|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-1526 |
0e+00 |
|
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: 2947.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 7 SGELGSKFWDSNLSVHTENPDLTPCFQNSLLAWVPCIYLWVALPCYLLYLRHHCRGYIILSHLSKLKMVLGVLLWCVSWA 86
Cdd:TIGR00957 2 SADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCWA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 87 DLFYSFHGLVHGRAPAPVFFVTPLVVGVTMLLATLLIQYERLQGVQSSGVLIIFWFLCVVCAIVPFRSKILLAKAEGEIS 166
Cdd:TIGR00957 82 DLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 167 DPFRFTTFYIHFALVLSALILACFREKPPFFSAKNVDPNPYPETSAGFLSRLFFWWFTKMAIYGYRHPLEEKDLWSLKEE 246
Cdd:TIGR00957 162 DPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 247 DRSQMVVQQLLEAWRKQEKQTARHKASAAPGK------------NASGEDEVLLGARP-RPRKPSFLKALLATFGSSFLI 313
Cdd:TIGR00957 242 DTSEMVVPVLVENWKKECKKTRKQPVSAVYGKkdpskpkgssqlDANEEVEALIVKSPhKPRKPSLFKVLYKTFGPYFLM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 314 SACFKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYRKA 393
Cdd:TIGR00957 322 SFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 394 LVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAVKM 473
Cdd:TIGR00957 402 LVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKT 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 474 RAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITLWV 553
Cdd:TIGR00957 482 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 554 YVYVDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRIQQFLSQEELDPQSVERKTISPG--YAITIHS 631
Cdd:TIGR00957 562 YVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGegNSITVHN 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 632 GTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLF 711
Cdd:TIGR00957 642 ATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILF 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 GKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFD 791
Cdd:TIGR00957 722 GKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 792 HVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFANFLCNYAPDEDQGHLEDSWTALEGA 871
Cdd:TIGR00957 802 HVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALVSG 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 872 EDKEALLIEDTLSnhtdltdndpVTYVVQKQFMRQLSALSSDGEGQGRpvprrHLGPSEKVQVTEAK-ADGALTQEEKAA 950
Cdd:TIGR00957 882 EGKEAKLIENGML----------VTDVVGKQLQRQLSASSSDSGDQSR-----HHGSSAELQKAEAKeETWKLMEADKAQ 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 951 IGTVELSVFWDYAKAVGLCTTLAICLLYVGQSAAAIGANVWLSAWTNDAMADSRQNNTSLRLGVYAALGILQGFLVMLAA 1030
Cdd:TIGR00957 947 TGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYS 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1031 MAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPL 1110
Cdd:TIGR00957 1027 MAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPI 1106
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1111 FTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYII 1190
Cdd:TIGR00957 1107 AAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIV 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1191 SNRWLSIGVEFVGNCVVLFAALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEA 1270
Cdd:TIGR00957 1187 ANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEA 1266
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1271 PWVVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRID 1350
Cdd:TIGR00957 1267 PWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID 1346
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1351 GLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQ 1430
Cdd:TIGR00957 1347 GLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQ 1426
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1431 RQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANL 1510
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
1530
....*....|....*.
gi 9955970 1511 IAARGIFYGMARDAGL 1526
Cdd:TIGR00957 1507 LQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
208-1527 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1020.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 208 PETSAGFLSRLFFWWFTKMAIYGYRHPLEEKDLWSLKEEDRSQMVVQQLLEAWRKQEKqtarhkasaapgknasgedevl 287
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELK---------------------- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 288 lgaRPRPRkpsFLKALLATFGSSFLISACFKLIQDLLSFINPQLLSILIRFISNPmAPSWWGFLVAGLMFLCSMMQSLIL 367
Cdd:PLN03130 286 ---KPKPW---LLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNG-EPAWIGYIYAFSIFVGVVLGVLCE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 368 QHYYHYIFVTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQN 447
Cdd:PLN03130 359 AQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 448 LGPSVLAGVAFMVLLIPLNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRT 527
Cdd:PLN03130 439 LGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 528 AAYLHTTTTFTWMCSPFLVTLITLWVYVYVdpNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRIQQFLS 607
Cdd:PLN03130 519 AQLLSAFNSFILNSIPVLVTVVSFGVFTLL--GGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLL 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 608 QEE--LDPQSverkTISPGY-AITIHSGTFTWAQDLP-PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLE- 682
Cdd:PLN03130 597 AEErvLLPNP----PLEPGLpAISIKNGYFSWDSKAErPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSd 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 683 GKVHMKGSVAYVPQQAWIQNCTLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLA 762
Cdd:PLN03130 673 ASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 763 RAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRN 842
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDE--LRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNG 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 843 GSFANFLcnyapdEDQGHLEDSwtalegaedkeallIEDTLSNHTDLTDNDPVTyvvqkqfmrqlsalssdgEGQGRPVP 922
Cdd:PLN03130 831 PLFQKLM------ENAGKMEEY--------------VEENGEEEDDQTSSKPVA------------------NGNANNLK 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 923 RRhlgPSEKVQVTEAKAdgALTQEEKAAIGTVELSVFWDYAKAVGLCTTLAICLL-YVGQSAAAIGANVWLSAWTNDAMa 1001
Cdd:PLN03130 873 KD---SSSKKKSKEGKS--VLIKQEERETGVVSWKVLERYKNALGGAWVVMILFLcYVLTEVFRVSSSTWLSEWTDQGT- 946
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1002 dSRQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDE 1081
Cdd:PLN03130 947 -PKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDR 1025
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1082 VLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVI 1161
Cdd:PLN03130 1026 NVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTI 1105
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1162 RAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVLFAALFAVIGRS-SLNP----GLVGLSVSYSLQV 1236
Cdd:PLN03130 1106 RAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGrAENQaafaSTMGLLLSYALNI 1185
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1237 TFALNWMIRMMSDLESNIVAVERVKEYSKTETEAPWVVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGG 1316
Cdd:PLN03130 1186 TSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPS 1265
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1317 EKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIW 1396
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLW 1345
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1397 WALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCT 1476
Cdd:PLN03130 1346 ESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCT 1425
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1477 VLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIA-ARGIFYGMARDAGLA 1527
Cdd:PLN03130 1426 MLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSnEGSAFSKMVQSTGAA 1477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
208-1527 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 971.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 208 PETSAGFLSRLFFWWFTKMAIYGYRHPLEEKDLWSLKEEDRSQMVVQQLLEAWRKQEKqtarhkasaapgknasgedevl 287
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESR---------------------- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 288 lgarpRPrKPSFLKALLATFGSSFLISACFKLIQDLLSFINPQLLSILIRFISNPmAPSWWGFLVAGLMFLCSMMQSLIL 367
Cdd:PLN03232 286 -----RP-KPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEG-DPAWVGYVYAFLIFFGVTFGVLCE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 368 QHYYHYIFVTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQN 447
Cdd:PLN03232 359 SQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 448 LGPSVLAGVAFMVLLIPLNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRT 527
Cdd:PLN03232 439 LGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 528 AAYLHTTTTFTWMCSPFLVTLITLWVYVYVDPNnvLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRIQQ-FL 606
Cdd:PLN03232 519 AQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEElLL 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 607 SQEELDPQSverKTISPGY-AITIHSGTFTWAQDLP-PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLE-G 683
Cdd:PLN03232 597 SEERILAQN---PPLQPGApAISIKNGYFSWDSKTSkPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtS 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 684 KVHMKGSVAYVPQQAWIQNCTLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLAR 763
Cdd:PLN03232 674 SVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMAR 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 764 AVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYpALLQRNG 843
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTF-AELSKSG 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 844 SFANFLcnyapdedqghledswtaLEGAEDKEALLIEDTLSNHTDltdndpvtyvvqkqfmrqlsalssdgegqgrpvpr 923
Cdd:PLN03232 831 SLFKKL------------------MENAGKMDATQEVNTNDENIL----------------------------------- 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 924 rHLGPSEKVQVTEAKADGA---------LTQEEKAAIGTVELSVFWDYAKAVGLCTTLAICLL-YVGQSAAAIGANVWLS 993
Cdd:PLN03232 858 -KLGPTVTIDVSERNLGSTkqgkrgrsvLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVcYLTTEVLRVSSSTWLS 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 994 AWTNDAMADSRQnnTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFS 1073
Cdd:PLN03232 937 IWTDQSTPKSYS--PGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFS 1014
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1074 KDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSE 1153
Cdd:PLN03232 1015 KDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGE 1094
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1154 TVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVLFAALFAVIGRSSLN-----PGLVGL 1228
Cdd:PLN03232 1095 ALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGL 1174
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1229 SVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEAPWVVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDLVLRD 1308
Cdd:PLN03232 1175 LLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHG 1254
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1309 LSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFG 1388
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS 1334
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1389 SYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATI 1468
Cdd:PLN03232 1335 EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI 1414
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1469 RTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARG-IFYGMARDAGLA 1527
Cdd:PLN03232 1415 REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTGPA 1474
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
292-1520 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 818.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 292 PRPRKPSFLKALLATFGSSFLISACFKLIQDLLSFINPQLLSILIRFISNPMApSW-WGFLVAGLMFLCSMMQSLILQHY 370
Cdd:PTZ00243 227 PTPKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNA-TWgRGLGLVLTLFLTQLIQSVCLHRF 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 371 YHYIFVTGVKFRTGIMGVIYRKALVITN-SVKRAS-TVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNL 448
Cdd:PTZ00243 306 YYISIRCGLQYRSALNALIFEKCFTISSkSLAQPDmNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLV 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 449 GPSVLAGVAFMVLLIPLNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTA 528
Cdd:PTZ00243 386 GWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDV 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 529 AYLHTTTTFTWMCSPFLVtlITLWVYVYVDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRIQQFL-- 606
Cdd:PTZ00243 466 QLARVATSFVNNATPTLM--IAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLec 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 --------------------------------------------------------------------------------
Cdd:PTZ00243 544 dnatcstvqdmeeywreqrehstacqlaavlenvdvtafvpvklprapkvktsllsralrmlcceqcrptkrhpspsvvv 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 607 -SQEELDPQSVERKTISPGY-------------AITIHSGTFTWAQDLPPTL-HSLDIQVPKGALVAVVGPVGCGKSSLV 671
Cdd:PTZ00243 624 eDTDYGSPSSASRHIVEGGTgggheatptsersAKTPKMKTDDFFELEPKVLlRDVSVSVPRGKLTVVLGATGSGKSTLL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 672 SALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINL 751
Cdd:PTZ00243 704 QSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 752 SGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIgpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVse 831
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRV-- 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 832 mgpypallQRNGSFANFLCNYAPDEDQGHLEDSWTALEGAEDKEALLIEdtlsnhtdltdndpvtyvvqkqfmrqlsALS 911
Cdd:PTZ00243 860 --------EFSGSSADFMRTSLYATLAAELKENKDSKEGDADAEVAEVD----------------------------AAP 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 912 SDGEGQGRPVPRRHLGPSEKVQVTEAKADGALTQEEKAAIGTVELSVFWDYAKAVG-LCTTLAICLLYVGQSAAAIGANV 990
Cdd:PTZ00243 904 GGAVDHEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGgLHAAGFVLATFAVTELVTVSSGV 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 991 WLSAWTndamADSRQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILN 1070
Cdd:PTZ00243 984 WLSMWS----TRSFKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILN 1059
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1071 CFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSH 1150
Cdd:PTZ00243 1060 RFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTL 1139
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1151 FSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVLFAALFAVIGR----SSLNPGLV 1226
Cdd:PTZ00243 1140 LEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTmlraTSQEIGLV 1219
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1227 GLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYS--------------------KTETEAP----WVVEGSRPPEG 1282
Cdd:PTZ00243 1220 SLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdevphedmpeldeevdalerRTGMAADvtgtVVIEPASPTSA 1299
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1283 WP---PRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGL 1359
Cdd:PTZ00243 1300 APhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGL 1379
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1360 HDLRSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARA 1439
Cdd:PTZ00243 1380 RELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1440 LLRK-SRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAAR-GIF 1517
Cdd:PTZ00243 1460 LLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRqSIF 1539
|
...
