 A 165
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
438-635 |
4.72e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 102.45 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG------------RISYSSQTAWIMPG-TIRDN 504
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 I-----LFGLTYDEY--RYKSVVKACQLEEDLaalpekdKTPMAegglNLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:COG1131 94 LrffarLYGLPRKEAreRIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 578 DIATEKEIFDkCLCKLMASKTRILVT----NKIEHLkrADKILLLHNGESFFYGTFPELQSE 635
Cdd:COG1131 163 DPEARRELWE-LLRELAAEGKTVLLSthylEEAERL--CDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1211-1421 |
6.34e-24 |
|
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: 101.01 E-value: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEA---GHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLK-LVYTDGEISIDGvnwnkmplqkwrkA 1286
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQKVFIFTGPLRMNL---DPYgchsDEE-LWRVAEEVGLKTVIEQFPDKLdfQLEYG--GYVLSNGHKQLICLARS 1360
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPF----DEErYEKVIKACALEPDLEILPDGD--LTEIGekGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 1361 ILSGARILLLDEPSAHLDPVT---I--KVLKKTLRQSfstCTILLSEHKVEPLLECQSFLMMDKGQ 1421
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVgrhIfeNCILGLLLNN---KTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1211-1423 |
9.87e-24 |
|
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: 99.69 E-value: 9.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLK-LVYTDGEISIDGVNWNKmpLQK-WRKAFG 1288
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSD--LEKaLSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTGPLRMNLdpygchsdeelwrvaeevglktvieqfpdkldfqleygGYVLSNGHKQLICLARSILSGARIL 1368
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1369 LLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVK 1423
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1211-1436 |
9.96e-24 |
|
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: 101.79 E-value: 9.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTGPLRMNL---DPygCHSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGAR 1366
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1367 ILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLLNETS 1436
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1211-1457 |
1.16e-23 |
|
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: 106.91 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV----YTDGEISIDGVNWNKMPLQKWRKA 1286
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQKVFIFTGPLR---------MNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKldfqleyggyvLSNGHKQLICL 1357
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1358 ARSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQSFSTcTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQKLLN 1433
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGT-TVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
250 260
....*....|....*....|....
gi 68390341 1434 ETSHLKQAISPAERLKLFPRRNSS 1457
Cdd:COG1123 233 APQALAAVPRLGAARGRAAPAAAA 256
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
439-621 |
1.21e-23 |
|
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: 100.79 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDNIL 506
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMVFQNYALYPHmTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 507 FGLTYDEY-------RYKSVVKACQLEEDLaalpekDKTPMAegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLD- 578
Cdd:cd03301 95 FGLKLRKVpkdeideRVREVAELLQIEHLL------DRKPKQ-----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDa 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68390341 579 ---IATEKEIfdKCLCKLMaSKTRILVT-NKIEHLKRADKILLLHNG 621
Cdd:cd03301 164 klrVQMRAEL--KRLQQRL-GTTTIYVThDQVEAMTMADRIAVMNDG 207
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
431-639 |
1.49e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 101.04 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 431 FTNLYVA----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG----------------RISYS 490
Cdd:cd03261 3 LRGLTKSfggrTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 491 SQTAWI---MpgTIRDNILFGL----TYDEYRYKSVVKACqleedLAAL---PEKDKTPmAEgglnLSGGQKARVALARA 560
Cdd:cd03261 83 FQSGALfdsL--TVFENVAFPLrehtRLSEEEIREIVLEK-----LEAVglrGAEDLYP-AE----LSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 561 VYRDADLYLLDAPFTHLD-IATEKeiFDKCLCKLMASK--TRILVTNKIEHLKR-ADKILLLHNGESFFYGTFPELQSER 636
Cdd:cd03261 151 LALDPELLLYDEPTAGLDpIASGV--IDDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASD 228
|
...
gi 68390341 637 PDF 639
Cdd:cd03261 229 DPL 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1211-1434 |
2.51e-23 |
|
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: 100.89 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLkPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKvFIFTGPL---------RMN-LDPYGCHSDEElWRVAEEVgLKTV-IEQFPDKldfqleyggYV--LSNGHKQLIC 1356
Cdd:COG1120 80 VPQE-PPAPFGLtvrelvalgRYPhLGLFGRPSAED-REAVEEA-LERTgLEHLADR---------PVdeLSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1357 LARSILSGARILLLDEPSAHLDPV-TIKVLkKTLRQSFST--CTILLSEHKVE-PLLECQSFLMMDKGQVKTYDSIQKLL 1432
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAhQLEVL-ELLRRLARErgRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
..
gi 68390341 1433 NE 1434
Cdd:COG1120 227 TP 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1211-1434 |
2.91e-23 |
|
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: 99.82 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAghAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKwRKAFGV 1289
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 --VPQKVFIFTG-----PLRMNLdpYGCHSDEELWRVAEevglktVIEQFPDKLDFQLEYGGyVLSNGHKQLICLARSIL 1362
Cdd:cd03224 78 gyVPEGRRIFPEltveeNLLLGA--YARRRAKRKARLER------VYELFPRLKERRKQLAG-TLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1363 SGARILLLDEPSAHLDPVTIKVLKKTLRQ--SFSTcTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQKLLNE 1434
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRElrDEGV-TILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
438-620 |
3.11e-23 |
|
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: 99.47 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR--------HSGRISYSSQTAWIMP-GTIRDNILFG 508
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgPGPDRGYVFQQDALLPwLTVLDNVALG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 509 LtydeyRYKSVVKACQLEEDLAALpekdktpmAEGGLN---------LSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:cd03293 98 L-----ELQGVPKAEARERAEELL--------ELVGLSgfenayphqLSGGMRQRVALARALAVDPDVLLLDEPFSALDA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 68390341 580 ATEKEIFDKcLCKLMAS--KTRILVTNKIE---HLkrADKILLLHN 620
Cdd:cd03293 165 LTREQLQEE-LLDIWREtgKTVLLVTHDIDeavFL--ADRVVVLSA 207
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
959-1442 |
4.12e-23 |
|
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: 106.36 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 959 KMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFVQLTVVVVGcilvvSIVRPY-------IFLAATPLA 1031
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIV-----GLFLVRqnmllflLSLLSIPVY 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1032 IIFIVMrkyFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAF--ERQAY------FEALFHKTL-NTHTATWFLYLS 1102
Cdd:TIGR01193 309 AVIIIL---FKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLtsEAERYskidseFGDYLNKSFkYQKADQGQQAIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1103 TLRWFlfradILFVFFFTLAAwIAVGTNQDKPGEIGIIICLAMLILGTFQWCVATSIAVDGMMRSVDRVFKFIDLPSEtp 1182
Cdd:TIGR01193 386 AVTKL-----ILNVVILWTGA-YLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSE-- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1183 KPDKGKDSDLIIENvdaqadsswphrGQIEVRNLTVKYTeAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV 1262
Cdd:TIGR01193 458 FINKKKRTELNNLN------------GDIVINDVSYSYG-YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1263 Y-TDGEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLdPYGCH---SDEELWRVAEEVGLKTVIEQFPDKLDF 1338
Cdd:TIGR01193 525 QaRSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL-LLGAKenvSQDEIWAACEIAEIKDDIENMPLGYQT 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1339 QLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVT-IKVLKKTLrqSFSTCTILLSEHKVEPLLECQSFLMM 1417
Cdd:TIGR01193 604 ELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITeKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVL 681
|
490 500
....*....|....*....|....*
gi 68390341 1418 DKGQVKTYDSIQKLLNETSHLKQAI 1442
Cdd:TIGR01193 682 DHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1172-1440 |
8.41e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 104.72 E-value: 8.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1172 FKFIDLpsETPKpDKGKdsdLIIENVdaqadsswphRGQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGK 1251
Cdd:PRK11176 319 FAILDL--EQEK-DEGK---RVIERA----------KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGK 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1252 SSLFNaLLKLVY--TDGEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLdPYGC---HSDEELWRVAEEVGLK 1326
Cdd:PRK11176 383 STIAN-LLTRFYdiDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNI-AYARteqYSREQIEEAARMAYAM 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1327 TVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVE 1406
Cdd:PRK11176 461 DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS 540
|
250 260 270
....*....|....*....|....*....|....
gi 68390341 1407 PLLECQSFLMMDKGQVKTYDSIQKLLNETSHLKQ 1440
Cdd:PRK11176 541 TIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
436-645 |
9.09e-23 |
|
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: 98.91 E-value: 9.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 436 VAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPG-TI 501
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNI-----LFGltYDEYRYKSVVKacQLEEdLAALPEK---DKTPMaegglNLSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:cd03295 93 EENIalvpkLLK--WPKEKIRERAD--ELLA-LVGLDPAefaDRYPH-----ELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 574 FTHLDIATEKEIFDKCL-CKLMASKTRILVTNKI-EHLKRADKILLLHNGESFFYGTfPE--LQSERPDFSSLLLG 645
Cdd:cd03295 163 FGALDPITRDQLQEEFKrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGT-PDeiLRSPANDFVAEFVG 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1211-1403 |
1.31e-22 |
|
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: 98.02 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKLVY---TDGEISIDGVN---WNKMPLQ 1281
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLlrlLNRLNDLIPgapDEGEVLLDGKDiydLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1282 kWRKAFGVVPQKVFIFTGPLRMNLD----PYGCHSDEELWRVAEEVgLKTVieQFPDKLDFQLEYGGyvLSNGHKQLICL 1357
Cdd:cd03260 79 -LRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEELDERVEEA-LRKA--ALWDEVKDRLHALG--LSGGQQQRLCL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 68390341 1358 ARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEH 1403
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH 198
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
438-622 |
1.47e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.92 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDNI 505
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQSYALYPHmTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LFGLTY-----DEY--RYKSVVKACQLEEDLAALPEkdktpmaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:COG3839 97 AFPLKLrkvpkAEIdrRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 579 ----IATEKEIFdkclcKLMAS--KTRILVT-NKIEHLKRADKILLLHNGE 622
Cdd:COG3839 166 aklrVEMRAEIK-----RLHRRlgTTTIYVThDQVEAMTLADRIAVMNDGR 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
438-622 |
2.28e-22 |
|
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: 95.54 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAW-----IMPGtirDNILFG-LTY 511
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrrigYLPE---EPSLYEnLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 512 DEYryksvvkacqleedlaalpekdktpmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLc 591
Cdd:cd03230 91 REN------------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR- 139
|
170 180 190
....*....|....*....|....*....|...
gi 68390341 592 KLMAS-KTRILVTNKIEHL-KRADKILLLHNGE 622
Cdd:cd03230 140 ELKKEgKTILLSSHILEEAeRLCDRVAILNNGR 172
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
438-622 |
2.77e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 97.04 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAW----------------IMPG- 499
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdISSLSERELarlrrrhigfvfqffnLLPEl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIRDNILFGLTY-------DEYRYKSVVKACQLEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:COG1136 102 TALENVALPLLLagvsrkeRRERARELLERVGLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 573 PFTHLDIATEKEIFDkCLCKLMAS--KTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:COG1136 171 PTGNLDSKTGEEVLE-LLRELNRElgTTIVMVTHDPELAARADRVIRLRDGR 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
438-643 |
2.88e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.65 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDN 504
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGLTY-DEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:TIGR00958 575 IAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 584 EIF-DKCLcklmASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSLL 643
Cdd:TIGR00958 655 LLQeSRSR----ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
438-621 |
3.65e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.85 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG--------RISYSSQTAWIMP-GTIRDNILFG 508
Cdd:COG1116 25 TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQEPALLPwLTVLDNVALG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 509 LtydeyRYKSVVKACQLEEDLAALPE------KDKTPmAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATe 582
Cdd:COG1116 105 L-----ELRGVPKAERRERARELLELvglagfEDAYP-HQ----LSGGMRQRVAIARALANDPEVLLMDEPFGALDALT- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68390341 583 KEIFDKCLCKLMAS--KTRILVTNKIE---HLkrADKILLLHNG 621
Cdd:COG1116 174 RERLQDELLRLWQEtgKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
397-632 |
3.72e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 102.87 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 397 DVTASWDEGPGELLERIKQENKANGHHngdaglfftnlyvaPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVP 476
Cdd:PRK10789 302 DGSEPVPEGRGELDVNIRQFTYPQTDH--------------PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 477 SSGKIR-HS------------GRISYSSQTAWIMPGTIRDNILFG---LTYDEYRYksVVKACQLEEDLAALPEKDKTPM 540
Cdd:PRK10789 368 SEGDIRfHDipltklqldswrSRLAVVSQTPFLFSDTVANNIALGrpdATQQEIEH--VARLASVHDDILRLPQGYDTEV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 541 AEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFdKCLCKLMASKTRILVTNKIEHLKRADKILLLHN 620
Cdd:PRK10789 446 GERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQIL-HNLRQWGEGRTVIISAHRLSALTEASEILVMQH 524
|
250
....*....|..
gi 68390341 621 GESFFYGTFPEL 632
Cdd:PRK10789 525 GHIAQRGNHDQL 536
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1030-1422 |
6.12e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.35 E-value: 6.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1030 LAIIFIVMRKYFLRTGQQLkQLETEAR-SPIFSHLIMSLKGLWTIRAFER-QAYFEALFHKTLNTHTA-----TWFLYLS 1102
Cdd:PRK13657 165 LGIVYTLITTLVMRKTKDG-QAAVEEHyHDLFAHVSDAIGNVSVVQSYNRiEAETQALRDIADNLLAAqmpvlSWWALAS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1103 TLRwflfRAD--ILFVFFFTLAAWIaVGTNQDKPGEIGIIICLAMLILGTFQWCVATsiaVDGMMRSVDRVFKFIDLPSE 1180
Cdd:PRK13657 244 VLN----RAAstITMLAILVLGAAL-VQKGQLRVGEVVAFVGFATLLIGRLDQVVAF---INQVFMAAPKLEEFFEVEDA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1181 TP---KPDKGKDsdliIENVdaqadsswphRGQIEVRNLTVKYTEAGHAVlKNLSFSAEGRQRVGILGRTGSGKSSLFNa 1257
Cdd:PRK13657 316 VPdvrDPPGAID----LGRV----------KGAVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLIN- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1258 LLKLVY--TDGEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLDpYGCH--SDEELWRVAEEVGLKTVIEQFP 1333
Cdd:PRK13657 380 LLQRVFdpQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR-VGRPdaTDEEMRAAAERAQAHDFIERKP 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1334 DKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKK---TLRQSFSTCTIllsEHKVEPLLE 1410
Cdd:PRK13657 459 DGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAaldELMKGRTTFII---AHRLSTVRN 535
|
410
....*....|..
gi 68390341 1411 CQSFLMMDKGQV 1422
Cdd:PRK13657 536 ADRILVFDNGRV 547
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
431-633 |
1.12e-21 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 95.82 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 431 FTNLYVA----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAWI--------- 496
Cdd:COG1127 8 VRNLTKSfgdrVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSEKELYelrrrigml 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 497 ---------MpgTIRDNILFGLtyDEYRYKSVVKACQL-EEDLAA--LPE-KDKTPmAEgglnLSGGQKARVALARAVYR 563
Cdd:COG1127 88 fqggalfdsL--TVFENVAFPL--REHTDLSEAEIRELvLEKLELvgLPGaADKMP-SE----LSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 564 DADLYLLDAPFTHLDIATEKEIfDKCLCKLMASK--TRILVTNKIEHLKR-ADKILLLHNGESFFYGTFPELQ 633
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVI-DELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1168-1422 |
1.33e-21 |
|
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: 101.05 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1168 VDRVFKFIDLPSE-TPKPDKgkdSDLIIEnvdaqadsswphRGQIEVRNLTVKYtEAGHAVLKNLSFSAEGRQRVGILGR 1246
Cdd:COG5265 329 MERMFDLLDQPPEvADAPDA---PPLVVG------------GGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1247 TGSGKSSLFNALLKLvY--TDGEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLdPYGCH--SDEELWRVAEE 1322
Cdd:COG5265 393 SGAGKSTLARLLFRF-YdvTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI-AYGRPdaSEEEVEAAARA 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1323 VGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSE 1402
Cdd:COG5265 471 AQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIA 550
|
250 260
....*....|....*....|
gi 68390341 1403 HKVEPLLECQSFLMMDKGQV 1422
Cdd:COG5265 551 HRLSTIVDADEILVLEAGRI 570
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1211-1440 |
1.40e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAG---HAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKLvyTDGEISIDGVNW--NKMPLQK 1282
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLiqhLNGLLKP--TSGKIIIDGVDItdKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVPQ----KVF-------IFTGPLRMNLdpygchSDEELW-RVAEE---VGLKtvIEQFPDKLDFQleyggyvL 1347
Cdd:PRK13637 81 IRKKVGLVFQypeyQLFeetiekdIAFGPINLGL------SEEEIEnRVKRAmniVGLD--YEDYKDKSPFE-------L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1348 SNGHKQLICLARSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQSFSTCTILLSeHKVEPLLE-CQSFLMMDKGQVK 1423
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeILNKIKELHKEYNMTIILVS-HSMEDVAKlADRIIVMNKGKCE 224
|
250
....*....|....*..
gi 68390341 1424 TYDSIQKLLNETSHLKQ 1440
Cdd:PRK13637 225 LQGTPREVFKEVETLES 241
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
438-622 |
1.41e-21 |
|
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: 95.27 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRI----------SYSSQTAWIM--PG------ 499
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkIRRKEIQMVFqdPMsslnpr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 -TIRDNILFGLTydeyRYKSVVKACQLEEdlAALPEKDKTPMAEGGLN-----LSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:cd03257 99 mTIGEQIAEPLR----IHGKLSKKEARKE--AVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 574 FTHLDIATEKEIFD--KCLCKLMaSKTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:cd03257 173 TSALDVSVQAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGK 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1211-1421 |
3.09e-21 |
|
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: 92.64 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKM--PLQKWRKAF 1287
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDsGSILIDGEDLTDLedELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKVFIFTGplrmnldpygchsdeelwrvaeevglKTVIEQFpdkldfqleygGYVLSNGHKQLICLARSILSGARI 1367
Cdd:cd03229 79 GMVFQDFALFPH--------------------------LTVLENI-----------ALGLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1368 LLLDEPSAHLDPVTIKVLKKTLRQSFST--CTILLSEHKVEPLLE-CQSFLMMDKGQ 1421
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
438-635 |
4.50e-21 |
|
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: 93.27 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR--------------ISYSSQTAWIMPG-TIR 502
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 503 DNILFGLTydeYRYKSVVKAcQLEEDLA---ALPEKDKTPmaeGGlNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:cd03224 94 ENLLLGAY---ARRRAKRKA-RLERVYElfpRLKERRKQL---AG-TLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 580 ATEKEIFDkCLCKLMASKTRILVtnkIEH-----LKRADKILLLHNGESFFYGTFPELQSE 635
Cdd:cd03224 166 KIVEEIFE-AIRELRDEGVTILL---VEQnarfaLEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1211-1433 |
5.15e-21 |
|
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: 93.89 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMP---LQKWRKA 1286
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQK--------VF---IFtgPLRMNLDpygcHSDEELWRVAEE----VGLKTVIEQFPDkldfqlEyggyvLSNGH 1351
Cdd:COG1127 84 IGMLFQGgalfdsltVFenvAF--PLREHTD----LSEAEIRELVLEklelVGLPGAADKMPS------E-----LSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1352 KQLICLARSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQSFSTCTILLSeHKVEPLLE-CQSFLMMDKGQVKTYDS 1427
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITsavIDELIRELRDELGLTSVVVT-HDLDSAFAiADRVAVLADGKIIAEGT 225
|
....*.
gi 68390341 1428 IQKLLN 1433
Cdd:COG1127 226 PEELLA 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1208-1435 |
1.00e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 98.25 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1208 RGQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFnALLKLVY--TDGEISIDGVNWNKMPLQKWRK 1285
Cdd:PRK10789 311 RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRHFdvSEGDIRFHDIPLTKLQLDSWRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 AFGVVPQKVFIFTGPLRMNLdPYGC--HSDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILS 1363
Cdd:PRK10789 390 RLAVVSQTPFLFSDTVANNI-ALGRpdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1364 GARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLLNET 1435
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
439-622 |
1.01e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 91.93 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQ---TAWIMPGTIRDNILFGLTYDEYR 515
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErrkSIGYVMQDVDYQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 Y------KSVVKACQLEEDLAALPEKDKTPMAegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIfdkc 589
Cdd:cd03226 95 LglkeldAGNEQAETVLKDLDLYALKERHPLS-----LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV---- 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 68390341 590 lCKLM-----ASKTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:cd03226 166 -GELIrelaaQGKAVIVITHDYEFLAKvCDRVLLLANGA 203
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1211-1422 |
1.16e-20 |
|
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: 91.81 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPlqKWRKAFGV 1289
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDGRDVTGVP--PERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTG---------PLRMNLDPYGCHSDEELWrVAEEVGLKTVIEQFPDKLdfqleyggyvlSNGHKQLICLARS 1360
Cdd:cd03259 77 VFQDYALFPHltvaeniafGLKLRGVPKAEIRARVRE-LLELVGLEGLLNRYPHEL-----------SGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1361 ILSGARILLLDEPSAHLDPVTIKVLKKTLR---QSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKelqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
439-647 |
1.49e-20 |
|
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: 92.40 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-----------RISYSSQTAWIMPG-TIRDNIL 506
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 507 FGL---TYDEYRYKSVVKacQLEEDLAALPEKDKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATeK 583
Cdd:cd03299 94 YGLkkrKVDKKEIERKVL--EIAEMLGIDHLLNRKP-----ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT-K 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 584 EIFDKCLCKLMASK--TRILVTNK-IEHLKRADKILLLHNGESFFYGTFPE-LQSERPDFSSLLLGLE 647
Cdd:cd03299 166 EKLREELKKIRKEFgvTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEvFKKPKNEFVAEFLGFN 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
438-622 |
3.07e-20 |
|
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: 90.99 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-------------ISYSSQTAWIMPGTIRDN 504
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGLTYDEYryKSVVKACQ---LEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:cd03248 108 IAYGLQSCSF--ECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68390341 582 EKEIfDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:cd03248 186 EQQV-QQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
438-622 |
3.54e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.88 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI----RHSGRISYSS------------QTAWIMPG-T 500
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngQDLSRLKRREipylrrrigvvfQDFRLLPDrT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFGLTYDEYRyKSVVKAcQLEE--DLAALPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:COG2884 96 VYENVALPLRVTGKS-RKEIRR-RVREvlDLVGLSDKAKALPHE----LSGGEQQRVAIARALVNRPELLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 68390341 579 IATEKEIFDkCLCKLMASKTRILVT----NKIEHLKRadKILLLHNGE 622
Cdd:COG2884 170 PETSWEIME-LLEEINRRGTTVLIAthdlELVDRMPK--RVLELEDGR 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1211-1422 |
4.31e-20 |
|
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: 90.35 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKmPLQKWRKAfGV 1289
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDsGEITFDGKSYQK-NIEALRRI-GA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 V---PqkvfIFTGPL--RMNLDPYGCH---SDEELWRVAEEVGLKTVieqfPDKldfqlEYGGYVLsnGHKQLICLARSI 1361
Cdd:cd03268 77 LieaP----GFYPNLtaRENLRLLARLlgiRKKRIDEVLDVVGLKDS----AKK-----KVKGFSL--GMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1362 LSGARILLLDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVEPL-LECQSFLMMDKGQV 1422
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSlRDQGITVLISSHLLSEIqKVADRIGIINKGKL 204
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
438-621 |
4.75e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.29 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSS------QTAWI---------MpgTIR 502
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlpprerRVGFVfqhyalfphM--TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 503 DNILFGLTyDEYRYKSVVKA---CQLE----EDLAalpekDKTPMaegglNLSGGQKARVALARAVYRDADLYLLDAPFT 575
Cdd:COG1118 94 ENIAFGLR-VRPPSKAEIRArveELLElvqlEGLA-----DRYPS-----QLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 576 HLDIATEKE-------IFDKClcklmaSKTRILVT-NKIEHLKRADKILLLHNG 621
Cdd:COG1118 163 ALDAKVRKElrrwlrrLHDEL------GGTTVFVThDQEEALELADRVVVMNQG 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
438-636 |
6.15e-20 |
|
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: 90.71 E-value: 6.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-----------RiSYSSQTAWIMPG------- 499
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalR-QLRRQIGMIFQQfnlierl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIRDNILFGLtydeYRYKSVVKAC----QLEEDLAALPEKDKTPMAEGGL----NLSGGQKARVALARAVYRDADLYLLD 571
Cdd:cd03256 94 SVLENVLSGR----LGRRSTWRSLfglfPKEEKQRALAALERVGLLDKAYqradQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 572 APFTHLDIATEKEIFD--KCLCKLMAsKTRILVTNKIEHLKR-ADKILLLHNGESFFYGTFPELQSER 636
Cdd:cd03256 170 EPVASLDPASSRQVMDllKRINREEG-ITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
438-632 |
8.00e-20 |
|
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: 94.97 E-value: 8.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGeLVPSSGKIR-----------------HSGRISYSSQTAW--IMP 498
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISgevlldgrdllelsealRGRRIGMVFQDPMtqLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 499 GTIRDNILFGLtydeyRYKSVVKACQLEEDLAALPE------KDKTPMAegglnLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:COG1123 99 VTVGDQIAEAL-----ENLGLSRAEARARVLELLEAvglerrLDRYPHQ-----LSGGQRQRVAIAMALALDPDLLIADE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 573 PFTHLDIATEKEIFD--KCLCKlMASKTRILVTNKIEH-LKRADKILLLHNGESFFYGTFPEL 632
Cdd:COG1123 169 PTTALDVTTQAEILDllRELQR-ERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1210-1391 |
8.51e-20 |
|
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: 89.08 E-value: 8.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1210 QIEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQkWRKAFG 1288
Cdd:COG4133 2 MLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLpPSAGEVLWNGEPIRDARED-YRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTGP-----LRMNLDPYGCH-SDEELWRVAEEVGLKTVIEQFPdkldfqleyggYVLSNGHKQLICLARSIL 1362
Cdd:COG4133 79 YLGHADGLKPELtvrenLRFWAALYGLRaDREAIDEALEAVGLAGLADLPV-----------RQLSAGQKRRVALARLLL 147
|
170 180
....*....|....*....|....*....
gi 68390341 1363 SGARILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1208-1422 |
8.61e-20 |
|
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: 89.84 E-value: 8.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1208 RGQIEVRNLTVKY-TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLvY--TDGEISIDGVNWNKMPLQKWR 1284
Cdd:cd03248 9 KGIVKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF-YqpQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1285 KAFGVVPQKVFIFTGPLRMNLdPYGCH--SDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSIL 1362
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNI-AYGLQscSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1363 SGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1211-1381 |
9.37e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.73 E-value: 9.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYtEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSlfnaLLKLVY-----TDGEISIDGVNWNKMP---LQK 1282
Cdd:COG2884 2 IRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYgeerpTSGQVLVNGQDLSRLKrreIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVPQ--------KVF---IFtgPLRMNldpyGCHSDEELWRVAE---EVGLKTVIEQFPDKldfqleyggyvLS 1348
Cdd:COG2884 77 LRRRIGVVFQdfrllpdrTVYenvAL--PLRVT----GKSRKEIRRRVREvldLVGLSDKAKALPHE-----------LS 139
|
170 180 190
....*....|....*....|....*....|...
gi 68390341 1349 NGHKQLICLARSILSGARILLLDEPSAHLDPVT 1381
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
438-636 |
1.15e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 95.17 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR----ISYSS---------QTAWIMPGTIRDN 504
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplssLSHSVlrqgvamvqQDPVVLADTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKE 584
Cdd:PRK10790 435 VTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 585 IfDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSER 636
Cdd:PRK10790 515 I-QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
121-366 |
2.10e-19 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 90.31 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 121 GYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSIIYKKTLKLSSrvLDKISTGQLVSLMSANLGK-FDQSLgMA 199
Cdd:cd18592 38 GILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRS--LGDKSVGELINIFSNDGQRlFDAAV-FG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 200 HFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQAFLSHKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWE 279
Cdd:cd18592 115 PLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 280 EIMETLIKNIRQDEVKLTRKIGslrYFYSSAYFFSAIFVIVAAVVP---HALSrGINLR--RIFTTLSYCMVLRMTVtRQ 354
Cdd:cd18592 195 KPFAKKIADIRKEERKILEKAG---YLQSISISLAPIVPVIASVVTflaHVAL-GNDLTaaQAFTVIAVFNSMRFSL-RM 269
|
250
....*....|..
gi 68390341 355 LPGSIQMWYDTM 366
Cdd:cd18592 270 LPYAVKALAEAK 281
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1211-1403 |
2.14e-19 |
|
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: 88.32 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAG--HAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEISIDGVNWNKMPLQKW---- 1283
Cdd:cd03255 1 IELKNLSKTYGGGGekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKAFGVVPQkvfiftgplRMNLDPY-------------GCHSDEELWRVAEE----VGLKTVIEQFPDKldfqleyggyv 1346
Cdd:cd03255 81 RRHIGFVFQ---------SFNLLPDltalenvelplllAGVPKKERRERAEEllerVGLGDRLNHYPSE----------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 1347 LSNGHKQLICLARSILSGARILLLDEPSAHLDPVT----IKVLKKtLRQSFSTcTILLSEH 1403
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRE-LNKEAGT-TIVVVTH 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
438-622 |
2.55e-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: 85.96 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG--RISYSSQtawimpgtirdnilfgltydeyr 515
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ----------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 yksvvkacqleedlaalpekdktpmaegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT----EKEI--FDKC 589
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESiealEEALkeYPGT 119
|
170 180 190
....*....|....*....|....*....|....
gi 68390341 590 LcklmasktrILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:cd03221 120 V---------ILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1211-1440 |
3.05e-19 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 89.43 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKY---TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKLvyTDGEISIDGVNWN---KMPLQ 1281
Cdd:TIGR04521 1 IKLKNVSYIYqpgTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLiqhLNGLLKP--TSGTVTIDGRDITakkKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1282 KWRKAFGVVPQ----KVF-------IFTGPLRMNLdpygchSDEELWRVAEE----VGLKtviEQFPDKLDFQLeyggyv 1346
Cdd:TIGR04521 79 DLRKKVGLVFQfpehQLFeetvykdIAFGPKNLGL------SEEEAEERVKEalelVGLD---EEYLERSPFEL------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1347 lSNGHKQLICLArSILsgA---RILLLDEPSAHLDPVTIKVLK---KTLRQSFSTCTILLSeHKVEPLLE-CQSFLMMDK 1419
Cdd:TIGR04521 144 -SGGQMRRVAIA-GVL--AmepEVLILDEPTAGLDPKGRKEILdlfKRLHKEKGLTVILVT-HSMEDVAEyADRVIVMHK 218
|
250 260
....*....|....*....|.