gi 9955970 1518 YGM 1520
Cdd:PTZ00243 1540 HSM 1542
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
208-1517 |
4.07e-169 |
|
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: 549.13 E-value: 4.07e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 208 PETSAGFLSRLFFWWFTKMAIYGYRHPLEEKDLWSLKEEDRSQMVVQQLLEAWRkqekqtaRHKASAApgknasgedevl 287
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWD-------RELASAK------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 288 lgarprpRKPSFLKALLATFGSSFLISACFKLIQDLLSFINPQLLSILIRFISNPMAP--SWWGFLVAGLMFLCsMMQSL 365
Cdd:TIGR01271 66 -------KNPKLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPerEIAYYLALGLCLLF-IVRTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 366 ILQHYYHYIFVTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLW 445
Cdd:TIGR01271 138 LLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIW 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 446 QNLGPSVLAGVAFMVLLIPLNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLL 525
Cdd:TIGR01271 218 ELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 526 RTAAYLHTTTTFTWMCSPFLVTLITLWVYVYVdpnNVLDAEKAFVSVSLFNILRLPLN-MLPQLISNLTQASVSLKRIQQ 604
Cdd:TIGR01271 298 RKIAYLRYFYSSAFFFSGFFVVFLSVVPYALI---KGIILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 605 FLSQEE-------LDPQSVERKTISPGYAITI-------------------HSGTF--TWAQDLPPTLHSLDIQVPKGAL 656
Cdd:TIGR01271 375 FLCKEEyktleynLTTTEVEMVNVTASWDEGIgelfekikqnnkarkqpngDDGLFfsNFSLYVTPVLKNISFKLEKGQL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 657 VAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLFGKALNPKRYQQTLEACALLADLEML 736
Cdd:TIGR01271 455 LAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 737 PGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGPegVLAGKTRVLVTHGISFLP 816
Cdd:TIGR01271 535 PEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKTRILVTSKLEHLK 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 817 QTDFIIVLADGQVSEMGPYPAL----------LQRNGSFANF-------------------------------------- 848
Cdd:TIGR01271 613 KADKILLLHEGVCYFYGTFSELqakrpdfsslLLGLEAFDNFsaerrnsiltetlrrvsidgdstvfsgpetikqsfkqp 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 849 ------------------------LCNYAPDEDQGHLEDSWTAlEGAEDKEALLIEDTLSNHT----DLTDNDPVTYVVQ 900
Cdd:TIGR01271 693 ppefaekrkqsiilnpiasarkfsFVQMGPQKAQATTIEDAVR-EPSERKFSLVPEDEQGEESlprgNQYHHGLQHQAQR 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 901 KQFMRQLSALSSDGEGQGRPVPRRHLGPSEKVQVTEAKADGALTQEEKAAIGTVELS----------VFWDYAKAVGLCT 970
Cdd:TIGR01271 772 RQSVLQLMTHSNRGENRREQLQTSFRKKSSITQQNELASELDIYSRRLSKDSVYEISeeineedlkeCFADERENVFETT 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 971 T-----------------LAICLLYVGQSAAAIGANVWLSAWTNDAMADSRQN----------------NTSLRLGVYAA 1017
Cdd:TIGR01271 852 TwntylryittnrnlvfvLIFCLVIFLAEVAASLLGLWLITDNPSAPNYVDQQhanasspdvqkpviitPTSAYYIFYIY 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1018 LGILQGFLVM--LAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFF 1095
Cdd:TIGR01271 932 VGTADSVLALgfFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTL 1011
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1096 NAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISD 1175
Cdd:TIGR01271 1012 IVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFH 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1176 TKVDANQRSCYPYIISNRWLSIGVEFVgncVVLF--AALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESN 1253
Cdd:TIGR01271 1092 KALNLHTANWFLYLSTLRWFQMRIDII---FVFFfiAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGL 1168
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1254 IVAVERVKEYSKTETEAP--------------WVVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKV 1319
Cdd:TIGR01271 1169 MRSVSRVFKFIDLPQEEPrpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRV 1248
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1320 GIVGRTGAGKSSMTLCLFRILeAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWAL 1399
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVA 1327
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1400 ELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLT 1479
Cdd:TIGR01271 1328 EEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL 1407
|
1450 1460 1470
....*....|....*....|....*....|....*...
gi 9955970 1480 IAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIF 1517
Cdd:TIGR01271 1408 SEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
313-602 |
5.01e-164 |
|
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: 495.45 E-value: 5.01e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 313 ISACFKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYRK 392
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 393 ALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAVK 472
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 473 MRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITLW 552
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 9955970 553 VYVYVDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd18595 241 TYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
971-1264 |
1.55e-157 |
|
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: 478.51 E-value: 1.55e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 971 TLAICLLYVGQSAAAIGANVWLSAWTNDAMADSRQNNTS--LRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQAL 1048
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQrdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1049 LHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRF 1128
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1129 YAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVL 1208
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 1209 FAALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYS 1264
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1287-1507 |
4.40e-134 |
|
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: 413.04 E-value: 4.40e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1287 GEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQL 1366
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRI 1446
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1447 LVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSP 1507
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
956-1522 |
1.45e-119 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 387.60 E-value: 1.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 956 LSVFWDYAKAVGLCTTLAICllyvgqSAAAIGANVWLSAWTNDAMADSRQNNTSLRL-GVYAALGILQGFLVMLAAMAMA 1034
Cdd:COG1132 13 LRYLRPYRGLLILALLLLLL------SALLELLLPLLLGRIIDALLAGGDLSALLLLlLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1035 AGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVV 1114
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1115 ILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRW 1194
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1195 LSIGVEFVGNCVVLFAALFAV--IGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEapw 1272
Cdd:COG1132 247 FFPLMELLGNLGLALVLLVGGllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE--- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1273 VVEGSRPPEGWPPRGEVEFRNYSVRYRPGlDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGL 1352
Cdd:COG1132 324 IPDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1353 NVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFG--SYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQ 1430
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGrpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1431 RQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANL 1510
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|..
gi 9955970 1511 IAARGIFYGMAR 1522
Cdd:COG1132 562 LARGGLYARLYR 573
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
313-602 |
9.12e-116 |
|
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: 366.04 E-value: 9.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 313 ISACFKLIQDLLSFINPQLLSILIRFISN-PMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYR 391
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 392 KALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAV 471
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 472 KMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITL 551
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 552 WVYVYVDpnNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd18579 241 ATYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
627-828 |
1.96e-114 |
|
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: 358.71 E-value: 1.96e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTW---AQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNC 703
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 704 TLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS 783
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9955970 784 HVAKHIFDHVIGPEGvLAGKTRVLVTHGISFLPQTDFIIVLADGQ 828
Cdd:cd03250 161 HVGRHIFENCILGLL-LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
972-1264 |
2.25e-101 |
|
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: 326.38 E-value: 2.25e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 972 LAICLLYVGQSAAAIGANVWLSAWTnDAMADSRQNNTSLRLGVYAALGIL-QGFLVMLAAMAMAAGGIQAARVLHQALLH 1050
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWS-SDWSSSPNSSSGYYLGVYAALLVLaSVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1051 NKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYA 1130
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1131 ATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVLFA 1210
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1211 ALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYS 1264
Cdd:cd18580 241 ALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1283-1507 |
7.13e-100 |
|
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: 318.59 E-value: 7.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1283 WPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDL 1362
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1363 RSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELshlhtfvssqpagldfqcSEGGENLSVGQRQLVCLARALLR 1442
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1443 KSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSP 1507
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
971-1264 |
5.60e-92 |
|
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: 299.78 E-value: 5.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 971 TLAICLLYVGQsAAAIGANVWLSAWTndamADSRQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLH 1050
Cdd:cd18606 2 PLLLLLLILSQ-FAQVFTNLWLSFWT----EDFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1051 NKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYA 1130
Cdd:cd18606 77 RVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1131 ATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVLFA 1210
Cdd:cd18606 157 ASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1211 ALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYS 1264
Cdd:cd18606 237 ALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1053-1522 |
7.69e-91 |
|
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: 311.38 E-value: 7.69e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1053 IRSPQSFFDTTPSGRILNCFSkDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAAT 1132
Cdd:COG2274 240 LRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPR 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1133 SRQLKRLESVSRSPIYSHFSETVTGASVIRAYN----RSRDFEIISDTKVDANQRScypYIISNR--WLSIGVEFVGNCV 1206
Cdd:COG2274 319 LRRLSREESEASAKRQSLLVETLRGIETIKALGaesrFRRRWENLLAKYLNARFKL---RRLSNLlsTLSGLLQQLATVA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1207 VLFAALFAVIGRSsLNPG-LVGlSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEAPWVVEGSRPPEgwpP 1285
Cdd:COG2274 396 LLWLGAYLVIDGQ-LTLGqLIA-FNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR---L 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1286 RGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQ 1365
Cdd:COG2274 471 KGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQDPILFSGTLRMNL---DPfgSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLR 1442
Cdd:COG2274 551 IGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1443 KSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGMAR 1522
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
313-602 |
3.17e-85 |
|
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: 281.31 E-value: 3.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 313 ISACFKLIQDLLSFINPQLLSILIRFISNPMAPS-WWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYR 391
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDPGEDAtVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 392 KALVI-------------------TNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSV 452
Cdd:cd18596 81 KALRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 453 LAGVAFMVLLIPLNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLH 532
Cdd:cd18596 161 LVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 533 TTTTFTWMCSPFLVTLITLWVYVYVDpNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd18596 241 LLLSLLWFLIPILVTVVTFATYTLVM-GQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
317-602 |
1.61e-84 |
|
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: 278.71 E-value: 1.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 317 FKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYRKALVI 396
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 397 TNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAVKMRAF 476
Cdd:cd18559 85 PISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 477 QVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITLWVYVY 556
Cdd:cd18559 165 KRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVS 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 9955970 557 VDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd18559 245 RHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
972-1264 |
3.04e-84 |
|
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: 278.20 E-value: 3.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 972 LAICLLYVGQSAAAIGANVWLSAWTN----DAMADSRQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQA 1047
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASayetSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1048 LLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQR 1127
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1128 FYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVV 1207
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 1208 LFAALFAVIGRsSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYS 1264
Cdd:cd18604 242 FATAALLVYGP-GIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
971-1264 |
8.49e-81 |
|
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: 268.70 E-value: 8.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 971 TLAICLLYVGQSAAAIGANVWLSAWT-----------NDAMADSRQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQ 1039
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTeanhdvasvvfNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1040 AARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLA 1119
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1120 VLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQrSCYPYI-ISNRWLSIG 1198
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNN-TAFLFLnTANRWLGIR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1199 VEFVGNCVVLFAALFAVIG--RSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYS 1264
Cdd:cd18602 240 LDYLGAVIVFLAALSSLTAalAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1287-1522 |
6.53e-79 |
|
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: 261.38 E-value: 6.53e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1287 GEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQL 1366
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRI 1446
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 1447 LVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAAR-GIFYGMAR 1522
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVR 254
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
313-602 |
4.68e-78 |
|
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: 260.08 E-value: 4.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 313 ISACFKLIQDLLSFINPQLLSILIRFISN-----PMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMG 387
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDaylggPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 388 VIYRKALVITNSVKRASTVGEIVNLMSVDAQRfMDLA-PFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLN 466
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSR-IDFAlGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 467 GAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLV 546
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 547 TLITLWVYVYVdpNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd18597 240 SMLSFITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
317-602 |
7.18e-77 |
|
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: 256.71 E-value: 7.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 317 FKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYRKALVI 396
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKALRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 397 TNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAVKMRAF 476
Cdd:cd18598 85 RSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIGAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 477 QVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITLWVYVY 556
Cdd:cd18598 165 SEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATYVL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 9955970 557 VdpNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd18598 245 M--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
971-1263 |
6.05e-74 |
|
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: 248.60 E-value: 6.05e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 971 TLAICLLYVGQSAAAIGANVWLSAWTNDAmADSRQNNTSLR----LGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQ 1046
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHS-NNSFFNFINDSfnffLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1047 ALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLaPVILM-LLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLV 1125
Cdd:cd18605 80 KLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSL-PFILNiLLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1126 QRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNC 1205
Cdd:cd18605 159 QRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1206 VVLFAALFAVIGRS---SLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEY 1263
Cdd:cd18605 239 IVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
313-602 |
5.29e-73 |
|
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: 246.38 E-value: 5.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 313 ISACFKLIQDLLSFINPQLLSILIRFISNPMAPSWW------------------GFLVAGLMFLCSMMQSLILQHYYHYI 374
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 375 FVTGVKFRTGIMGVIYRKALVIT--NSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSV 452
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 453 LAGVAFMVLLIPLNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLH 532
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 533 TTTTFTWMCSPFLVTLITLWVYVYVDpNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYPYLE-GEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
982-1515 |
2.19e-72 |
|
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: 253.53 E-value: 2.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 982 SAAAIGANVWLSAWTNDAMADSRQNNTSLR--LGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSF 1059
Cdd:COG4988 29 SGLLIIAQAWLLASLLAGLIIGGAPLSALLplLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1060 FDTTPSGRILNCFSK-----DIY-------VVDEVLAPVILMLLNSFFNAISTLVVimastpLFTVVILPLAVLytLVQR 1127
Cdd:COG4988 109 LRGKSTGELATLLTEgvealDGYfarylpqLFLAALVPLLILVAVFPLDWLSGLIL------LVTAPLIPLFMI--LVGK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1128 FYA-ATSRQLKRLESVSrspiySHFSETVTGASVIRAYNRSRD----FEIISDtkvdanqrscypyiiSNR--------- 1193
Cdd:COG4988 181 GAAkASRRQWRALARLS-----GHFLDRLRGLTTLKLFGRAKAeaerIAEASE---------------DFRkrtmkvlrv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1194 -WLSIGV-EFVgncVVLFAALFAV-IGRSSLNPGLvglsvsySLQVTFAL----------------NWMIRMMsdlesNI 1254
Cdd:COG4988 241 aFLSSAVlEFF---ASLSIALVAVyIGFRLLGGSL-------TLFAALFVlllapefflplrdlgsFYHARAN-----GI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1255 VAVERVKEYSktETEAPWVVEGSRPPEgWPPRGEVEFRNYSVRYrPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTL 1334
Cdd:COG4988 306 AAAEKIFALL--DAPEPAAPAGTAPLP-AAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1335 CLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGS--YSEEDIWWALELSHLHTFVSSQP 1412
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR-LGRpdASDEELEAALEAAGLDEFVAALP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1413 AGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTR 1492
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADR 540
|
570 580
....*....|....*....|...