gi 68390341 1420 GQVKTYDSIQKLLNETSHLKQ 1440
Cdd:TIGR04521 219 GKIVLDGTPREVFSDVDELEK 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1211-1403 |
3.09e-19 |
|
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: 93.04 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAG---HAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMP---LQKW 1283
Cdd:COG1123 261 LEVRNLSKRYPVRGkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRpTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKAFGVVPQ----------KVF-IFTGPLRMnldpYGCHSDEELW-RVAE---EVGLKT-VIEQFPdkldFQLeyggyvl 1347
Cdd:COG1123 341 RRRVQMVFQdpysslnprmTVGdIIAEPLRL----HGLLSRAERReRVAElleRVGLPPdLADRYP----HEL------- 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 1348 SNGHKQLICLARSILSGARILLLDEPSAHLDP-VTIKVLK--KTLRQSFStCTILLSEH 1403
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVsVQAQILNllRDLQRELG-LTYLFISH 463
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
443-638 |
3.52e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.27 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 443 ISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRiSYSSQTawimPG-----------------TIRDNI 505
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-DLTALP----PAerpvsmlfqennlfphlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LFGLT----YDEYRYKSVVKACQ---LEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:COG3840 93 GLGLRpglkLTAEQRAQVEQALErvgLAGLLDRLPGQ-----------LSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 579 IATEKEIFDkcLCKLMASKTRI---LVTNKIEHLKR-ADKILLLHNGESFFYGTFPELQSERPD 638
Cdd:COG3840 162 PALRQEMLD--LVDELCRERGLtvlMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
82-351 |
5.10e-19 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 89.20 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 82 FLLFGFLLYIGEATktvqPQLLGRIIASFDPAHEPErANGYFLAFGLGLLFTARFLLLQPAMFGLHHLGMQIRIALFSII 161
Cdd:cd18559 3 LLIKLVLCNHVFSG----PSNLWLLLWFDDPVNGPQ-EHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 162 YKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLIWELIDVNSFCALAAISLLGVLQAFL 241
Cdd:cd18559 78 YHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 242 SHKMGPYKAQKVLLTNKRLALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRY---FYSSAYFFSAIFV 318
Cdd:cd18559 158 AASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRAlavRLWCVGPCIVLFA 237
|
250 260 270
....*....|....*....|....*....|...
gi 68390341 319 IVAAVVPHALSRGINLRRIFTTLSYCMVLRMTV 351
Cdd:cd18559 238 SFFAYVSRHSLAGLVALKVFYSLALTTYLNWPL 270
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
425-622 |
5.32e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 86.33 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 425 GDAGLFFTNLYVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAWIMPG---- 499
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpVTRRSPRDAIRAGiayv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 -------------TIRDNILfgltydeyryksvvkacqleedLAALpekdktpmaegglnLSGG--QKarVALARAVYRD 564
Cdd:cd03215 81 pedrkreglvldlSVAENIA----------------------LSSL--------------LSGGnqQK--VVLARWLARD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 565 ADLYLLDAPFTHLDIATEKEIFDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEGR 181
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
439-627 |
5.57e-19 |
|
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: 87.59 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISyssqtAWIMPG-------TIRDNILF---- 507
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGggfnpelTGRENIYLngrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 508 -GLTYDEY--RYKSVVKACQLEEDLaalpekdKTPMaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKE 584
Cdd:cd03220 112 lGLSRKEIdeKIDEIIEFSELGDFI-------DLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68390341 585 IFDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGESFFYG 627
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1194-1399 |
8.36e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.18 E-value: 8.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1194 IENVDAQADSSW----PHRGQIEVRNLTVkYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEI 1268
Cdd:COG4178 342 LEAADALPEAASrietSEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPYGSGRI 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1269 SidgvnwnkMPlQKWRKAFgvVPQKVFIFTGPLRMNL---DPYGCHSDEELWRVAEEVGLktviEQFPDKLDFQLEYGgY 1345
Cdd:COG4178 421 A--------RP-AGARVLF--LPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL----GHLAERLDEEADWD-Q 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1346 VLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTIL 1399
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVI 538
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1422 |
8.59e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.12 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSS---LFNALLKLvyTDGEISIDGVNWNKMPLQKWRKAF 1287
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKP--QSGEIKIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVV---PQKVFI---------FtGPLRMNLDPygchsdEELWRVAEEVGLKTVIEQFpdkLDFQLEYggyvLSNGHKQLI 1355
Cdd:PRK13632 86 GIIfqnPDNQFIgatveddiaF-GLENKKVPP------KKMKDIIDDLAKKVGMEDY---LDKEPQN----LSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 1356 CLArSILS-GARILLLDEPSAHLDPV---TIKVLKKTLRQSFSTCTILLSeHKVEPLLECQSFLMMDKGQV 1422
Cdd:PRK13632 152 AIA-SVLAlNPEIIIFDESTSMLDPKgkrEIKKIMVDLRKTRKKTLISIT-HDMDEAILADKVIVFSEGKL 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
438-581 |
1.18e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG--RISYSSQTAWIMPG-TIRDNILFGLTydey 514
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLDGDA---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 515 RYKSVVKacQLEEDLAALPEKDKTPMAEG-----------------------GL------------NLSGGQKARVALAR 559
Cdd:COG0488 88 ELRALEA--ELEELEAKLAEPDEDLERLAelqeefealggweaearaeeilsGLgfpeedldrpvsELSGGWRRRVALAR 165
|
170 180
....*....|....*....|..
gi 68390341 560 AVYRDADLYLLDAPFTHLDIAT 581
Cdd:COG0488 166 ALLSEPDLLLLDEPTNHLDLES 187
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1211-1422 |
1.54e-18 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 86.65 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTeAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMP---LQKWRKA 1286
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEpTSGEILVDGQDVTALRgraLRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQK------------VFI----FTGPLRMNLdpyGCHSDEELWRVA---EEVGLKTVIEQFPDKLdfqleyggyvl 1347
Cdd:COG3638 82 IGMIFQQfnlvprlsvltnVLAgrlgRTSTWRSLL---GLFPPEDRERALealERVGLADKAYQRADQL----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1348 SNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQsfsTC-----TILLSEHKVEPLLE-CQSFLMMDKGQ 1421
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRR---IAredgiTVVVNLHQVDLARRyADRIIGLRDGR 224
|
.
gi 68390341 1422 V 1422
Cdd:COG3638 225 V 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1211-1381 |
1.91e-18 |
|
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: 85.60 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAG--HAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGvnwnkMPLQKWRKAF 1287
Cdd:cd03293 1 LEVRNVSKTYGGGGgaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLErPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKVFIF---------TGPLRMNldpygCHSDEELWRVA----EEVGLKTVIEQFPDKldfqleyggyvLSNGHKQL 1354
Cdd:cd03293 76 GYVFQQDALLpwltvldnvALGLELQ-----GVPKAEARERAeellELVGLSGFENAYPHQ-----------LSGGMRQR 139
|
170 180
....*....|....*....|....*..
gi 68390341 1355 ICLARSILSGARILLLDEPSAHLDPVT 1381
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALT 166
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
438-632 |
2.17e-18 |
|
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: 91.03 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAW-----IMP-------GTIRDN 504
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdIRDVTQASLraaigIVPqdtvlfnDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFG---LTYDEYRykSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:COG5265 452 IAYGrpdASEEEVE--AAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 582 EKEIFDkCLCKLMASKTrILVtnkIEH----LKRADKILLLHNGESFFYGTFPEL 632
Cdd:COG5265 530 ERAIQA-ALREVARGRT-TLV---IAHrlstIVDADEILVLEAGRIVERGTHAEL 579
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1212-1422 |
3.67e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 85.42 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1212 EVRNLTVKYteaGHA-VLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQK-WRKAFG 1288
Cdd:COG0410 5 EVENLHAGY---GGIhVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLpPRSGSIRFDGEDITGLPPHRiARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTgplRM----NLD--PYGCHSDEEL-WRVAEevglktVIEQFP---DKLDfQLeyGGYvLSNGHKQLICLA 1358
Cdd:COG0410 82 YVPEGRRIFP---SLtveeNLLlgAYARRDRAEVrADLER------VYELFPrlkERRR-QR--AGT-LSGGEQQMLAIG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1359 RSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ--SFSTcTILLSEHKVEPLLE-CQSFLMMDKGQV 1422
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRlnREGV-TILLVEQNARFALEiADRAYVLERGRI 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
438-628 |
4.80e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 85.94 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAW----------------IMPGTI 501
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvgmvfqnpdnqFVGATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGL-----TYDEY--RYKSVVKACQLEEdlaalpEKDKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:TIGR04520 96 EDDVAFGLenlgvPREEMrkRVDEALKLVGMED------FRDREP-----HLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 575 THLDIATEKEIFDKCLcKLMAS--KTRILVTNKIEHLKRADKILLLHNGESFFYGT 628
Cdd:TIGR04520 165 SMLDPKGRKEVLETIR-KLNKEegITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
439-628 |
5.27e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISyssqtaWIM-PGTI-------RDNILF--- 507
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLeLGAGfhpeltgRENIYLngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 508 --GLTYDEYRYKsvvkacqLEE--DLAALPEKDKTPMAegglNLSGGQKARVALARAVYRDADLYLLD-------APFTH 576
Cdd:COG1134 115 llGLSRKEIDEK-------FDEivEFAELGDFIDQPVK----TYSSGMRARLAFAVATAVDPDILLVDevlavgdAAFQK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 577 ldiatekeifdKCLCKLMA----SKTRILVTNKIEHLKR-ADKILLLHNGESFFYGT 628
Cdd:COG1134 184 -----------KCLARIRElresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
439-621 |
7.04e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.06 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-----------RISYSSQT-AWIMPGTIRDNIL 506
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQHyALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 507 FGLTYDEYRYKSVV-----KACQLEE--DLAALPEKDKTpmaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:PRK10851 97 FGLTVLPRRERPNAaaikaKVTQLLEmvQLAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 580 ATEKEIfDKCLCKLMASK--TRILVT-NKIEHLKRADKILLLHNG 621
Cdd:PRK10851 170 QVRKEL-RRWLRQLHEELkfTSVFVThDQEEAMEVADRVVVMSQG 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1441 |
7.63e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAvLKNLSFSAEGRQRVGILGRTGSGKSSLF---NALLKLvyTDGEISIDGVNWNKMPLQKWRKAF 1287
Cdd:PRK13652 4 IETRDLCYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFrhfNGILKP--TSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQ----KVF-------IFTGPLRMNLDPYGC-HSDEELWRVaeeVGLKTVIEQFPdkldfqleyggYVLSNGHKQLI 1355
Cdd:PRK13652 81 GLVFQnpddQIFsptveqdIAFGPINLGLDEETVaHRVSSALHM---LGLEELRDRVP-----------HHLSGGEKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1356 CLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFST--CTILLSEHKVEPLLECQSFL-MMDKGQVKTYDSIQKLL 1432
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIyVMDKGRIVAYGTVEEIF 226
|
....*....
gi 68390341 1433 NETSHLKQA 1441
Cdd:PRK13652 227 LQPDLLARV 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
440-627 |
7.82e-18 |
|
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: 83.88 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLK---KGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAWIMPG----------------- 499
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkiglvfqqyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 -TIRDNILFGLTydeyRYKSVVKACQLEEDLAALpekDKTPMAEGG-LNLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:cd03297 90 lNVRENLAFGLK----RKRNREDRISVDELLDLL---GLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 578 DIATeKEIFDKCLCKLMAS--KTRILVTNKIEHLKR-ADKILLLHNGESFFYG 627
Cdd:cd03297 163 DRAL-RLQLLPELKQIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1211-1433 |
8.55e-18 |
|
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: 84.17 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAV--LKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKlvYTDGEISIDGVNWNKMP---LQK 1282
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER--PTSGSVLVDGTDLTLLSgkeLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVPQKVFIFTG---------PLRMnldpYGCHSDEELWRVAE---EVGLKTVIEQFPDKLdfqleyggyvlSNG 1350
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSrtvfenvalPLEI----AGVPKAEIEERVLElleLVGLEDKADAYPAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1351 HKQLICLARSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQSFSTcTILLSEHKVEPLLE-CQSFLMMDKGQVKTYD 1426
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETtqsILALLRDINRELGL-TIVLITHEMEVVKRiCDRVAVMEKGEVVEEG 223
|
....*..
gi 68390341 1427 SIQKLLN 1433
Cdd:cd03258 224 TVEEVFA 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
438-578 |
8.85e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 86.69 E-value: 8.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDNI 505
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDYALFPHlTVAENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LFGLtydeyRYKSVVKA------------CQLEeDLAalpekDKTPMAegglnLSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:COG3842 99 AFGL-----RMRGVPKAeirarvaellelVGLE-GLA-----DRYPHQ-----LSGGQQQRVALARALAPEPRVLLLDEP 162
|
....*
gi 68390341 574 FTHLD 578
Cdd:COG3842 163 LSALD 167
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
437-631 |
1.18e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.07 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRIsYSSQTAW----------------IMPGT 500
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvgmvfqnpdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFGL-----TYDEY--RYKSVVKACQLEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:PRK13635 99 VQDDVAFGLenigvPREEMveRVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 574 FTHLDIATEKEIFDkcLCKLMASKTRILV---TNKIEHLKRADKILLLHNGESFFYGTfPE 631
Cdd:PRK13635 168 TSMLDPRGRREVLE--TVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGT-PE 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
438-581 |
1.22e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.53 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSS-------QTAWIMPG-TIRDNILFG 508
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpVTGPGadrgvvfQKDALLPWlNVLDNVAFG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 509 LtydeyRYKSVVKA---CQLEEDLAA--LPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:COG4525 101 L-----RLRGVPKAerrARAEELLALvgLADFARRRIWQ----LSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1211-1422 |
1.25e-17 |
|
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: 83.77 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYtEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMP---LQKWRKA 1286
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEpTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGvvpqkvFIFTGPlrmNLDP---------YGCHSDEELWRVA----------------EEVGLKTVIEQFPDKLdfqle 1341
Cdd:cd03256 80 IG------MIFQQF---NLIErlsvlenvlSGRLGRRSTWRSLfglfpkeekqralaalERVGLLDKAYQRADQL----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1342 yggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFST--CTILLSEHKVEPLLE-CQSFLMMD 1418
Cdd:cd03256 146 ------SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAREyADRIVGLK 219
|
....
gi 68390341 1419 KGQV 1422
Cdd:cd03256 220 DGRI 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1211-1403 |
1.28e-17 |
|
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: 82.60 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTV----KYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNAL---LKLVYTDGEISIDGVNwnkMPLQKW 1283
Cdd:cd03213 4 LSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGVSGEVLINGRP---LDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKAFGVVPQKvFIFTGPLrmnldpygchsdeelwrvaeevglkTVIEQfpdkLDFQLEYGGyvLSNGHKQLICLARSILS 1363
Cdd:cd03213 81 RKIIGYVPQD-DILHPTL-------------------------TVRET----LMFAAKLRG--LSGGERKRVSIALELVS 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68390341 1364 GARILLLDEPSAHLDPVTIKVLKKTLRQSFST-CTILLSEH 1403
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIH 169
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
440-637 |
1.31e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 83.67 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR------------ISYSSQTAWImpgTIRDNILF 507
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrmvvFQNYSLLPWL---TVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 508 GLTYDEYRYKSVVKACQLEE--DLAALPE-KDKTPMaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKE 584
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEhiALVGLTEaADKRPG-----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 585 IFDkclcKLM-----ASKTRILVTNKI-EHLKRADKILLLHNGESFFYGTFPELQSERP 637
Cdd:TIGR01184 153 LQE----ELMqiweeHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEVPFPRP 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1211-1425 |
1.33e-17 |
|
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: 83.10 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGvnwNKMPLQKwRKAFGV 1289
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDsGEVLFDG---KPLDIAA-RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VP-----------QKVFIFTGPLR-MNLDPYGCHSDEELWRVAEEVGLKTVIEQfpdkldfqleyggyvLSNGHKQLICL 1357
Cdd:cd03269 75 LPeerglypkmkvIDQLVYLAQLKgLKKEEARRRIDEWLERLELSEYANKRVEE---------------LSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1358 ARSILSGARILLLDEPSAHLDPVTIKVLKKTLR-QSFSTCTILLSEHKVEPLLE-CQSFLMMDKGQVKTY 1425
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIReLARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLY 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
437-643 |
1.42e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.48 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG----RISYSS---------QTAWIMPGTIRD 503
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirTVTRASlrrniavvfQDAGLFNRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFG---LTYDEYRykSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:PRK13657 428 NIRVGrpdATDEEMR--AAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 581 TEKEIFDkCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSLL 643
Cdd:PRK13657 506 TEAKVKA-ALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
438-628 |
1.60e-17 |
|
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: 82.85 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDN 504
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 IlfgLTYDEYRYKSVVKACQLeedlaalpekdktpmAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKE 584
Cdd:cd03369 102 L---DPFDEYSDEEIYGALRV---------------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68390341 585 IfDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGT 628
Cdd:cd03369 164 I-QKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
438-632 |
1.62e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.15 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSL--LMTILGELvpSSGKIRHSG-------------RISYSSQTAWIMPGTIR 502
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDI--DEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 503 DNILFGLTyDEYRYKSVVKACQLE---EDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:PRK11176 435 NNIAYART-EQYSREQIEEAARMAyamDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 580 ATEKEIfDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPEL 632
Cdd:PRK11176 514 ESERAI-QAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
438-632 |
2.12e-17 |
|
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: 82.55 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI------------RHSGRISYSSQTAWIMPG-TIRDN 504
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdrkAARQSLGYCPQFDALFDElTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILF-----GLTYDEYRYKSVVKACQLEedlaaLPEKDKTPMAegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:cd03263 96 LRFyarlkGLPKSEIKEEVELLLRVLG-----LTDKANKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 580 ATEKEIFDkCLCKLMASKTRILVT---NKIEHLkrADKILLLHNGESFFYGTFPEL 632
Cdd:cd03263 167 ASRRAIWD-LILEVRKGRSIILTThsmDEAEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
438-622 |
2.56e-17 |
|
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: 80.94 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRisyssqtawimpgtirdnilfgltydEYRYK 517
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVSFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 518 SVVKACQLeedlaalpekdktpmaegGLN----LSGGQKARVALARAVYRDADLYLLDAPFTHLDiATEKEIFDKCLCKL 593
Cdd:cd03216 68 SPRDARRA------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALT-PAEVERLFKVIRRL 128
|
170 180 190
....*....|....*....|....*....|.
gi 68390341 594 MAS-KTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:cd03216 129 RAQgVAVIFISHRLDEVFEiADRVTVLRDGR 159
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1418 |
2.57e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.97 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLF---NALLKLvyTDGEISIDG--VNWNKMPLQKWRK 1285
Cdd:PRK13639 2 LETRDLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFlhfNGILKP--TSGEVLIKGepIKYDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 AFGVVPQ----KVFIFT-------GPLRMNLDpygchSDEELWRVAEevGLKTV-IEQFPDKLDFQleyggyvLSNGHKQ 1353
Cdd:PRK13639 79 TVGIVFQnpddQLFAPTveedvafGPLNLGLS-----KEEVEKRVKE--ALKAVgMEGFENKPPHH-------LSGGQKK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 1354 LICLARSILSGARILLLDEPSAHLDPV----TIKVLKKTLRQSFstcTILLSEHKVE--PLLECQSFLMMD 1418
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMgasqIMKLLYDLNKEGI---TIIISTHDVDlvPVYADKVYVMSD 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
430-632 |
2.67e-17 |
|
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: 82.63 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 430 FFTNLYVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRI----------SYSSQTAWIMPG 499
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllsgkelrKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 -------TIRDNILFGLTYDEYRyKSVVKAcQLEE--DLAALPEK-DKTPMaegglNLSGGQKARVALARAVYRDADLYL 569
Cdd:cd03258 91 fnllssrTVFENVALPLEIAGVP-KAEIEE-RVLEllELVGLEDKaDAYPA-----QLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 570 LDAPFTHLDIATEKEIFDkcLCKLMASKTRI---LVTNKIEHLKR-ADKILLLHNGESFFYGTFPEL 632
Cdd:cd03258 164 CDEATSALDPETTQSILA--LLRDINRELGLtivLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
438-631 |
3.87e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR--HSGRISYSSQTAWIMPG--TIRDNILfgltyDE 513
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKlgETVKIGYFDQHQEELDPdkTVLDELR-----DG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 514 YRYKSVVKACQLeedLAAL---PEKDKTPMAegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATeKEI----- 585
Cdd:COG0488 404 APGGTEQEVRGY---LGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET-LEAleeal 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 586 --FDKCLcklmasktrILVTnkieH----LKR-ADKILLLHNGE-SFFYGTFPE 631
Cdd:COG0488 476 ddFPGTV---------LLVS----HdryfLDRvATRILEFEDGGvREYPGGYDD 516
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1222-1406 |
4.46e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 80.93 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1222 EAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLF---NALLKLvyTDGEISIDG--VNWNKMPLQKWRKAFGVVPQ---- 1292
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLlhlNGLLRP--QSGAVLIDGepLDYSRKGLLERRQRVGLVFQdpdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1293 KVFIFT-------GPLRMNLdpygchSDEELWRVAEEVGLKTVIEQFPDKLDFQLeyggyvlSNGHKQLICLARSILSGA 1365
Cdd:TIGR01166 80 QLFAADvdqdvafGPLNLGL------SEAEVERRVREALTAVGASGLRERPTHCL-------SGGEKKRVAIAGAVAMRP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68390341 1366 RILLLDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVE 1406
Cdd:TIGR01166 147 DVLLLDEPTAGLDPAGREQMLAILRRlRAEGMTVVISTHDVD 188
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
439-634 |
4.59e-17 |
|
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: 82.10 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR--------------ISYSSQTAWIMPG-TIRD 503
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFGLTYDEYRYKSVVKACQLEEDLAA----------LPEKDKTPMAegglNLSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREAREraeellervgLADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 574 FTHLDiATEKEIFDKCLCKLMASKTRILVtnkIEH-----LKRADKILLLHNGESFFYGTFPELQS 634
Cdd:cd03219 171 AAGLN-PEETEELAELIRELRERGITVLL---VEHdmdvvMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1211-1431 |
5.09e-17 |
|
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: 81.78 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKmPLQKWRKAFGV 1289
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTG-----------PLRmnldpygCHSDEELWRVAEEVGLKTVIEQFPDKLDFQLeyggyvlSNGHKQLICLA 1358
Cdd:cd03263 80 CPQFDALFDEltvrehlrfyaRLK-------GLPKSEIKEEVELLLRVLGLTDKANKRARTL-------SGGMKRKLSLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 1359 RSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEpllECQsFL-----MMDKGQVKTYDSIQKL 1431
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMD---EAE-ALcdriaIMSDGKLRCIGSPQEL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
437-621 |
5.62e-17 |
|
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: 82.00 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQT-AWIMPGTIRDN 504
Cdd:cd03296 15 FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHyALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGL---------TYDEYRYK--SVVKACQLEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:cd03296 95 VAFGLrvkprserpPEAEIRAKvhELLKLVQLDWLADRYPAQ-----------LSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 574 FTHLDIATEKEIfDKCLCKLM--ASKTRILVT-NKIEHLKRADKILLLHNG 621
Cdd:cd03296 164 FGALDAKVRKEL-RRWLRRLHdeLHVTTVFVThDQEEALEVADRVVVMNKG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1211-1457 |
8.65e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.04 E-value: 8.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAG-------HAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISidgvnWNKMPLQK 1282
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVS-----WRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 W----RKAFGVVPQKVF---------------IFTGPLR--MNLDPygchsDEELWRVAE---EVGLKtviEQFPDKLDF 1338
Cdd:PRK10419 79 LnraqRKAFRRDIQMVFqdsisavnprktvreIIREPLRhlLSLDK-----AERLARASEmlrAVDLD---DSVLDKRPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1339 QleyggyvLSNGHKQLICLARSILSGARILLLDEPSAHLDPV----TIKVLKKtLRQSFSTCTILLSeHKVEpLLE--CQ 1412
Cdd:PRK10419 151 Q-------LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlqagVIRLLKK-LQQQFGTACLFIT-HDLR-LVErfCQ 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 68390341 1413 SFLMMDKGQVKTYDSIQKLLNETS----HLKQAISPAerlklFPRRNSS 1457
Cdd:PRK10419 221 RVMVMDNGQIVETQPVGDKLTFSSpagrVLQNAVLPA-----FPVRRRT 264
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
438-622 |
9.22e-17 |
|
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: 81.39 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRI-------------------SYSSqtawIMP 498
Cdd:COG1124 19 PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkafrrrvqmvfqdPYAS----LHP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 499 G-TIRDNI-----LFGLTYDEYRYKSVVKACQLEEDLAalpekDKTPMAegglnLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:COG1124 95 RhTVDRILaeplrIHGLPDREERIAELLEQVGLPPSFL-----DRYPHQ-----LSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 573 PFTHLDIATEKEIFDkCLCKLMASK--TRILVT---NKIEHLkrADKILLLHNGE 622
Cdd:COG1124 165 PTSALDVSVQAEILN-LLKDLREERglTYLFVShdlAVVAHL--CDRVAVMQNGR 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
439-627 |
9.41e-17 |
|
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: 80.40 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRisyssqtawimPGTIRDNILFGLTYDE---YR 515
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-----------PLDIAARNRIGYLPEErglYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 YKSVVKACQLEEDLAALPEKDKTPMAEGGLN--------------LSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:cd03269 84 KMKVIDQLVYLAQLKGLKKEEARRRIDEWLErlelseyankrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68390341 582 EKEIFDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGESFFYG 627
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
440-628 |
1.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGrISYSSQTA------------------WIMPGTI 501
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG-VDITDKKVklsdirkkvglvfqypeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGLT----YDEYRYKSVVKACQL----EEDLaalpeKDKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:PRK13637 102 EKDIAFGPInlglSEEEIENRVKRAMNIvgldYEDY-----KDKSP-----FELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 574 FTHLDIATEKEIFDKclCKLMASK---TRILVTNKIEHL-KRADKILLLHNGESFFYGT 628
Cdd:PRK13637 172 TAGLDPKGRDEILNK--IKELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1211-1422 |
1.34e-16 |
|
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: 80.49 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAV--LKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPLQKWRKaF 1287
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDaGFATVDGFDVVKEPAEARRR-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKVFIF---TGplRMNL----DPYGCHSDEELWRVaEEVGLKTVIEQFPDKldfqlEYGGyvLSNGHKQLICLARS 1360
Cdd:cd03266 81 GFVSDSTGLYdrlTA--RENLeyfaGLYGLKGDELTARL-EELADRLGMEELLDR-----RVGG--FSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 1361 ILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFST-CTILLSEH---KVEPLleCQSFLMMDKGQV 1422
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHimqEVERL--CDRVVVLHRGRV 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
432-631 |
1.49e-16 |
|
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: 81.54 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 432 TNLYVApvLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-----------------RISYSSQTA 494
Cdd:cd03294 34 TGQTVG--VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 495 WIMPG-TIRDNILFGLTY----DEYRYKSVVKACQ---LEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDAD 566
Cdd:cd03294 112 ALLPHrTVLENVAFGLEVqgvpRAEREERAAEALElvgLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 567 LYLLDAPFTHLDIATEKEIFDKcLCKLMAS--KTRILVTNK-IEHLKRADKILLLHNGESFFYGTfPE 631
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDE-LLRLQAElqKTIVFITHDlDEALRLGDRIAIMKDGRLVQVGT-PE 246
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
438-587 |
1.51e-16 |
|
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: 80.14 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG----------------RISYSSQTAWIMPG-T 500
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFRLLPDrN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:cd03292 95 VYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
....*..
gi 68390341 581 TEKEIFD 587
Cdd:cd03292 171 TTWEIMN 177
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
438-583 |
1.69e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR----ISYSSQTAWIMPG-------TIRDNIL 506
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYLGHRnamkpalTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 507 F-GLTYDEYRYKSVVKACQLE-EDLAALPEKdktpmaegglNLSGGQKARVALAR--AVYRdaDLYLLDAPFTHLDIATE 582
Cdd:PRK13539 96 FwAAFLGGEELDIAAALEAVGlAPLAHLPFG----------YLSAGQKRRVALARllVSNR--PIWILDEPTAALDAAAV 163
|
.
gi 68390341 583 K 583
Cdd:PRK13539 164 A 164
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
437-646 |
2.05e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 80.41 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR--------------ISYSSQTAWIMPG-TI 501
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGLtydeYRYKSVVKAcqlEEDLAA-------LPEKDKTPmaeGGlNLSGGQKARVALARAVYRDADLYLLDAPf 574
Cdd:COG0410 96 EENLLLGA----YARRDRAEV---RADLERvyelfprLKERRRQR---AG-TLSGGEQQMLAIGRALMSRPKLLLLDEP- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 575 thldiaTE-------KEIFDkCLCKLMASKTRILVtnkIEH-----LKRADKILLLHNGESFFYGTFPELQsERPDFSSL 642
Cdd:COG0410 164 ------SLglaplivEEIFE-IIRRLNREGVTILL---VEQnarfaLEIADRAYVLERGRIVLEGTAAELL-ADPEVREA 232
|
....
gi 68390341 643 LLGL 646
Cdd:COG0410 233 YLGV 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
437-607 |
2.20e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-RISYSS-------QTAWIMP-GTIRDNILF 507
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkPVEGPGaergvvfQNEGLLPwRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 508 GLtydeyRYKSVVKACQLEEDLAALpekDKTPMAEGG----LNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATeK 583
Cdd:PRK11248 94 GL-----QLAGVEKMQRLEIAHQML---KKVGLEGAEkryiWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT-R 164
|
170 180
....*....|....*....|....*.