gi 9955970 1493 VLVLDKGVVAEFDSPANLIAARG 1515
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1287-1515 |
7.74e-72 |
|
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: 239.82 E-value: 7.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1287 GEVEFRNYSVRYRPGlDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQL 1366
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSGTLRMNLDPFGSYS-EEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSR 1445
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1446 ILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARG 1515
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
299-848 |
1.00e-69 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 246.23 E-value: 1.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 299 FLKALLATFGSSFLISACFKLIQDLLSFINPQLLSILIRFISNPMAPS---WWGFLVAGLMFLCSMMQslILQHYYhyIF 375
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSallLLLLLLLGLALLRALLS--YLQRYL--LA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 376 VTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRFMD-LAPFLNLLWSAPLQIILAIYFL----WQnLGP 450
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLfvidWR-LAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 451 SVLAGVAFMVLLIPLNGAvavKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAY 530
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGR---RLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 531 LHTTTTFTWMCSPFLVTLITLWVYVYVDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRIQQFLSQEE 610
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 611 LDPQSVERKTISP-GYAITIHSGTFTWAQDlPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG 689
Cdd:COG1132 323 EIPDPPGAVPLPPvRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 690 -------------SVAYVPQQAWIQNCTLQENVLFGKalnPKRYQQTLEACALLADL----EMLPGGDQTEIGEKGINLS 752
Cdd:COG1132 402 vdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGR---PDATDEEVEEAAKAAQAhefiEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 753 GGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEM 832
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
570
....*....|....*.
gi 9955970 833 GPYPALLQRNGSFANF 848
Cdd:COG1132 556 GTHEELLARGGLYARL 571
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
627-827 |
1.07e-67 |
|
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: 227.60 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLPpTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHM-----------------KG 689
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesepsfeatrsrnRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 690 SVAYVPQQAWIQNCTLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDA 769
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 770 DIFLLDDPLSAVDSHVAKHIFDhvigpEGVLA-----GKTRVLVTHGISFLPQTDFIIVLADG 827
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
307-602 |
4.98e-67 |
|
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: 228.26 E-value: 4.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 307 FGSSFLISACFKLIQdllsfinPQLLSILIRFISNPMAP--SWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTG 384
Cdd:cd18593 2 LGIFLFLEEAIRVVQ-------PIFLGKLIRYFEGNGSSisLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 385 IMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIP 464
Cdd:cd18593 75 CSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 465 LNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPF 544
Cdd:cd18593 155 LQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 545 LVTLITLWVYVYVDpnNVLDAEKAFVSVSLFNILRLPLNM-LPQLISNLTQASVSLKRI 602
Cdd:cd18593 235 LILFLTFLAYILLG--NILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
967-1264 |
7.21e-67 |
|
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: 228.99 E-value: 7.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 967 GLCTTLAICLLYVGQSAAAIGANVWLSAWTND---AMADSRQNNTSLR------------LGVYAALGILQGFLVMLAAM 1031
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQgsgNTTNNVDNSTVDSgnisdnpdlnfyQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1032 AMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLF 1111
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1112 TVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIIS 1191
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1192 NRWLSIGVEFVGNCVVLFAALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYS 1264
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1065-1522 |
2.81e-66 |
|
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: 235.82 E-value: 2.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1065 SGRILNCFSKDIYVVDE----VLAP--------VILMLLNSFFNAisTLVVIMASTPLFTVVILPLavlytLVQRFYAAT 1132
Cdd:COG4987 111 SGDLLNRLVADVDALDNlylrVLLPllvallviLAAVAFLAFFSP--ALALVLALGLLLAGLLLPL-----LAARLGRRA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1133 SRQLKRLesvsRSPIYSHFSETVTGASVIRAYNRSRDFEI---ISDTKVDANQRScypyiisNRWLSIGVEFVGNCVVLF 1209
Cdd:COG4987 184 GRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALArldAAEARLAAAQRR-------LARLSALAQALLQLAAGL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1210 AALFAVI------GRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEAPWVVEGSRPPEGw 1283
Cdd:COG4987 253 AVVAVLWlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGG- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1284 pprGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLR 1363
Cdd:COG4987 332 ---PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 SQLTIIPQDPILFSGTLRMNL---DPfgSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARAL 1440
Cdd:COG4987 409 RRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARAL 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1441 LRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGM 1520
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
..
gi 9955970 1521 AR 1522
Cdd:COG4987 567 YQ 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1041-1517 |
5.01e-66 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 235.00 E-value: 5.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1041 ARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAV 1120
Cdd:TIGR02203 86 VRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1121 LYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYN----RSRDFEIISDTKVDANQRSCYPYIISNRWLS 1196
Cdd:TIGR02203 166 VLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGgqayETRRFDAVSNRNRRLAMKMTSAGSISSPITQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1197 IgVEFVGNCVVLFAALFAViGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEAPwvvEG 1276
Cdd:TIGR02203 246 L-IASLALAVVLFIALFQA-QAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD---TG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1277 SRPPEgwPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAD 1356
Cdd:TIGR02203 321 TRAIE--RARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1357 IGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQL 1433
Cdd:TIGR02203 399 YTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQR 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1434 VCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAA 1513
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
....
gi 9955970 1514 RGIF 1517
Cdd:TIGR02203 558 NGLY 561
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
317-603 |
9.69e-65 |
|
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: 221.74 E-value: 9.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 317 FKLIQDLLSFINPQLLSILIR-FISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYRKALV 395
Cdd:cd18594 5 LLFLEESLKIVQPLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 396 ITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAVKMRA 475
Cdd:cd18594 85 LSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 476 FQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITLWVYV 555
Cdd:cd18594 165 YRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 9955970 556 YVdpNNVLDAEKAFVSVSLFNILRLPLNM-LPQLISNLTQASVSLKRIQ 603
Cdd:cd18594 245 LT--GNTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1289-1520 |
1.25e-64 |
|
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: 219.41 E-value: 1.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSGTLRMNLdPFGSY--SEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRI 1446
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1447 LVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGM 1520
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1289-1499 |
1.50e-63 |
|
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: 213.40 E-value: 1.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSGTLRMNLdpfgsyseediwwalelshlhtfvssqpagldfqcseggenLSVGQRQLVCLARALLRKSRILV 1448
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1449 LDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKG 1499
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
293-848 |
2.30e-63 |
|
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: 230.88 E-value: 2.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 293 RPRKPSFLKALLAtfgsSFLISacfkliqdLLSFINPQLLSILI-RFISNPMAPSWW----GFLVAGLM-FLCSMMQSLI 366
Cdd:COG2274 152 RRYRRLLLQVLLA----SLLIN--------LLALATPLFTQVVIdRVLPNQDLSTLWvlaiGLLLALLFeGLLRLLRSYL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 367 LQHyyhyifvTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNlmsvdaqRFMDLAPFLNLLWSAPLQIILAIyflwq 446
Cdd:COG2274 220 LLR-------LGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-------RFRDVESIREFLTGSLLTALLDL----- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 447 nlgPSVLAGVAFM-----------VLLIPLNGAVAV----KMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFL 511
Cdd:COG2274 281 ---LFVLIFLIVLffyspplalvvLLLIPLYVLLGLlfqpRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 512 KQVEGI----RQGELQLLRTAAYLHTTTTFTwmcsPFLVTLITLWVYVYVdpnnVLDAE---KAFVSvslFNILRL---- 580
Cdd:COG2274 358 RRWENLlakyLNARFKLRRLSNLLSTLSGLL----QQLATVALLWLGAYL----VIDGQltlGQLIA---FNILSGrfla 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 581 PLNMLPQLISNLTQASVSLKRIQQFLSQE---ELDPQSVERKTISPgyAITIHSGTFTWAQDLPPTLHSLDIQVPKGALV 657
Cdd:COG2274 427 PVAQLIGLLQRFQDAKIALERLDDILDLPperEEGRSKLSLPRLKG--DIELENVSFRYPGDSPPVLDNISLTIKPGERV 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 658 AVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENVLFGKA-LNPKRYQQT 723
Cdd:COG2274 505 AIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPdATDEEIIEA 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 724 LEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVigpEGVLAGK 803
Cdd:COG2274 585 ARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGR 661
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 9955970 804 TRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFANF 848
Cdd:COG2274 662 TVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1289-1520 |
3.32e-60 |
|
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: 206.70 E-value: 3.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSGTLRMNLDpFG--SYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRI 1446
Cdd:cd03253 80 VPQDTVLFNDTIGYNIR-YGrpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1447 LVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGM 1520
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
984-1264 |
3.73e-59 |
|
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: 205.91 E-value: 3.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 984 AAIGANVWLSAWTNDAmADSRQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTT 1063
Cdd:cd18559 14 FSGPSNLWLLLWFDDP-VNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1064 PSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFtVVILPLAVLYTLVQRFYAATSRQLKRLESVS 1143
Cdd:cd18559 93 PSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMA-AVGIPLGLLYVPVNRVYAASSRQLKRLESVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1144 RSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDaNQRSCYPYIISNRWLSIGVEFVGNCVVLFAALFAVIGRSSLNp 1223
Cdd:cd18559 172 KDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLA- 249
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 9955970 1224 GLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYS 1264
Cdd:cd18559 250 GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1286-1520 |
9.73e-57 |
|
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: 208.52 E-value: 9.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1286 RGEVEFRNYSVRYRPGlDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQ 1365
Cdd:COG5265 355 GGEVRFENVSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQDPILFSGTLRMNLdpfgSY-----SEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARAL 1440
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1441 LRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGM 1520
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1289-1522 |
1.00e-56 |
|
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: 196.61 E-value: 1.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRY--RPGLdLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQL 1366
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSGTLRMNLDpFGSYS--EEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKS 1444
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIR-YGKPDatDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1445 RILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGMAR 1522
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1287-1517 |
5.19e-56 |
|
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: 196.23 E-value: 5.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1287 GEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAaKGEIRIDGLNVADIGLHDLRSQL 1366
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRI 1446
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1447 LVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIF 1517
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
423-849 |
1.22e-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: 201.53 E-value: 1.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 423 LAPFLNLLWSAPLqIILAIYFLWQNLGPSVLAGVAFMVLLIPLngAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLK 502
Cdd:COG4987 133 LLPLLVALLVILA-AVAFLAFFSPALALVLALGLLLAGLLLPL--LAARLGRRAGRRLAAARAALRARLTDLLQGAAELA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 503 LYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITLWVYVYVDPNNVLDAEK----AFVSVSLFNIL 578
Cdd:COG4987 210 AYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLlallVLAALALFEAL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 579 rlplNMLPQLISNLTQASVSLKRIQQFLSQEELDPQSVERKTISPGYAITIHSGTFTWAQDLPPTLHSLDIQVPKGALVA 658
Cdd:COG4987 290 ----APLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 659 VVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENVLFGK-ALNPKRYQQTL 724
Cdd:COG4987 366 IVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARpDATDEELWAAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 725 EACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIgpeGVLAGKT 804
Cdd:COG4987 446 ERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAGRT 522
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 9955970 805 RVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFANFL 849
Cdd:COG4987 523 VLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1287-1502 |
1.35e-54 |
|
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: 190.11 E-value: 1.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1287 GEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQL 1366
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSGTLRMNL---DPFGsySEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRK 1443
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1444 SRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKG-VVA 1502
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGrIVA 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1289-1518 |
1.24e-53 |
|
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: 187.69 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSGTLRMNL---DPfgSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSR 1445
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1446 ILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFY 1518
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
313-602 |
8.73e-53 |
|
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: 187.38 E-value: 8.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 313 ISACFKLIQDLLSFINPQ-LLSILIRFISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYR 391
Cdd:cd18592 1 FSILLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 392 KALVItNSVKRAStVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAV 471
Cdd:cd18592 81 KILRL-RSLGDKS-VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 472 KMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITL 551
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 552 WVYVYVDpnNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd18592 239 LAHVALG--NDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
971-1520 |
1.78e-52 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 195.71 E-value: 1.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 971 TLAICLLYVGqSAAAIGANVWLSAWTNDAMADSRqnntsLRLGVYAALGIlqGFLVMlaamamaagGIQAArVLH--QAL 1048
Cdd:PRK10790 26 GLAVLMLWVA-AAAEVSGPLLISYFIDNMVAKGN-----LPLGLVAGLAA--AYVGL---------QLLAA-GLHyaQSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1049 LHNK-----------------IRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFfNAISTLVVIMAS---- 1107
Cdd:PRK10790 88 LFNRaavgvvqqlrtdvmdaaLRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA-ALIGAMLVAMFSldwr 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1108 TPLFTVVILPlAVLYTLV--QRFYAATSRQLKRLesvsRSPIYSHFSETVTGASVIRAYNRSRDFeiisDTKVDANQRSC 1185
Cdd:PRK10790 167 MALVAIMIFP-AVLVVMViyQRYSTPIVRRVRAY----LADINDGFNEVINGMSVIQQFRQQARF----GERMGEASRSH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1186 YpyiiSNRWLSIGVE--FVGNCVVLFAA-----LFAVIGRSSlnPGLVGLSVSYSLqvtfaLNWMIRM----------MS 1248
Cdd:PRK10790 238 Y----MARMQTLRLDgfLLRPLLSLFSAlilcgLLMLFGFSA--SGTIEVGVLYAF-----ISYLGRLneplielttqQS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1249 DLESNIVAVERVKEyskteteapwVVEGSRPPEGWPPR----GEVEFRNYSVRYRPGlDLVLRDLSLHVHGGEKVGIVGR 1324
Cdd:PRK10790 307 MLQQAVVAGERVFE----------LMDGPRQQYGNDDRplqsGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGH 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1325 TGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHL 1404
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1405 HTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRL 1484
Cdd:PRK10790 456 AELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRL 535
|
570 580 590
....*....|....*....|....*....|....*.
gi 9955970 1485 NTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGM 1520
Cdd:PRK10790 536 STIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
967-1264 |
3.53e-52 |
|
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: 186.37 E-value: 3.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 967 GLCTTLAICLLYVGQSAAAIGANVWLSAWTN-----DAMADSRQNNTS-----------LRLGVYAAL-------GILQG 1023
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANleeklNDTTDRVQGENStnvdiedldrdFNLGIYAGLtaatfvfGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1024 FLVMlaamamaAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVV 1103
Cdd:cd18601 81 LLFF-------HVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1104 IMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQR 1183
Cdd:cd18601 154 AVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1184 SCYPYIISNRWLSIGVEFVGNCVVLFAALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEY 1263
Cdd:cd18601 234 AWFLFLATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
.
gi 9955970 1264 S 1264
Cdd:cd18601 314 S 314
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
956-1527 |
6.42e-50 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 187.86 E-value: 6.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 956 LSVFWDYAKAVGLCT-----TLAICLLYVGQSAAAIGANVwLSAWTNDAMADSRqnNTSLRLGVYAALG---ILQGFLVM 1027
Cdd:PRK13657 1 MSLFRLYARVLQYLGaekrlGILLAVANVLLAAATFAEPI-LFGRIIDAISGKG--DIFPLLAAWAGFGlfnIIAGVLVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1028 LaamamaaggiQAARVLH---QALLHNK----IRSPQSFFDTTPSGRILNCFSKDIyvvdEVLAPVILMLLNSFFNAIST 1100
Cdd:PRK13657 78 R----------HADRLAHrrrLAVLTEYferiIQLPLAWHSQRGSGRALHTLLRGT----DALFGLWLEFMREHLATLVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1101 LVVIMastPL-------FTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRsrdfeii 1173
Cdd:PRK13657 144 LVVLL---PLalfmnwrLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNR------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1174 sdtkVDANQRSCYPYIisNRWLSigvefVGNCVVLFAALFAVIGRSS--------LNPGL---------VGLSVSYslqV 1236
Cdd:PRK13657 214 ----IEAETQALRDIA--DNLLA-----AQMPVLSWWALASVLNRAAstitmlaiLVLGAalvqkgqlrVGEVVAF---V 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1237 TFAlNWMI----RMMSDLESNIVAVERVKEYSKTETEAPWVVE--GSRPPEGWppRGEVEFRNYSVRY---RPGLDlvlr 1307
Cdd:PRK13657 280 GFA-TLLIgrldQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDppGAIDLGRV--KGAVEFDDVSFSYdnsRQGVE---- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1308 DLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDpF 1387
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR-V 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1388 G--SYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQ 1465
Cdd:PRK13657 432 GrpDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVK 511
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1466 ATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGMARDAGLA 1527
Cdd:PRK13657 512 AALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGML 573
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
642-852 |
1.79e-49 |
|
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: 177.74 E-value: 1.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLFGKALNPKRYQ 721
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 722 QTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGPegVLA 801
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMA 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 802 GKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFANFLCNY 852
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGY 259
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1042-1520 |
1.90e-49 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 188.78 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1042 RVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVIL---PL 1118
Cdd:TIGR00958 234 LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLinlPL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1119 AVLYTLV-QRFYAATSRQLKrlESVSRSPIYSHfsETVTGASVIRA-----YNRSRDFEIISDTKvDANQRSCYPYII-- 1190
Cdd:TIGR00958 314 VFLAEKVfGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSfaaeeGEASRFKEALEETL-QLNKRKALAYAGyl 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1191 -SNRWLSIGVeFVGncvVLFAALFAVIgRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETE 1269
Cdd:TIGR00958 389 wTTSVLGMLI-QVL---VLYYGGQLVL-TGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPN 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1270 APwvVEGSRPPEgwPPRGEVEFRNYSVRY--RPGLdLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEI 1347
Cdd:TIGR00958 464 IP--LTGTLAPL--NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1348 RIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFG--SYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGEN 1425
Cdd:TIGR00958 539 LLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI-AYGltDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQ 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1426 LSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATiRTQFDTcTVLTIAHRLNTIMDYTRVLVLDKGVVAEFD 1505
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES-RSRASR-TVLLIAHRLSTVERADQILVLKKGSVVEMG 695
|
490
....*....|....*
gi 9955970 1506 SPANLIAARGIFYGM 1520
Cdd:TIGR00958 696 THKQLMEDQGCYKHL 710
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1206-1517 |
2.62e-48 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 182.91 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1206 VVLFAALFAVIgRSSLNPGlvglsvsySLQVTFALnwMIRMMSDLES----------NIVAVERVKEYSKTETEAPwvvE 1275
Cdd:PRK11176 265 FVLYAASFPSV-MDTLTAG--------TITVVFSS--MIALMRPLKSltnvnaqfqrGMAACQTLFAILDLEQEKD---E 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1276 GSRPPEgwPPRGEVEFRNYSVRYrPGLD-LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNV 1354
Cdd:PRK11176 331 GKRVIE--RAKGDIEFRNVTFTY-PGKEvPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1355 ADIGLHDLRSQLTIIPQDPILFSGTLRMNLD--PFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQ 1432
Cdd:PRK11176 408 RDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1433 LVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIA 1512
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
....*
gi 9955970 1513 ARGIF 1517
Cdd:PRK11176 568 QNGVY 572
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1206-1522 |
4.60e-48 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 184.00 E-value: 4.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1206 VVLFAALFAVIGRSSLNPG-LVGLSVSYSlQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEapwvVEGSRPPEGwP 1284
Cdd:TIGR03797 374 AALFAAAISLLGGAGLSLGsFLAFNTAFG-SFSGAVTQLSNTLISILAVIPLWERAKPILEALPE----VDEAKTDPG-K 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1285 PRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVADIGLH 1360
Cdd:TIGR03797 448 LSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKST----LLRLLlgfeTPESGSVFYDGQDLAGLDVQ 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1361 DLRSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARAL 1440
Cdd:TIGR03797 524 AVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1441 LRKSRILVLDEATAAIDLETdnliQATIRTQFDT--CTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFY 1518
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRT----QAIVSESLERlkVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFA 679
|
....
gi 9955970 1519 GMAR 1522
Cdd:TIGR03797 680 QLAR 683
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
600-843 |
5.29e-47 |
|
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: 178.41 E-value: 5.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 600 KRIQQFLSQEELDPQSVERKTISPGY-AITIHSGTFTWAQDlPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEM 678
Cdd:COG4988 309 EKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 679 EKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENVLFGK-ALNPKRYQQTLEACALLADLEMLPGGDQTEI 744
Cdd:COG4988 388 PPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 745 GEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVL 824
Cdd:COG4988 468 GEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQADRILVL 544
|
250
....*....|....*....
gi 9955970 825 ADGQVSEMGPYPALLQRNG 843
Cdd:COG4988 545 DDGRIVEQGTHEELLAKNG 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1082-1496 |
1.49e-46 |
|
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: 176.32 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1082 VLAPVILMLLNSFFNAISTLVVimastpLFTVVILPLAVLYTLvqrfYAATSRQLKRLESVSRspIYSHFSETVTGASVI 1161
Cdd:TIGR02857 129 VIVPLAILAAVFPQDWISGLIL------LLTAPLIPIFMILIG----WAAQAAARKQWAALSR--LSGHFLDRLRGLPTL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1162 RAYNRSRDfEIISDTKVDANQRSCYPYIISNRWLS------------------IGVEFVGNCVVLFAALFAVIgrssLNP 1223
Cdd:TIGR02857 197 KLFGRAKA-QAAAIRRSSEEYRERTMRVLRIAFLSsavlelfatlsvalvavyIGFRLLAGDLDLATGLFVLL----LAP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1224 G----LVGLSVSY--SLQVTFALNWMIRMMsdlesnivavervkeysktetEAPWVVEGSRPPEGWPPRGEVEFRNYSVR 1297
Cdd:TIGR02857 272 EfylpLRQLGAQYhaRADGVAAAEALFAVL---------------------DAAPRPLAGKAPVTAAPASSLEFSGVSVA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1298 YrPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFS 1377
Cdd:TIGR02857 331 Y-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFA 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1378 GTLRMNL---DPFGSysEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATA 1454
Cdd:TIGR02857 410 GTIAENIrlaRPDAS--DAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 9955970 1455 AIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVL 1496
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1286-1501 |
1.21e-43 |
|
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: 158.79 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1286 RGEVEFRNYSVRYRPGLD-LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRS 1364
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1365 QLTIIPQDPILFSGTLRMNLD-PFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRK 1443
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1444 SRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVV 1501
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1056-1518 |
6.77e-43 |
|
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: 168.76 E-value: 6.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1056 PQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVlYTLVQRFYAATSRQ 1135
Cdd:TIGR01193 243 PMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPV-YAVIIILFKRTFNK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1136 LKRLESVSRSPIYSHFSETVTGASVIRAYN-RSRDFEIISDTKVDANQRScYPYIISN---RWLSIGVEFVGNCVVLFAA 1211
Cdd:TIGR01193 322 LNHDAMQANAVLNSSIIEDLNGIETIKSLTsEAERYSKIDSEFGDYLNKS-FKYQKADqgqQAIKAVTKLILNVVILWTG 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1212 LFAVIgRSSLNpglVGLSVSYSLQVTFALNWM---IRMMSDLESNIVAVERVKEYSKTETEapwVVEGSRPPEGWPPRGE 1288
Cdd:TIGR01193 401 AYLVM-RGKLT---LGQLITFNALLSYFLTPLeniINLQPKLQAARVANNRLNEVYLVDSE---FINKKKRTELNNLNGD 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGlDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:TIGR01193 474 IVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINY 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSGTLRMNLdPFGS---YSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSR 1445
Cdd:TIGR01193 553 LPQEPYIFSGSILENL-LLGAkenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1446 ILVLDEATAAIDLETDNLIQATIRTQFDTcTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFY 1518
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYA 703
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
972-1240 |
1.99e-41 |
|
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: 153.95 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 972 LAICLLYVGQSAAAIGANVWLSAWTNDAM--ADSRQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALL 1049
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLpdGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1050 HNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFY 1129
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1130 AATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVLF 1209
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 9955970 1210 AALFAV--IGRSSLNPGLVGLSVSYSLQVTFAL 1240
Cdd:pfam00664 242 ALWFGAylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1309-1520 |
4.16e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 161.55 E-value: 4.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1309 LSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILeAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNL---D 1385
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1386 PfgSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQ 1465
Cdd:PRK11174 448 P--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1466 ATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGM 1520
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
633-847 |
2.55e-40 |
|
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: 149.30 E-value: 2.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 633 TFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAW 699
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 700 IQNCTLQENVLFGKalnPKRYQQTLEACALLADL----EMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLD 775
Cdd:cd03251 87 LFNDTVAENIAYGR---PGATREEVEEAARAANAhefiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 776 DPLSAVDSHVAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFAN 847
Cdd:cd03251 164 EATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1065-1484 |
4.47e-40 |
|
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: 157.14 E-value: 4.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1065 SGRILNCFSKDiyvVDEVLApvilMLLNSFFNAISTLVVIMASTPLFTVVILP--------LAVLYTLVQRFYAATSRQL 1136
Cdd:TIGR02868 109 RGDLLGRLGAD---VDALQD----LYVRVIVPAGVALVVGAAAVAAIAVLSVPaalilaagLLLAGFVAPLVSLRAARAA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1137 KRLESVSRSPIYSHFSETVTGASVIRAYNRSRDF----EIISDTKVDANQRSCYPyiisNRWLSIGVEFVGNCVVLFAAL 1212
Cdd:TIGR02868 182 EQALARLRGELAAQLTDALDGAAELVASGALPAAlaqvEEADRELTRAERRAAAA----TALGAALTLLAAGLAVLGALW 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1213 FAVIGRSS--LNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEAPwvvEGSRPPEGWPPRGEV- 1289
Cdd:TIGR02868 258 AGGPAVADgrLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVA---EGSAPAAGAVGLGKPt 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 -EFRNYSVRYrPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:TIGR02868 335 lELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSGTLRMNLD-PFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRIL 1447
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPIL 493
|
410 420 430
....*....|....*....|....*....|....*..