gi 68390341 584 EIFDKCLCKLMA--SKTRILVTNKIE 607
Cdd:PRK11248 165 EQMQTLLLKLWQetGKQVLLITHDIE 190
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1210-1406 |
2.58e-16 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 80.03 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1210 QIEVRNLTVKYTEaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKM---PLQKWRK 1285
Cdd:TIGR02315 1 MLEVENLSKVYPN-GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVePSSGSILLEGTDITKLrgkKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 AFGVVPQK------------VFI----FTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLdfqleyggyvlSN 1349
Cdd:TIGR02315 80 RIGMIFQHynlierltvlenVLHgrlgYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQL-----------SG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1350 GHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLR---QSFSTcTILLSEHKVE 1406
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKrinKEDGI-TVIINLHQVD 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
439-622 |
2.98e-16 |
|
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: 79.11 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAWI------------------MpgT 500
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrqkvgmvfqqfnlfphL--T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFGLTYDEYRYKSVVKACQLEE-DLAALPEK-DKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:cd03262 93 VLENITLAPIKVKGMSKAEAEERALELlEKVGLADKaDAYP-----AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 579 IATEKEIFDkclckLMAS-----KTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:cd03262 168 PELVGEVLD-----VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGR 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
438-632 |
3.42e-16 |
|
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: 79.51 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR--------------ISYSSQTAWIMPG-TIR 502
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 503 DNILFGLtydEYRYKSvvKACQLEEDLAALPEKDKTPMAEG-GLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:cd03218 94 ENILAVL---EIRGLS--KKEREEKLEELLEEFHITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 582 EKEIfDKCLCKLMASKTRILVT--NKIEHLKRADKILLLHNGESFFYGTFPEL 632
Cdd:cd03218 169 VQDI-QKIIKILKDRGIGVLITdhNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1211-1422 |
5.02e-16 |
|
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: 77.08 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGvnwnkmplqkwrkafgv 1289
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYkPDSGEILVDG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 vpqKVFIFTGPLRmnldpygchsdeelwrvAEEVGLKTVieqfpdkldFQLeyggyvlSNGHKQLICLARSILSGARILL 1369
Cdd:cd03216 62 ---KEVSFASPRD-----------------ARRAGIAMV---------YQL-------SVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1370 LDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVEPLLE-CQSFLMMDKGQV 1422
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1211-1433 |
5.44e-16 |
|
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: 79.27 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYtEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFtgplrmnldPYgchsdeelWRVAEEVGL--------KTVIEQFPDKL--DFQLEYGGYV------LSNGHKQ 1353
Cdd:cd03295 80 VIQQIGLF---------PH--------MTVEENIALvpkllkwpKEKIRERADELlaLVGLDPAEFAdrypheLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1354 LICLARSILSGARILLLDEPSAHLDPVT-------IKVLKKTLRQsfstcTILLSEHKV-EPLLECQSFLMMDKGQVKTY 1425
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITrdqlqeeFKRLQQELGK-----TIVFVTHDIdEAFRLADRIAIMKNGEIVQV 217
|
....*...
gi 68390341 1426 DSIQKLLN 1433
Cdd:cd03295 218 GTPDEILR 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1208-1389 |
5.81e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.93 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1208 RGQIEVRNLTVKY-TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLK-------------------------- 1260
Cdd:PTZ00265 1163 KGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1261 -----------------------------LVYTDGEISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRMNLDpYGCH 1311
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1312 --SDEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTL 1389
Cdd:PTZ00265 1322 daTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1211-1422 |
6.04e-16 |
|
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: 79.02 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL-KLVYTDGEISIDGVN-WNKMPLQKWRKAFG 1288
Cdd:cd03219 1 LEVRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISgFLRPTSGSVLFDGEDiTGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTG---------------PLRMNLDPYgCHSDEELWRVAEEVglktvIEQF--PDKLDFQLEYggyvLSNGH 1351
Cdd:cd03219 79 RTFQIPRLFPEltvlenvmvaaqartGSGLLLARA-RREEREARERAEEL-----LERVglADLADRPAGE----LSYGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1352 KQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVEPLLE-CQSFLMMDKGQV 1422
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1434 |
8.63e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAvLKNLSFSAEGRQRVGILGRTGSGKSSLfnaLLKL--VYT--DGEISIDGVNWNKMPLQKWRKA 1286
Cdd:PRK13647 5 IEVEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTL---LLHLngIYLpqRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQ----KVFIFT-------GPLRMNLDPygchsDEELWRVAEevGLKTV-IEQFPDKLDFQLEYggyvlsnGHKQL 1354
Cdd:PRK13647 81 VGLVFQdpddQVFSSTvwddvafGPVNMGLDK-----DEVERRVEE--ALKAVrMWDFRDKPPYHLSY-------GQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1355 ICLARSILSGARILLLDEPSAHLDPVTIKVLKKTL-RQSFSTCTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQKLL 1432
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
..
gi 68390341 1433 NE 1434
Cdd:PRK13647 227 DE 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
440-627 |
1.04e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.66 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTI--LGELVPS---SGKIRHSGRISYSSQTAWI---------------MPG 499
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTVdlrkeigmvfqqpnpFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIRDNILFGLTYDEYRYKSVVKACqLEEDL--AALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDEA-VEKSLkgASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 578 DIATEKEIfDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGESFFYG 627
Cdd:PRK14239 180 DPISAGKI-EETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
442-621 |
1.15e-15 |
|
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: 77.53 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 442 DISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDNILFGL 509
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 510 T-------YDEYRYKSVVKACQLEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATE 582
Cdd:cd03298 96 SpglkltaEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68390341 583 KEIFDkCLCKLMASK--TRILVTNKIEHLKR-ADKILLLHNG 621
Cdd:cd03298 165 AEMLD-LVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
439-622 |
1.23e-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: 77.86 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-----------------RISYSSQTAWIMPG-T 500
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararlrarHVGFVFQSFQLLPTlT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNI-----LFGLTYDEYRYKSVVKACQLEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDADLYLLDAPFT 575
Cdd:COG4181 107 ALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 576 HLDIATEKEIFDkclckLMASKTR------ILVTNKIEHLKRADKILLLHNGE 622
Cdd:COG4181 176 NLDAATGEQIID-----LLFELNRergttlVLVTHDPALAARCDRVLRLRAGR 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
438-622 |
1.85e-15 |
|
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: 81.10 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-IS---------------------YSSqtaw 495
Cdd:COG1123 279 RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdLTklsrrslrelrrrvqmvfqdpYSS---- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 496 IMPG-TIRDNILFGLTY-----DEYRYKSVV---KACQLEEDLAalpekDKTPMAegglnLSGGQKARVALARAVYRDAD 566
Cdd:COG1123 355 LNPRmTVGDIIAEPLRLhgllsRAERRERVAellERVGLPPDLA-----DRYPHE-----LSGGQRQRVAIARALALEPK 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 567 LYLLDAPFTHLDIATEKEIFDkclckLMAS------KTRILVT---NKIEHLkrADKILLLHNGE 622
Cdd:COG1123 425 LLILDEPTSALDVSVQAQILN-----LLRDlqrelgLTYLFIShdlAVVRYI--ADRVAVMYDGR 482
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1211-1381 |
1.87e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 77.82 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAG--HAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVnwnkmPLQKWRKAF 1287
Cdd:COG1116 8 LELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKpTSGEVLVDGK-----PVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQK--------VF---IFtgPLRMNldpyGCHSDEELWRVAE---EVGLKTVIEQFPdkldfqleyggYVLSNGHKQ 1353
Cdd:COG1116 83 GVVFQEpallpwltVLdnvAL--GLELR----GVPKAERRERARElleLVGLAGFEDAYP-----------HQLSGGMRQ 145
|
170 180
....*....|....*....|....*...
gi 68390341 1354 LICLARSILSGARILLLDEPSAHLDPVT 1381
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALT 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
439-622 |
1.96e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.77 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTI--LGELVPS---SGKIRHSG---------------RISYSSQTAWIMP 498
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLDGediydpdvdvvelrrRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 499 GTIRDNILFGLTYDEYRYKSVVKAcQLEEDL--AALPE--KDKtpMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:COG1117 106 KSIYDNVAYGLRLHGIKSKSELDE-IVEESLrkAALWDevKDR--LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 575 THLD-IATEKeifdkcLCKLMAS-KTR---ILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:COG1117 183 SALDpISTAK------IEELILElKKDytiVIVTHNMQQAARvSDYTAFFYLGE 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
437-578 |
2.08e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.75 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVP---SSGKIR-----------HSGRISYSSQTAWIMPG-TI 501
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLlngrrltalpaEQRRIGILFQDDLLFPHlSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGLTYD---EYRYKSVVKAcqLEE-DLAALPEKDktPMaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:COG4136 94 GENLAFALPPTigrAQRRARVEQA--LEEaGLAGFADRD--PA-----TLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
.
gi 68390341 578 D 578
Cdd:COG4136 165 D 165
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1211-1439 |
3.37e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.82 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAG----HAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALlkLVYTDGEISIDGVNWNKMP-LQK 1282
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNAL--LIPSEGKVYVDGLDTSDEEnLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVV---PQKVFIFT--------GPLRMNLDPygchsDEELWRVAEevGLKTVieqfpDKLDFQlEYGGYVLSNGH 1351
Cdd:PRK13633 83 IRNKAGMVfqnPDNQIVATiveedvafGPENLGIPP-----EEIRERVDE--SLKKV-----GMYEYR-RHAPHLLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1352 KQLICLARSILSGARILLLDEPSAHLDPV-------TIKVLKKTlrqsfSTCTILLSEHKVEPLLECQSFLMMDKGQVKT 1424
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSgrrevvnTIKELNKK-----YGITIILITHYMEEAVEADRIIVMDSGKVVM 224
|
250
....*....|....*
gi 68390341 1425 YDSIQKLLNETSHLK 1439
Cdd:PRK13633 225 EGTPKEIFKEVEMMK 239
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
438-643 |
3.74e-15 |
|
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: 77.26 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDN 504
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKe 584
Cdd:cd03288 115 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN- 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 585 IFDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPD-FSSLL 643
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGvFASLV 253
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
444-643 |
3.84e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.54 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 444 SLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDNILFGL-- 509
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHlTVAQNIGLGLnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 510 -----TYDEYRYKSVVKACQLEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKE 584
Cdd:PRK10771 99 glklnAAQREKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 585 IF----DKCLCKLMaskTRILVTNKIEHLKR-ADKILLLHNGESFFYGTFPELQSERPDFSSLL 643
Cdd:PRK10771 168 MLtlvsQVCQERQL---TLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1224-1438 |
5.02e-15 |
|
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: 77.20 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1224 GHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL-KLVYTDGEISIDGvnwnkmplqkwRKAFGvvPQKVFIFTGPLR 1302
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSG-----------RISFS--SQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1303 MNLdPYGCHSDEELWR-VAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVT 1381
Cdd:cd03291 116 ENI-IFGVSYDEYRYKsVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1382 IK-VLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLLNE----TSHL 1438
Cdd:cd03291 195 EKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLrpdfSSKL 256
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
439-622 |
5.83e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.64 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRhSGRISYSS---------QTAWIMP-GTIRDNILFG 508
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGTAPLAEaredtrlmfQDARLLPwKKVIDNVGLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 509 LTYDeYRYKSvvkacqlEEDLAALPEKDKT---PMAegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEI 585
Cdd:PRK11247 106 LKGQ-WRDAA-------LQALAAVGLADRAnewPAA-----LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68390341 586 FDkclckLMASK------TRILVTNKI-EHLKRADKILLLHNGE 622
Cdd:PRK11247 173 QD-----LIESLwqqhgfTVLLVTHDVsEAVAMADRVLLIEEGK 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
439-585 |
6.45e-15 |
|
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: 74.84 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR------HSGRISYSSQTAWI--MPG-----TIRDNI 505
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggplDFQRDSIARGLLYLghAPGikttlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LFgltydeyrYKSVVKACQLEEDLA--ALPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:cd03231 95 RF--------WHADHSDEQVEEALArvGLNGFEDRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
..
gi 68390341 584 EI 585
Cdd:cd03231 163 RF 164
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
439-639 |
6.67e-15 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 76.82 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILgELVPSSGKIRHSGrISYSS--------------QTAWIMPGTIRDN 504
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDG-VSWNSvplqkwrkafgvipQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 I-LFGLTYDEYRYKsVVKACQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:cd03289 97 LdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 584 eIFDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDF 639
Cdd:cd03289 176 -VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
423-627 |
6.69e-15 |
|
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: 75.83 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 423 HNGDAGL------FFTNLYVA-PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYS----- 490
Cdd:cd03267 13 YSKEPGLigslksLFKRKYREvEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrrkkf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 491 -----------SQTAWIMPgtIRDNI-----LFGLTYDEY--RYKSVVKACQLEEDLaalpekdKTPMAegglNLSGGQK 552
Cdd:cd03267 93 lrrigvvfgqkTQLWWDLP--VIDSFyllaaIYDLPPARFkkRLDELSELLDLEELL-------DTPVR----QLSLGQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 553 ARVALARAVYRDADLYLLDAPFTHLDIATEKEI--FDKCLCKLmaSKTRILVTN----KIEHLkrADKILLLHNGESFFY 626
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIrnFLKEYNRE--RGTTVLLTShymkDIEAL--ARRVLVIDKGRLLYD 235
|
.
gi 68390341 627 G 627
Cdd:cd03267 236 G 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1441 |
6.84e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.81 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAvLKNLSFSAEGRQRVGILGRTGSGKSSLF---NALLKLVytDGEISIDG--VNWNKMPLQKWRK 1285
Cdd:PRK13636 6 LKVEELNYNYSDGTHA-LKGININIKKGEVTAILGGNGAGKSTLFqnlNGILKPS--SGRILFDGkpIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 AFGVVPQ----KVF-------IFTGPLRMNLdpygchSDEELWRVAEEVGLKTVIEQFPDKldfqleyGGYVLSNGHKQL 1354
Cdd:PRK13636 83 SVGMVFQdpdnQLFsasvyqdVSFGAVNLKL------PEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1355 ICLARSILSGARILLLDEPSAHLDPVTI----KVLKKTLRQsfSTCTILLSEHKVEPL-LECQSFLMMDKGQVKTYDSIQ 1429
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVseimKLLVEMQKE--LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPK 227
|
250
....*....|..
gi 68390341 1430 KLLNETSHLKQA 1441
Cdd:PRK13636 228 EVFAEKEMLRKV 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
438-622 |
7.71e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.76 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVP---SSGKIRHSGrISYSSQTAW----------------IMP 498
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDG-ITLTAKTVWdirekvgivfqnpdnqFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 499 GTIRDNILFGLtydEYR------YKSVVKacQLEEDLAALPEKDKTPMaegglNLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:PRK13640 100 ATVGDDVAFGL---ENRavprpeMIKIVR--DVLADVGMLDYIDSEPA-----NLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 573 PFTHLDIATEKEIFdKCLCKLMASK--TRILVTNKIEHLKRADKILLLHNGE 622
Cdd:PRK13640 170 STSMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1211-1423 |
8.75e-15 |
|
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: 74.92 E-value: 8.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEaGHAvLKNLSFSAeGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPlQKWRKAFGV 1289
Cdd:cd03264 1 LQLENLTKRYGK-KRA-LDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSsGTIRIDGQDVLKQP-QKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKvfiFTGPLRMN----LD----PYGCHS---DEELWRVAEEVGLKTVIEQFPDKLdfqleyggyvlSNGHKQLICLA 1358
Cdd:cd03264 77 LPQE---FGVYPNFTvrefLDyiawLKGIPSkevKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 1359 RSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVEPLLE-CQSFLMMDKGQVK 1423
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
440-621 |
1.20e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.02 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRiSYSSQT--------------------AWIMPG 499
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY-HITPETgnknlkklrkkvslvfqfpeAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIRDNIL-----FGLTYDEYRYKSV--VKACQLEEDLAalpekDKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:PRK13641 102 TVLKDVEfgpknFGFSEDEAKEKALkwLKKVGLSEDLI-----SKSP-----FELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 573 PFTHLDIATEKEIFDKCLCKLMASKTRILVTNKIEHL-KRADKILLLHNG 621
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHG 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
438-627 |
1.31e-14 |
|
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: 75.12 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGK----------------IRHSGRISYSSQTAWIMPG-T 500
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRKRIGLVSPALQLRFPRDeT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFGLT-----YDEYRYKSVVKACQLEEDLAALPEKDKtPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFT 575
Cdd:COG1119 97 VLDVVLSGFFdsiglYREPTDEQRERARELLELLGLAHLADR-PFGT----LSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 576 HLDIAtEKEIFDKCLCKLMAS--KTRILVTNKIEHLKRA-DKILLLHNGESFFYG 627
Cdd:COG1119 172 GLDLG-ARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
433-622 |
1.31e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 433 NLYVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR--------------ISYSS----QTA 494
Cdd:COG1129 261 GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 495 WIMPGTIRDNILFGlTYDEYRYKSVVKACQLEEDLAALPEK-------DKTPMAegglNLSGG--QKarVALARAVYRDA 565
Cdd:COG1129 341 LVLDLSIRENITLA-SLDRLSRGGLLDRRRERALAEEYIKRlriktpsPEQPVG----NLSGGnqQK--VVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 566 DLYLLDAPfTH-LDIATEKEIFdkclcKLMASKTR-----ILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:COG1129 414 KVLILDEP-TRgIDVGAKAEIY-----RLIRELAAegkavIVISSELPELLGlSDRILVMREGR 471
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1211-1403 |
1.73e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 72.10 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTeaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL-KLVYTDGEISIDGVNwnkmplqkwrkAFGV 1289
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTWGSTV-----------KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQkvfiftgplrmnldpygchsdeelwrvaeevglktvieqfpdkldfqleyggyvLSNGHKQLICLARSILSGARILL 1369
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 68390341 1370 LDEPSAHLDPVTIKVLKKTLrQSFStCTILLSEH 1403
Cdd:cd03221 94 LDEPTNHLDLESIEALEEAL-KEYP-GTVILVSH 125
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1211-1400 |
1.92e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.07 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKL---VYTDGEISIDGVN--WNKMPLQK 1282
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLlrcLNRMNDLipgARVEGEILLDGEDiyDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVPQK--VF---IF---TGPLRMNldpyGCHSDEE-------------LWrvaEEVglKtvieqfpDKLDFQle 1341
Cdd:COG1117 90 LRRRVGMVFQKpnPFpksIYdnvAYGLRLH----GIKSKSEldeiveeslrkaaLW---DEV--K-------DRLKKS-- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1342 ygGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPV-TIKV--LKKTLRQSFstcTILL 1400
Cdd:COG1117 152 --ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKIeeLILELKKDY---TIVI 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
438-580 |
1.97e-14 |
|
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: 73.55 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR------HSGRISYSSQTAWI--MPG-----TIRDN 504
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngtplAEQRDEPHENILYLghLPGlkpelSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFgltydeyrYKSVVKACQL--EEDLAA--LPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:TIGR01189 94 LHF--------WAAIHGGAQRtiEDALAAvgLTGFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1211-1381 |
2.24e-14 |
|
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: 73.60 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTeAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMP---LQKWRKA 1286
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQKVFIFTG---------PLRMNLDPygchsdEELWR-----VAEEVGLKTVIEQFPDKldfqleyggyvLSNGHK 1352
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyenvafALEVTGVP------PREIRkrvpaALELVGLSHKHRALPAE-----------LSGGEQ 142
|
170 180
....*....|....*....|....*....
gi 68390341 1353 QLICLARSILSGARILLLDEPSAHLDPVT 1381
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1211-1426 |
2.79e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL-KLVYTDGEISIdGVNwnkmpLQkwrkaFGV 1289
Cdd:COG0488 316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAgELEPDSGTVKL-GET-----VK-----IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKvfiftgplRMNLDPygchsD----EELWRVAEEVGLKTVI---EQF---PDKLDFQLEyggyVLSNGHKQLICLAR 1359
Cdd:COG0488 383 FDQH--------QEELDP-----DktvlDELRDGAPGGTEQEVRgylGRFlfsGDDAFKPVG----VLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 1360 SILSGARILLLDEPSAHLDPVTIKVLKKTLrQSFSTCTILLSeHKVEpLLE--CQSFLMMDKGQVKTYD 1426
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEAL-DDFPGTVLLVS-HDRY-FLDrvATRILEFEDGGVREYP 511
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
433-636 |
2.84e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 433 NLYVA----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAW 495
Cdd:PRK11231 7 NLTVGygtkRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 496 IMPG-TIRDNILFG----LTY-------DEYRYKSVVKACQLEEdLAALPEKDktpmaegglnLSGGQKARVALARAVYR 563
Cdd:PRK11231 87 TPEGiTVRELVAYGrspwLSLwgrlsaeDNARVNQAMEQTRINH-LADRRLTD----------LSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 564 DADLYLLDAPFTHLDIATEKEifdkcLCKLM-----ASKTRILVTNKIEHLKR-ADKILLLHNGESFFYGTFPELQSER 636
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVE-----LMRLMrelntQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
438-646 |
3.69e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.64 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTawiMPGtIRDniLFGLTYDEYRYK 517
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK---LQG-IRK--LVGIVFQNPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 518 SVVKAcqLEEDLAALPEKDKTP-----------MAEGGL---------NLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:PRK13644 90 FVGRT--VEEDLAFGPENLCLPpieirkrvdraLAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 578 DIATEKEIFDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTfPElqSERPDFSSLLLGL 646
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE-PE--NVLSDVSLQTLGL 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
447-608 |
3.85e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 73.98 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 447 LKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-RISYSSQTAWI-MPGTIRDnILFGLTYDEY---RYKS-VV 520
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKAdYEGTVRD-LLSSITKDFYthpYFKTeIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 521 KACQLEEDL-AALPEkdktpmaegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIatEKeifdkclcKLMASKT- 598
Cdd:cd03237 101 KPLQIEQILdREVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQ--------RLMASKVi 158
|
170
....*....|....*.
gi 68390341 599 -RILVTNK-----IEH 608
Cdd:cd03237 159 rRFAENNEktafvVEH 174
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1215-1434 |
4.25e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.77 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1215 NLTVKYTeaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPL-QKWRKAFGVVPQ 1292
Cdd:PRK10895 8 NLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPLhARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1293 KVFIF---------TGPLRMNLDpygcHSDEELWRVAEEVGLKTVIEQFPDKLdfqleygGYVLSNGHKQLICLARSILS 1363
Cdd:PRK10895 86 EASIFrrlsvydnlMAVLQIRDD----LSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1364 GARILLLDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKV-EPLLECQSFLMMDKGQVKTYDSIQKLLNE 1434
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHlRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1211-1403 |
4.27e-14 |
|
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: 72.95 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKlvYTDGEISIDG--VNWNKMPLQKWRK 1285
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE--PDSGTIIIDGlkLTDDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 AFGVVPQkvfiftgplRMNLDPygcH-----------------SDEELWRVAEE----VGLKTVIEQFPDKldfqleygg 1344
Cdd:cd03262 77 KVGMVFQ---------QFNLFP---HltvlenitlapikvkgmSKAEAEERALEllekVGLADKADAYPAQ--------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1345 yvLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIK-VLKKTLRQSFSTCTILLSEH 1403
Cdd:cd03262 136 --LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGeVLDVMKDLAEEGMTMVVVTH 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1211-1422 |
4.73e-14 |
|
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: 73.35 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPL-QKWRKAFG 1288
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDsGKILLDGQDITKLPMhKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTgplRMNLDpygchsdEELWRVAEEVGL-KTVIEQFPDKL--DFQLEY----GGYVLSNGHKQLICLARSI 1361
Cdd:cd03218 79 YLPQEASIFR---KLTVE-------ENILAVLEIRGLsKKEREEKLEELleEFHITHlrksKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1362 LSGARILLLDEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHKVEPLLE-CQSFLMMDKGQV 1422
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKV 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
439-642 |
5.43e-14 |
|
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: 77.68 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDNI 505
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 -LFGLTYDEYRYKSVVKAcQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKE 584
Cdd:TIGR00957 1381 dPFSQYSDEEVWWALELA-HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 1459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 585 I-------FDKClcklmaskTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSL 642
Cdd:TIGR00957 1460 IqstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
488-634 |
6.31e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 488 SYSSQTAWIMPGTIRDNILFGltYDEYRYKSVVKACQ---LEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRD 564
Cdd:PTZ00265 1299 SIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLRE 1376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 565 ADLYLLDAPFTHLDIATEKEIfDKCLC--KLMASKTRILVTNKIEHLKRADKILLLHNGE---SFF--YGTFPELQS 634
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEKLI-EKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgSFVqaHGTHEELLS 1452
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
438-696 |
6.45e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.26 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDNI 505
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpINMMFQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LFGLTYDEYRYKSVvkACQLEEDLAALPEKD---KTPMaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDiate 582
Cdd:PRK11607 113 AFGLKQDKLPKAEI--ASRVNEMLGLVHMQEfakRKPH-----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 583 KEIFDKCLCKLMASKTRILVT------NKIEHLKRADKILLLHNGESFFYGTfPELQSERPD--FSSLLLG-LEAYDNIS 653
Cdd:PRK11607 182 KKLRDRMQLEVVDILERVGVTcvmvthDQEEAMTMAGRIAIMNRGKFVQIGE-PEEIYEHPTtrYSAEFIGsVNVFEGVL 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 68390341 654 AERRCSILT----ETLHRVSVDESAGMQ---PERSAFRqvpPTKPMYIDE 696
Cdd:PRK11607 261 KERQEDGLVidspGLVHPLKVDADASVVdnvPVHVALR---PEKIMLCEE 307
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
442-578 |
6.95e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 442 DISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR------HSGRISYSSQTAWI--MPGtIRDNilfgLTYDE 513
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQDLLYLghQPG-IKTE----LTALE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 514 -YRYKSVVKACQLEEDL-AALpekdktpmAEGGL---------NLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:PRK13538 94 nLRFYQRLHGPGDDEALwEAL--------AQVGLagfedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
440-646 |
8.05e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.90 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRIsyssqtawIMPG-------------------- 499
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV--------ITAGkknkklkplrkkvgivfqfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 -------TIRDNILFG-----LTYDE--YRYKSVVKACQLEEDLAalpekDKTPMAegglnLSGGQKARVALARAVYRDA 565
Cdd:PRK13634 95 ehqlfeeTVEKDICFGpmnfgVSEEDakQKAREMIELVGLPEELL-----ARSPFE-----LSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 566 DLYLLDAPFTHLDIATEKEIFDkCLCKLMASK--TRILVTNKIEHLKR-ADKILLLHNGESFFYGTFPELQSERPDFSSL 642
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMME-MFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
....
gi 68390341 643 LLGL 646
Cdd:PRK13634 244 GLDL 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
432-580 |
8.14e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 432 TNLYV----APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRiSYSSQTAWIM---------- 497
Cdd:PRK13548 6 RNLSVrlggRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR-PLADWSPAELarrravlpqh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 498 -----PGTIRDNILFGL---TYDEYRYKSVVKACQLEEDLAALPEKDKtpmaeggLNLSGGQKARVALARA---VYRDAD 566
Cdd:PRK13548 85 sslsfPFTVEEVVAMGRaphGLSRAEDDALVAAALAQVDLAHLAGRDY-------PQLSGGEQQRVQLARVlaqLWEPDG 157
|
170
....*....|....*..
gi 68390341 567 ---LYLLDAPFTHLDIA 580
Cdd:PRK13548 158 pprWLLLDEPTSALDLA 174
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
438-622 |
8.98e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.10 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGrISYSSQTAWIMPG----------------TI 501
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG-ITISKENLKEIRKkigiifqnpdnqfigaTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGLTYDEYRYK-------SVVKACQLEEDLaalpekDKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:PRK13632 102 EDDIAFGLENKKVPPKkmkdiidDLAKKVGMEDYL------DKEP-----QNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 575 THLDIATEKEIFdkclcKLM------ASKTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:PRK13632 171 SMLDPKGKREIK-----KIMvdlrktRKKTLISITHDMDEAILADKVIVFSEGK 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
439-642 |
9.05e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG--RISYSSQTAWI--------------MPGTIR 502
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQKLYLdttlpltvnrflrlRPGTKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 503 DNILFGLTYdeyryksvVKACQLEEdlaalpekdkTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATE 582
Cdd:PRK09544 99 EDILPALKR--------VQAGHLID----------APMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 583 KEIFD---------KCLCkLMASKTRILVTNKIehlkraDKILLLhNGESFFYGTfPELQSERPDFSSL 642
Cdd:PRK09544 157 VALYDlidqlrrelDCAV-LMVSHDLHLVMAKT------DEVLCL-NHHICCSGT-PEVVSLHPEFISM 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
438-621 |
1.02e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG------------RISYSSQTAWIMPG-TIRDN 504
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQFDNLDLEfTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 IL-FGltydeyRYKSVvKACQLEE------DLAALPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:PRK13536 135 LLvFG------RYFGM-STREIEAvipsllEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 578 DIATEKEIFDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNG 621
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAG 248
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
438-622 |
1.22e-13 |
|
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: 71.88 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDNI 505
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNYALFPHlTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LFGLTYDEYRyKSVVKAcQLEE--DLAALPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:cd03300 94 AFGLRLKKLP-KAEIKE-RVAEalDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 584 EIfdkcLCKLMASKTR-----ILVT-NKIEHLKRADKILLLHNGE 622
Cdd:cd03300 168 DM----QLELKRLQKElgitfVFVThDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1211-1406 |
1.27e-13 |
|
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: 71.98 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAghaVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPLQKwrKAFGV 1289
Cdd:cd03299 1 LKVENLSKDWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILLNGKDITNLPPEK--RDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFtgP-----------LRMNLDPYGcHSDEELWRVAEEVGLKTVIEQFPDKldfqleyggyvLSNGHKQLICLA 1358
Cdd:cd03299 76 VPQNYALF--PhmtvykniaygLKKRKVDKK-EIERKVLEIAEMLGIDHLLNRKPET-----------LSGGEQQRVAIA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 1359 RSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQSFSTcTILLSEHKVE 1406
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTkekLREELKKIRKEFGV-TVLHVTHDFE 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
438-627 |
1.30e-13 |
|
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: 71.04 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPS--SGKIRHSGRISYSSQTAWIMPGTIRDNILFG-LTYDEY 514
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKIIGYVPQDDILHPtLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 515 RYKSvvkacqleedlAALPekdktpmaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFdKCLCKLM 594
Cdd:cd03213 103 LMFA-----------AKLR------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM-SLLRRLA 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 68390341 595 ASKTRILVT-----NKIEHLkrADKILLLHNGESFFYG 627
Cdd:cd03213 159 DTGRTIICSihqpsSEIFEL--FDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
439-627 |
1.33e-13 |
|
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: 71.92 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGeLVPSSGKIrhSGRISYSSQTawIMPGTIRDNILF---------GL 509
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTT--SGQILFNGQP--RKPDQFQKCVAYvrqddillpGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 510 TYDEYRYKSVVKACQLEedlaaLPEKDKTPMAEGGL---------------NLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:cd03234 97 TVRETLTYTAILRLPRK-----SSDAIRKKRVEDVLlrdlaltriggnlvkGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 575 THLDIATEKEIFdKCLCKLMASKTRILVTnkiEHLKRA------DKILLLHNGESFFYG 627
Cdd:cd03234 172 SGLDSFTALNLV-STLSQLARRNRIVILT---IHQPRSdlfrlfDRILLLSSGEIVYSG 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1211-1431 |
1.70e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.83 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVnwnkmPLQKW-RKAFG 1288
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDsGEVLWDGE-----PLDPEdRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVP--------QKVF---IFTGPLRmNLDPygchsdeelwRVAEEVgLKTVIEQF--PDKLDFQLEyggyVLSNGHKQLI 1355
Cdd:COG4152 75 YLPeerglypkMKVGeqlVYLARLK-GLSK----------AEAKRR-ADEWLERLglGDRANKKVE----ELSKGNQQKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1356 CLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFST-CTILLSEH---KVEPLleCQSFLMMDKGQVKTYDSIQKL 1431
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHqmeLVEEL--CDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
447-579 |
2.11e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 447 LKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQtaWIMP---GTIRDnILFGLT--YDEYRYKS-VV 520
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIKPdydGTVED-LLRSITddLGSSYYKSeII 438
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 521 KACQLEEdlaaLPEKDKTpmaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:PRK13409 439 KPLQLER----LLDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
442-648 |
2.70e-13 |
|
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: 73.21 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 442 DISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR-----------------HSGRISYSSQTAWIMPG-TIRD 503
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflppHRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFGL-----TYDEYRYKSVVKACQLEEDLAALPEkdktpmaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:COG4148 97 NLLYGRkraprAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 579 IATEKEIFDkCLCKLmASKTRI---LVTNKIEHLKR-ADKILLLHNGESFFYGTFPELQSeRPDFSSLLLGLEA 648
Cdd:COG4148 166 LARKAEILP-YLERL-RDELDIpilYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS-RPDLLPLAGGEEA 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
438-622 |
3.04e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.69 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRIsYSSQTAW----------------IMPGTI 501
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVWdirhkigmvfqnpdnqFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGLTYDEYRYKSVVKACQLEEDLAALPE-KDKTPMaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLD-- 578
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDfKEREPA-----RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpe 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 68390341 579 -----IATEKEIFDKclcklmASKTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:PRK13650 175 grlelIKTIKGIRDD------YQMTVISITHDLDEVALSDRVLVMKNGQ 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1211-1422 |
3.21e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKY---------TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTDGEISIDGvnwnkMPLQ 1281
Cdd:PRK15134 276 LDVEQLQVAFpirkgilkrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDG-----QPLH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1282 KW--RKAFGVVPQKVFIFTGPL-----RMNL-------------DPYGCHSDEELWRVAEEVGLKTVIEQ-FPDKLdfql 1340
Cdd:PRK15134 351 NLnrRQLLPVRHRIQVVFQDPNsslnpRLNVlqiieeglrvhqpTLSAAQREQQVIAVMEEVGLDPETRHrYPAEF---- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1341 eyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQSFSTCTILLSE--HKVEPLleCQSFL 1415
Cdd:PRK15134 427 -------SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVqaqILALLKSLQQKHQLAYLFISHdlHVVRAL--CHQVI 497
|
....*..