gi 9955970 1448 VLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRL 1484
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
642-846 |
1.47e-39 |
|
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: 147.38 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQEN 708
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGkalNPKRYQQTLEACALLADL----EMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH 784
Cdd:cd03253 95 IRYG---RPDATDEEVIEAAKAAQIhdkiMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 785 VAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFA 846
Cdd:cd03253 172 TEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYA 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
627-828 |
3.98e-37 |
|
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: 137.90 E-value: 3.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAY 693
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 694 VPQQAWIQNCTLQENVLfgkalnpkryqqtleacalladlemlpggdqteigekginlSGGQRQRVSLARAVYSDADIFL 773
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 774 LDDPLSAVDSHVAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQ 828
Cdd:cd03228 120 LDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
642-843 |
4.42e-37 |
|
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: 140.05 E-value: 4.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQEN 708
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGKALNPKryQQTLEACALL-AD--LEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHV 785
Cdd:cd03254 97 IRLGRPNATD--EEVIEAAKEAgAHdfIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 786 AKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNG 843
Cdd:cd03254 175 EKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
642-848 |
5.23e-37 |
|
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: 139.98 E-value: 5.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS-------------VAYVPQQAWIQNCTLQEN 708
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGKalnPKRYQQTLEACALLADL----EMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH 784
Cdd:cd03249 97 IRYGK---PDATDEEVEEAAKKANIhdfiMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 785 VAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFANF 848
Cdd:cd03249 174 SEKLVQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1289-1514 |
8.35e-37 |
|
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: 139.00 E-value: 8.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGlDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPI--LFSGTLR-------MNLDpfgsYSEEDIW----WALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQLVC 1435
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpENLG----LPREEIRerveEALELVGLEHLADRPPH-----------ELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1436 LARALLRKSRILVLDEATAAIDLETDNLIQATIRT-QFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVAEFDSPANLIAA 1513
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREVFSD 224
|
.
gi 9955970 1514 R 1514
Cdd:COG1122 225 Y 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1290-1501 |
2.40e-36 |
|
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: 135.81 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTII 1369
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1370 PQDPILFSGTLRMNLdpfgsyseediwwalelshlhtfvssqpagldfqcseggenLSVGQRQLVCLARALLRKSRILVL 1449
Cdd:cd03246 82 PQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1450 DEATAAIDLETDNLI-QATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVV 1501
Cdd:cd03246 121 DEPNSHLDVEGERALnQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
288-846 |
2.11e-35 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 143.70 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 288 LGARPRPRKPSFLKALLATFG----SSFLISACFKLIQDLLSFINPQLLsilirfisnpmapsWW-GFLVAGLMFL---C 359
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVAMILvaatESTLAALLKPLLDDGFGGRDRSVL--------------WWvPLVVIGLAVLrgiC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 360 SMMQSLILQHyyhyifvTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLAP-FLNLLWSAPLQII 438
Cdd:TIGR02203 71 SFVSTYLLSW-------VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATdAFIVLVRETLTVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 439 -LAIYFLWQNLGPSVLagvafMVLLIPLngaVAVKMRAFQVKQMKLKDSRIKLM-------SEILNGIKVLKLYAWEPSF 510
Cdd:TIGR02203 144 gLFIVLLYYSWQLTLI-----VVVMLPV---LSILMRRVSKRLRRISKEIQNSMgqvttvaEETLQGYRVVKLFGGQAYE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 511 LKQVEGIRQgelQLLRTAAYLHTTTTFTwmcSPF--LVTLITLWVYVYVdpnNVLDAEKAFVSVSLFNILRLPLNMLPQL 588
Cdd:TIGR02203 216 TRRFDAVSN---RNRRLAMKMTSAGSIS---SPItqLIASLALAVVLFI---ALFQAQAGSLTAGDFTAFITAMIALIRP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 589 ISNLTQASVSLKRIqqFLSQEEL-----DPQSVERKTISPGYA---ITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVV 660
Cdd:TIGR02203 287 LKSLTNVNAPMQRG--LAAAESLftlldSPPEKDTGTRAIERArgdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 661 GPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENVLFGK--ALNPKRYQQTLE 725
Cdd:TIGR02203 365 GRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlaslrrQVALVSQDVVLFNDTIANNIAYGRteQADRAEIERALA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 726 ACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVigpEGVLAGKTR 805
Cdd:TIGR02203 445 AAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL---ERLMQGRTT 521
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 9955970 806 VLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFA 846
Cdd:TIGR02203 522 LVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYA 562
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
593-824 |
4.91e-35 |
|
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: 142.04 E-value: 4.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 593 TQASVSLKRIQQFLSQEELDPQSVERKTISPGYAITIHSGTFTWAqDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVS 672
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 673 ALLGEMEKLEGKV-------------HMKGSVAYVPQQAWIQNCTLQENVLFGKA-LNPKRYQQTLEACALLADLEMLPG 738
Cdd:TIGR02857 367 LLLGFVDPTEGSIavngvpladadadSWRDQIAWVPQHPFLFAGTIAENIRLARPdASDAEIREALERAGLDEFVAALPQ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 739 GDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQT 818
Cdd:TIGR02857 447 GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALA 523
|
....*.
gi 9955970 819 DFIIVL 824
Cdd:TIGR02857 524 DRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1254-1518 |
7.74e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 142.27 E-value: 7.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1254 IVAVERVKEYskTETEAPWVVEGSRPPEgwPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMT 1333
Cdd:PRK11160 308 IASARRINEI--TEQKPEVTFPTTSTAA--ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1334 LCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfgSYSEEDIWWALELSHLHTFVsS 1410
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLL-E 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1411 QPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTI--M 1488
Cdd:PRK11160 461 DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLeqF 540
|
250 260 270
....*....|....*....|....*....|
gi 9955970 1489 DytRVLVLDKGVVAEFDSPANLIAARGIFY 1518
Cdd:PRK11160 541 D--RICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
602-849 |
2.56e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 140.75 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 602 IQQFLSQEELDPQSvERKTISPGYAITIHsgtftwAQDLP-------PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSAL 674
Cdd:PRK11174 324 LVTFLETPLAHPQQ-GEKELASNDPVTIE------AEDLEilspdgkTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 675 LGEMeKLEGKVHMKG------SVAYVPQQ-AWI-QN-----CTLQENVLFGK-ALNPKRYQQTLEACALLADLEMLPGGD 740
Cdd:PRK11174 397 LGFL-PYQGSLKINGielrelDPESWRKHlSWVgQNpqlphGTLRDNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 741 QTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDhviGPEGVLAGKTRVLVTHGISFLPQTDF 820
Cdd:PRK11174 476 DTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ---ALNAASRRQTTLMVTHQLEDLAQWDQ 552
|
250 260
....*....|....*....|....*....
gi 9955970 821 IIVLADGQVSEMGPYPALLQRNGSFANFL 849
Cdd:PRK11174 553 IWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1239-1522 |
3.08e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 137.15 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1239 ALNWMIrmmsdlesNIVavER-VKEYSKTET---EAPWVVEGSRP-PEGwppRGEVEFRNYSVRYRPGLDLVLRDLSLHV 1313
Cdd:PRK10789 272 ALAWMF--------NIV--ERgSAAYSRIRAmlaEAPVVKDGSEPvPEG---RGELDVNIRQFTYPQTDHPALENVNFTL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1314 HGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFG--SYS 1391
Cdd:PRK10789 339 KPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI-ALGrpDAT 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1392 EEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQ 1471
Cdd:PRK10789 418 QQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1472 FDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGMAR 1522
Cdd:PRK10789 498 GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
490-846 |
2.37e-32 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 136.03 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 490 LMSEILNGIKVLKLYAWEPSFLkqvegiRQGELQLlrtAAYLHT----TTTFTWMCSPF-----LVTLITLWVYVYVdpn 560
Cdd:TIGR01846 319 FLVESVTGIETIKATATEPQFQ------NRWDRQL---AAYVAAsfrvTNLGNIAGQAIeliqkLTFAILLWFGAHL--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 561 nVLDAEKAFVSVSLFNIL----RLPLNMLPQLISNLTQASVSLKRIQQFL-SQEELDPQSVERKTISPGyAITIHSGTFT 635
Cdd:TIGR01846 387 -VIGGALSPGQLVAFNMLagrvTQPVLRLAQLWQDFQQTGIALERLGDILnSPTEPRSAGLAALPELRG-AITFENIRFR 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 636 WAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQ---NCTLQENVLFG 712
Cdd:TIGR01846 465 YAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRrqmGVVLQENVLFS 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 713 KAL-------NPKRYQQTLEACALLAD----LEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAV 781
Cdd:TIGR01846 545 RSIrdnialcNPGAPFEHVIHAAKLAGahdfISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSAL 624
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 782 DSHVAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFA 846
Cdd:TIGR01846 625 DYESEALIMRNM---REICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1290-1499 |
3.54e-32 |
|
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: 125.27 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTII 1369
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1370 PQDP------------ILFSgtLRmNLdpfgSYSEEDIW----WALELSHLHTFVSSQPagldfqcseggENLSVGQRQL 1433
Cdd:cd03225 81 FQNPddqffgptveeeVAFG--LE-NL----GLPEEEIEerveEALELVGLEGLRDRSP-----------FTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1434 VCLARALLRKSRILVLDEATAAIDLETDNLIQATIRT-QFDTCTVLTIAHRLNTIMDY-TRVLVLDKG 1499
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1290-1499 |
5.95e-32 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 122.74 E-value: 5.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTII 1369
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1370 PQdpilfsgtlrmnldpfgsyseediwwalelshlhtfvssqpagldfqcseggenLSVGQRQLVCLARALLRKSRILVL 1449
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1450 DEATAAIDLETDNLIQATIRTQFDT-CTVLTIAHRLNTIMDYT-RVLVLDKG 1499
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAAdRVIVLKDG 156
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1284-1513 |
1.16e-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: 132.18 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1284 PPRGEVEFRNYSVRYrPGLD-LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGlnvADIGLHDl 1362
Cdd:COG4618 326 RPKGRLSVENLTVVP-PGSKrPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---ADLSQWD- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1363 RSQL-TII---PQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLAR 1438
Cdd:COG4618 401 REELgRHIgylPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 1439 ALLRKSRILVLDEATAAIDLETD-NLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAA 1513
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEaALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
633-829 |
1.22e-31 |
|
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: 123.85 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 633 TFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAW 699
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 700 IQNCTLQENVLFGkalNPKRYQQTLEACALLADLEML----PGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLD 775
Cdd:cd03245 89 LFYGTLRDNITLG---APLADDERILRAAELAGVTDFvnkhPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9955970 776 DPLSAVDSHVAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQV 829
Cdd:cd03245 166 EPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
626-829 |
1.26e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.82 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 626 AITIHSGTFTWAQDlpPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG--------SVAYVPQQ 697
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 698 A---WIQNCTLQENVLFG--------KALNPKRYQQTLEAcalLADLEMLPGGDQTeIGEkginLSGGQRQRVSLARAVY 766
Cdd:COG1121 84 AevdWDFPITVRDVVLMGrygrrglfRRPSRADREAVDEA---LERVGLEDLADRP-IGE----LSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 767 SDADIFLLDDPLSAVDSHVAKHIFDhvigpegVLA-----GKTRVLVTHGISFLPQ-TDFIIVLADGQV 829
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
311-582 |
2.28e-31 |
|
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: 125.06 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 311 FLISACFKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLV-AGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVI 389
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVySLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 390 YRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSV-LAGVAFMVLLIPLNGA 468
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 469 VAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHT-TTTFTWMCSPFLVT 547
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGlSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 9955970 548 LITLWVYVYVDpNNVLDAEKAFVSVSLFNILRLPL 582
Cdd:pfam00664 241 LALWFGAYLVI-SGELSVGDLVAFLSLFAQLFGPL 274
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1289-1511 |
4.00e-31 |
|
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: 123.62 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLdlVLRDLSLHVHGGEKVGIVGRTGAGKSsmTL--CLFRILEAAKGEIRIDGLNVADIGLHDLRSQL 1366
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKS--TLlrALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPIL-FSGTLR----M----NLDPFGSYSEED---IWWALE---LSHL-HTFVSSqpagldfqcseggenLSVGQ 1430
Cdd:COG1120 78 AYVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALErtgLEHLaDRPVDE---------------LSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1431 RQLVCLARALLRKSRILVLDEATAAIDL----ETDNLIQATIRTQfdTCTVLTIAHRLNTIMDY-TRVLVLDKGVVAEFD 1505
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQG 220
|
....*.
gi 9955970 1506 SPANLI 1511
Cdd:COG1120 221 PPEEVL 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
438-810 |
4.49e-31 |
|
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: 129.79 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 438 ILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAvkMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEgi 517
Cdd:TIGR02868 145 VAAIAVLSVPAALILAAGLLLAGFVAPLVSLRA--ARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVE-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 518 rQGELQLL----RTAAYLHTTTTFT-WMCSpfLVTLITLWVYVyvdpNNVLDAEKAFVSVSLFNILRLPL----NMLPQL 588
Cdd:TIGR02868 221 -EADRELTraerRAAAATALGAALTlLAAG--LAVLGALWAGG----PAVADGRLAPVTLAVLVLLPLAAfeafAALPAA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 589 ISNLTQASVSLKRIQQFLSQEEL--DPQSVERKTISPGYA-ITIHSGTFTWAQDlPPTLHSLDIQVPKGALVAVVGPVGC 665
Cdd:TIGR02868 294 AQQLTRVRAAAERIVEVLDAAGPvaEGSAPAAGAVGLGKPtLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGS 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 666 GKSSLVSALLGEMEKLEGKVHMKGS-------------VAYVPQQAWIQNCTLQENVLFGKA-LNPKRYQQTLEACALLA 731
Cdd:TIGR02868 373 GKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLAD 452
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 732 DLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIgpeGVLAGKTRVLVTH 810
Cdd:TIGR02868 453 WLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL---AALSGRTVVLITH 528
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1285-1504 |
4.67e-31 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 130.16 E-value: 4.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1285 PRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRS 1364
Cdd:TIGR01842 313 PEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1365 QLTIIPQDPILFSGTLRMNLDPFGSYSE-EDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRK 1443
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1444 SRILVLDEATAAIDLETDN-LIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEF 1504
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQaLANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARF 534
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
402-848 |
5.96e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 131.23 E-value: 5.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 402 RASTVGEIVN-LMSVDAQRfmdlapflNLLWSAPLQIILAIYFLWQNLG-------PSVLAGVAFMVLLIPLNGAVAVKM 473
Cdd:TIGR03797 228 RQYSTGDLASrAMGISQIR--------RILSGSTLTTLLSGIFALLNLGlmfyyswKLALVAVALALVAIAVTLVLGLLQ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 474 RAFQVKQMKLKDSRIKLMSEILNGIKVLK--------LYAWEPSFLKQVEgirqgeLQLL-RTAAYLHTTTTFTWmcsPF 544
Cdd:TIGR03797 300 VRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK------LELSaQRIENLLTVFNAVL---PV 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 545 LVTLITLWVYVYVDPNNVLDAeKAFVS-VSLFNILRLPLNMLPQLISNLTQASVSLKRIQQFLSQEeldPQSVERKTiSP 623
Cdd:TIGR03797 371 LTSAALFAAAISLLGGAGLSL-GSFLAfNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEAL---PEVDEAKT-DP 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 624 GY---AITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGeMEKLEgkvhmKGSVAY------- 693
Cdd:TIGR03797 446 GKlsgAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLG-FETPE-----SGSVFYdgqdlag 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 694 ------------VPQQAWIQNCTLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSL 761
Cdd:TIGR03797 520 ldvqavrrqlgvVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 762 ARAVYSDADIFLLDDPLSAVDSHVAKhifdHVIGPEGVLAGkTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQR 841
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRTQA----IVSESLERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAR 674
|
....*..
gi 9955970 842 NGSFANF 848
Cdd:TIGR03797 675 EGLFAQL 681
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
587-834 |
1.00e-30 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 129.00 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 587 QLISNLTQ---ASVSLKRIQQFLSQEELDPQSVERKtiSPGYAITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPV 663
Cdd:TIGR01842 276 GAIGGWKQfsgARQAYKRLNELLANYPSRDPAMPLP--EPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 664 GCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENVL-FGKALNPkryQQTLEAcAL 729
Cdd:TIGR01842 354 GSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADP---EKIIEA-AK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 730 LADL-EM---LPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIgpEGVLAGKTR 805
Cdd:TIGR01842 430 LAGVhELilrLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIK--ALKARGITV 507
|
250 260
....*....|....*....|....*....
gi 9955970 806 VLVTHGISFLPQTDFIIVLADGQVSEMGP 834
Cdd:TIGR01842 508 VVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1289-1499 |
2.49e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 118.57 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGlHDLRSQLTI 1368
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSGTLRMNLdpfgsyseediwwalelshlhtfvssqpagldfqcsegGENLSVGQRQLVCLARALLRKSRILV 1448
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1449 LDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKG 1499
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENG 172
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1289-1513 |
2.64e-30 |
|
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: 127.33 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAA---KGEIRIDGLNVADIGLHDLRSQ 1365
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQDP------------ILFsgTLRmNLDPFGSYSEEDIWWALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQL 1433
Cdd:COG1123 85 IGMVFQDPmtqlnpvtvgdqIAE--ALE-NLGLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1434 VCLARALLRKSRILVLDEATAAIDLETDNLIQATIR--TQFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVAEFDSPANL 1510
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEI 230
|
...
gi 9955970 1511 IAA 1513
Cdd:COG1123 231 LAA 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1289-1515 |
3.10e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.58 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFR----ILEAAKGEIRIDGLNVadiglHDLRS 1364
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKST----LLKailgLLPPTSGTVRLFGKPP-----RRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1365 QLTIIPQD-------PILFSGTLRMNLDP----FGSYSEED---IWWALE---LSHLhtfvSSQPAGldfqcseggeNLS 1427
Cdd:COG1121 76 RIGYVPQRaevdwdfPITVRDVVLMGRYGrrglFRRPSRADreaVDEALErvgLEDL----ADRPIG----------ELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1428 VGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDT-CTVLTIAHRLNTIMDY-TRVLVLDKGVVA--- 1502
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYfDRVLLLNRGLVAhgp 221
|
250
....*....|....*
gi 9955970 1503 --EFDSPANLIAARG 1515
Cdd:COG1121 222 peEVLTPENLSRAYG 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
627-847 |
3.35e-30 |
|
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: 120.28 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQ---NC 703
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 704 TLQENVLFGKAL-------NPKRYQQTLEACALLAD----LEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIF 772
Cdd:cd03252 81 VLQENVLFNRSIrdnialaDPGMSMERVIEAAKLAGahdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 773 LLDDPLSAVDSHVAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFAN 847
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1306-1454 |
3.37e-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: 117.36 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGT-----L 1380
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1381 RMNLDPFGSYSEEDIWWALELshLHTFvsSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATA 1454
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEA--LEKL--GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
596-843 |
5.29e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 127.14 E-value: 5.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 596 SVSLKRIQQFLSQEEL-----DPQSVERKTIspgyAITIHsgTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSL 670
Cdd:PRK10789 284 SAAYSRIRAMLAEAPVvkdgsEPVPEGRGEL----DVNIR--QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 671 VSALLGEMEKLEGKV-------------HMKGSVAYVPQQAWIQNCTLQENVLFGKalnPKRYQQTLEACALLA----DL 733
Cdd:PRK10789 358 LSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIALGR---PDATQQEIEHVARLAsvhdDI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 734 EMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFdHVIGPEGvlAGKTRVLVTHGIS 813
Cdd:PRK10789 435 LRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQIL-HNLRQWG--EGRTVIISAHRLS 511
|
250 260 270
....*....|....*....|....*....|
gi 9955970 814 FLPQTDFIIVLADGQVSEMGPYPALLQRNG 843
Cdd:PRK10789 512 ALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
972-1260 |
6.35e-30 |
|
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: 122.22 E-value: 6.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 972 LAICLLYVGQSAAAIGANVWLSAWTNDAMADSRQNNTSLRLGV-----------YAALGILQGFLVM--LAAMAMAAGGI 1038
Cdd:cd18600 20 LILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVivtftssyyvfYIYVGVADSLLAMgfFRGLPLVHTLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1039 QAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPL 1118
Cdd:cd18600 100 TVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1119 AVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIG 1198
Cdd:cd18600 180 IIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMR 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1199 VEFVgncVVLF--AALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERV 1260
Cdd:cd18600 260 IEMI---FVIFftAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
627-834 |
1.30e-29 |
|
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: 117.98 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAY 693
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 694 VPQQAWIQNCTLQENV-LFGKAlNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIF 772
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdPFGEY-SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 773 LLDDPLSAVDSHVAKHIFDhVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGP 834
Cdd:cd03244 162 VLDEATASVDPETDALIQK-TIREA--FKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
291-846 |
2.38e-29 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 126.60 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 291 RPRPRKPSFLKALLATFGSS-----FLISACFKLIqdLLSFINPQLLSILIRFISNPMAPSWWGFLVAGlMFLCSMMQSl 365
Cdd:TIGR03796 133 QKGGRKPSLLRALWRRLRGSrgallYLLLAGLLLV--LPGLVIPAFSQIFVDEILVQGRQDWLRPLLLG-MGLTALLQG- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 366 ILQHYYHYIFV-----TGVKFRTGIMGVIYRkaLVITNSVKRAStvGEIVNLMSVDAQrfmdLAPFLN-LLWSAPLQIIL 439
Cdd:TIGR03796 209 VLTWLQLYYLRrleikLAVGMSARFLWHILR--LPVRFFAQRHA--GDIASRVQLNDQ----VAEFLSgQLATTALDAVM 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 440 AI-YFLWQNLGPSVLAGVAFMVLLIPLnGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKV---LKLYAWEPSFLKQVE 515
Cdd:TIGR03796 281 LVfYALLMLLYDPVLTLIGIAFAAINV-LALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSietLKASGLESDFFSRWA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 516 GIR----QGELQLLRTAAYLHTTttftwmcsPFLVTLIT----LWV--YVYVDPNNVLDAEKAFVSVsLFNILrLPLNML 585
Cdd:TIGR03796 360 GYQakllNAQQELGVLTQILGVL--------PTLLTSLNsaliLVVggLRVMEGQLTIGMLVAFQSL-MSSFL-EPVNNL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 586 PQLISNLTQASVSLKRIQQFLSQEeLDPQSVERKTISP---------GYaITIHSGTFTWAQDLPPTLHSLDIQVPKGAL 656
Cdd:TIGR03796 430 VGFGGTLQELEGDLNRLDDVLRNP-VDPLLEEPEGSAAtsepprrlsGY-VELRNITFGYSPLEPPLIENFSLTLQPGQR 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 657 VAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENV-LFGKALNPKRYQQ 722
Cdd:TIGR03796 508 VALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGipreeiprevlanSVAMVDQDIFLFEGTVRDNLtLWDPTIPDADLVR 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 723 TLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHvigpegvLA- 801
Cdd:TIGR03796 588 ACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDN-------LRr 660
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 9955970 802 -GKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFA 846
Cdd:TIGR03796 661 rGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYA 706
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1269-1513 |
4.47e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.47 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1269 EAPWVVEGSRPPEGWPPRGE--VEFRNYSVRY---RPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAA 1343
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEplLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1344 KGEIRIDGLNVADIG---LHDLRSQLTIIPQDPilfSGTL--RMN--------LDPFGSYSEEDIW----WALELSHLht 1406
Cdd:COG1123 319 SGSILFDGKDLTKLSrrsLRELRRRVQMVFQDP---YSSLnpRMTvgdiiaepLRLHGLLSRAERRervaELLERVGL-- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1407 fvssQPAGLD---FQcseggenLSVGQRQLVCLARALLRKSRILVLDEATAAIDLetdnLIQATI-------RTQFDtCT 1476
Cdd:COG1123 394 ----PPDLADrypHE-------LSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQIlnllrdlQRELG-LT 457
|
250 260 270
....*....|....*....|....*....|....*...