gi 68390341 1416 MMDKGQV 1422
Cdd:PRK15134 498 VLRQGEV 504
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1211-1422 |
3.72e-13 |
|
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: 70.88 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLfnalLKLVYTD------GEISIDGVNWNKMPLQKWR 1284
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTL----LSLITGDlpptygNDVRLFGERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1285 KAFGVV----------PQKVF--IFTGpLRMNLDPYGCHSDEEL---WRVAEEVGLKTVIEQfpdkldfqlEYGGyvLSN 1349
Cdd:COG1119 78 KRIGLVspalqlrfprDETVLdvVLSG-FFDSIGLYREPTDEQReraRELLELLGLAHLADR---------PFGT--LSQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 1350 GHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ--SFSTCTILLSEHKVEPLLECQS-FLMMDKGQV 1422
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGIThVLLLKDGRV 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
438-635 |
4.81e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAWimpgTIRDNIlfGLTYDEYRYK 517
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLW----DIRNKA--GMVFQNPDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 518 SVvkACQLEEDLAALPEK----------------DKTPMAEGGLN----LSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:PRK13633 98 IV--ATIVEEDVAFGPENlgippeeirervdeslKKVGMYEYRRHaphlLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 578 DIATEKEIFDKclCKLMASK---TRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSE 635
Cdd:PRK13633 176 DPSGRREVVNT--IKELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1211-1422 |
5.20e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGvnwnkMPLQKwrkafgv 1289
Cdd:PRK15056 7 IVVNDVTVTWRN-GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISILG-----QPTRQ------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 vpqkvfiftgPLRMNLDPYGCHSDEELW---------------------RVAEEVGLKTVIEQFP--DKLDFQLEYGGYv 1346
Cdd:PRK15056 74 ----------ALQKNLVAYVPQSEEVDWsfpvlvedvvmmgryghmgwlRRAKKRDRQIVTAALArvDMVEFRHRQIGE- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 1347 LSNGHKQLICLARSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQsfSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRD--EGKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1208-1403 |
5.45e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.71 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1208 RGQIEVRNLTVKYTEAghAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKL---VYTDGEISIDGVNWNKMPLQ 1281
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLlrvFNRLIELypeARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1282 KWRKAFgvvpQKVFIFTGP-----------LRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDFQleygGYVLSNG 1350
Cdd:PRK14247 79 ELRRRV----QMVFQIPNPipnlsifenvaLGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAP----AGKLSGG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1351 HKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEH 1403
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
439-632 |
5.80e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.37 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-----RISYSSQTAWIMPG--------TIRDNI 505
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsRARHARQRVGVVPQfdnldpdfTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 L-----FGLTYDEYRyksvvKACQLEEDLAALPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:PRK13537 102 LvfgryFGLSAAAAR-----ALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 581 TEKEIFDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGESFFYGTFPEL 632
Cdd:PRK13537 173 ARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
440-587 |
5.87e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR----------ISY---SSQTAWIMPGTIRDNIL 506
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYvpqSEEVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 507 FGlTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGL-NLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEI 585
Cdd:PRK15056 103 MG-RYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
..
gi 68390341 586 FD 587
Cdd:PRK15056 182 IS 183
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1211-1422 |
6.51e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 71.65 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAV--LKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKlvYTDGEISIDGVNWNKMP---LQK 1282
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLER--PTSGSVLVDGVDLTALSereLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVPQK--------VF--I-FtgPLrmnldpygchsdeELW---------RVAE---EVGLKTVIEQFPDKldfq 1339
Cdd:COG1135 80 ARRKIGMIFQHfnllssrtVAenVaL--PL-------------EIAgvpkaeirkRVAElleLVGLSDKADAYPSQ---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1340 leyggyvLSNGHKQLICLARSILSGARILLLDEPSAHLDPVT----IKVLKKtLRQSFSTcTILLSEH------KVepll 1409
Cdd:COG1135 141 -------LSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsiLDLLKD-INRELGL-TIVLITHemdvvrRI---- 207
|
250
....*....|...
gi 68390341 1410 eCQSFLMMDKGQV 1422
Cdd:COG1135 208 -CDRVAVLENGRI 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
439-635 |
7.35e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.91 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR---------HSGRISYssqtawiMP---G-----TI 501
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldpeDRRRIGY-------LPeerGlypkmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILF-----GLTydeyryKSVVKAcQLEEDLAA--LPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:COG4152 89 GEQLVYlarlkGLS------KAEAKR-RADEWLERlgLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 575 THLD-IATE---KEIFDkclckLMAS-KTRILVTNKIEHLKR-ADKILLLHNGESFFYGTFPELQSE 635
Cdd:COG4152 158 SGLDpVNVEllkDVIRE-----LAAKgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
440-636 |
7.76e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAWI---------------MPGTIRDN 504
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFG-----LTYDEY--RYKSVVKACQLEEdlaalpEKDKTPMaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:PRK13647 101 VAFGpvnmgLDKDEVerRVEEALKAVRMWD------FRDKPPY-----HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 578 DIATEKEIFDkCLCKL-MASKTRILVTNKIE-HLKRADKILLLHNGESFFYGTfPELQSER 636
Cdd:PRK13647 170 DPRGQETLME-ILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDE 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
440-632 |
9.32e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.99 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-----------------RISYSSQTAWIMPG-TI 501
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGLtydeyRYKSVVKACQLEEDLAALPEKDKTPMAEGGLN-LSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:PRK10070 124 LDNTAFGM-----ELAGINAEERREKALDALRQVGLENYAHSYPDeLSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 581 TEKEIFDKcLCKLMA--SKTRILVTNKI-EHLKRADKILLLHNGESFFYGTFPEL 632
Cdd:PRK10070 199 IRTEMQDE-LVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1211-1422 |
1.26e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.04 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGvnwnkMPLQK---W--R 1284
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGG-----MVLSEetvWdvR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1285 KAFGVV---PQKVFIFT---GPLRMNLDPYGCHSDEELWRVAE---EVGLKTVIEQFPDKldfqleyggyvLSNGHKQLI 1355
Cdd:PRK13635 81 RQVGMVfqnPDNQFVGAtvqDDVAFGLENIGVPREEMVERVDQalrQVGMEDFLNREPHR-----------LSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1356 CLARSILSGARILLLDEPSAHLDPV-------TIKVLKKTLRqsfstCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRgrrevleTVRQLKEQKG-----ITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
437-627 |
1.39e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.06 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTI---LGELVPSSGKI------------RHSGRISYSSQTAWIMPG-T 500
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIhyngipykefaeKYPGEIIYVSEEDVHFPTlT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFGLTydeyryksvvkaCQLEEdlaalpekdktpMAEGglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:cd03233 100 VRETLDFALR------------CKGNE------------FVRG---ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 581 TEKEIFdKCLcKLMASKTR--ILVT-----NKIEHLkrADKILLLHNGESFFYG 627
Cdd:cd03233 153 TALEIL-KCI-RTMADVLKttTFVSlyqasDEIYDL--FDKVLVLYEGRQIYYG 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1211-1382 |
2.04e-12 |
|
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: 71.64 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYT--------EAGH--AVlKNLSFS-AEGrQRVGILGRTGSGKSSLFNALLKLVYTDGEISIDGVNWNKMP 1279
Cdd:COG4172 276 LEARDLKVWFPikrglfrrTVGHvkAV-DGVSLTlRRG-ETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1280 ---LQKWRKAFGVVPQkvfiftgplrmnlDPYGC-----------------H----SDEELW-RVA---EEVGLKtvieq 1331
Cdd:COG4172 354 rraLRPLRRRMQVVFQ-------------DPFGSlsprmtvgqiiaeglrvHgpglSAAERRaRVAealEEVGLD----- 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1332 fPDKLD-----FqleyggyvlSNGHKQLICLARSILSGARILLLDEP-SAhLDpVTI 1382
Cdd:COG4172 416 -PAARHrypheF---------SGGQRQRIAIARALILEPKLLVLDEPtSA-LD-VSV 460
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1211-1379 |
2.28e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.64 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL-KLVYTDGEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:PRK13548 3 LEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKV---FIFTGP--LRMNLDPYGCHSDEELwRVAEEVGLKTVIEQFPDKlDFQleyggyVLSNGHKQLICLAR----- 1359
Cdd:PRK13548 81 LPQHSslsFPFTVEevVAMGRAPHGLSRAEDD-ALVAAALAQVDLAHLAGR-DYP------QLSGGEQQRVQLARvlaql 152
|
170 180
....*....|....*....|.
gi 68390341 1360 -SILSGARILLLDEPSAHLDP 1379
Cdd:PRK13548 153 wEPDGPPRWLLLDEPTSALDL 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
446-579 |
2.45e-12 |
|
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: 71.35 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 446 KLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQtaWI---MPGTIRDnILFGLTYDEYR---YKS- 518
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ--YIspdYDGTVEE-FLRSANTDDFGssyYKTe 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 519 VVKACQLEEdlaaLPEKDKTpmaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:COG1245 439 IIKPLGLEK----LLDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1211-1451 |
2.97e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.20 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEISIDG--VNWNKMPLQKWRKAF 1287
Cdd:PRK09493 2 IEFKNVSKHFGP--TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLeEITSGDLIVDGlkVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKVFIFT----------GPLRMNldpyGChSDEELWRVAEE----VGLKTVIEQFPDKLdfqleyggyvlSNGHKQ 1353
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR----GA-SKEEAEKQAREllakVGLAERAHHYPSEL-----------SGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1354 LICLARSILSGARILLLDEPSAHLDP-VTIKVLK--KTLRQSFSTCTILLSE----HKVEPLLecqsfLMMDKGQVKTYD 1426
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPeLRHEVLKvmQDLAEEGMTMVIVTHEigfaEKVASRL-----IFIDKGRIAEDG 218
|
250 260
....*....|....*....|....*
gi 68390341 1427 SIQKLLNEtshlkqaiSPAERLKLF 1451
Cdd:PRK09493 219 DPQVLIKN--------PPSQRLQEF 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
439-622 |
3.16e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.29 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSlLMTILGEL-VPSSGKIRHSGR-ISyssqtawimpgTIRDNIL-------FGL 509
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKST-LMNILGCLdKPTSGTYRVAGQdVA-----------TLDADALaqlrrehFGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 510 TYDEYRYKSVVKACQLEE---DLAALPEKDKTPMAEG-----GL---------NLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:PRK10535 91 IFQRYHLLSHLTAAQNVEvpaVYAGLERKQRLLRAQEllqrlGLedrveyqpsQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 573 PFTHLDIATEKEIFD--KCLCKlmASKTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:PRK10535 171 PTGALDSHSGEEVMAilHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGE 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
408-586 |
3.27e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 408 ELLERIKQENKANG--HHNGDAGLFFTNLYVA-----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGeLVPS-SG 479
Cdd:COG4178 340 EALEAADALPEAASriETSEDGALALEDLTLRtpdgrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 480 KIRH--SGRISYSSQTAWIMPGTIRDNILF---GLTYDEYRYKSVVKACQLeEDLAALPEKDktpmAEGGLNLSGGQKAR 554
Cdd:COG4178 419 RIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGL-GHLAERLDEE----ADWDQVLSLGEQQR 493
|
170 180 190
....*....|....*....|....*....|..
gi 68390341 555 VALARAVYRDADLYLLDAPFTHLDIATEKEIF 586
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1211-1403 |
3.40e-12 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 67.42 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKwrkaFGV 1289
Cdd:TIGR03740 1 LETKNLSKRF--GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRpTSGEIIFDGHPWTRKDLHK----IGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VpqkvfIFTGPLRMNLDPY---GCH------SDEELWRVAEEVGLkTVIEQFPDKlDFQLeyggyvlsnGHKQLICLARS 1360
Cdd:TIGR03740 75 L-----IESPPLYENLTARenlKVHttllglPDSRIDEVLNIVDL-TNTGKKKAK-QFSL---------GMKQRLGIAIA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 1361 ILSGARILLLDEPSAHLDPVTIKVLKKTLRqSFST--CTILLSEH 1403
Cdd:TIGR03740 139 LLNHPKLLILDEPTNGLDPIGIQELRELIR-SFPEqgITVILSSH 182
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
439-587 |
3.50e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAwimPGTIRDNILfGLTYDEYRYK 517
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpMSKLSSAA---KAELRNQKL-GFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 518 SVVKAcqLEEdlAALP------------EKDKTPMAEGGLN---------LSGGQKARVALARAVYRDADLYLLDAPFTH 576
Cdd:PRK11629 100 PDFTA--LEN--VAMPlligkkkpaeinSRALEMLAAVGLEhranhrpseLSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170
....*....|.
gi 68390341 577 LDIATEKEIFD 587
Cdd:PRK11629 176 LDARNADSIFQ 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1211-1423 |
3.61e-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: 70.60 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL----------KLVYT---------------D 1265
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmdqyeptsgRIIYHvalcekcgyverpskV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1266 GE-----------ISIDGVNWNKMPLQKWRKAFGVVPQKVFIFTGPLRM------NLDPYGCHSDEELWRVAEevglktV 1328
Cdd:TIGR03269 79 GEpcpvcggtlepEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVldnvleALEEIGYEGKEAVGRAVD------L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1329 IEQFpdKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSF--STCTILLSEHKVE 1406
Cdd:TIGR03269 153 IEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPE 230
|
250
....*....|....*...
gi 68390341 1407 PLLECQSF-LMMDKGQVK 1423
Cdd:TIGR03269 231 VIEDLSDKaIWLENGEIK 248
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1211-1431 |
4.79e-12 |
|
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: 67.01 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKY--TEAghavLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPlQKWRKAF 1287
Cdd:cd03265 1 IEVENLVKKYgdFEA----VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGHDVVREP-REVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKVFI---FTG--PLRMNLDPYGCHSDEELWRVAEevglktVIEqFPDKLDFQLEYGGYvLSNGHKQLICLARSIL 1362
Cdd:cd03265 76 GIVFQDLSVddeLTGweNLYIHARLYGVPGAERRERIDE------LLD-FVGLLEAADRLVKT-YSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1363 SGARILLLDEPSAHLDPVT----IKVLKKtLRQSFSTcTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQKL 1431
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTrahvWEYIEK-LKEEFGM-TILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
440-638 |
5.35e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.73 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLL----------------MTILGELVPSSGKIRHSGRISySSQTAWIMPG---- 499
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdksagshIELLGRTVQREGRLARDIRKS-RANTGYIFQQfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 ---TIRDNILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMAEGGLN----LSGGQKARVALARAVYRDADLYLLDA 572
Cdd:PRK09984 99 nrlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQrvstLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 573 PFTHLDIATEKEIFDKCLCKLMASKTRILVT-NKIEH-LKRADKILLLHNGESFFYGTFPELQSERPD 638
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFD 246
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
439-622 |
6.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI----------RHSGRISYSSQTAWIMP---------- 498
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEKLVIQKtrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 499 -------------------GTIRDNILFG-LTYDEYRYKSVVKACQLEEdLAALPEK--DKTPmaeggLNLSGGQKARVA 556
Cdd:PRK13651 102 eirrrvgvvfqfaeyqlfeQTIEKDIIFGpVSMGVSKEEAKKRAAKYIE-LVGLDESylQRSP-----FELSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 557 LARAVYRDADLYLLDAPFTHLDIATEKEIFDkCLCKLMAS-KTRILVTNKIEH-LKRADKILLLHNGE 622
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNKQgKTIILVTHDLDNvLEWTKRTIFFKDGK 242
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1227-1404 |
6.44e-12 |
|
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: 66.91 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1227 VLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY----TDGEISIDGVNWNKmplQKWRKAFGVVPQKVFI------ 1296
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggtTSGQILFNGQPRKP---DQFQKCVAYVRQDDILlpgltv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1297 -----FTGPLRMnldPYgCHSDEELWRVAEEVGLKTV-IEQFPDKLdfqleYGGyvLSNGHKQLICLARSILSGARILLL 1370
Cdd:cd03234 99 retltYTAILRL---PR-KSSDAIRKKRVEDVLLRDLaLTRIGGNL-----VKG--ISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190
....*....|....*....|....*....|....*
gi 68390341 1371 DEPSAHLDPVTIKVLKKTLRQ-SFSTCTILLSEHK 1404
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHQ 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
437-623 |
6.52e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRD 503
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFGLtydEYRYKSVVKAcQLEEDLA--ALPEKdktpMAEGGLN-LSGGQKARVALARAVYRDADLYLLDAPFTHLDiA 580
Cdd:PRK10247 100 NLIFPW---QIRNQQPDPA-IFLDDLErfALPDT----ILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD-E 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68390341 581 TEKEIFDKCLCKLMASK--TRILVTNKIEHLKRADKILLL--HNGES 623
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITLqpHAGEM 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1211-1463 |
7.51e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKLvyTDGEISIDGVNWNKMP-LQKWRKA 1286
Cdd:PRK13644 2 IRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRP--QKGKVLVSGIDTGDFSkLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVV---PQKVFIFT--------GPLRMNLDPYGCHSDEElwRVAEEVGLKTVIEQFPDkldfqleyggyVLSNGHKQLI 1355
Cdd:PRK13644 79 VGIVfqnPETQFVGRtveedlafGPENLCLPPIEIRKRVD--RALAEIGLEKYRHRSPK-----------TLSGGQGQCV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1356 CLARSILSGARILLLDEPSAHLDPVT-IKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLLNE 1434
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 68390341 1435 TSHLKQAISP------AERLKL----FPRRNSSmrTPQS 1463
Cdd:PRK13644 226 VSLQTLGLTPpslielAENLKMhgvvIPWENTS--SPSS 262
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
438-620 |
7.74e-12 |
|
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: 65.25 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLmTILGELVPS-SGKIRH--SGRISYSSQTAWIMPGTIRDNILFgltydey 514
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLWPWgSGRIGMpeGEDLLFLPQRPYLPLGTLREQLIY------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 515 ryksvvkacqleedlaalPEKDKtpmaegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCKLM 594
Cdd:cd03223 87 ------------------PWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI 139
|
170 180
....*....|....*....|....*.
gi 68390341 595 askTRILVTNKIEHLKRADKILLLHN 620
Cdd:cd03223 140 ---TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
439-627 |
9.22e-12 |
|
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: 66.24 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-RISYSSQTAW----IMPG--------TIRDNI 505
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlgFVSDstglydrlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 -----LFGLTYDEY--RYKSVVKACQLEEDLaalpekDKTpmAEGglnLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:cd03266 100 eyfagLYGLKGDELtaRLEELADRLGMEELL------DRR--VGG---FSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 579 IATEKEIFD--KCLCKlmASKTRILVTNKIEHLKR-ADKILLLHNGESFFYG 627
Cdd:cd03266 169 VMATRALREfiRQLRA--LGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1210-1440 |
9.61e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1210 QIEVRNLTVKY---TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLklVYTDGEISIDGVNWN------- 1276
Cdd:PRK13651 2 QIKVKNIVKIFnkkLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALL--LPDTGTIEWIFKDEKnkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1277 ------KMPLQK-----------WRKAFGVVPQ------------KVFIFtGPLRMNLDPygchsDEELWRVAEEVGLKT 1327
Cdd:PRK13651 80 kekvleKLVIQKtrfkkikkikeIRRRVGVVFQfaeyqlfeqtieKDIIF-GPVSMGVSK-----EEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1328 VIEQFPDKLDFQLeyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDPV-TIKVLK--KTLRQSFStcTILLSEHK 1404
Cdd:PRK13651 154 LDESYLQRSPFEL-------SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEifDNLNKQGK--TIILVTHD 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 68390341 1405 VEPLLE-CQSFLMMDKGQV----KTYDsiqkLLNETSHLKQ 1440
Cdd:PRK13651 225 LDNVLEwTKRTIFFKDGKIikdgDTYD----ILSDNKFLIE 261
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1228-1440 |
1.01e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 67.55 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1228 LKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKLvyTDGEISIDG----VNWNKMPLQKWRKAFGVVPQ----KVF- 1295
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLmqhFNALLKP--SSGTITIAGyhitPETGNKNLKKLRKKVSLVFQfpeaQLFe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1296 ------IFTGPLRMNLdpygchSDEELWRVA----EEVGLKtviEQFPDKLDFQleyggyvLSNGHKQLICLARSILSGA 1365
Cdd:PRK13641 101 ntvlkdVEFGPKNFGF------SEDEAKEKAlkwlKKVGLS---EDLISKSPFE-------LSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1366 RILLLDEPSAHLDPVTikvlKKTLRQSF-----STCTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQKLLNETSHLK 1439
Cdd:PRK13641 165 EILCLDEPAAGLDPEG----RKEMMQLFkdyqkAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKEWLK 240
|
.
gi 68390341 1440 Q 1440
Cdd:PRK13641 241 K 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
440-611 |
1.62e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.34 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTI--LGELVPS---SGKIRHSG---------------RISYSSQTAWIMPG 499
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGknlyapdvdpvevrrRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIRDNILFGLTYDEYR--YKSVVkacqlEEDL--AALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFT 575
Cdd:PRK14243 106 SIYDNIAYGARINGYKgdMDELV-----ERSLrqAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 68390341 576 HLD-IATEKeiFDKCLCKLMASKTRILVTNKIEHLKR 611
Cdd:PRK14243 181 ALDpISTLR--IEELMHELKEQYTIIIVTHNMQQAAR 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
439-635 |
1.70e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.64 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSS-------QTAWIM----------PgT 500
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYDKksllevrKTVGIVfqnpddqlfaP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFG-----LTYDEY--RYKSVVKACQLEEdlaalpEKDKTPMaegglNLSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:PRK13639 96 VEEDVAFGplnlgLSKEEVekRVKEALKAVGMEG------FENKPPH-----HLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 574 FTHLDIATEKEIFdKCLCKLMASKTRILVTNKIEHL--KRADKILLLHNGESFFYGTFPELQSE 635
Cdd:PRK13639 165 TSGLDPMGASQIM-KLLYDLNKEGITIIISTHDVDLvpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
440-628 |
1.91e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSG--------------KIRHSGRISYSSQTAWIMP------G 499
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyaipanlkKIKEVKRLRKEIGLVFQFPeyqlfqE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIRDNILFGLTYDEYRYKSVVKACQLEEDLAALPEK--DKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyvKRSP-----FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 578 DIATEKEIFDKCLCKLMASKTR-ILVTNKIEH-LKRADKILLLHNGESFFYGT 628
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRiIMVTHNMDQvLRIADEVIVMHEGKVISIGS 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
438-621 |
2.57e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.28 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDNI 505
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrhVNTVFQSYALFPHmTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LFGLTYD-------EYRYKSVVKACQLEEdLAalpekDKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:PRK09452 108 AFGLRMQktpaaeiTPRVMEALRMVQLEE-FA-----QRKP-----HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 579 IATEKEifdkclcklMASK----------TRILVT-NKIEHLKRADKILLLHNG 621
Cdd:PRK09452 177 YKLRKQ---------MQNElkalqrklgiTFVFVThDQEEALTMSDRIVVMRDG 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
438-628 |
2.89e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTI-LGElVPSSGKIRHSG-RISYSSQTA--------------------W 495
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLE-TPDSGQLNIAGhQFDFSQKPSekairllrqkvgmvfqqynlW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 496 imPG-TIRDNIL------FGLTYDEYRYK--SVVKACQLEEDLAALPekdktpmaeggLNLSGGQKARVALARAVYRDAD 566
Cdd:COG4161 95 --PHlTVMENLIeapckvLGLSKEQAREKamKLLARLRLTDKADRFP-----------LHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 567 LYLLDAPFTHLDIATEKEIFDkcLCKLMASK--TRILVTNKIEHLKR-ADKILLLHNGESFFYGT 628
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVE--IIRELSQTgiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1213-1426 |
3.26e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1213 VRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL-KLVYTDGEISIDGvnwnkmplqKWRkaFGVVP 1291
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgELEPDSGEVSIPK---------GLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1292 QKVFIFTG------------PLRMNLDPY------GCHSDEELWRVAE-------------EVGLKTVIEQ--FPDkLDF 1338
Cdd:COG0488 68 QEPPLDDDltvldtvldgdaELRALEAELeeleakLAEPDEDLERLAElqeefealggweaEARAEEILSGlgFPE-EDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1339 QLEYGgyVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQsfSTCTILLSEHKVEpLLE--CQSFLM 1416
Cdd:COG0488 147 DRPVS--ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHDRY-FLDrvATRILE 221
|
250
....*....|
gi 68390341 1417 MDKGQVKTYD 1426
Cdd:COG0488 222 LDRGKLTLYP 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-622 |
3.28e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTI-----LGELVPSSGKIRHSGRISYSSQTAWI-----------MPG--- 499
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIevrrevgmvfqYPNpfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 --TIRDNILFGLTYDeyryKSVVKACQLEEDL------AALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLD 571
Cdd:PRK14267 99 hlTIYDNVAIGVKLN----GLVKSKKELDERVewalkkAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 572 APFTHLDIATEKEIfDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:PRK14267 175 EPTANIDPVGTAKI-EELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGK 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1212-1406 |
3.73e-11 |
|
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: 65.06 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1212 EVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNAL---LKLvyTDGEISIDGVNWNKMPLQKwRKAFG 1288
Cdd:COG0411 6 EVRGLTKRF--GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItgfYRP--TSGRILFDGRDITGLPPHR-IARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VV------------------------PQKVFIFTGPLRMnldPYGCHSDEELWRVAEE----VGLKTVIEQFPDKldfql 1340
Cdd:COG0411 81 IArtfqnprlfpeltvlenvlvaahaRLGRGLLAALLRL---PRARREEREARERAEEllerVGLADRADEPAGN----- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 1341 eyggyvLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ--SFSTCTILLSEHKVE 1406
Cdd:COG0411 153 ------LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlrDERGITILLIEHDMD 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1199-1405 |
4.36e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.50 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1199 AQADSSWPHRGQIevrNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL------VYTDGEISIDG 1272
Cdd:PRK14271 13 ADVDAAAPAMAAV---NLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1273 VN-WNKMPLQKWRKAFGVVPQKVFIFTGPLRMNL----DPYGCHSDEELWRVAE----EVGLKTVIEQfpdkldfQLEYG 1343
Cdd:PRK14271 88 RSiFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVlagvRAHKLVPRKEFRGVAQarltEVGLWDAVKD-------RLSDS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1344 GYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKV 1405
Cdd:PRK14271 161 PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1211-1396 |
4.39e-11 |
|
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: 62.94 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVkYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEISidgvnwnkMPlqkWRKAFGV 1289
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSGRIG--------MP---EGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTGPLRmnldpygchsdeelwrvaeevglktviEQ--FP-DKldfqleyggyVLSNGHKQLICLARSILSGAR 1366
Cdd:cd03223 69 LPQRPYLPLGTLR---------------------------EQliYPwDD----------VLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|
gi 68390341 1367 ILLLDEPSAHLDPVTIKVLKKTLRQSFSTC 1396
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELGITV 141
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1211-1406 |
4.74e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.01 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVnwnKMPLQK--WRKAF 1287
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDaGKITVLGV---PVPARArlARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKVFI---FTgpLRMNLDPYGCHsdeelwrvaeeVGLKT--VIEQFPDKLDF-QLEYGGYV----LSNGHKQLICL 1357
Cdd:PRK13536 117 GVVPQFDNLdleFT--VRENLLVFGRY-----------FGMSTreIEAVIPSLLEFaRLESKADArvsdLSGGMKRRLTL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 1358 ARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTC-TILLSEHKVE 1406
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTHFME 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1211-1441 |
5.15e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSS---LFNALLkLVYTDGE--ISIDGVNWNKMPLQKWRK 1285
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLL-LPDDNPNskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 AFGVV---PQKVFI---FTGPLRMNLDPYGCHSDEEL---WRVAEEVGLktvieqfpdkLDFQLEYGGYvLSNGHKQLIC 1356
Cdd:PRK13640 85 KVGIVfqnPDNQFVgatVGDDVAFGLENRAVPRPEMIkivRDVLADVGM----------LDYIDSEPAN-LSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1357 LARSILSGARILLLDEPSAHLDPVTIKVLKKTLR--QSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLLNE 1434
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
....*..
gi 68390341 1435 TSHLKQA 1441
Cdd:PRK13640 234 VEMLKEI 240
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1228-1431 |
8.11e-11 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 64.72 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1228 LKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPlQKWRKAFGVVPQKVF---IFTG--PL 1301
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRpTSGTARVAGYDVVREP-RKVRRSIGIVPQYASvdeDLTGreNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1302 RMNLDPYGCHSDEELWRVAEevglktVIEQFpDKLDFQLEYGGYvLSNGHKQLICLARSILSGARILLLDEPSAHLDPVT 1381
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERAEE------LLELF-ELGEAADRPVGT-YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 1382 -------IKVLKKtlrqsfSTCTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQKL 1431
Cdd:TIGR01188 160 rraiwdyIRALKE------EGVTILLTTHYMEEADKlCDRIAIIDHGRIIAEGTPEEL 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
428-628 |
8.34e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 64.47 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 428 GLFFTNLYVApvLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR------HSGRISYSSQTAWIM---P 498
Cdd:COG4167 19 GLFRRQQFEA--VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILinghklEYGDYKYRCKHIRMIfqdP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 499 GTI---RDNIlfGLTYDE-----------YRYKSVVKACQLeedLAALPEK--DKTPMaegglnLSGGQKARVALARAVY 562
Cdd:COG4167 97 NTSlnpRLNI--GQILEEplrlntdltaeEREERIFATLRL---VGLLPEHanFYPHM------LSSGQKQRVALARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 563 RDADLYLLDAPFTHLDIATEKEIFDkclckLMASKTR------ILVTNK---IEHLkrADKILLLHNGESFFYGT 628
Cdd:COG4167 166 LQPKIIIADEALAALDMSVRSQIIN-----LMLELQEklgisyIYVSQHlgiVKHI--SDKVLVMHQGEVVEYGK 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
440-636 |
8.90e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.48 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAWIMPGTI------RDNILFGLT-Y 511
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRKGLMKLRESVgmvfqdPDNQLFSASvY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 512 DEYRYKSVvkACQLEEDlaALPEKDKTPMAEGGLN---------LSGGQKARVALARAVYRDADLYLLDAPFTHLDIATE 582
Cdd:PRK13636 102 QDVSFGAV--NLKLPED--EVRKRVDNALKRTGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 583 KEIFDkcLCKLMASK---TRILVTNKIEHLK-RADKILLLHNGESFFYGTFPELQSER 636
Cdd:PRK13636 178 SEIMK--LLVEMQKElglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
438-621 |
1.02e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR--ISYSSQ------TAWIMPGTIRDNILFGL 509
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQdglangIVYISEDRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 510 TYDE------YRYKSvVKACQL---EEDLAALPEKD----KTPMAEGGL-NLSGGQKARVALARAVYRDADLYLLDAPFT 575
Cdd:PRK10762 346 SVKEnmsltaLRYFS-RAGGSLkhaDEQQAVSDFIRlfniKTPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 576 HLDIATEKEIFDkclcklMASKTR------ILVTNKI-EHLKRADKILLLHNG 621
Cdd:PRK10762 425 GVDVGAKKEIYQ------LINQFKaeglsiILVSSEMpEVLGMSDRILVMHEG 471
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1211-1406 |
1.17e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.44 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGvnwNKMP--LQKWRKAF 1287
Cdd:PRK13537 8 IDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLCG---EPVPsrARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQkvfiFTgplrmNLDPyGCHSDEELWRVAEEVGLK--TVIEQFPDKLDF-QLEYGGYV----LSNGHKQLICLARS 1360
Cdd:PRK13537 83 GVVPQ----FD-----NLDP-DFTVRENLLVFGRYFGLSaaAARALVPPLLEFaKLENKADAkvgeLSGGMKRRLTLARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68390341 1361 ILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTC-TILLSEHKVE 1406
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHFME 199
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1227-1422 |
1.32e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1227 VLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL-KLVYTDGEISIDGVNWNKMPLQK-WRKAFGVVPQKVFIFTgplRM- 1303
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCgDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFS---RMt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1304 ---NLDPYGCHSDEELWRVAeevgLKTVIEQFPDKLDFQLEYGGyVLSNGHKQLICLARSILSGARILLLDEPSAHLDPV 1380
Cdd:PRK11614 97 veeNLAMGGFFAERDQFQER----IKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 68390341 1381 TIKVLKKTLRQSFST-CTILLSEHKVEpllecQSFLMMDKGQV 1422
Cdd:PRK11614 172 IIQQIFDTIEQLREQgMTIFLVEQNAN-----QALKLADRGYV 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-632 |
1.43e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.53 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLmTILGELVP-SSGKIRHSGRISYSSQTAWIMPG------------------ 499
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLL-KVLNRLIEiYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 --TIRDNILFGLTY----DEYRYKSVVKACQLEEDL-AALPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:PRK14246 104 hlSIYDNIAYPLKShgikEKREIKKIVEECLRKVGLwKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 573 PFTHLDIATEKEIfDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGESFFYGTFPEL 632
Cdd:PRK14246 180 PTSMIDIVNSQAI-EKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
438-621 |
1.88e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.80 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTI-------LGELV--------PSSGK--IRHSGRISYssQTAWIMPG- 499
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIvdglkvndPKVDErlIRQEAGMVF--QQFYLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIRDNILFGLTydEYRYKSVVKACQLEEDLAA---LPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTH 576
Cdd:PRK09493 93 TALENVMFGPL--RVRGASKEEAEKQARELLAkvgLAERAHHYPSE----LSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 577 LDIATEKEIFdkclcKLMAS-----KTRILVTNKIEHLKR-ADKILLLHNG 621
Cdd:PRK09493 167 LDPELRHEVL-----KVMQDlaeegMTMVIVTHEIGFAEKvASRLIFIDKG 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
439-628 |
2.28e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR----HSG-RISYSSQTAWIMPGTI------RDNILF 507
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGdKKNNHELITNPYSKKIknfkelRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 508 GLTYDEYR-YKSVVkacqlEEDLAALP-----------EKDKTPMAEGGLN----------LSGGQKARVALARAVYRDA 565
Cdd:PRK13631 121 VFQFPEYQlFKDTI-----EKDIMFGPvalgvkkseakKLAKFYLNKMGLDdsylerspfgLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 566 DLYLLDAPFTHLDIATEKEIFDKCLCKLMASKTRILVTNKIEH-LKRADKILLLHNGESFFYGT 628
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGT 259
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1211-1422 |
2.43e-10 |
|
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: 61.89 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEISIDGVNWNKMPLQKWRKA--- 1286
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTSGRIYIGGRDVTDLPPKDRDIAmvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 --FGVVPQK-VF---IFtgPLRMNLDPYGcHSDEELWRVAEEVGLKTVIEQFPDKldfqleyggyvLSNGHKQLICLARS 1360
Cdd:cd03301 79 qnYALYPHMtVYdniAF--GLKLRKVPKD-EIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1361 ILSGARILLLDEPSAHLDP---VTIKVLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
440-628 |
2.82e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI----------------RHSGrISYSSQTAWIMPGTIRD 503
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklrKHIG-IVFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFGLTYDEYRYKSVV-KACQLEEDLAALPEKDKTPMAegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATE 582
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHrRVSEALKQVDMLERADYEPNA-----LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 68390341 583 KEIFDkCLCKLMASK--TRILVTNKIEHLKRADKILLLHNGESFFYGT 628
Cdd:PRK13648 179 QNLLD-LVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
438-578 |
3.18e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG------RISYSSQTAW------IMPG-TIRDN 504
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTYQKQLCFvghrsgINPYlTLREN 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 505 ILFGLTYDEYRYKsVVKACQL--EEDLAALPekdktpmaeGGLnLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:PRK13540 95 CLYDIHFSPGAVG-ITELCRLfsLEHLIDYP---------CGL-LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1210-1389 |
3.33e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1210 QIEVRNLTVKY-TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNaLLKLVY--TDGEISI-DGVNWNKMPLQKWRK 1285
Cdd:PTZ00265 382 KIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILK-LIERLYdpTEGDIIInDSHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 AFGVVPQKVFIFTGPLRMNLDpYGCHS----------------------------------------------------- 1312
Cdd:PTZ00265 461 KIGVVSQDPLLFSNSIKNNIK-YSLYSlkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1313 ------DEELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLK 1386
Cdd:PTZ00265 540 nyqtikDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
...
gi 68390341 1387 KTL 1389
Cdd:PTZ00265 620 KTI 622
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
439-636 |
3.36e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.44 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILG--ELVPSSGKIRHsgRISYSSQTAWIMP------------GTI--- 501
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIY--HVALCEKCGYVERpskvgepcpvcgGTLepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 -----------------RDNILFGLTYDEYRYKSVvkacqLEEDLAALPE-----KDKTPMAEGGL-------------- 545
Cdd:TIGR03269 93 evdfwnlsdklrrrirkRIAIMLQRTFALYGDDTV-----LDNVLEALEEigyegKEAVGRAVDLIemvqlshrithiar 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 546 NLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCKLMASKTRILVTNK----IEHLkrADKILLLHNG 621
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevIEDL--SDKAIWLENG 245
|
250 260
....*....|....*....|....*.
gi 68390341 622 E-----------SFFYGTFPELQSER 636
Cdd:TIGR03269 246 EikeegtpdevvAVFMEGVSEVEKEC 271
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1209-1379 |
3.98e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 63.17 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1209 GQIEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLfnalLKLVY-----TDGEISIDGVNWNKMPLQKw 1283
Cdd:COG3839 2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIAgledpTSGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKaFGVVPQ--------KVF--I-FtgPLRM-NLDPygchsdEELWR----VAEEVGLKTVIEQFPDKldfqleyggyvL 1347
Cdd:COG3839 75 RN-IAMVFQsyalyphmTVYenIaF--PLKLrKVPK------AEIDRrvreAAELLGLEDLLDRKPKQ-----------L 134
|
170 180 190
....*....|....*....|....*....|..
gi 68390341 1348 SNGHKQLICLARSILSGARILLLDEPSAHLDP 1379
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
454-621 |
4.61e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 454 AVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------------ISYSSQTAWIMPG-TIRDNILFGLT-YDEY 514
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLFPHyKVRGNLRYGMAkSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 515 RYKSVVKACQLEEDLAALPekdktpmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKcLCKLM 594
Cdd:PRK11144 108 QFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY-LERLA 175
|
170 180 190
....*....|....*....|....*....|
gi 68390341 595 AS-KTRIL-VTNKIEHLKR-ADKILLLHNG 621
Cdd:PRK11144 176 REiNIPILyVSHSLDEILRlADRVVVLEQG 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1211-1422 |
5.86e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 62.86 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWN-KMPLQKwRKAfG 1288
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDsGRIVLNGRDLFtNLPPRE-RRV-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQ--------KVF--IFTGpLRMnldpyGCHSDEELWRVAEE----VGLKTVIEQFPDKLdfqleyggyvlSNGHKQL 1354
Cdd:COG1118 79 FVFQhyalfphmTVAenIAFG-LRV-----RPPSKAEIRARVEEllelVQLEGLADRYPSQL-----------SGGQRQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 1355 ICLARSILSGARILLLDEPSAHLDpvtIKVlKKTLRQSFST------CTILLSEHKVEPLLE-CQSFLMMDKGQV 1422
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALD---AKV-RKELRRWLRRlhdelgGTTVFVTHDQEEALElADRVVVMNQGRI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1211-1378 |
5.99e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 63.32 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:PRK09536 4 IDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTaGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKV---FIFTG---------PLRMNLDPYGcHSDEelwRVAEEVGLKTVIEQFPDKlDFQleyggyVLSNGHKQLICL 1357
Cdd:PRK09536 82 VPQDTslsFEFDVrqvvemgrtPHRSRFDTWT-ETDR---AAVERAMERTGVAQFADR-PVT------SLSGGERQRVLL 150
|
170 180
....*....|....*....|.
gi 68390341 1358 ARSILSGARILLLDEPSAHLD 1378
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD 171
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1435 |
6.09e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.56 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGH---AVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKLVYTDGEIS-------IDGVNWNK 1277
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLvthFNGLIKSKYGTIQVGdiyigdkKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1278 MPLQK-------WRKAFGVVPQ----KVF-------IFTGPLRMnldpyGCHSDEELWRVA---EEVGLKtviEQFPDKL 1336
Cdd:PRK13631 102 NPYSKkiknfkeLRRRVSMVFQfpeyQLFkdtiekdIMFGPVAL-----GVKKSEAKKLAKfylNKMGLD---DSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1337 DFQLeyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDPV-------TIKVLKKTLRqsfstcTILLSEHKVEPLL 1409
Cdd:PRK13631 174 PFGL-------SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKgehemmqLILDAKANNK------TVFVITHTMEHVL 240
|
250 260
....*....|....*....|....*...
gi 68390341 1410 ECQSF-LMMDKGQ-VKTYDSIQKLLNET 1435
Cdd:PRK13631 241 EVADEvIVMDKGKiLKTGTPYEIFTDQH 268
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1243-1379 |
7.41e-10 |
|
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: 61.51 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1243 ILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMP---LQKWR-KAFGVVPQKVFIFtgPLRMNLD--PYGCH---- 1311
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSrkeLRELRrKKISMVFQSFALL--PHRTVLEnvAFGLEvqgv 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1312 SDEELWRVAEE----VGLKTVIEQFPDKLdfqleyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDP 1379
Cdd:cd03294 133 PRAEREERAAEalelVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
439-621 |
7.68e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG--------------------------RISYSSQ 492
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 493 --TAWIMPgTIRDNIL------FGLTYDEYRYKSVVKACQLEEDLAAlpeKDKTPMaegglNLSGGQKARVALARAVYRD 564
Cdd:PRK10619 100 hfNLWSHM-TVLENVMeapiqvLGLSKQEARERAVKYLAKVGIDERA---QGKYPV-----HLSGGQQQRVSIARALAME 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 565 ADLYLLDAPFTHLDIATEKEIFdKCLCKLMAS-KTRILVTNKIEHLKR-ADKILLLHNG 621
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVL-RIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQG 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-623 |
8.29e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.21 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTiLGELVPSSGKIRHSGRISYSSQTAW---------------------IM 497
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYerrvnlnrlrrqvsmvhpkpnLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 498 PGTIRDNILFGLTYDEYRYK--------SVVKACQLEEDLaalpekdKTPMAEGGLNLSGGQKARVALARAVYRDADLYL 569
Cdd:PRK14258 101 PMSVYDNVAYGVKIVGWRPKleiddiveSALKDADLWDEI-------KHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 570 LDAPFTHLDIATEKEIFDKCLCKLMASK-TRILVTNKIEHLKR-ADKILLLHNGES 623
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRlSDFTAFFKGNEN 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
438-573 |
9.27e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR--------------ISYSSQTAWIMPG-TIR 502
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 503 DNILFGLTYDEYRYKsvvkacQLEEDLAALPEKDKTPMAEGGLNLSGGQkaRVALARAVYRDADLYLLDAP 573
Cdd:PRK15439 105 ENILFGLPKRQASMQ------KMKQLLAALGCQLDLDSSAGSLEVADRQ--IVEILRGLMRDSRILILDEP 167
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
921-1130 |
9.30e-10 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 61.46 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 921 YYILYIYVATSESLLAMGFFRGLPFVhtTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMF 1000
Cdd:cd18559 40 YLSVLGALAILQGITVFQYSMAVSIG--GIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1001 DFVQLTVVVVGCILVVSIVRPyIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQA 1080
Cdd:cd18559 118 MWMGPLQNVIGLYLLILLAGP-MAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1081 YFEALFHKTLNTHTATW--FLYLSTLRWFLFRADILFVFFFTLAAWIAVGTN 1130
Cdd:cd18559 197 AFIRQVDAKRDNELAYLpsIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSL 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
435-628 |
9.71e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 435 YVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-RISYSSQTAWIMPGTIRDNILFGLTYDE 513
Cdd:PRK13643 17 FASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKPVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 514 YRYKSVVKACQL---------EEDLAALPEK------DKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:PRK13643 97 LFEETVLKDVAFgpqnfgipkEKAEKIAAEKlemvglADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 579 IATEKEIFDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGESFFYGT 628
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
441-622 |
1.05e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.97 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 441 KDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI--------------RHSGRI--SYSsqtawIMPG-TIRD 503
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmndvppaeRGVGMVfqSYA-----LYPHlSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFGL-------TYDEYRYKSVVKACQLEEDLaalpekDKTPMAegglnLSGGQKARVALARAVYRDADLYLLDAPFTH 576
Cdd:PRK11000 95 NMSFGLklagakkEEINQRVNQVAEVLQLAHLL------DRKPKA-----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 577 LDIA----TEKEIfDKCLCKLmaSKTRILVT-NKIEHLKRADKILLLHNGE 622
Cdd:PRK11000 164 LDAAlrvqMRIEI-SRLHKRL--GRTMIYVThDQVEAMTLADKIVVLDAGR 211
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
432-622 |
1.12e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.62 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 432 TNLYVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGeLVPSSGKIRHSGR-IS------------YSSQ---TAW 495
Cdd:COG4138 4 NDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRpLSdwsaaelarhraYLSQqqsPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 496 IMPGtirdnilfgltydeYRY--------KSVVKACQLEEDLA-ALPEKDKTPMAeggLN-LSGGQKARVALARAVYR-- 563
Cdd:COG4138 83 AMPV--------------FQYlalhqpagASSEAVEQLLAQLAeALGLEDKLSRP---LTqLSGGEWQRVRLAAVLLQvw 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 564 -----DADLYLLDAPFTHLDIAtEKEIFDKCLCKLMASKTRILVTN-KIEH-LKRADKILLLHNGE 622
Cdd:COG4138 146 ptinpEGQLLLLDEPMNSLDVA-QQAALDRLLRELCQQGITVVMSShDLNHtLRHADRVWLLKQGK 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
439-628 |
1.48e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGeLVPssgkiRHSGRISYSSQTAWIMPGTIRDNILFGLTYDE---YR 515
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG-IVP-----RDAGNIIIDDEDISLLPLHARARRGIGYLPQEasiFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 ----YKSVVKACQLEEDLAALPEKDKTP--MAEG---------GLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:PRK10895 92 rlsvYDNLMAVLQIRDDLSAEQREDRANelMEEFhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 581 TEKEIfDKCLCKLMASKTRILVT--NKIEHLKRADKILLLHNGESFFYGT 628
Cdd:PRK10895 172 SVIDI-KRIIEHLRDSGLGVLITdhNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1211-1406 |
1.56e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.17 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL------VYTDGEISIDGVNW--NKMPLQK 1282
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVPQKVFIFTGPLRMNLdPYGCH----SDEELWRVAEEVGLK--TVIEQFPDKL-DFQLEyggyvLSNGHKQLI 1355
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENV-VYGLRlkgiKDKQVLDEAVEKSLKgaSIWDEVKDRLhDSALG-----LSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 68390341 1356 CLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEHKVE 1406
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1211-1420 |
1.68e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.44 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTDGEISIDG--------VNWNKMPLQK 1282
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqnIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVPQKVFIFTGPLRMNLdPYGC-----HSDEELWRVAEEvGLKTVieQFPDKLDFQLEYGGYVLSNGHKQLICL 1357
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNV-AYGVkivgwRPKLEIDDIVES-ALKDA--DLWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1358 ARSILSGARILLLDEPSAHLDPV-TIKVlkKTLRQSF---STCTILLSEHKVEPLLECQSFLMMDKG 1420
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIaSMKV--ESLIQSLrlrSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1211-1406 |
1.80e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.18 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKLVYT---DGEISIDGVNWNKMPLQ--K 1282
Cdd:PRK14243 11 LRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNRLNDLIPGfrvEGKVTFHGKNLYAPDVDpvE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVPQKVFIFTGPLRMNL------DPYGCHSDEELWRVAEEVGLKtvieqfpDKLDFQLEYGGYVLSNGHKQLIC 1356
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIaygariNGYKGDMDELVERSLRQAALW-------DEVKDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1357 LARSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQSFstcTILLSEHKVE 1406
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPIStlrIEELMHELKEQY---TIIIVTHNMQ 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1211-1403 |
2.08e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.86 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKL---VYTDGEISIDGVN--WNKMPLQK 1282
Cdd:PRK14267 5 IETVNLRVYYGS--NHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLLELneeARVEGEVRLFGRNiySPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGVVpqkvFIFTGP-----------LRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDfqlEYGGYvLSNGH 1351
Cdd:PRK14267 83 VRREVGMV----FQYPNPfphltiydnvaIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLN---DYPSN-LSGGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1352 KQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTCTILLSEH 1403
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1241-1481 |
2.15e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1241 VGILGRTGSGKSSLFNALLKLVYTDGEISIDgvnwnkmplqkWRKAFGVVPQKVFIFTGPLRMNLDPYGCHSDEELWRVA 1320
Cdd:PLN03232 646 VAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAI 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1321 EEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDP-VTIKVLKKTLRQSFSTCTIL 1399
Cdd:PLN03232 715 DVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRV 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1400 LSEHKVEPLLECQSFLMMDKGQVKTYDSIQKLLNETSHLKQAISPAERLKLFPRRNSSMRTPQSKLSSVTQTLQEEAEDN 1479
Cdd:PLN03232 795 LVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENILKLGPTVTIDVSERNLGS 874
|
..
gi 68390341 1480 IQ 1481
Cdd:PLN03232 875 TK 876
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1226-1403 |
2.28e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1226 AVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYT-DGEISIDG--VNWNKMPLQ----KWRKAFGVVPQKVFIFT 1298
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGkvLYFGKDIFQidaiKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1299 -----GPLRMNLDPYGCHSDEELWRVAEEVGLKTVI-EQFPDKLDFQLEYggyvLSNGHKQLICLARSILSGARILLLDE 1372
Cdd:PRK14246 104 hlsiyDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|.
gi 68390341 1373 PSAHLDPVTIKVLKKTLRQSFSTCTILLSEH 1403
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
439-621 |
2.77e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTI-LGElVPSSGKIRHSG-RISYSSQTA--------------------Wi 496
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLE-MPRSGTLNIAGnHFDFSKTPSdkairelrrnvgmvfqqynlW- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 497 mPG-TIRDNIL------FGLTYDEY--RYKSVVKACQLEEDLAALPekdktpmaeggLNLSGGQKARVALARAVYRDADL 567
Cdd:PRK11124 95 -PHlTVQQNLIeapcrvLGLSKDQAlaRAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 568 YLLDAPFTHLDIATEKEIFDkcLCKLMASK--TRILVTNKIEHLKR-ADKILLLHNG 621
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHEVEVARKtASRVVYMENG 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1211-1392 |
2.99e-09 |
|
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: 59.17 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLfnalLKLVY-----TDGEISIDGVNWNKMPLQKwrK 1285
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAgfetpTSGEILLDGKDITNLPPHK--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 AFGVVPQKVFIFTG---------PLRMNldpyGCHSDEELWRVAEE---VGLKTVIEQFPDKLdfqleyggyvlSNGHKQ 1353
Cdd:cd03300 73 PVNTVFQNYALFPHltvfeniafGLRLK----KLPKAEIKERVAEAldlVQLEGYANRKPSQL-----------SGGQQQ 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 68390341 1354 LICLARSILSGARILLLDEPSAHLDpvtikvlkKTLRQS 1392
Cdd:cd03300 138 RVAIARALVNEPKVLLLDEPLGALD--------LKLRKD 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
428-587 |
3.08e-09 |
|
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: 61.24 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 428 GLFFTNLYVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGeLVPSSGKIRHSGR-ISYSSQTAWI---------- 496
Cdd:COG4172 290 GLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdLDGLSRRALRplrrrmqvvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 497 ----------MpgTIRDNILFGL-------TYDEyRYKSVVKAcqLEE---DLAALpekDKTPMAegglnLSGGQKARVA 556
Cdd:COG4172 369 qdpfgslsprM--TVGQIIAEGLrvhgpglSAAE-RRARVAEA--LEEvglDPAAR---HRYPHE-----FSGGQRQRIA 435
|
170 180 190
....*....|....*....|....*....|.
gi 68390341 557 LARAVYRDADLYLLDAPFTHLDIATEKEIFD 587
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQAQILD 466
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
439-578 |
3.12e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.38 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRH-----SGRISYSSQTAWI----------------M 497
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditiDTARSLSQQKGLIrqlrqhvgfvfqnfnlF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 498 PG-TIRDNILFG--LTYDEYRYKSVVKACQLEEDLAALPEKDKTPMaegglNLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:PRK11264 98 PHrTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYPR-----RLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
....
gi 68390341 575 THLD 578
Cdd:PRK11264 173 SALD 176
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
421-621 |
3.52e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.32 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 421 GHHNGDAGLFFTNLYVApVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR----ISYSSQTAWI 496
Cdd:PRK10419 10 SHHYAHGGLSGKHQHQT-VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplakLNRAQRKAFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 497 ---------MPG------TIRDNI------LFGL--TYDEYRYKSVVKACQLEEDLAalpekDKTPMaegglNLSGGQKA 553
Cdd:PRK10419 89 rdiqmvfqdSISavnprkTVREIIreplrhLLSLdkAERLARASEMLRAVDLDDSVL-----DKRPP-----QLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 554 RVALARAVYRDADLYLLDAPFTHLDIATEKEIFDkcLCKLMASKTRI---LVTNKIEHLKR-ADKILLLHNG 621
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR--LLKKLQQQFGTaclFITHDLRLVERfCQRVMVMDNG 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1211-1391 |
3.69e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.99 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTeaGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD------GEISIDG---VNWNKMPLQ 1281
Cdd:PRK11264 4 IEVKNLVKKFH--GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirvGDITIDTarsLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1282 KWRKAFGVVPQKVFIF----------TGPLRMNLDPYGchSDEELWR-VAEEVGLKTVIEQFPDKLdfqleyggyvlSNG 1350
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFphrtvleniiEGPVIVKGEPKE--EATARAReLLAKVGLAGKETSYPRRL-----------SGG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68390341 1351 HKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQ 189
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1211-1379 |
3.82e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.61 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteaGHAVLkNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPLQKwRK---- 1285
Cdd:COG3840 2 LRLDDLTYRY---GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDsGRILWNGQDLTALPPAE-RPvsml 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 ----------------AFGVVPqkvfiftgplRMNLdpygchSDEELWRV---AEEVGLKTVIEQFPDKLdfqleyggyv 1346
Cdd:COG3840 77 fqennlfphltvaqniGLGLRP----------GLKL------TAEQRAQVeqaLERVGLAGLLDRLPGQL---------- 130
|
170 180 190
....*....|....*....|....*....|...
gi 68390341 1347 lSNGHKQLICLARSILSGARILLLDEPSAHLDP 1379
Cdd:COG3840 131 -SGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
440-641 |
4.59e-09 |
|
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: 57.33 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGElvpsSGKIRHSGRISYSSQTAWIMPGTIRDNILFGLTYdeyryksv 519
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 520 vkacqleedlaaLPEKDKTPmaegglNLSGGQKARVALARAVYRDAD--LYLLDAPFTHLDIATeKEIFDKCLCKLMASK 597
Cdd:cd03238 79 ------------LTLGQKLS------TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD-INQLLEVIKGLIDLG 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 68390341 598 TRILVtnkIEH----LKRADKILllhngesfFYGTFPELQSERPDFSS 641
Cdd:cd03238 140 NTVIL---IEHnldvLSSADWII--------DFGPGSGKSGGKVVFSG 176
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1212-1391 |
4.68e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.44 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1212 EVRNLTVKyteaghAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEISIDGVNWNKMPLQKWRKA-FGV 1289
Cdd:cd03215 6 EVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLrPPASGEITLDGKPVTRRSPRDAIRAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VP---QKVFIFTGplrmnldpygchsdeelWRVAEEVGLktvieqfpdkldfqleygGYVLSNGHKQLICLARSILSGAR 1366
Cdd:cd03215 80 VPedrKREGLVLD-----------------LSVAENIAL------------------SSLLSGGNQQKVVLARWLARDPR 124
|
170 180
....*....|....*....|....*
gi 68390341 1367 ILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRE 149
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1243-1430 |
5.57e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1243 ILGRTGSGKSSLFNALLKLVYTD-GEISID---------GVNwnkMPLQKWRkaFGVVPQKVFIFtgP---LRMNLDpYG 1309
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQkGRIVLNgrvlfdaekGIC---LPPEKRR--IGYVFQDARLF--PhykVRGNLR-YG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1310 C-HSDEELW-RVAEEVGLKTVIEQFPdkldfqleyggYVLSNGHKQLICLARSILSGARILLLDEPSAHLD-PVTIKVLK 1386
Cdd:PRK11144 101 MaKSMVAQFdKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68390341 1387 --KTLRQSFSTcTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQK 1430
Cdd:PRK11144 170 ylERLAREINI-PILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
438-632 |
6.25e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.12 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR--------------ISYSSQTAWIMPG-TIR 502
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 503 DNILFGLtydEYRYKSvvKAcQLEEDLAALpekdktpMAEGGLN---------LSGGQKARVALARAVYRDADLYLLDAP 573
Cdd:COG1137 97 DNILAVL---ELRKLS--KK-EREERLEEL-------LEEFGIThlrkskaysLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 574 FTHLD-IATE--KEIfdkcLCKLmasKTR---ILVT--NKIEHLKRADKILLLHNGESFFYGTFPEL 632
Cdd:COG1137 164 FAGVDpIAVAdiQKI----IRHL---KERgigVLITdhNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1232-1406 |
6.50e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.05 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1232 SFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPlqkwrkafgvvPQKvfiftGPLRM-----NL 1305
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAsGSLTLNGQDHTTTP-----------PSR-----RPVSMlfqenNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1306 DPY---------GCH--------SDEELWRVAEEVGLKTVIEQFPDKLdfqleyggyvlSNGHKQLICLARSILSGARIL 1368
Cdd:PRK10771 83 FSHltvaqniglGLNpglklnaaQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 68390341 1369 LLDEPSAHLDPvtikvlkkTLRQSFST-----C-----TILLSEHKVE 1406
Cdd:PRK10771 152 LLDEPFSALDP--------ALRQEMLTlvsqvCqerqlTLLMVSHSLE 191
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1231-1379 |
6.53e-09 |
|
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: 57.50 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1231 LSFSAEGRQRVGILGRTGSGKSSLFNALLK-LVYTDGEISIDGVNWNKMP--------LQKWRKAFG--VVPQKVFIFTG 1299
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVTAAPpadrpvsmLFQENNLFAhlTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1300 PlRMNLDPygcHSDEELWRVAEEVGLKTVIEQFPDKLdfqleyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDP 1379
Cdd:cd03298 97 P-GLKLTA---EDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1210-1391 |
6.73e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1210 QIEVRNLTVkytEAGHAVL-KNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISidgvnWNKMPLQKWRKAF 1287
Cdd:PRK13538 1 MLEARNLAC---ERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDaGEVL-----WQGEPIRRQRDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GvvpQKVFiFTG-------------PLRMNLDPYGCHSDEELWRVAEEVGLKTViEQFPDKldfqleyggyVLSNGHKQL 1354
Cdd:PRK13538 73 H---QDLL-YLGhqpgikteltaleNLRFYQRLHGPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRR 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 68390341 1355 ICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1211-1422 |
6.96e-09 |
|
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: 58.12 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKwrKAFGV 1289
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERpDSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFT----------GpLRMNLDPYGCHSDEELWRVAE---EVGLKTVIEQFPDKLdfqleyggyvlSNGHKQLIC 1356
Cdd:cd03296 79 VFQHYALFRhmtvfdnvafG-LRVKPRSERPPEAEIRAKVHEllkLVQLDWLADRYPAQL-----------SGGQRQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 1357 LARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ---SFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRlhdELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
440-622 |
7.49e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.99 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAW--IMPGTIRDNILFG-LTYDEyr 515
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYrkLFSAVFTDFHLFDqLLGPE-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 yKSVVKACQLEEDLAALPEKDKTPMAEG---GLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDKCLCK 592
Cdd:PRK10522 417 -GKPANPALVEKWLERLKMAHKLELEDGrisNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPL 495
|
170 180 190
....*....|....*....|....*....|.