gi 9955970 1477 VLTIAHRLNTIMDYT-RVLVLDKGVVAEFDSPANLIAA 1513
Cdd:COG1123 458 YLFISHDLAVVRYIAdRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
587-834 |
4.57e-29 |
|
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: 124.09 E-value: 4.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 587 QLISN---LTQASVSLKRIQQFLSQEELDPQ-----------SVERKTISPgyaitihSGTFTwaqdlpPTLHSLDIQVP 652
Cdd:COG4618 290 QAIGGwkqFVSARQAYRRLNELLAAVPAEPErmplprpkgrlSVENLTVVP-------PGSKR------PILRGVSFSLE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 653 KGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENV-LFGKAlNPk 718
Cdd:COG4618 357 PGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAENIaRFGDA-DP- 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 719 ryQQTLEAcALLADL-EM---LPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDShvakhifdhvi 794
Cdd:COG4618 435 --EKVVAA-AKLAGVhEMilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD----------- 500
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 795 gpEGVLA-----------GKTRVLVTHGISFLPQTDFIIVLADGQVSEMGP 834
Cdd:COG4618 501 --EGEAAlaaairalkarGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1289-1504 |
5.10e-29 |
|
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: 116.84 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLV--LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDL---R 1363
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 SQLTIIPQDPILfsgtlrmNLDPfgSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGEN-----------LSVGQRQ 1432
Cdd:cd03257 82 KEIQMVFQDPMS-------SLNP--RMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLpeevlnrypheLSGGQRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1433 LVCLARALLRKSRILVLDEATAAIDLetdnLIQATI-------RTQFDTcTVLTIAHRLNTIMDYT-RVLVLDKGVVAEF 1504
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDV----SVQAQIldllkklQEELGL-TLLFITHDLGVVAKIAdRVAVMYAGKIVEE 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
642-813 |
1.30e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 114.94 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG--------SVAYVPQQAWIQNC---TLQENVL 710
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSIDRDfpiSVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FG--KALNPKRYQQTLEACALLADLEMLpggDQTEIGEKGI-NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAK 787
Cdd:cd03235 93 MGlyGHKGLFRRLSKADKAKVDEALERV---GLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170 180
....*....|....*....|....*...
gi 9955970 788 HIFDHVIGpegvLA--GKTRVLVTHGIS 813
Cdd:cd03235 170 DIYELLRE----LRreGMTILVVTHDLG 193
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1289-1513 |
4.45e-28 |
|
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: 114.52 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDL--VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQL 1366
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPIlfsGTL--RMNLD-----PF----GSYSEEDIWWALELSHLH-TFVSSQPAgldfQcseggenLSVGQRQLV 1434
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVDrilaePLrihgLPDREERIAELLEQVGLPpSFLDRYPH----Q-------LSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1435 CLARALLRKSRILVLDEATAAIDL----ETDNLIQAtIRTQFDTcTVLTIAHRLNTImDY--TRVLVLDKGVVAEFDSPA 1508
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVsvqaEILNLLKD-LREERGL-TYLFVSHDLAVV-AHlcDRVAVMQNGRIVEELTVA 224
|
....*
gi 9955970 1509 NLIAA 1513
Cdd:COG1124 225 DLLAG 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1290-1502 |
6.68e-28 |
|
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: 113.01 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRY--RPgldlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAD----IGLhdlR 1363
Cdd:cd03235 1 EVEDLTVSYggHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKerkrIGY---V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 SQLTIIPQD-PILFSGTLRMNLDP----FGSYSEED---IWWALE---LSHLHtfvssqpaglDFQCSEggenLSVGQRQ 1432
Cdd:cd03235 74 PQRRSIDRDfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALErvgLSELA----------DRQIGE----LSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1433 LVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRT-QFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVA 1502
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFdRVLLLNRTVVA 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
633-829 |
7.89e-28 |
|
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: 111.54 E-value: 7.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 633 TFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGsvayVPQQAWiqnctlqenvlfg 712
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQW------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 713 kalNPKRYQQTLEAcaLLADLEMLPGGDQTEIgekginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDH 792
Cdd:cd03246 70 ---DPNELGDHVGY--LPQDDELFSGSIAENI------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 9955970 793 VIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQV 829
Cdd:cd03246 139 IAALK--AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1290-1501 |
2.58e-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: 110.22 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSsmTL--CLFRILEAAKGEIRIDGLNVADIGLHDLRSQLT 1367
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKS--TLlkTLAGLLKPSSGEILLDGKDLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQdpilfsgtlrmNLDpfgsyseediwwALELSHLhtfvssqpagLDFQCSEggenLSVGQRQLVCLARALLRKSRIL 1447
Cdd:cd03214 77 YVPQ-----------ALE------------LLGLAHL----------ADRPFNE----LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 1448 VLDEATAAIDL----ETDNLIQAtIRTQFDTCTVLTIaHRLNTIMDY-TRVLVLDKGVV 1501
Cdd:cd03214 120 LLDEPTSHLDIahqiELLELLRR-LARERGKTVVMVL-HDLNLAARYaDRVILLKDGRI 176
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1289-1499 |
4.03e-27 |
|
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: 109.58 E-value: 4.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLH--DLRSQL 1366
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSG-TLRMNLdpfgsyseediwwalelshlhtfvssqpagldfqcsegGENLSVGQRQLVCLARALLRKSR 1445
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI--------------------------------------ALGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 1446 ILVLDEATAAIDLETDNLIQATIRTQFDT--CTVLTIAHRLNTIMDYT-RVLVLDKG 1499
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLAdRVVVLRDG 177
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1235-1499 |
4.91e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 114.90 E-value: 4.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1235 QVTFALNWMIRMMSDLeSNIVA-VERVKEYS---KTETEAPWVVEGSRPPEGwpprGEVEFRNYSVRyRPGLDLVLRDLS 1310
Cdd:COG4178 310 QVQGALSWFVDNYQSL-AEWRAtVDRLAGFEealEAADALPEAASRIETSED----GALALEDLTLR-TPDGRPLLEDLS 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1311 LHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRidglnvadigLHDLRSQLtIIPQDPILFSGTLRMNL-- 1384
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKST----LLRAIaglwPYGSGRIA----------RPAGARVL-FLPQRPYLPLGTLREALly 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1385 -DPFGSYSEEDIWWALELSHLHTFVSSqpagLDfQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNL 1463
Cdd:COG4178 449 pATAEAFSDAELREALEAVGLGHLAER----LD-EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA 523
|
250 260 270
....*....|....*....|....*....|....*..
gi 9955970 1464 IQATIRTQFDTCTVLTIAHRlNTIMDY-TRVLVLDKG 1499
Cdd:COG4178 524 LYQLLREELPGTTVISVGHR-STLAAFhDRVLELTGD 559
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
592-848 |
1.13e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.77 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 592 LTQASVSLKRIQQFLSQEELDPQSVERKTISPGYAITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLV 671
Cdd:PRK11160 304 LGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 672 SALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENVLFGKA-LNPKRYQQTLEACALLADLEMLP 737
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 738 GGDqTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHI----FDHVigpegvlAGKTRVLVTHGIS 813
Cdd:PRK11160 464 GLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIlellAEHA-------QNKTVLMITHRLT 535
|
250 260 270
....*....|....*....|....*....|....*
gi 9955970 814 FLPQTDFIIVLADGQVSEMGPYPALLQRNGSFANF 848
Cdd:PRK11160 536 GLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1286-1497 |
1.16e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 115.90 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1286 RGEVEFRNYSVRY--RPGLDlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAK------------------- 1344
Cdd:PTZ00265 1163 KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1345 -----------------------------------GEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFG- 1388
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGk 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1389 -SYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQAT 1467
Cdd:PTZ00265 1321 eDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270
....*....|....*....|....*....|..
gi 9955970 1468 IRTQFDTC--TVLTIAHRLNTIMDYTRVLVLD 1497
Cdd:PTZ00265 1401 IVDIKDKAdkTIITIAHRIASIKRSDKIVVFN 1432
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
647-833 |
2.90e-25 |
|
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: 105.29 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-----------SVAYVPQQ-AWIQNCTLQENVLFGKA 714
Cdd:cd03259 19 LSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDyALFPHLTVAENIAFGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 715 LNPKRYQQTLEACALLADLEMLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVi 794
Cdd:cd03259 99 LRGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREEL- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9955970 795 gpEGVLA--GKTRVLVTHGIS-FLPQTDFIIVLADGQVSEMG 833
Cdd:cd03259 174 --KELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
644-779 |
3.60e-25 |
|
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: 102.73 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV-------------HMKGSVAYVPQQAWIQN-CTLQENV 709
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltdderkSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 710 LFG---KALNPKRYQQTLEAcaLLADLEMLPGGDQTeIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:pfam00005 81 RLGlllKGLSKREKDARAEE--ALEKLGLGDLADRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1305-1515 |
4.98e-25 |
|
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: 105.71 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHdLRSQLTIIPQDPILFSG-TLRMN 1383
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1384 LDPF----GSYSEEDIWWALELSHLHTFVSSqpagLDFQCSEggenLSVGQRQLVCLARALLRKSRILVLDEATAAIDLE 1459
Cdd:COG4555 95 IRYFaelyGLFDEELKKRIEELIELLGLEEF----LDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1460 TDNLIQATIRT--QFDTCTVLT--IAHRLNTIMDytRVLVLDKGVVAEFDSPANLIAARG 1515
Cdd:COG4555 167 ARRLLREILRAlkKEGKTVLFSshIMQEVEALCD--RVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
633-828 |
7.11e-25 |
|
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: 104.09 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 633 TFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAW 699
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 700 IQ--NCTLQENVLFG-------KALNPKRYQQTLEACALLADLEMLPggdqteigekgINLSGGQRQRVSLARAVYSDAD 770
Cdd:cd03225 86 DQffGPTVEEEVAFGlenlglpEEEIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 771 IFLLDDPLSAVDSHVAKHIFDHVIGpegvL--AGKTRVLVTHGISFL-PQTDFIIVLADGQ 828
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKK----LkaEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1290-1509 |
2.16e-24 |
|
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: 103.80 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYrPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIG---LHDLRSQL 1366
Cdd:cd03256 2 EVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPIL----------FSGTL-RMNLDP--FGSYSEEDIWWALE------LSHLHtfvsSQPAGldfqcseggeNLS 1427
Cdd:cd03256 81 GMIFQQFNLierlsvlenvLSGRLgRRSTWRslFGLFPKEEKQRALAalervgLLDKA----YQRAD----------QLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1428 VGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIR--TQFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVAeF 1504
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYAdRIVGLKDGRIV-F 225
|
....*
gi 9955970 1505 DSPAN 1509
Cdd:cd03256 226 DGPPA 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
642-846 |
2.24e-24 |
|
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: 109.91 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQEN 708
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraAIGIVPQDTVLFNDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGkalNPKRYQQTLEACALLADL----EMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH 784
Cdd:COG5265 452 IAYG---RPDASEEEVEAAARAAQIhdfiESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 785 VAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFA 846
Cdd:COG5265 529 TERAIQAAL---REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
644-824 |
2.41e-24 |
|
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: 102.94 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG--------SVAYVPQQA----WIqncTLQENVLF 711
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDallpWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 G-KALNPKRYQQTLEACALLAdlemlpggdqtEIGEKGI------NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH 784
Cdd:cd03293 97 GlELQGVPKAEARERAEELLE-----------LVGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9955970 785 VAKHIFDHVIGpegvL---AGKTRVLVTHGIS---FLpqTDFIIVL 824
Cdd:cd03293 166 TREQLQEELLD----IwreTGKTVLLVTHDIDeavFL--ADRVVVL 205
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
568-849 |
3.06e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 109.67 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 568 AFVSVSLFNILRLPlnmlpQLISNLTQASVSLKRIQQFLSQEELDPQSVER-KTISPGY---AITIHSGTFTWAQDlPPT 643
Cdd:PRK13657 277 AFVGFATLLIGRLD-----QVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPpGAIDLGRvkgAVEFDDVSFSYDNS-RQG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENVL 710
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FGKA-LNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHI 789
Cdd:PRK13657 431 VGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 790 FDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFANFL 849
Cdd:PRK13657 511 KAAL---DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1289-1499 |
3.09e-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: 102.16 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPG---LDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGlNVAdiglhdlrsq 1365
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIA---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 ltIIPQDPILFSGTLRMNLdPFGS-YSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKS 1444
Cdd:cd03250 70 --YVSQEPWIQNGTIRENI-LFGKpFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1445 RILVLDEATAAIDLETDNLIqatirtqFDTC---------TVLTIAHRLNTIMDYTRVLVLDKG 1499