gi 68390341 593 LMAS-KTRILVTNKIEHLKRADKILLLHNGE 622
Cdd:PRK10522 496 LQEMgKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
440-633 |
8.40e-09 |
|
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: 57.38 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG------------RISYSSQTAWIMPG-TIRDNI- 505
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LFGLTYDeyrYKSVVKACQLEEDLA--ALPEKDKTPMAegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:cd03265 96 IHARLYG---VPGAERRERIDELLDfvGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 584 EIFDKcLCKLMASK--TRILVTNKIEHL-KRADKILLLHNGESFFYGTFPELQ 633
Cdd:cd03265 169 HVWEY-IEKLKEEFgmTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
440-621 |
8.59e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.58 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG----RISYSS------QTAWI-------MPGTIR 502
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditRLKNREvpflrrQIGMIfqdhhllMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 503 DNILFGLTYDEYRYKSVVKACQLEEDLAALPEKDKT-PmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNfP-----IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68390341 582 EKEI------FDKC-LCKLMASKTRILVTnkiehlKRADKILLLHNG 621
Cdd:PRK10908 173 SEGIlrlfeeFNRVgVTVLMATHDIGLIS------RRSYRMLTLSDG 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
433-621 |
1.11e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 433 NLYVAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGeLVPSSGKI----------------RHSGRISYSSQTAWI 496
Cdd:PRK03695 5 DVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIqfagqpleawsaaelaRHRAYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 497 MPgtirdniLFgltydEYRYKSVVKACQLEEDLAALPE-------KDKTPMAEGglNLSGGQKARVALARA---VYRDAD 566
Cdd:PRK03695 84 MP-------VF-----QYLTLHQPDKTRTEAVASALNEvaealglDDKLGRSVN--QLSGGEWQRVRLAAVvlqVWPDIN 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 567 LY----LLDAPFTHLDIATEKeIFDKCLCKLMASKTRILVTN-KIEH-LKRADKILLLHNG 621
Cdd:PRK03695 150 PAgqllLLDEPMNSLDVAQQA-ALDRLLSELCQQGIAVVMSShDLNHtLRHADRVWLLKQG 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1211-1440 |
1.20e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.82 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKY-TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSS---LFNALLKL----VYTDGE-ISIDGVnWNKmplq 1281
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAesgqIIIDGDlLTEENV-WDI---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1282 kwRKAFGVV---PQKVFI---FTGPLRMNLDPYGCHSDEELWRVAEE---VGLKTVIEQFPDKldfqleyggyvLSNGHK 1352
Cdd:PRK13650 80 --RHKIGMVfqnPDNQFVgatVEDDVAFGLENKGIPHEEMKERVNEAlelVGMQDFKEREPAR-----------LSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1353 QLICLARSILSGARILLLDEPSAHLDPV----TIKVLKKtLRQSFSTCTILLSeHKVEPLLECQSFLMMDKGQVKTYDSI 1428
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEgrleLIKTIKG-IRDDYQMTVISIT-HDLDEVALSDRVLVMKNGQVESTSTP 224
|
250
....*....|..
gi 68390341 1429 QKLLNETSHLKQ 1440
Cdd:PRK13650 225 RELFSRGNDLLQ 236
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
438-578 |
1.25e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 58.70 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILG-ELVpSSGKIRHSGR-----------ISYSSQTAWIMPG-TIRDN 504
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGlERI-TSGEIWIGGRvvnelepadrdIAMVFQNYALYPHmSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFGL-------TYDEYRYKSVVKACQLEEDLaalpekDKTPMAegglnLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:PRK11650 97 MAYGLkirgmpkAEIEERVAEAARILELEPLL------DRKPRE-----LSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
.
gi 68390341 578 D 578
Cdd:PRK11650 166 D 166
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1227-1441 |
1.27e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.71 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1227 VLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDG--VNWNKMPLQKWRKAFGVV---PQKVFIFT-- 1298
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRpQKGAVLWQGkpLDYSKRGLLALRQQVATVfqdPEQQIFYTdi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1299 -GPLRMNLDPYGCHSDEELWRVAEEVGLktVIEQFPDKLDFQleyggyVLSNGHKQLICLARSILSGARILLLDEPSAHL 1377
Cdd:PRK13638 96 dSDIAFSLRNLGVPEAEITRRVDEALTL--VDAQHFRHQPIQ------CLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 1378 DPV----TIKVLKKTLRQSFStctILLSEHKVEPLLECQ-SFLMMDKGQVKTYDSIQKLLNETSHLKQA 1441
Cdd:PRK13638 168 DPAgrtqMIAIIRRIVAQGNH---VIISSHDIDLIYEISdAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
439-621 |
1.29e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.20 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAWIMPG---------------TIRD 503
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFGLTY-DEYRYKSvvkacQLEEDLAALPEKDKTPMAEGGlNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATE 582
Cdd:PRK11614 100 NLAMGGFFaERDQFQE-----RIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 68390341 583 KEIFDKCLCKLMASKTRILV-TNKIEHLKRADKILLLHNG 621
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVeQNANQALKLADRGYVLENG 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
438-642 |
1.39e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAWIMPGTIRDN 504
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 I-LFGLTYDEYRYKSVVKAcQLEEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEK 583
Cdd:PLN03130 1333 LdPFNEHNDADLWESLERA-HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68390341 584 EIfDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTfPE--LQSERPDFSSL 642
Cdd:PLN03130 1412 LI-QKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDT-PEnlLSNEGSAFSKM 1470
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
439-578 |
1.55e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSS----------QTAWIMPG-TIRDNIL 506
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdVTHRSiqqrdicmvfQSYALFPHmSLGENVG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 507 FGLTY----DEYRYKSVVKACQLEeDLAALPEK--DKtpmaegglnLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:PRK11432 101 YGLKMlgvpKEERKQRVKEALELV-DLAGFEDRyvDQ---------ISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1211-1422 |
1.64e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.40 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKY---TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPLQKwRKA 1286
Cdd:COG1101 2 LELKNLSKTFnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDsGSILIDGKDVTKLPEYK-RAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 F-GVVPQKVFIFTGPlRM----NL-------DPYGCHsdeelWRVaeevgLKTVIEQFPDKLDfQLEYG---------GY 1345
Cdd:COG1101 81 YiGRVFQDPMMGTAP-SMtieeNLalayrrgKRRGLR-----RGL-----TKKRRELFRELLA-TLGLGlenrldtkvGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1346 vLSNGHKQLICLARSILSGARILLLDEPSAHLDPVT-IKVLKKTLR--QSFSTCTILLSeHKVEPLLECQSFL-MMDKGQ 1421
Cdd:COG1101 149 -LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTaALVLELTEKivEENNLTTLMVT-HNMEQALDYGNRLiMMHEGR 226
|
.
gi 68390341 1422 V 1422
Cdd:COG1101 227 I 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1211-1391 |
1.68e-08 |
|
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: 56.21 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTvkYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISidgvnWNKMPLQKWRKafgv 1289
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDsGEVR-----WNGTPLAEQRD---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTGPL---------RMNLDPYG-CHSDEEL--WRVAEEVGLkTVIEQFPdkldfqleygGYVLSNGHKQLICL 1357
Cdd:TIGR01189 70 EPHENILYLGHLpglkpelsaLENLHFWAaIHGGAQRtiEDALAAVGL-TGFEDLP----------AAQLSAGQQRRLAL 138
|
170 180 190
....*....|....*....|....*....|....
gi 68390341 1358 ARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
438-578 |
1.92e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.79 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLL--MT-----ILGELVPSSGKirhsgRISYSSQTAWIMPG-TIRDNILFGL 509
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLriMAgvdkdFNGEARPQPGI-----KVGYLPQEPQLDPTkTVRENVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 510 -----TYDEY-----RY--------KSVVKACQLEEDLAA------------------LPEKDkTPMAegglNLSGGQKA 553
Cdd:TIGR03719 94 aeikdALDRFneisaKYaepdadfdKLAAEQAELQEIIDAadawdldsqleiamdalrCPPWD-ADVT----KLSGGERR 168
|
170 180
....*....|....*....|....*
gi 68390341 554 RVALARAVYRDADLYLLDAPFTHLD 578
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1211-1378 |
2.26e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNL--TVKY---------TEAghavLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGvnwnkM 1278
Cdd:PRK15112 5 LEVRNLskTFRYrtgwfrrqtVEA----VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDD-----H 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1279 PL---------QKWRKAF-----GVVPQKVF--IFTGPLRMNLDPYGCHSDEELWRVAEEVGLktvieqFPDkldfQLEY 1342
Cdd:PRK15112 76 PLhfgdysyrsQRIRMIFqdpstSLNPRQRIsqILDFPLRLNTDLEPEQREKQIIETLRQVGL------LPD----HASY 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 68390341 1343 GGYVLSNGHKQLICLARSILSGARILLLDEPSAHLD 1378
Cdd:PRK15112 146 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1211-1378 |
2.51e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.92 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTvKYTEAGHAVlKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPlqKWRKAFGV 1289
Cdd:PRK11607 20 LEIRNLT-KSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQpTAGQIMLDGVDLSHVP--PYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 VPQKVFIFTgplRMNLD---PYGCHSD-----EELWRVAEEVGLkTVIEQFPDKLDFQLeyggyvlSNGHKQLICLARSI 1361
Cdd:PRK11607 96 MFQSYALFP---HMTVEqniAFGLKQDklpkaEIASRVNEMLGL-VHMQEFAKRKPHQL-------SGGQRQRVALARSL 164
|
170
....*....|....*..
gi 68390341 1362 LSGARILLLDEPSAHLD 1378
Cdd:PRK11607 165 AKRPKLLLLDEPMGALD 181
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
439-622 |
2.56e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.33 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----------------ISYSSQTAWIMPG-T 500
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeearaklrakhVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNI-LFGLTYDEYRYKSVVKACQLEEDLAALPEKDKTPMaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:PRK10584 105 ALENVeLPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPA-----QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 68390341 580 ATEKEIFDkclckLMASKTR------ILVTNKIEHLKRADKILLLHNGE 622
Cdd:PRK10584 180 QTGDKIAD-----LLFSLNRehgttlILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1211-1401 |
2.83e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.41 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteaGHAVL-KNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISI-DGVNwnkmplqkwrkaF 1287
Cdd:TIGR03719 323 IEAENLTKAF---GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDsGTIEIgETVK------------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVPQKvfiftgplRMNLDPYgchsdeelwrvaeevglKTVIEQFPDKLDfQLEYGGY---------------------- 1345
Cdd:TIGR03719 388 AYVDQS--------RDALDPN-----------------KTVWEEISGGLD-IIKLGKReipsrayvgrfnfkgsdqqkkv 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1346 -VLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLrQSFSTCTILLS 1401
Cdd:TIGR03719 442 gQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAGCAVVIS 497
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
439-645 |
4.48e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-------------ISYSSQTAWIMPGTIRDNI 505
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReigayglrelrrqFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 lfgltyDEYRYKS---VVKACQL---EEDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVY-RDADLYLLDAPFTHLD 578
Cdd:PTZ00243 1405 ------DPFLEASsaeVWAALELvglRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANID 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 579 IATEKEIfDKCLCKLMASKTRILVTNKIEHLKRADKILLLHNG---------------ESFFYGTFPEL-QSERPDFSSL 642
Cdd:PTZ00243 1479 PALDRQI-QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGavaemgsprelvmnrQSIFHSMVEALgRSEAKRFLQL 1557
|
...
gi 68390341 643 LLG 645
Cdd:PTZ00243 1558 VGR 1560
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
439-585 |
4.90e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 56.62 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG----------------RIS--------YSSQTA 494
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalserelraarrKIGmifqhfnlLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 495 WimpgtirDNILFGLtydeyRYKSVVKAcQLEE------DLAALPEK-DKTPmAEgglnLSGGQKARVALARAVYRDADL 567
Cdd:COG1135 100 A-------ENVALPL-----EIAGVPKA-EIRKrvaellELVGLSDKaDAYP-SQ----LSGGQKQRVGIARALANNPKV 161
|
170
....*....|....*...
gi 68390341 568 YLLDAPFTHLDIATEKEI 585
Cdd:COG1135 162 LLCDEATSALDPETTRSI 179
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1225-1440 |
4.90e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1225 HAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKLvyTDGEISIDGVNWNKMPLQKW----RKAFGVVPQ----K 1293
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLKP--TTGTVTVDDITITHKTKDKYirpvRKRIGMVFQfpesQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1294 VF-------IFTGP--LRMNLDpygcHSDEELWRVAEEVGL-KTVIEQFPdkldFQleyggyvLSNGHKQLICLArSILS 1363
Cdd:PRK13646 98 LFedtvereIIFGPknFKMNLD----EVKNYAHRLLMDLGFsRDVMSQSP----FQ-------MSGGQMRKIAIV-SILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1364 -GARILLLDEPSAHLDPVT----IKVLKKTlrQSFSTCTILLSEHKVEPLLE-CQSFLMMDKGQVKTYDSIQKLLNETSH 1437
Cdd:PRK13646 162 mNPDIIVLDEPTAGLDPQSkrqvMRLLKSL--QTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
...
gi 68390341 1438 LKQ 1440
Cdd:PRK13646 240 LAD 242
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1422 |
5.04e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.91 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEISIDGVNWNKMPLQKWRKAFGV 1289
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIeKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 V---PQKVFI---------FTgpLRMNLDPYgchsdEELWRVAEEVgLKTVieqfpDKLDfQLEYGGYVLSNGHKQLICL 1357
Cdd:PRK13648 88 VfqnPDNQFVgsivkydvaFG--LENHAVPY-----DEMHRRVSEA-LKQV-----DMLE-RADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1358 ARSILSGARILLLDEPSAHLDPVTIKVLKKTLR--QSFSTCTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
440-587 |
5.59e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 56.73 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI-------------------RHSGRIS-----YSSQTAW 495
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltalsekelrkarRQIGMIFqhfnlLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 496 impgtirDNILFGLTYDEYRyKSVVKAcQLEE--DLAALPEK-DKTPMaegglNLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:PRK11153 101 -------DNVALPLELAGTP-KAEIKA-RVTEllELVGLSDKaDRYPA-----QLSGGQKQRVAIARALASNPKVLLCDE 166
|
170
....*....|....*
gi 68390341 573 PFTHLDIATEKEIFD 587
Cdd:PRK11153 167 ATSALDPATTRSILE 181
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1211-1390 |
5.69e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKM-PLQKWRKAFG 1288
Cdd:PRK15439 12 LCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIGGNPCARLtPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTgplrmNLdpygchSDEE--LWRVAEEVGLKTVIEQFPDKLDFQL--EYGGYVLSNGHKQLICLARSILSG 1364
Cdd:PRK15439 90 LVPQEPLLFP-----NL------SVKEniLFGLPKRQASMQKMKQLLAALGCQLdlDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180
....*....|....*....|....*.
gi 68390341 1365 ARILLLDEPSAHLDPVTIKVLKKTLR 1390
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIR 184
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1347-1447 |
5.92e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1347 LSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFST--CTILLSEHKVEPLLE-CQSFLMMDKGQVK 1423
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHVF 232
|
90 100
....*....|....*....|....*
gi 68390341 1424 TYDSIQKLLNET-SHLKQAISPAER 1447
Cdd:PRK09984 233 YDGSSQQFDNERfDHLYRSINRVEE 257
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
439-638 |
5.96e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.96 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGK---------------IRHSGRISYSSQTAWIMPGTIRD 503
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlirgepitkenireVRKFVGLVFQNPDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFG---LTYDE----YRYKSVVKACQLEEDLAALPEkdktpmaegglNLSGGQKARVALARAVYRDADLYLLDAPFTH 576
Cdd:PRK13652 99 DIAFGpinLGLDEetvaHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 577 LDIATEKEIFD--KCLCKLMASkTRILVTNKIEHL-KRADKILLLHNGESFFYGTFPELQSeRPD 638
Cdd:PRK13652 168 LDPQGVKELIDflNDLPETYGM-TVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFL-QPD 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
439-628 |
6.18e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPS--SGKIRHSGRISY----------------------SSQTA 494
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGDVTLngeplaaidaprlarlravlpqAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 495 WimPGTIRDNILFGltydeyRYKSVVKACQL---EEDLA--ALPEKDKTPMAEGGL-NLSGGQKARVALARAV------- 561
Cdd:PRK13547 96 F--AFSAREIVLLG------RYPHARRAGALthrDGEIAwqALALAGATALVGRDVtTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 562 --YRDADLYLLDAPFTHLDIATEKEIFDKclCKLMASKTRILVTnKIEH-----LKRADKILLLHNGESFFYGT 628
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDT--VRRLARDWNLGVL-AIVHdpnlaARHADRIAMLADGAIVAHGA 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
439-589 |
6.90e-08 |
|
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: 57.07 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLmTILGELVPSSGKIRH---SGRISYSSQTAWIMPGTIRDNILFGLTYDEYR 515
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLF-RILGELWPVYGGRLTkpaKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 YKSVVKAcQLEE-----DLAALPEKdktpmaEGGLN--------LSGGQKARVALARAVYRDADLYLLDAPFTHLDIATE 582
Cdd:TIGR00954 546 RRGLSDK-DLEQildnvQLTHILER------EGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
....*..
gi 68390341 583 KEIFDKC 589
Cdd:TIGR00954 619 GYMYRLC 625
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
438-585 |
8.75e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSlLMTIL-GELVPSSGKIRHSGR-ISYSS-QTAW------------IMPG-TI 501
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKST-LMKILsGVYQPDSGEILLDGEpVRFRSpRDAQaagiaiihqelnLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGltyDEYRYKSVVKACQLEEDLAALpekdktpMAEGGLN---------LSGGQKARVALARAVYRDADLYLLDA 572
Cdd:COG1129 97 AENIFLG---REPRRGGLIDWRAMRRRAREL-------LARLGLDidpdtpvgdLSVAQQQLVEIARALSRDARVLILDE 166
|
170
....*....|...
gi 68390341 573 PFTHLdiaTEKEI 585
Cdd:COG1129 167 PTASL---TEREV 176
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1211-1431 |
1.17e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.50 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLfnalLKLVY-----TDGEISIDGVNWNKMPLQKwrK 1285
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVAglekpTEGQIFIDGEDVTHRSIQQ--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1286 AFGVVPQKVFIFtgP-----------LRMnldpYGCHSDEELWRVAEevGLKTV-IEQFPDKldfqleyggYV--LSNGH 1351
Cdd:PRK11432 79 DICMVFQSYALF--PhmslgenvgygLKM----LGVPKEERKQRVKE--ALELVdLAGFEDR---------YVdqISGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1352 KQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLR---QSFSTCTILLSEHKVEPLLECQSFLMMDKGQVKTYDSI 1428
Cdd:PRK11432 142 QQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
...
gi 68390341 1429 QKL 1431
Cdd:PRK11432 222 QEL 224
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
426-646 |
1.29e-07 |
|
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: 53.34 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 426 DAGLFFTNlYVAPVLKDislklkkGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-RISYSSQTawimpgtirdn 504
Cdd:cd03222 9 RYGVFFLL-VELGVVKE-------GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ilfgltydeyryksvvkacqleedlaalpekdktpmaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIaTEKE 584
Cdd:cd03222 70 ----------------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI-EQRL 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 585 IFDKCLCKLM--ASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSLLLGL 646
Cdd:cd03222 109 NAARAIRRLSeeGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGY 172
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
921-1119 |
1.29e-07 |
|
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: 54.86 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 921 YYILYIYVATSESLLAMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMF 1000
Cdd:cd07346 39 LWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1001 DFVQLTVVVVGCILVVSIVRPYIFLAATPLAIIFIVMRKYFLRTGQQLKQLETEARSPIFSHLIMSLKGLWTIRAFERQA 1080
Cdd:cd07346 119 QLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 1081 YFEALFHKTLNTH------TATWFLYLSTLRWFLFRADILFVFFF 1119
Cdd:cd07346 199 REIERFREANRDLrdanlrAARLSALFSPLIGLLTALGTALVLLY 243
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
433-621 |
1.34e-07 |
|
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: 53.68 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 433 NLYVA----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILG--ELVPSSGKIRHSGR-ISYSSQT---------AWI 496
Cdd:cd03217 5 DLHVSvggkEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEdITDLPPEerarlgiflAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 497 MPGTIRdnilfGLTYDEY-RYksvvkacqleedlaalpekdktpMAEGglnLSGGQKARVALARAVYRDADLYLLDAPFT 575
Cdd:cd03217 85 YPPEIP-----GVKNADFlRY-----------------------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 68390341 576 HLDIATEKEIFDKcLCKLMASKTRILV---TNKIEHLKRADKILLLHNG 621
Cdd:cd03217 134 GLDIDALRLVAEV-INKLREEGKSVLIithYQRLLDYIKPDRVHVLYDG 181
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1211-1385 |
1.34e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVkyTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSL---FNALLKLVytDGEISIDGVNW------------ 1275
Cdd:PRK13539 3 LEGEDLAC--VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrlIAGLLPPA--AGTIKLDGGDIddpdvaeachyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1276 ---NKMP--------LQKWRKAFGvvpqkvfifTGPLRmnldpygchsdeeLWRVAEEVGLKTVIEqfpdkldfqLEYGg 1344
Cdd:PRK13539 79 ghrNAMKpaltvaenLEFWAAFLG---------GEELD-------------IAAALEAVGLAPLAH---------LPFG- 126
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68390341 1345 yVLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVL 1385
Cdd:PRK13539 127 -YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
438-581 |
1.41e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG----------------RISYSSQT-AWIMPGT 500
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrsrlytvrkRMSMLFQSgALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 IRDNILFGL----TYDEYRYKSVV----KACQLEEDLAALPEKdktpmaegglnLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:PRK11831 101 VFDNVAYPLrehtQLPAPLLHSTVmmklEAVGLRGAAKLMPSE-----------LSGGMARRAALARAIALEPDLIMFDE 169
|
....*....
gi 68390341 573 PFTHLDIAT 581
Cdd:PRK11831 170 PFVGQDPIT 178
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1211-1406 |
1.56e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNAL-LKLVYTDGEISIDG--VNWNKMP----LQKW 1283
Cdd:COG4161 3 IQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDSGQLNIAGhqFDFSQKPsekaIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKAFGVVPQKVFIFtgP---LRMNLDPYGCH----SDEELWRVAEEVgLKTVieQFPDKLD-FQLEyggyvLSNGHKQLI 1355
Cdd:COG4161 81 RQKVGMVFQQYNLW--PhltVMENLIEAPCKvlglSKEQAREKAMKL-LARL--RLTDKADrFPLH-----LSGGQQQRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1356 CLARSILSGARILLLDEPSAHLDP-VTIKVLKKTLRQSFSTCTILLSEHKVE 1406
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPeITAQVVEIIRELSQTGITQVIVTHEVE 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
437-622 |
1.65e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLmTILGELVPSSGKIRHSGRISYSSQTAWIMPG----------------- 499
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLL-RVFNRLIELYPEARVSGEVYLDGQDIFKMDVielrrrvqmvfqipnpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 ---TIRDNILFGLTYD---------EYRYKSVVKACQLEEDLaalpeKDKTPMAEGglNLSGGQKARVALARAVYRDADL 567
Cdd:PRK14247 95 pnlSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-----KDRLDAPAG--KLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 568 YLLDAPFTHLDIATEKEIfDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:PRK14247 168 LLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQ 222
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
438-631 |
1.82e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVL-KDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSG------KIR-------HSGRISYSSQTAWIM----PG 499
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGtvfrsaKVRmavfsqhHVDGLDLSSNPLLYMmrcfPG 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIrdnilfgltydEYRYKSVVKACQLEEDLAAlpekdkTPMaeggLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:PLN03073 602 VP-----------EQKLRAHLGSFGVTGNLAL------QPM----YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 580 -ATEKEIFDKCLCK---LMASKTRILVTNKIehlkraDKILLLHNGE-SFFYGTFPE 631
Cdd:PLN03073 661 dAVEALIQGLVLFQggvLMVSHDEHLISGSV------DELWVVSEGKvTPFHGTFHD 711
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
437-579 |
1.83e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR----HSGRISYSSQTAWI--MPGTIRD-----NI 505
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidgkTATRGDRSRFMAYLghLPGLKADlstleNL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 506 LFGLTYDEYRYKSVVKACQLeedLAALPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALA---IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1211-1406 |
1.84e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.86 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNAL-LKLVYTDGEISIDGVNWN--KMP----LQKW 1283
Cdd:PRK11124 3 IQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPRSGTLNIAGNHFDfsKTPsdkaIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKAFGVVPQKVFI---FTgpLRMNLDPYGCH----SDEELWRVAEEVGLKTVIEQFPDKLDFQLeyggyvlSNGHKQLIC 1356
Cdd:PRK11124 81 RRNVGMVFQQYNLwphLT--VQQNLIEAPCRvlglSKDQALARAEKLLERLRLKPYADRFPLHL-------SGGQQQRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1357 LARSILSGARILLLDEPSAHLDP-VTIKVLK--KTLRQSFSTCTILlsEHKVE 1406
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPeITAQIVSiiRELAETGITQVIV--THEVE 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1210-1378 |
2.19e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 53.86 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1210 QIEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKWRKAFG 1288
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTpQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVFIFTGPLRMNLDPYG-----------CHSDEELWRVAEEvglKTVIEQFPDKL--DfqleyggyvLSNGHKQLI 1355
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGrspwlslwgrlSAEDNARVNQAME---QTRINHLADRRltD---------LSGGQRQRA 147
|
170 180
....*....|....*....|...
gi 68390341 1356 CLARSILSGARILLLDEPSAHLD 1378
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLD 170
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1211-1408 |
2.68e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNwnkmpLQKWRKAFgv 1289
Cdd:PRK13540 2 LDVIELDFDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQS-----IKKDLCTY-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1290 vpQKVFIFTGPlRMNLDPY-----GCHSDeeLWRVAEEVGLKTVIEQFpdKLDFQLEYGGYVLSNGHKQLICLARSILSG 1364
Cdd:PRK13540 73 --QKQLCFVGH-RSGINPYltlreNCLYD--IHFSPGAVGITELCRLF--SLEHLIDYPCGLLSSGQKRQVALLRLWMSK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 1365 ARILLLDEPSAHLDPVTIKV-LKKTLRQSFSTCTILLSEHKVEPL 1408
Cdd:PRK13540 146 AKLWLLDEPLVALDELSLLTiITKIQEHRAKGGAVLLTSHQDLPL 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
440-622 |
3.31e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.65 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSlLMTIL-GELVPSSGKIRHSGR---ISySSQTAwIMPG--------------TI 501
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKST-LMKILyGLYQPDSGEILIDGKpvrIR-SPRDA-IALGigmvhqhfmlvpnlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGLtydEYRYKSVVKACQLEEDLAALpekdktpMAEGGLN---------LSGGQKARVALARAVYRDADLYLLDA 572
Cdd:COG3845 98 AENIVLGL---EPTKGGRLDRKAARARIREL-------SERYGLDvdpdakvedLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 573 PFTHLdiaTEKEI---FDkcLCKLMAS--KTRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:COG3845 168 PTAVL---TPQEAdelFE--ILRRLAAegKSIIFITHKLREVMAiADRVTVLRRGK 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
438-578 |
4.21e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKirhsgrisyssqtAWIMPG----------------TI 501
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-------------ARPAPGikvgylpqepqldpekTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFGL------------TYDEY---------------RYKSVVKAC-------QLEEDLAAL--PEKDkTPMAeggl 545
Cdd:PRK11819 88 RENVEEGVaevkaaldrfneIYAAYaepdadfdalaaeqgELQEIIDAAdawdldsQLEIAMDALrcPPWD-AKVT---- 162
|
170 180 190
....*....|....*....|....*....|...
gi 68390341 546 NLSGGQKARVALARAVYRDADLYLLDAPFTHLD 578
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
439-585 |
4.63e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.33 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILgELVPSSGKIRHSGRISYSSQTAWIMPGTIRDNILF----------- 507
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFqdpnsslnprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 508 --------GLtydEYRYKSVVKACQLEEDLAAlpekdktpMAEGGLN----------LSGGQKARVALARAVYRDADLYL 569
Cdd:PRK15134 380 nvlqiieeGL---RVHQPTLSAAQREQQVIAV--------MEEVGLDpetrhrypaeFSGGQRQRIAIARALILKPSLII 448
|
170
....*....|....*.
gi 68390341 570 LDAPFTHLDIATEKEI 585
Cdd:PRK15134 449 LDEPTSSLDKTVQAQI 464
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
442-486 |
4.72e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.01 E-value: 4.72e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 68390341 442 DISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR 486
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR 68
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
438-634 |
5.33e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.27 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELV--PSSGKIRHSGRISYSSqtawimpGTIRDNIlfGLTYDEYR 515
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGRE-------ASLIDAI--GRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 YKSVVKACQLEEdlAALPekdKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDApFT-HLDIATEKEI---FDKcLC 591
Cdd:COG2401 115 AVELLNAVGLSD--AVLW---LRRFKE----LSTGQKFRFRLALLLAERPKLLVIDE-FCsHLDRQTAKRVarnLQK-LA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 592 KlMASKTRILVTNKIEHLK--RADKILLLHngesffYGTFPELQS 634
Cdd:COG2401 184 R-RAGITLVVATHHYDVIDdlQPDLLIFVG------YGGVPEEKR 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
440-581 |
5.55e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIrHSG---RISYSSQ-TAWIMP-GTIRDNILFG------ 508
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGtklEVAYFDQhRAELDPeKTVMDNLAEGkqevmv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 509 -------LTYdeyryksvvkacqLEEDLAAlPEKDKTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:PRK11147 414 ngrprhvLGY-------------LQDFLFH-PKRAMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1223-1420 |
6.41e-07 |
|
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: 51.95 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1223 AGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLklvytdGEI-SIDG-VNW-NKMPLQKW--------RKAFGVVP 1291
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAIL------GEMqTLEGkVHWsNKNESEPSfeatrsrnRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1292 QKVFIFTGPLRMNLdPYGCHSDEELWR-VAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLL 1370
Cdd:cd03290 86 QKPWLLNATVEENI-TFGSPFNKQRYKaVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 1371 DEPSAHLD---------PVTIKVLKKTLRqsfstcTILLSEHKVEPLLECQSFLMMDKG 1420
Cdd:cd03290 165 DDPFSALDihlsdhlmqEGILKFLQDDKR------TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
440-657 |
6.49e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.79 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRiSYSSQTAW----------------IMPGTIRD 503
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrkigmvfqnpdnqFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 NILFGLTYDEYRYKSVVKacQLEEDLAA---LPEKDKTPMaegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIA 580
Cdd:PRK13642 102 DVAFGMENQGIPREEMIK--RVDEALLAvnmLDFKTREPA-----RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 581 TEKEIFDKCL-CKLMASKTRILVTNKIEHLKRADKILLLHNGESFFYGTFPELQSERPDFSSLLLGLEAYDNISAERR 657
Cdd:PRK13642 175 GRQEIMRVIHeIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMKDLR 252
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1228-1477 |
6.73e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1228 LKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV--YTDGEISIdgvnwnkmplqkwRKAFGVVPQKVFIFTGPLRMNL 1305
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELppRSDASVVI-------------RGTVAYVPQVSWIFNATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1306 dPYGCHSD-EELWRVAEEVGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDP-VTIK 1383
Cdd:PLN03130 700 -LFGSPFDpERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQ 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1384 VLKKTLRQSFSTCTILLSEHKVEPLLECQSFLMMDKGQVK---TYDSI-------QKLL-------------NETSHLKQ 1440
Cdd:PLN03130 779 VFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKeegTYEELsnngplfQKLMenagkmeeyveenGEEEDDQT 858
|
250 260 270
....*....|....*....|....*....|....*....
gi 68390341 1441 AISPAE--RLKLFPRRNSSMRTPQSKLSSVTQtlQEEAE 1477
Cdd:PLN03130 859 SSKPVAngNANNLKKDSSSKKKSKEGKSVLIK--QEERE 895
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1228-1437 |
9.31e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.11 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1228 LKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKWR-----------KAFGVVPQKVF 1295
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1296 IFTGPLRMNLDPYGC-HSDEELWRVAEEVGLKTVIEQFPDKLdfqleyggyvlSNGHKQLICLARSILSGARILLLDEPS 1374
Cdd:PRK10070 124 LDNTAFGMELAGINAeERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 1375 AHLDPVTIKVLKKTL--RQSFSTCTILLSEHKVEPLLEC-QSFLMMDKGQVKTYDSIQKLLNETSH 1437
Cdd:PRK10070 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
439-622 |
9.87e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG--RISYSSQtawimpgtirdNILFGLTYDEYRY 516
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQ-----------HQLEFLRADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 517 KSVVKAC------QLEEDLAALP-EKDKtpMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIFDkc 589
Cdd:PRK10636 396 QHLARLApqeleqKLRDYLGGFGfQGDK--VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE-- 471
|
170 180 190
....*....|....*....|....*....|....*
gi 68390341 590 lcKLMASKTRILVTNKIEHLKRA--DKILLLHNGE 622
Cdd:PRK10636 472 --ALIDFEGALVVVSHDRHLLRSttDDLYLVHDGK 504
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1211-1426 |
1.01e-06 |
|
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: 53.27 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHAVLK---NLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISID-GVNWNKM----PLQ 1281
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVNVRvGDEWVDMtkpgPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1282 KWR--KAFGVVPQKVFIFtgPLRMNLD----PYGCHSDEELWRVAEEVGLKTV----------IEQFPDKLdfqleyggy 1345
Cdd:TIGR03269 360 RGRakRYIGILHQEYDLY--PHRTVLDnlteAIGLELPDELARMKAVITLKMVgfdeekaeeiLDKYPDEL--------- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1346 vlSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTL---RQSFSTCTILLSeHKVEPLLE-CQSFLMMDKGQ 1421
Cdd:TIGR03269 429 --SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQTFIIVS-HDMDFVLDvCDRAALMRDGK 505
|
....*.
gi 68390341 1422 -VKTYD 1426
Cdd:TIGR03269 506 iVKIGD 511
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
438-628 |
1.02e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-----ISYSSQTAWIMPgtiRDNILFG---- 508
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnLDAVRQSLGMCP---QHNILFHhltv 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 509 ----LTYDEYRYKSVVKAcQLE-----EDLAALPEKDktpmaEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI 579
Cdd:TIGR01257 1021 aehiLFYAQLKGRSWEEA-QLEmeamlEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 580 ATEKEIFDkCLCKLMASKTRILVTNkieHLKRA----DKILLLHNGESFFYGT 628
Cdd:TIGR01257 1095 YSRRSIWD-LLLKYRSGRTIIMSTH---HMDEAdllgDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1211-1422 |
1.06e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKY-TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSS---LFNALLKLVytDGEISIDGVNWNKMPLQKWRKA 1286
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFEEF--EGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVV---PQKVFI---FTGPLRMNLDPYGCHSDEELWRVAEevGLKTVieqfpDKLDFQLEYGGYvLSNGHKQLICLARS 1360
Cdd:PRK13642 83 IGMVfqnPDNQFVgatVEDDVAFGMENQGIPREEMIKRVDE--ALLAV-----NMLDFKTREPAR-LSGGQKQRVAVAGI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1361 ILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFST--CTILLSEHKVEPLLECQSFLMMDKGQV 1422
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
438-587 |
1.08e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.05 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAWIMPgtIRDNIlfGLT------ 510
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlITSTSKNKDIKQ--IRKKV--GLVfqfpes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 511 --YDEYRYKSVVKACQ-----LEEDLAALPEK-----------DKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:PRK13649 97 qlFEETVLKDVAFGPQnfgvsQEEAEALAREKlalvgiseslfEKNP-----FELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170
....*....|....*
gi 68390341 573 PFTHLDIATEKEIFD 587
Cdd:PRK13649 172 PTAGLDPKGRKELMT 186
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
82-320 |
1.46e-06 |
|
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: 51.78 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 82 FLLFGFLLYIGEATKTVQPQLLGRIIASFDPAHEPERANGYFLAFGLGLLFTARFLLLQPAMFGLhhLGMQIRIALFSII 161
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAAR--LGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 162 YKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMA-HFIWISPLQCILCTGLI----WELidvnsfcALAAISLLgV 236
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGlLQLLSDVLTLIGALVILfylnWKL-------TLVALLLL-P 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 237 LQAFLSHKMGPYKAQKVLLTNKRLA-LTSEIMENLHS---VKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYSSA-Y 311
Cdd:cd07346 151 LYVLILRYFRRRIRKASREVRESLAeLSAFLQESLSGirvVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLiG 230
|
....*....
gi 68390341 312 FFSAIFVIV 320
Cdd:cd07346 231 LLTALGTAL 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1211-1403 |
1.54e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.14 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLvY--TDGEISIDGVNWNKMPLQK-WRKaf 1287
Cdd:PRK11300 6 LSVSGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF-YkpTGGTILLRGQHIEGLPGHQiARM-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GVVP--QKVFIF------------------TGPLR--MNLDPYGCHSDEELWRVA---EEVGLKTVIEQfpdkldfqlEY 1342
Cdd:PRK11300 81 GVVRtfQHVRLFremtvienllvaqhqqlkTGLFSglLKTPAFRRAESEALDRAAtwlERVGLLEHANR---------QA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1343 GGyvLSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKK---TLRQSFSTcTILLSEH 1403
Cdd:PRK11300 152 GN--LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDEliaELRNEHNV-TVLLIEH 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1211-1382 |
1.56e-06 |
|
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: 52.76 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHA--VLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-----VYTDGEISIDGVNWNKMPLQKW 1283
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpaAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKAFGvvpQKV-FIFTGPlrMN-LDPYgcH----------------SDEELWRVA----EEVGL---KTVIEQFPdkldF 1338
Cdd:COG4172 87 RRIRG---NRIaMIFQEP--MTsLNPL--HtigkqiaevlrlhrglSGAAARARAlellERVGIpdpERRLDAYP----H 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68390341 1339 QleyggyvLSNGHKQLICLARSILSGARILLLDEPSAHLDpVTI 1382
Cdd:COG4172 156 Q-------LSGGQRQRVMIAMALANEPDLLIADEPTTALD-VTV 191
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1211-1272 |
1.64e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.85 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKY-----------------TEAGHA---VLKNLSFSAEGRQRVGILGRTGSGKSSlfnaLLKL---VY--TD 1265
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkelllrrRRTRREefwALKDVSFEVERGESVGIIGRNGAGKST----LLKLiagILepTS 80
|
....*..
gi 68390341 1266 GEISIDG 1272
Cdd:COG1134 81 GRVEVNG 87
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1211-1426 |
1.73e-06 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 50.61 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKY--------------------TEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSlfnaLLKLVY-----TD 1265
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLLAgiyppDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1266 GEISIDG-VNWnkmPLqkwrkAFGV--VPQkvfiFTG--PLRMNLDPYGChSDEELWRVAEEvglktvIEQFPDKLDF-Q 1339
Cdd:cd03220 77 GTVTVRGrVSS---LL-----GLGGgfNPE----LTGreNIYLNGRLLGL-SRKEIDEKIDE------IIEFSELGDFiD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1340 LEYGGYvlSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQSFSTC-TILLSEHKVEPLLE-CQSFLMM 1417
Cdd:cd03220 138 LPVKTY--SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVL 215
|
....*....
gi 68390341 1418 DKGQVKTYD 1426
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
447-579 |
1.83e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 447 LKKGEMLAVTGSMGSGKSSLLmTIL-GELVP------------------------------SSGKIRHSGRISYSSQTAW 495
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAV-KILsGELIPnlgdyeeepswdevlkrfrgtelqnyfkklYNGEIKVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 496 IMPGTIRDnILfgLTYDEY-RYKSVVKACQLEEDLaalpEKDKTpmaegglNLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:PRK13409 175 VFKGKVRE-LL--KKVDERgKLDEVVERLGLENIL----DRDIS-------ELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
....*
gi 68390341 575 THLDI 579
Cdd:PRK13409 241 SYLDI 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
440-634 |
1.87e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR-ISYSSQTAWIMPG--------------TIRDN 504
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQeMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 505 ILFG--------LTYDEYRYKSVVKACQLEEDLAalPEkdkTPMAEgglnLSGGQKARVALARAVYRDADLYLLDAPFTH 576
Cdd:PRK11288 100 LYLGqlphkggiVNRRLLNYEAREQLEHLGVDID--PD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 577 LDiATEKEIFDKCLCKLMASKTRIL-VTNKIEHLKR-ADKILLLHNGEsfFYGTFPELQS 634
Cdd:PRK11288 171 LS-AREIEQLFRVIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGR--YVATFDDMAQ 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1211-1440 |
2.06e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYT----EAG----------------HAVlKNLSFSAEGRQRVGILGRTGSGKSSlfnaLLK-----LVYTD 1265
Cdd:COG4586 2 IEVENLSKTYRvyekEPGlkgalkglfrreyrevEAV-DDISFTIEPGEIVGFIGPNGAGKST----TIKmltgiLVPTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1266 GEISIDGVNwnkmPlQKWRKAF----GVvpqkVFiftG---------PLRMNLDPYGchsdeELWRVAEEVGLKTVieqf 1332
Cdd:COG4586 77 GEVRVLGYV----P-FKRRKEFarriGV----VF---GqrsqlwwdlPAIDSFRLLK-----AIYRIPDAEYKKRL---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1333 pDKLDFQLEYGGYV------LSNGHKQLICLARSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQSFSTcTILLSEH 1403
Cdd:COG4586 136 -DELVELLDLGELLdtpvrqLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeaIREFLKEYNRERGT-TILLTSH 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 68390341 1404 ---KVEPLleCQSFLMMDKGQVKTYDSIQKLLNETSHLKQ 1440
Cdd:COG4586 214 dmdDIEAL--CDRVIVIDHGRIIYDGSLEELKERFGPYKT 251
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1241-1423 |
2.11e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.17 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1241 VGILGRTGSGKSSL---FNALLKLvyTDGEISI------DGVNwNKmPLQKWRKAFGVVPQ----KVF-------IFTGP 1300
Cdd:PRK13634 36 VAIIGHTGSGKSTLlqhLNGLLQP--TSGTVTIgervitAGKK-NK-KLKPLRKKVGIVFQfpehQLFeetvekdICFGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1301 lrMNldpYGCHSDEELWRVAEEVGLKTVIEQFPDKLDFQLeyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDPV 1380
Cdd:PRK13634 112 --MN---FGVSEEDAKQKAREMIELVGLPEELLARSPFEL-------SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 1381 TikvlKKTLRQSFSTC------TILLSEHKVEPLLE-CQSFLMMDKGQVK 1423
Cdd:PRK13634 180 G----RKEMMEMFYKLhkekglTTVLVTHSMEDAARyADQIVVMHKGTVF 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
440-647 |
2.11e-06 |
|
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: 52.13 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSlLMTILGELVPS---SGKIRHSGR--------------ISYSSQTAWIMPG-TI 501
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKST-LMKILSGVYPHgtwDGEIYWSGSplkasnirdteragIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFG--LTYDEYR--YKSVVKACQleeDLAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHL 577
Cdd:TIGR02633 96 AENIFLGneITLPGGRmaYNAMYLRAK---NLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 578 diaTEKEIfdKCLCKLMASKTR-----ILVTNKIEHLKR-ADKILLLHNGESFfyGTFPELQSERPDFSSLLLGLE 647
Cdd:TIGR02633 173 ---TEKET--EILLDIIRDLKAhgvacVYISHKLNEVKAvCDTICVIRDGQHV--ATKDMSTMSEDDIITMMVGRE 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
440-622 |
2.19e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.94 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR------HSGRISYSSQ------------------TAW 495
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplHFGDYSYRSQrirmifqdpstslnprqrISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 496 IMPGTIRDNILFGLTYDEYRYKSVVKACQLEEDLAALpekdkTPMAegglnLSGGQKARVALARAVYRDADLYLLDAPFT 575
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASY-----YPHM-----LAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 576 HLDIATEKEIFDKCLcKLMASK--TRILVTNKIEHLKR-ADKILLLHNGE 622
Cdd:PRK15112 179 SLDMSMRSQLINLML-ELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGE 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
437-582 |
2.41e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGR--------------ISYSSQ----TAWIMP 498
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 499 GTIRDNILFGLTYDE-------YRYKSVVKACQ-LEEDLAALPEKDKTPMAegglNLSGG--QKarVALARAVYRDADLY 568
Cdd:COG3845 351 MSVAENLILGRYRRPpfsrggfLDRKAIRAFAEeLIEEFDVRTPGPDTPAR----SLSGGnqQK--VILARELSRDPKLL 424
|
170
....*....|....*
gi 68390341 569 LLDAPFTHLDI-ATE 582
Cdd:COG3845 425 IAAQPTRGLDVgAIE 439
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1163-1383 |
2.59e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.17 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1163 GMMRSVD--RVFKFIDLPsetpKPDKgkdsdliiENVDAQADSSWPHRGQIEVRNLTVKY----------TEAGHAVlKN 1230
Cdd:PRK10261 276 GAMKGLDypRRFPLISLE----HPAK--------QEPPIEQDTVVDGEPILQVRNLVTRFplrsgllnrvTREVHAV-EK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1231 LSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYT-DGEISIDGVNWNKMP---LQKWRKAFGvvpqkvFIFTGPLrMNLD 1306
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESqGGEIIFNGQRIDTLSpgkLQALRRDIQ------FIFQDPY-ASLD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1307 P--------------YGC-HSDEELWRVA---EEVGLKtvieqfPD-KLDFQLEYGGyvlsnGHKQLICLARSILSGARI 1367
Cdd:PRK10261 416 PrqtvgdsimeplrvHGLlPGKAAAARVAwllERVGLL------PEhAWRYPHEFSG-----GQRQRICIARALALNPKV 484
|
250
....*....|....*.
gi 68390341 1368 LLLDEPSAHLDpVTIK 1383
Cdd:PRK10261 485 IIADEAVSALD-VSIR 499
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
440-628 |
2.63e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.97 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPS---SGKIRHSGRISYSSQ----TAWIMpgtiRDNILFG-LTY 511
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEmraiSAYVQ----QDDLFIPtLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 512 DEY-----------RYKSVVKACQLEEDLAALPEKD--KTPMAEGGL--NLSGGQKARVALARAVYRDADLYLLDAPFTH 576
Cdd:TIGR00955 117 REHlmfqahlrmprRVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 68390341 577 LDIATEKEIFDkcLCKLMASKTRILV------TNKIEHLkrADKILLLHNGESFFYGT 628
Cdd:TIGR00955 197 LDSFMAYSVVQ--VLKGLAQKGKTIIctihqpSSELFEL--FDKIILMAEGRVAYLGS 250
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1228-1422 |
2.94e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.97 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1228 LKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTDGEISIDgVNWNKMPLQKW----RKAFgVVPQKVFI------- 1296
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGS-VLLNGMPIDAKemraISAY-VQQDDLFIptltvre 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1297 ---FTGPLRMNLDPYgchSDEELWRVAE---EVGL----KTVIeQFPDKLDfqleyggyVLSNGHKQLICLARSILSGAR 1366
Cdd:TIGR00955 119 hlmFQAHLRMPRRVT---KKEKRERVDEvlqALGLrkcaNTRI-GVPGRVK--------GLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 1367 ILLLDEPSAHLDPVT----IKVLKKtLRQSFStcTILLSEHKVEPLLECQ--SFLMMDKGQV 1422
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMaysvVQVLKG-LAQKGK--TIICTIHQPSSELFELfdKIILMAEGRV 245
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1243-1446 |
3.02e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1243 ILGRTGSGKSSLFNALLklvyTDGEISiDGVNWNKmplqkwrKAFGVVPQKVFIFTGPLRMNLDPYGCHSDEELWRVAEE 1322
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLL----SQFEIS-EGRVWAE-------RSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRV 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1323 VGLKTVIEQFPDKLDFQLEYGGYVLSNGHKQLICLARSILSGARILLLDEPSAHLDP-VTIKVLKKTLRQSFSTCTILLS 1401
Cdd:PTZ00243 759 SQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERVVEECFLGALAGKTRVLA 838
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 1402 EHKVEPLLECQSFLMMDKGQVK------------TYDSIQKLLNETSHLKQAISPAE 1446
Cdd:PTZ00243 839 THQVHVVPRADYVVALGDGRVEfsgssadfmrtsLYATLAAELKENKDSKEGDADAE 895
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
441-622 |
3.59e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 441 KDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-RISYSSQTAWIMPG-----------------TIR 502
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkDISPRSPLDAVKKGmayitesrrdngffpnfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 503 DNILFGLTYDEYRYKSVVKAC-QLEEDLAALPEKDKTPMAEGGLN-----LSGGQKARVALARAVYRDADLYLLDAPFTH 576
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMGLFhEVDEQRTAENQRELLALKCHSVNqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68390341 577 LDIATEKEIFdkclcKLMAS-----KTRILVTNKI-EHLKRADKILLLHNGE 622
Cdd:PRK09700 440 IDVGAKAEIY-----KVMRQladdgKVILMVSSELpEIITVCDRIAVFCEGR 486
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1211-1390 |
4.41e-06 |
|
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: 50.98 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNaLLKLVYTDGeiSIDG-VNWNKMPLQKW------ 1283
Cdd:TIGR02633 2 LEMKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHG--TWDGeIYWSGSPLKASnirdte 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKAFGVVPQKVF----------IFTGPlRMNLdPYGCHSDEELWRVAEEVGLKTVIEQFPDKLDFqLEYGGyvlsnGHKQ 1353
Cdd:TIGR02633 77 RAGIVIIHQELTlvpelsvaenIFLGN-EITL-PGGRMAYNAMYLRAKNLLRELQLDADNVTRPV-GDYGG-----GQQQ 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 68390341 1354 LICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLR 1390
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIR 185
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1211-1391 |
4.42e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.47 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTvKYTeaGH-AVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKWRKAFg 1288
Cdd:PRK10851 3 IEIANIK-KSF--GRtQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEhQTSGHIRFHGTDVSRLHARDRKVGF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 vVPQKVFIFTG--------------PLRMNldPYGCHSDEELWRVAEEVGLKTVIEQFPDKLdfqleyggyvlSNGHKQL 1354
Cdd:PRK10851 79 -VFQHYALFRHmtvfdniafgltvlPRRER--PNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQR 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 68390341 1355 ICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQ 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
437-581 |
5.01e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 437 APVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYS--SQTawimP-----GTIRDNILFGL 509
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlQQD----PprnveGTVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 510 --------TY--------DEYRYKSVVKACQLEEDLA-----ALPEKDKTPMAEGGLN-------LSGGQKARVALARAV 561
Cdd:PRK11147 92 eeqaeylkRYhdishlveTDPSEKNLNELAKLQEQLDhhnlwQLENRINEVLAQLGLDpdaalssLSGGWLRKAALGRAL 171
|
170 180
....*....|....*....|
gi 68390341 562 YRDADLYLLDAPFTHLDIAT 581
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIET 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
440-632 |
5.36e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.09 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYS----------------SQTAWIMPgtIRD 503
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKrrkefarrigvvfgqrSQLWWDLP--AID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 504 --NIL---FGLTYDEY--RYKSVVKACQLEEDLaalpekdKTPMAegglNLSGGQKARVALARAVYRDADLYLLDAPFTH 576
Cdd:COG4586 116 sfRLLkaiYRIPDAEYkkRLDELVELLDLGELL-------DTPVR----QLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68390341 577 LDIATEKEI--FDKCLCKlmASKTRILVT----NKIEHLkrADKILLLHNGESFFYGTFPEL 632
Cdd:COG4586 185 LDVVSKEAIreFLKEYNR--ERGTTILLTshdmDDIEAL--CDRVIVIDHGRIIYDGSLEEL 242
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1228-1378 |
6.10e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.40 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1228 LKNLSFSAEGRQ------------RV-GILGRTGSGKSSLfnalLKLV-----YTDGEISIDGvnwnkMPLQKWR-KAFG 1288
Cdd:PRK10575 14 LRNVSFRVPGRTllhplsltfpagKVtGLIGHNGSGKSTL----LKMLgrhqpPSEGEILLDA-----QPLESWSsKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 ----VVPQK------------VFIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTVIEQFPDKLdfqleyggyvlSNGHK 1352
Cdd:PRK10575 85 rkvaYLPQQlpaaegmtvrelVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSL-----------SGGER 153
|
170 180
....*....|....*....|....*.
gi 68390341 1353 QLICLARSILSGARILLLDEPSAHLD 1378
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
439-627 |
6.15e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSsgKIRHSGRISYSSQT-AWIMPGTIRDNILFGLTYDEYRYK 517
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGF--HIGVEGVITYDGITpEEIKKHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 518 SV------VKACQ--------LEEDLAALPEKDKTpMAEGGLN--------------LSGGQKARVALARAVYRDADLYL 569
Cdd:TIGR00956 154 TVgetldfAARCKtpqnrpdgVSREEYAKHIADVY-MATYGLShtrntkvgndfvrgVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68390341 570 LDAPFTHLDIATEKEiFDKCLcKLMASKTRILVTNKI-----EHLKRADKILLLHNGESFFYG 627
Cdd:TIGR00956 233 WDNATRGLDSATALE-FIRAL-KTSANILDTTPLVAIyqcsqDAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1200-1379 |
6.16e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1200 QADSSWPhrgQIEVRNLTVKYTEAGHAVlKNLSFSAEGRQRVGILGRTGSGKSSlFNALLKLVYTD--GEISIDGVNWNK 1277
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKST-LAMLLTGLYQPqsGEILLDGKPVTA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1278 MPLQKWRKAFGVVPQKVFIFTgplRMnLDPYGCHSDEEL---WrvaeevgLKTVieQFPDKLDFQleyGGYV----LSNG 1350
Cdd:PRK10522 390 EQPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekW-------LERL--KMAHKLELE---DGRIsnlkLSKG 453
|
170 180
....*....|....*....|....*....
gi 68390341 1351 HKQLICLARSILSGARILLLDEPSAHLDP 1379
Cdd:PRK10522 454 QKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
438-621 |
7.56e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.31 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVP----SSGKIRHSGRISYSSQ-----TAWIMPG--------- 499
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCAlrgrkIATIMQNprsafnplh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 TIRDNIL-----FGLTYDEYRYKSVVKACQLEEDLAALpekDKTPmaeggLNLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:PRK10418 97 TMHTHARetclaLGKPADDATLTAALEAVGLENAARVL---KLYP-----FEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 575 THLDIATEKEIFDkCLCKLMASKT--RILVTNKIEHLKR-ADKILLLHNG 621
Cdd:PRK10418 169 TDLDVVAQARILD-LLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1211-1406 |
7.62e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNaLLKLVYT----DGEISIDGvnwnkMPLQKW--- 1283
Cdd:PRK13549 6 LEMKNITKTF--GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPhgtyEGEIIFEG-----EELQASnir 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 ---RKAFGVVPQKVF----------IFTGPlrmNLDPYGCHSDEELWRVAEEVgLKTVieqfpdKLDFQ-----LEYGGy 1345
Cdd:PRK13549 78 dteRAGIAIIHQELAlvkelsvlenIFLGN---EITPGGIMDYDAMYLRAQKL-LAQL------KLDINpatpvGNLGL- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1346 vlsnGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLK---KTLRQSFSTCtILLSeHKVE 1406
Cdd:PRK13549 147 ----GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLdiiRDLKAHGIAC-IYIS-HKLN 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
447-579 |
8.69e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 447 LKKGEMLAVTGSMGSGKSSLLmTIL-GELVPSSGKI-----------RHSG---------------RISYSSQTAWIMP- 498
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTAL-KILsGELKPNLGDYdeepswdevlkRFRGtelqdyfkklangeiKVAHKPQYVDLIPk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 499 ---GTIRDnILFGltYDEY-RYKSVVKACQLEEDLaalpEKDKTpmaegglNLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:COG1245 175 vfkGTVRE-LLEK--VDERgKLDELAEKLGLENIL----DRDIS-------ELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
....*
gi 68390341 575 THLDI 579
Cdd:COG1245 241 SYLDI 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1211-1391 |
9.21e-06 |
|
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: 48.29 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKytEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALL---KLVYTDGEISIDGVNWNKMPLQKwRKAF 1287
Cdd:cd03217 1 LEIKDLHVS--VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGEDITDLPPEE-RARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 GvvpqkvfIFTGplrmnldpygchsdeelWRVAEEV-GLKTvieqfpdkLDFqLEYGGYVLSNGHKQLICLARSILSGAR 1366
Cdd:cd03217 78 G-------IFLA-----------------FQYPPEIpGVKN--------ADF-LRYVNEGFSGGEKKRNEILQLLLLEPD 124
|
170 180
....*....|....*....|....*
gi 68390341 1367 ILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINK 149
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1242-1439 |
9.23e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.35 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1242 GILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKW----RKAFGVVPQ----KVFIFTGPLRMNLDP--YGC 1310
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKQKEikpvRKKVGVVFQfpesQLFEETVLKDVAFGPqnFGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1311 HSDEELWRVAEEVGLKTVIEQFPDKLDFQLeyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDP-VTIKVLK--K 1387
Cdd:PRK13643 116 PKEKAEKIAAEKLEMVGLADEFWEKSPFEL-------SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPkARIEMMQlfE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68390341 1388 TLRQSFStcTILLSEHKVEPLLECQSFL-MMDKGQVKTYDSIQKLLNETSHLK 1439
Cdd:PRK13643 189 SIHQSGQ--TVVLVTHLMDDVADYADYVyLLEKGHIISCGTPSDVFQEVDFLK 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
440-585 |
9.94e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSlLMTILGELVPS---SGKIRHSGR--------------ISYSSQTAWIMPG-TI 501
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKST-LMKVLSGVYPHgtyEGEIIFEGEelqasnirdteragIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 502 RDNILFG--------LTYDEY--RYKSVVKACQLEEDLAalpekdkTPMAegglNLSGGQKARVALARAVYRDADLYLLD 571
Cdd:PRK13549 100 LENIFLGneitpggiMDYDAMylRAQKLLAQLKLDINPA-------TPVG----NLGLGQQQLVEIAKALNKQARLLILD 168
|
170
....*....|....
gi 68390341 572 APFTHLdiaTEKEI 585
Cdd:PRK13549 169 EPTASL---TESET 179
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
439-587 |
1.03e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.83 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSG-------------RISYSSQTAwIMPGTIRDNI 505
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLAQNA-TTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LfgLTYDEYRYKSVVKACQLEEDLA---ALPEKDKTPMAEGGLN-LSGGQKARVALARAVYRDADLYLLDAPFTHLDIAT 581
Cdd:PRK10253 101 L--VARGRYPHQPLFTRWRKEDEEAvtkAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
....*.
gi 68390341 582 EKEIFD 587
Cdd:PRK10253 179 QIDLLE 184
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
439-586 |
1.12e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGElvpSSGKiRHSGRISYSSQTAWImpGTIRDNILFGLTY---DEYR 515
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SYGR-NISGTVFKDGKEVDV--STVSDAIDAGLAYvteDRKG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 YKSVvkacqLEED------LAALPE-----------------------KDKTP-MAEGGLNLSGGQKARVALARAVYRDA 565
Cdd:NF040905 349 YGLN-----LIDDikrnitLANLGKvsrrgvideneeikvaeeyrkkmNIKTPsVFQKVGNLSGGNQQKVVLSKWLFTDP 423
|
170 180
....*....|....*....|.
gi 68390341 566 DLYLLDAPFTHLDIATEKEIF 586
Cdd:NF040905 424 DVLILDEPTRGIDVGAKYEIY 444
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1213-1405 |
1.18e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.52 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1213 VRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTDGEISIDGvnwnKMPLQKWRKAFGVVPQ 1292
Cdd:PRK11247 15 LNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG----TAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1293 KVFIFtgPLRMNLDPYGchsdeeL-----WRVA-----EEVGLKTVIEQFPDkldfqleyggyVLSNGHKQLICLARSIL 1362
Cdd:PRK11247 89 DARLL--PWKKVIDNVG------LglkgqWRDAalqalAAVGLADRANEWPA-----------ALSGGQKQRVALARALI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 68390341 1363 SGARILLLDEPSAHLDPVT---IKVLKKTL--RQSFstcTILLSEHKV 1405
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTrieMQDLIESLwqQHGF---TVLLVTHDV 194
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-621 |
1.33e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTiLGELVPSSGKIRHSG--------------------RISYSSQTAWIMP 498
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRT-LNRMNDKVSGYRYSGdvllggrsifnyrdvlefrrRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 499 GTIRDNILFGLTYDEY----RYKSVVKAcQLEEdlAALPEKDKTPMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLvprkEFRGVAQA-RLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 68390341 575 THLDIATEKEIfDKCLCKLMASKTRILVTNKIEHLKR-ADKILLLHNG 621
Cdd:PRK14271 192 SALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDG 238
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1211-1381 |
1.41e-05 |
|
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: 47.81 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYT--EAGHA---VLKNLSFSAEGRQRVGILGRTGSGKSSLfnalLKLVY-----TDGEISID----GVNWN 1276
Cdd:COG4778 5 LEVENLSKTFTlhLQGGKrlpVLDGVSFSVAAGECVALTGPSGAGKSTL----LKCIYgnylpDSGSILVRhdggWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1277 KMP----LQKWRKAFGVVPQkvF-----------IFTGPL-------------------RMNLDpygchsdEELWRVAee 1322
Cdd:COG4778 81 QASpreiLALRRRTIGYVSQ--FlrviprvsaldVVAEPLlergvdreearararellaRLNLP-------ERLWDLP-- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 68390341 1323 vglktvieqfPdkLDFqleyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDPVT 1381
Cdd:COG4778 150 ----------P--ATF---------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1211-1403 |
1.41e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.19 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEagHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTDgeisiDGVNWNKMPLQkwrkaFGVV 1290
Cdd:PRK09544 5 VSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD-----EGVIKRNGKLR-----IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1291 PQKVFI-FTGPLR----MNLDPyGCHSDEELwrvaeeVGLKTVieQFPDKLDFQLEYggyvLSNGHKQLICLARSILSGA 1365
Cdd:PRK09544 73 PQKLYLdTTLPLTvnrfLRLRP-GTKKEDIL------PALKRV--QAGHLIDAPMQK----LSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68390341 1366 RILLLDEPSAHLD---PVTIKVLKKTLRQSFStCTILLSEH 1403
Cdd:PRK09544 140 QLLVLDEPTQGVDvngQVALYDLIDQLRRELD-CAVLMVSH 179
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
432-611 |
1.51e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 432 TNLYVA----PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGElvPSSGKIrhSGRISYSSQTAWIMPGTIRDN--I 505
Cdd:CHL00131 11 KNLHASvnenEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAYKIL--EGDILFKGESILDLEPEERAHlgI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 506 LFGLTY----------DEYR--YKSVVKACQLEED-----LAALPEK-DKTPMAEGGLN------LSGGQKARVALARAV 561
Cdd:CHL00131 87 FLAFQYpieipgvsnaDFLRlaYNSKRKFQGLPELdplefLEIINEKlKLVGMDPSFLSrnvnegFSGGEKKRNEILQMA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 562 YRDADLYLLDAPFTHLDIATEKEIfDKCLCKLMASKTRILVtnkIEHLKR 611
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKII-AEGINKLMTSENSIIL---ITHYQR 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
438-579 |
1.73e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHS--GRISYSSQ----------------TAWIMPG 499
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIGYYAQdhaydfendltlfdwmSQWRQEG 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 ----TIRD---NILFGltYDEYRyKSVVkacqleedlaalpekdktpmaegglNLSGGQKARVALARAVYRDADLYLLDA 572
Cdd:PRK15064 413 ddeqAVRGtlgRLLFS--QDDIK-KSVK-------------------------VLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
....*..
gi 68390341 573 PFTHLDI 579
Cdd:PRK15064 465 PTNHMDM 471
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
444-605 |
2.02e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 444 SLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGK----IRHSGRISYsSQTAWIMPGTIRDNILFGLTYDEYRY-KS 518
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqFSHITRLSF-EQLQKLVSDEWQRNNTDMLSPGEDDTgRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 519 VVKACQLEEDLAALPEKDKTPMAEGGL------NLSGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEiFDKCLCK 592
Cdd:PRK10938 102 TAEIIQDEVKDPARCEQLAQQFGITALldrrfkYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ-LAELLAS 180
|
170
....*....|....
gi 68390341 593 LMASK-TRILVTNK 605
Cdd:PRK10938 181 LHQSGiTLVLVLNR 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1211-1423 |
2.21e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.47 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGH--AVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQ---KWR 1284
Cdd:PRK10584 7 VEVHHLKKSVGQGEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDdGSSGEVSLVGQPLHQMDEEaraKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1285 -KAFGVVPQKVFI-----------FTGPLRMNLDPygcHSDEELWRVAEEVGLKTVIEQFPDKLdfqleyggyvlSNGHK 1352
Cdd:PRK10584 87 aKHVGFVFQSFMLiptlnalenveLPALLRGESSR---QSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1353 QLICLARSILSGARILLLDEPSAHLDPVT---IKVLKKTLRQSFSTcTILLSEHKVEPLLECQSFLMMDKGQVK 1423
Cdd:PRK10584 153 QRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADLLFSLNREHGT-TLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1225-1401 |
2.41e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1225 HAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDG-VNWNKMPLQKWRKAFGVVPQkvFIFTG--- 1299
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVlLDDGRIIYEQdLIVARLQQDPPRNVEGTVYD--FVAEGiee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1300 -----------PLRMNLDPygchSDEELWRVAEevgLKTVIE-----QFPDKLDFQLEYGGY-------VLSNGHKQLIC 1356
Cdd:PRK11147 94 qaeylkryhdiSHLVETDP----SEKNLNELAK---LQEQLDhhnlwQLENRINEVLAQLGLdpdaalsSLSGGWLRKAA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68390341 1357 LARSILSGARILLLDEPSAHLDPVTIKVLKKTLRqSFSTCTILLS 1401
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK-TFQGSIIFIS 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
439-627 |
2.41e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.11 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 439 VLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSS--GKIRHSGRisysSQTAWIMPGT---IRDNILfgltYDE 513
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNR----KPTKQILKRTgfvTQDDIL----YPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 514 YRYKSVVKACQLEEDLAALPEKDKTPMAEG-----GLN--------------LSGGQKARVALARAVYRDADLYLLDAPF 574
Cdd:PLN03211 155 LTVRETLVFCSLLRLPKSLTKQEKILVAESviselGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68390341 575 THLDiATEKEIFDKCLCKLmASKTRILVTNKIEHLKRA----DKILLLHNGESFFYG 627
Cdd:PLN03211 235 SGLD-ATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFG 289
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
438-492 |
2.52e-05 |
|
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: 48.53 E-value: 2.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGeLVPSSGkIRHSGRISYSSQ 492
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSVTALSILR-LLPDPA-AHPSGSILFDGQ 76
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
440-643 |
2.53e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIRHSGRISYSSQTAWIMPG-TIRDNILFGLTYDEYRYKS 518
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQlTGIENIEFKMLCMGFKRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 519 VVKACQLEEDLAALPEKDKTPMAegglNLSGGQKARVALARAVYRDADLYLLDAPFTHLDiateKEIFDKCLCKLM---- 594
Cdd:PRK13546 120 IKAMTPKIIEFSELGEFIYQPVK----KYSSGMRAKLGFSINITVNPDILVIDEALSVGD----QTFAQKCLDKIYefke 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 68390341 595 ASKTRILVTNKIEHLKR-ADKILLLHNGesfFYGTFPELQSERPDFSSLL 643
Cdd:PRK13546 192 QNKTIFFVSHNLGQVRQfCTKIAWIEGG---KLKDYGELDDVLPKYEAFL 238
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1211-1383 |
3.28e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTE-----AGHAVLKNL---SFSAEGRQRVGILGRTGSGKSSLfNALLKLVY--TDGEISIDGVNWNKMPL 1280
Cdd:PRK11308 6 LQAIDLKKHYPVkrglfKPERLVKALdgvSFTLERGKTLAVVGESGCGKSTL-ARLLTMIEtpTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1281 QKW---RKAFGVVPQ----------KV-FIFTGPLRMNLDPYGCHSDEELWRVAEEVGLKTviEQfpdkldfqleYGGY- 1345
Cdd:PRK11308 85 EAQkllRQKIQIVFQnpygslnprkKVgQILEEPLLINTSLSAAERREKALAMMAKVGLRP--EH----------YDRYp 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 68390341 1346 -VLSNGHKQLICLARSILSGARILLLDEPSAHLDpVTIK 1383
Cdd:PRK11308 153 hMFSGGQRQRIAIARALMLDPDVVVADEPVSALD-VSVQ 190
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1214-1378 |
3.67e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.73 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1214 RNLTVKYTEAGHA--VLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL-VYTDGEISIDGVNWNKMP------LQKWR 1284
Cdd:PRK11629 9 DNLCKRYQEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSsaakaeLRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1285 KAF-----GVVPQkvFIFTGPLRMNLDPYGCHSDEELWRVAE---EVGLKTVIEQFPDKldfqleyggyvLSNGHKQLIC 1356
Cdd:PRK11629 89 LGFiyqfhHLLPD--FTALENVAMPLLIGKKKPAEINSRALEmlaAVGLEHRANHRPSE-----------LSGGERQRVA 155
|
170 180
....*....|....*....|..
gi 68390341 1357 LARSILSGARILLLDEPSAHLD 1378
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLD 177
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1206-1390 |
5.73e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.10 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1206 PHRGQIEVRNLTVKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTDGEISIDGVNWNKMPLQK--- 1282
Cdd:COG2401 24 SERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREAsli 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 ---WRKafGVVPQKVFIFTgplRMNLdpygchSDEELWR--VAEevglktvieqfpdkldfqleyggyvLSNGHKQLICL 1357
Cdd:COG2401 104 daiGRK--GDFKDAVELLN---AVGL------SDAVLWLrrFKE-------------------------LSTGQKFRFRL 147
|
170 180 190
....*....|....*....|....*....|...
gi 68390341 1358 ARSILSGARILLLDEPSAHLDPVTIKVLKKTLR 1390
Cdd:COG2401 148 ALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1228-1379 |
5.85e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1228 LKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTDGEISIDG-----VNWNKMP-LQKWRKAFGVVPQ----KVF-- 1295
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipANLKKIKeVKRLRKEIGLVFQfpeyQLFqe 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1296 -----IFTGPLRMnldpyGCHSDEELWRVAEEVGLKTVIEQFPDKLDFQLeyggyvlSNGHKQLICLARSILSGARILLL 1370
Cdd:PRK13645 107 tiekdIAFGPVNL-----GENKQEAYKKVPELLKLVQLPEDYVKRSPFEL-------SGGQKRRVALAGIIAMDGNTLVL 174
|
....*....
gi 68390341 1371 DEPSAHLDP 1379
Cdd:PRK13645 175 DEPTGGLDP 183
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1211-1391 |
6.65e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.32 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLfnalLKL---VY--TDGEISIDG--VNWNKmPLQKW 1283
Cdd:COG1129 5 LEMRGISKSF--GGVKALDGVSLELRPGEVHALLGENGAGKSTL----MKIlsgVYqpDSGEILLDGepVRFRS-PRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1284 RKAFGVVPQK------------VFIFTGPLRmnldpYGCHSDEELWRVAEEVglktvIEQF-----PDKLdfqleyggyV 1346
Cdd:COG1129 78 AAGIAIIHQElnlvpnlsvaenIFLGREPRR-----GGLIDWRAMRRRAREL-----LARLgldidPDTP---------V 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68390341 1347 --LSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:COG1129 139 gdLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRR 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1244-1422 |
7.43e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.28 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1244 LGRTGSGKSS---LFNALLklVYTDGEISIDGV-----NWNKmPLQKWRKAFGVVPQ----KVFIFT-------GPLRMN 1304
Cdd:PRK13649 39 IGHTGSGKSTimqLLNGLH--VPTQGSVRVDDTlitstSKNK-DIKQIRKKVGLVFQfpesQLFEETvlkdvafGPQNFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1305 LdpygchSDEELWRVAEE-VGLKTVIEQFPDKLDFQLeyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDPVTIK 1383
Cdd:PRK13649 116 V------SQEEAEALAREkLALVGISESLFEKNPFEL-------SGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 68390341 1384 VLK---KTLRQsfSTCTILLSEHKVEPLLECQSFL-MMDKGQV 1422
Cdd:PRK13649 183 ELMtlfKKLHQ--SGMTIVLVTHLMDDVANYADFVyVLEKGKL 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
438-621 |
9.98e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 438 PVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKIR-HSGRISYSSQTAWIMPGtirdnilFGLTYDEYR- 515
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITlHGKKINNHNANEAINHG-------FALVTEERRs 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 516 --------------------YKS---VVKACQLEEDLAALPE--KDKTPMAEGGL-NLSGGQKARVALARAVYRDADLYL 569
Cdd:PRK10982 335 tgiyayldigfnslisnirnYKNkvgLLDNSRMKSDTQWVIDsmRVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 570 LDAPFTHLDIATEKEIFDkcLCKLMASKTR--ILVTNKI-EHLKRADKILLLHNG 621
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQ--LIAELAKKDKgiIIISSEMpELLGITDRILVMSNG 467
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
94-280 |
1.09e-04 |
|
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: 45.94 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 94 ATKTVQPQLLGRIIAsfDPAHEPERAN-----GYFLAFGL---GLLFTARFLLLQPAmfglhhLGMQ--IRIALfsiiYK 163
Cdd:cd18543 13 LAGLAIPLLTRRAID--GPIAHGDRSAlwplvLLLLALGVaeaVLSFLRRYLAGRLS------LGVEhdLRTDL----FA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 164 KTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMAHFIWISPLQCILCTGLI----WELIDVnsfcALAAISLLGVLQA 239
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMlvlsPPLALV----ALASLPPLVLVAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68390341 240 FLSHKMGP--YKAQkvlltnKRLA-LTSEIMENLHS---VKAYGWEE 280
Cdd:cd18543 157 RFRRRYFPasRRAQ------DQAGdLATVVEESVTGirvVKAFGRER 197
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
434-579 |
1.11e-04 |
|
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: 45.44 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 434 LYVAPVLKDislklkkGEMLAVTGSMGSGKSSLLMTILGELVPSSGKirhsgrisYSSQTAWimpgtirDNILfgltyDE 513
Cdd:cd03236 17 LHRLPVPRE-------GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDW-------DEIL-----DE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 514 YR---------------YKSVVKACQLEEDLAA--------LPEKDKTPMAEGGL--------------NLSGGQKARVA 556
Cdd:cd03236 70 FRgselqnyftkllegdVKVIVKPQYVDLIPKAvkgkvgelLKKKDERGKLDELVdqlelrhvldrnidQLSGGELQRVA 149
|
170 180
....*....|....*....|...
gi 68390341 557 LARAVYRDADLYLLDAPFTHLDI 579
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDI 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1211-1391 |
1.11e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYTEAGHA--VLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKL------VYTDGEISIDGVNWNKMPLQK 1282
Cdd:PRK15134 6 LAIENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1283 WRKAFGvvPQKVFIFTGPLrMNLDPYgcHSDE--------------------ELWRVAEEVGlktvIEQFPDKL-DFQle 1341
Cdd:PRK15134 86 LRGVRG--NKIAMIFQEPM-VSLNPL--HTLEkqlyevlslhrgmrreaargEILNCLDRVG----IRQAAKRLtDYP-- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1342 yggYVLSNGHKQLICLARSILSGARILLLDEPSAHLDpVTIKV----LKKTLRQ 1391
Cdd:PRK15134 155 ---HQLSGGERQRVMIAMALLTRPELLIADEPTTALD-VSVQAqilqLLRELQQ 204
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1240-1260 |
1.76e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 42.61 E-value: 1.76e-04
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1242-1383 |
2.08e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 45.08 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1242 GILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNWNKMPLQKWRKafgVVPQKVFIFTGPL-----RMN--------LDP 1307
Cdd:PRK15079 51 GVVGESGCGKSTFARAIIGLVkATDGEVAWLGKDLLGMKDDEWRA---VRSDIQMIFQDPLaslnpRMTigeiiaepLRT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1308 YGCH-SDEELW-RVAE---EVGL-KTVIEQFPDKLdfqleyggyvlSNGHKQLICLARSILSGARILLLDEPSAHLDpVT 1381
Cdd:PRK15079 128 YHPKlSRQEVKdRVKAmmlKVGLlPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICDEPVSALD-VS 195
|
..
gi 68390341 1382 IK 1383
Cdd:PRK15079 196 IQ 197
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1211-1387 |
2.12e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 44.76 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTvkYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMP---LQKWRKA 1286
Cdd:PRK11831 8 VDMRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDhGEILFDGENIPAMSrsrLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1287 FGVVPQKVFIFTG---------PLRMNldpygCHSDEELWRVA-----EEVGLKTVIEQFPDKLdfqleyggyvlSNGHK 1352
Cdd:PRK11831 86 MSMLFQSGALFTDmnvfdnvayPLREH-----TQLPAPLLHSTvmmklEAVGLRGAAKLMPSEL-----------SGGMA 149
|
170 180 190
....*....|....*....|....*....|....*
gi 68390341 1353 QLICLARSILSGARILLLDEPSAHLDPVTIKVLKK 1387
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
440-616 |
2.45e-04 |
|
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: 44.53 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTIL---------------GELVPSSGkIRHSGRISYSSQ-----TAWIMPG 499
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEG-LEHIDKVIVIDQspigrTPRSNPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 T-------IRDniLF-----GLTYD----EYRYK----------SVVKACQLEEDLAALPEKDKTpMAEGGLN------- 546
Cdd:cd03271 90 TytgvfdeIRE--LFcevckGKRYNretlEVRYKgksiadvldmTVEEALEFFENIPKIARKLQT-LCDVGLGyiklgqp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 547 ---LSGGQKARVALARAVYRDAD---LYLLDAPFTHLDIATEKEIFDkCLCKLMASKTRILVtnkIEH----LKRADKIL 616
Cdd:cd03271 167 attLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLE-VLQRLVDKGNTVVV---IEHnldvIKCADWII 242
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1218-1378 |
2.63e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.32 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1218 VKYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVY-TDGEISIDGVNWNKMPLQKWRKAFGVVPQKVFI 1296
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISpTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1297 FTGPLRMNLD-PYGCHSDEelwrvAEEVGLKTVIEQF--PDKLdfqLEYGGYVLSNGHKQLICLARSILSGARILLLDEP 1373
Cdd:PRK10247 93 FGDTVYDNLIfPWQIRNQQ-----PDPAIFLDDLERFalPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
....*
gi 68390341 1374 SAHLD 1378
Cdd:PRK10247 165 TSALD 169
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1212-1291 |
2.74e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1212 EVRNLTVKyTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLV-YTDGEISIDGVNW-NKMPLQKWRKAFGV 1289
Cdd:COG3845 259 EVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRpPASGSIRLDGEDItGLSPRERRRLGVAY 337
|
..
gi 68390341 1290 VP 1291
Cdd:COG3845 338 IP 339
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
923-1091 |
3.41e-04 |
|
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: 44.36 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 923 ILYIYVATSesllAMGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTkDMATIDD--------- 993
Cdd:cd18570 48 LILLYLFQS----LLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREaissttisl 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 994 MLPLLMFDFV---------QLTvvvvgcilvvsivrpYIFLAATPL-AIIFIVMRKYFLRtgQQLKQLETEARSPifSHL 1063
Cdd:cd18570 123 FLDLLMVIISgiilffynwKLF---------------LITLLIIPLyILIILLFNKPFKK--KNREVMESNAELN--SYL 183
|
170 180 190
....*....|....*....|....*....|..
gi 68390341 1064 IMSLKGLWTIRAF--ERQAY--FEALFHKTLN 1091
Cdd:cd18570 184 IESLKGIETIKSLnaEEQFLkkIEKKFSKLLK 215
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1240-1258 |
4.13e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 44.37 E-value: 4.13e-04
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1211-1404 |
6.68e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.25 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1211 IEVRNLTVKYteAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGvnwNKMPLQKWRKAF-- 1287
Cdd:COG3845 6 LELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDsGEILIDG---KPVRIRSPRDAIal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1288 --GVVPQ--KVF-IFT------------GPLRMNLDpygcHSDEELWRVAEEVGLK----TVIEQfpdkldfqleyggyv 1346
Cdd:COG3845 81 giGMVHQhfMLVpNLTvaenivlgleptKGGRLDRK----AARARIRELSERYGLDvdpdAKVED--------------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68390341 1347 LSNGHKQLI----CLARsilsGARILLLDEPSAHLDPVTIKVLKKTLRQsFST--CTILLSEHK 1404
Cdd:COG3845 142 LSVGEQQRVeilkALYR----GARILILDEPTAVLTPQEADELFEILRR-LAAegKSIIFITHK 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1220-1389 |
7.04e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.53 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1220 YTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTD-GEISIDGVNWNKMPLQKWRKAFGVVPQkvfift 1298
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGKTATRGDRSRFMAYLGHLPG------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1299 gpLRMNLDP----------YGCHSDEELWRVAEEVGL----KTVIEQfpdkldfqleyggyvLSNGHKQLICLARSILSG 1364
Cdd:PRK13543 93 --LKADLSTlenlhflcglHGRRAKQMPGSALAIVGLagyeDTLVRQ---------------LSAGQKKRLALARLWLSP 155
|
170 180
....*....|....*....|....*
gi 68390341 1365 ARILLLDEPSAHLDPVTIKVLKKTL 1389
Cdd:PRK13543 156 APLWLLDEPYANLDLEGITLVNRMI 180
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
440-578 |
7.05e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSLLMTILGELVPSSGKI----------RH----SGRISYssqtawiMP-G----- 499
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdmadaRHrravCPRIAY-------MPqGlgknl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 500 ----TIRDNI-----LFGLTYDE--YRYKSVVKACqleeDLAALPEKdktPMAegglNLSGGQKARVALARAVYRDADLY 568
Cdd:NF033858 90 yptlSVFENLdffgrLFGQDAAErrRRIDELLRAT----GLAPFADR---PAG----KLSGGMKQKLGLCCALIHDPDLL 158
|
170
....*....|
gi 68390341 569 LLDAPFTHLD 578
Cdd:NF033858 159 ILDEPTTGVD 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
436-587 |
7.43e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 436 VAPVLKDISLKLKKGEMLAVTGSMGSGKSSLLMTILgELVPS------SGKIRHSGR--ISYSSQTAWIMPGT------- 500
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSIL-RLLPSppvvypSGDIRFHGEslLHASEQTLRGVRGNkiamifq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 501 ---IRDNILFGLTYDEYRYKSVVKACQLE----EDLAALpEKDKTPMAEGGLN-----LSGGQKARVALARAVYRDADLY 568
Cdd:PRK15134 100 epmVSLNPLHTLEKQLYEVLSLHRGMRREaargEILNCL-DRVGIRQAAKRLTdyphqLSGGERQRVMIAMALLTRPELL 178
|
170
....*....|....*....
gi 68390341 569 LLDAPFTHLDIATEKEIFD 587
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQ 197
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
548-636 |
9.43e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 548 SGGQKARVALARAVYRDADLYLLDAPFTHLDIATEKEIfDKCLCKLmaSKTRILVTNKIEHLKR-ADKILLLHN------ 620
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ETYLLKW--PKTFIVVSHAREFLNTvVTDILHLHGqklvty 422
|
90
....*....|....*..
gi 68390341 621 -GEsffYGTFPELQSER 636
Cdd:PLN03073 423 kGD---YDTFERTREEQ 436
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
1242-1258 |
1.04e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 40.79 E-value: 1.04e-03
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
952-1093 |
1.50e-03 |
|
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: 42.41 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 952 ISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDMLPLLMFDFV------------------QLTVvvvgci 1013
Cdd:cd18552 70 VVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVrdpltvigllgvlfyldwKLTL------ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1014 lvvsivrpyIFLAATPLAIIFIV-----MRKYFLRTGQQLKQletearspIFSHLIMSLKGLWTIRAFERQAYFEALFHK 1088
Cdd:cd18552 144 ---------IALVVLPLAALPIRrigkrLRKISRRSQESMGD--------LTSVLQETLSGIRVVKAFGAEDYEIKRFRK 206
|
....*
gi 68390341 1089 TLNTH 1093
Cdd:cd18552 207 ANERL 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1219-1391 |
1.74e-03 |
|
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: 42.61 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1219 KYTEAGHAVLKNLSFSAEGRQRVGILGRTGSGKSSLfnalLKL---VYTD--GEISI-DGVNWNKMP----LQKWRKAFG 1288
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTL----LRImagVDKDfnGEARPqPGIKVGYLPqepqLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1289 VVPQKVfiftGPLRMNLDPYG------CHSDEELWRVAEEVG-LKTVIEQfPD--KLDFQLEYGG------------YVL 1347
Cdd:TIGR03719 88 NVEEGV----AEIKDALDRFNeisakyAEPDADFDKLAAEQAeLQEIIDA-ADawDLDSQLEIAMdalrcppwdadvTKL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68390341 1348 SNGHKQLICLARSILSGARILLLDEPSAHLDPVTIKVLKKTLRQ 1391
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE 206
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
454-616 |
2.21e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 454 AVTGSMGSGKSSLL----MTILGELVPSSGKIRHSGRISYSSQTAWIMPGTIRDNIlfGLTYDEYRYKSVVKA---CQLE 526
Cdd:cd03240 26 LIVGQNGAGKTTIIealkYALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENAN--GKKYTITRSLAILENvifCHQG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 527 EDLAALPEkdktpMAEgglNLSGGQKA------RVALARAVYRDADLYLLDAPFTHLDiateKEIFDKCLCKLMASKTR- 599
Cdd:cd03240 104 ESNWPLLD-----MRG---RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD----EENIEESLAEIIEERKSq 171
|
170 180
....*....|....*....|..
gi 68390341 600 -----ILVTNKIEHLKRADKIL 616
Cdd:cd03240 172 knfqlIVITHDEELVDAADHIY 193
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1231-1378 |
3.88e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.69 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1231 LSFSAEGRQRVGILGRTGSGKSSLFNALLKLVYTDGEISIDGVNWNKMPL-----------QKWRKAFgVVPqkVFIFtg 1299
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAaelarhraylsQQQTPPF-AMP--VFQY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1300 pLRMNLdPYGCHSDE---ELWRVAEEVGLKtvieqfpDKLDFQLEYggyvLSNGHKQLICLARSIL-------SGARILL 1369
Cdd:PRK03695 90 -LTLHQ-PDKTRTEAvasALNEVAEALGLD-------DKLGRSVNQ----LSGGEWQRVRLAAVVLqvwpdinPAGQLLL 156
|
....*....
gi 68390341 1370 LDEPSAHLD 1378
Cdd:PRK03695 157 LDEPMNSLD 165
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
1242-1260 |
4.50e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 39.54 E-value: 4.50e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
440-466 |
4.74e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 4.74e-03
10 20
....*....|....*....|....*..
gi 68390341 440 LKDISLKLKKGEMLAVTGSMGSGKSSL 466
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
952-1141 |
5.10e-03 |
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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: 40.83 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 952 ISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATIDDM----LPLLMFDFV--------------QLTVvvvgci 1013
Cdd:cd18544 72 IIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELftsgLVTLIGDLLlligiliamfllnwRLAL------ 145
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 1014 lvvsivrpyIFLAATPLAIIFIV-----MRKYFLRTGQQLkqletearSPIFSHLIMSLKGLWTIRAFERQAYFEALFHK 1088
Cdd:cd18544 146 ---------ISLLVLPLLLLATYlfrkkSRKAYREVREKL--------SRLNAFLQESISGMSVIQLFNREKREFEEFDE 208
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170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68390341 1089 TLNTHTATwflYLSTLRWF-LFRADILFVFFFTLAAWIAVGTNQ--DKPGEIGIII 1141
Cdd:cd18544 209 INQEYRKA---NLKSIKLFaLFRPLVELLSSLALALVLWYGGGQvlSGAVTLGVLY 261
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| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
862-991 |
5.13e-03 |
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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: 40.54 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 862 IFILFIAAIeIAGSVAGIFLI-----TDelwreehqrsepNMTKHSNASSSGQTYAITVTpTSSYYILYIYVATseslLA 936
Cdd:cd18577 1 LIIGLLAAI-AAGAALPLMTIvfgdlFD------------AFTDFGSGESSPDEFLDDVN-KYALYFVYLGIGS----FV 62
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 68390341 937 MGFFRGLPFVHTTITISKKLHQKMLHAVLSAPMSVLNTMKTGRIMNRFTKDMATI 991
Cdd:cd18577 63 LSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLI 117
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| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
87-324 |
7.15e-03 |
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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: 40.24 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 87 FLLYIGEATKTVQPQLLGRIIASFDPAHEPERANGYFLAFGLgllftarFLLLQPAMfglhhlgMQIRIALFSII-YKKT 165
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLA-------IYLLQSVF-------TFVRYYLFNIAgERIV 68
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 166 LKLSSRVL-----------DKISTGQLVSLMSANLGKFDQ--SLGMAHFIWiSPLQCILCTGLI----WELIDVnSFCAL 228
Cdd:cd18557 69 ARLRRDLFssllrqeiaffDKHKTGELTSRLSSDTSVLQSavTDNLSQLLR-NILQVIGGLIILfilsWKLTLV-LLLVI 146
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68390341 229 AAISLLGVLQAFLSHKMGPYKAQKVLLTNkrlALTSEIMENLHSVKAYGWEEIMETLIKNIRQDEVKLTRKIGSLRYFYS 308
Cdd:cd18557 147 PLLLIASKIYGRYIRKLSKEVQDALAKAG---QVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQ 223
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250
....*....|....*.
gi 68390341 309 SAYFFsAIFVIVAAVV 324
Cdd:cd18557 224 GITSL-LIYLSLLLVL 238
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