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1289-1501 |
3.53e-24 |
|
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: 100.94 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGlHDLRSQLTI 1368
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSG-TLRMNLDpfgsyseediwwalelshlhtfvssqpagldfqcseggenLSVGQRQLVCLARALLRKSRIL 1447
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 1448 VLDEATAAIDLETDNLIQATIRT-QFDTCTVLTIAHRLNTIMDY-TRVLVLDKGVV 1501
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1289-1507 |
3.62e-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: 102.64 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAK-----GEIRIDGLNVADIGLHD-- 1361
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 LRSQLTIIPQDPILFSGTLRMNLDpFG---------SYSEEDIWWALELSHLHTFVSSQPAGLDfqcseggenLSVGQRQ 1432
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA-YGlrlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1433 LVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNT---IMDYTrvLVLDKGVVAEFDSP 1507
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADRT--AFLLNGRLVEFGPT 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
633-846 |
7.16e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 108.18 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 633 TFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAW 699
Cdd:PRK11176 348 TFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 700 IQNCTLQENVLFgkALNPKRYQQTLEACALLAD----LEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLD 775
Cdd:PRK11176 428 LFNDTIANNIAY--ARTEQYSREQIEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 776 DPLSAVDSHVAKHIFDHVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFA 846
Cdd:PRK11176 506 EATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1289-1513 |
1.40e-23 |
|
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: 101.12 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRY--RPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLfRILEA-AKGEIRIDGLNVADI---GLHDL 1362
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERpTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1363 RSQLTIIPQDPILFSG-TLRMNLD-PF------GSYSEEDIWWALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQLV 1434
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1435 CLARALLRKSRILVLDEATAAIDLETDNLIQATIRT---QFDTcTVLTIAHRLNTIMDY-TRVLVLDKGVVAEFDSPANL 1510
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDinrELGL-TIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 9955970 1511 IAA 1513
Cdd:cd03258 229 FAN 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
644-829 |
1.55e-23 |
|
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: 99.43 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS-------------VAYVPQqawiqnctlqenvl 710
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 fgkalnpkryqqtleacaLLADLEMlpggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHI 789
Cdd:cd03214 81 ------------------ALELLGL------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9955970 790 FDHVIGpegvLA---GKTRVLVTHGISFLPQ-TDFIIVLADGQV 829
Cdd:cd03214 137 LELLRR----LArerGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
644-827 |
2.95e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.93 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG--------SVAYVPQQA----WIqncTLQENVLF 711
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQEPallpWL---TVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 G----KALNPKRYQQTLEACAL--LADLEM-LPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH 784
Cdd:COG1116 104 GlelrGVPKAERRERARELLELvgLAGFEDaYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9955970 785 VAKHIFDHVIgpeGVLA--GKTRVLVTHGIS---FLpqTDFIIVLADG 827
Cdd:COG1116 173 TRERLQDELL---RLWQetGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
627-833 |
8.33e-23 |
|
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: 97.00 E-value: 8.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS------------VAYV 694
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 695 PQQAWIQNCTLQENVlfgkalnpkryqqtleacalladlemlpggdqteigekGINLSGGQRQRVSLARAVYSDADIFLL 774
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 775 DDPLSAVD----SHVAKHIFDHvigpegvLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMG 833
Cdd:cd03247 123 DEPTVGLDpiteRQLLSLIFEV-------LKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
642-810 |
9.30e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 9.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG--SVAYVPQQ---AWIQNCTLQENVLFGK--- 713
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGRwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 714 --------ALNPKRYQQTLEACALlADLEMLPggdqteIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHV 785
Cdd:NF040873 86 rglwrrltRDDRAAVDDALERVGL-ADLAGRQ------LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....*
gi 9955970 786 AKHIFDHVigPEGVLAGKTRVLVTH 810
Cdd:NF040873 155 RERIIALL--AEEHARGATVVVVTH 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
642-829 |
1.36e-22 |
|
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: 97.95 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSaLLGEMEKL-EGKVHMKG-----------------SVAYVPQQ-AWIQN 702
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 CTLQENVLFG-------KALNPKRYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLD 775
Cdd:cd03255 97 LTALENVELPlllagvpKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9955970 776 DPLSAVDSHVAKHIFDhVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQV 829
Cdd:cd03255 166 EPTGNLDSETGKEVME-LLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1289-1502 |
1.47e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 95.96 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLdlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAdiglhdlrsqlti 1368
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 ipqdpilfsgtlrmnldpFGSYSEediwwALELshlhtfvssqPAGLDFQcseggenLSVGQRQLVCLARALLRKSRILV 1448
Cdd:cd03216 66 ------------------FASPRD-----ARRA----------GIAMVYQ-------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 1449 LDEATAAIDL-ETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVA 1502
Cdd:cd03216 106 LDEPTAALTPaEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIAdRVTVLRDGRVV 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1289-1469 |
1.63e-22 |
|
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: 97.16 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVADIGlHDLRS 1364
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRILagllPPSAGEVLWNGEPIRDAR-EDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1365 QLTIIPQDPILFSG-TLRMNLDpF------GSYSEEDIWWALE---LSHLhtfvssqpagLDFQCSeggeNLSVGQRQLV 1434
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEavgLAGL----------ADLPVR----QLSAGQKRRV 140
|
170 180 190
....*....|....*....|....*....|....*
gi 9955970 1435 CLARALLRKSRILVLDEATAAIDLETDNLIQATIR 1469
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1273-1496 |
2.60e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 105.11 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1273 VVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDL-VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRI-D 1350
Cdd:PTZ00265 367 LVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInD 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1351 GLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNL-------------------DPFGSYSEEDIWWAL------------ 1399
Cdd:PTZ00265 447 SHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyyneDGNDSQENKNKRNSCrakcagdlndms 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1400 ------ELSH---------------------LHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEA 1452
Cdd:PTZ00265 527 nttdsnELIEmrknyqtikdsevvdvskkvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEA 606
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 9955970 1453 TAAIDLETDNLIQATI---RTQFDTCTVLtIAHRLNTIMDYTRVLVL 1496
Cdd:PTZ00265 607 TSSLDNKSEYLVQKTInnlKGNENRITII-IAHRLSTIRYANTIFVL 652
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1289-1499 |
2.65e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.52 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPIlfsgtlrmnlDPF-GSYSEEDIWWALE-----LSHLHTFV--SSQPAGLDFQCSEGGENLSVGQRQLVCLARAL 1440
Cdd:PRK13632 88 IFQNPD----------NQFiGATVEDDIAFGLEnkkvpPKKMKDIIddLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1441 LRKSRILVLDEATAAIDLETDNLIQATIRTQFDTC--TVLTIAHRLNTIMDYTRVLVLDKG 1499
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEG 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
644-834 |
3.58e-22 |
|
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: 97.42 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQ---AWiqNCTLQE 707
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEppaPF--GLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 NVLFG--------KALNPKRYQQTLEAcalLADLEMlpggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDADIFLLDDPL 778
Cdd:COG1120 95 LVALGryphlglfGRPSAEDREAVEEA---LERTGL------EHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 779 SAVDSHVAKHIFDHVIGpegvLA---GKTRVLVTHGISF-LPQTDFIIVLADGQVSEMGP 834
Cdd:COG1120 166 SHLDLAHQLEVLELLRR----LArerGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGP 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1289-1513 |
4.26e-22 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 96.97 E-value: 4.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIG---LHDLRSQ 1365
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQDPILFSG-TLRMN----LDPFGSYSEEDI----WWALELSHLHTFVSSQPagldfqcSEggenLSVGQRQLVCL 1436
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENvafpLREHTDLSEAEIrelvLEKLELVGLPGAADKMP-------SE----LSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1437 ARALLRKSRILVLDEATAAID----LETDNLIQaTIRTQFDTcTVLTIAHRLNTIMDY-TRVLVLDKGVVAEFDSPANLI 1511
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDpitsAVIDELIR-ELRDELGL-TSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELL 230
|
..
gi 9955970 1512 AA 1513
Cdd:COG1127 231 AS 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
634-810 |
4.70e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.04 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 634 FTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQ-AW 699
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEpAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 700 IQNcTLQENVLFGKALNPKRYQQTlEACALLADLEMlpggdQTEIGEKGI-NLSGGQRQRVSLARAVYSDADIFLLDDPL 778
Cdd:COG4619 86 WGG-TVRDNLPFPFQLRERKFDRE-RALELLERLGL-----PPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190
....*....|....*....|....*....|....
gi 9955970 779 SAVDSHVAKHIFDHVigpEGVLA--GKTRVLVTH 810
Cdd:COG4619 159 SALDPENTRRVEELL---REYLAeeGRAVLWVSH 189
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
642-846 |
7.48e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.49 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQEN 708
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGKALNPKRYQQTLEACALLADLEM-LPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVak 787
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMeFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-- 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 788 hifDHVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFA 846
Cdd:TIGR00958 653 ---EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1289-1505 |
1.03e-21 |
|
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: 94.89 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHdlRSQLTI 1368
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILF----------SGtLRMNLDPFGSySEEDIWWALELSHLHTFVSSQPAGldfqcseggenLSVGQRQLVCLAR 1438
Cdd:cd03259 77 VFQDYALFphltvaeniaFG-LKLRGVPKAE-IRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1439 ALLRKSRILVLDEATAAIDLETDNLIQATIRT---QFDTCTVLtIAHRLNTIMDYT-RVLVLDKGVVAEFD 1505
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKElqrELGITTIY-VTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
581-845 |
2.18e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.56 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 581 PLNMLPQLISNLTQASVSLKRIQQFLSQEELDPQSVERkTISPGyAITIHSGTFTWAQDlPPTLHSLDIQVPKGALVAVV 660
Cdd:PRK10790 297 PLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDR-PLQSG-RIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALV 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 661 GPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQNCTLQENVLFGKALNPKRYQQTLEAC 727
Cdd:PRK10790 374 GHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETV 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 728 ALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS-------HVAKHIFDHVigpegvl 800
Cdd:PRK10790 454 QLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSgteqaiqQALAAVREHT------- 526
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 9955970 801 agkTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSF 845
Cdd:PRK10790 527 ---TLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1290-1512 |
2.91e-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: 94.04 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHD-LRSQLTI 1368
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSG-TLRMNLD-----PFGSYSEEDIWWALEL-SHLHTFvSSQPAGldfqcseggeNLSVGQRQLVCLARALL 1441
Cdd:cd03224 80 VPEGRRIFPElTVEENLLlgayaRRRAKRKARLERVYELfPRLKER-RKQLAG----------TLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 1442 RKSRILVLDEATA--AIDLETDnlIQATIRT--QFDTcTVLTIAHRLNTIMDY-TRVLVLDKGVVAEFDSPANLIA 1512
Cdd:cd03224 149 SRPKLLLLDEPSEglAPKIVEE--IFEAIRElrDEGV-TILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1289-1515 |
2.98e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLD-LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLT 1367
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPI-LFSGTLRMNLDPFG------SYSE--EDIWWALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQLVCLAR 1438
Cdd:PRK13650 85 MVFQNPDnQFVGATVEDDVAFGlenkgiPHEEmkERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1439 ALLRKSRILVLDEATAAID----LETDNLIQAtIRTQFDTcTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIaAR 1514
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDpegrLELIKTIKG-IRDDYQM-TVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF-SR 230
|
.
gi 9955970 1515 G 1515
Cdd:PRK13650 231 G 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
644-834 |
3.90e-21 |
|
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: 93.78 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGKVHMKGS---------------VAYVPQQAWIQNC 703
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 704 TLQENVLFGKALNPKRYQQTLEACALLAdLEM--LPG--GDQTeigeKGINLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:cd03260 96 SIYDNVAYGLRLHGIKLKEELDERVEEA-LRKaaLWDevKDRL----HALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 780 AVDShVAKHIFDHVIGPegvLAGK-TRVLVTHGisfLPQ----TDFIIVLADGQVSEMGP 834
Cdd:cd03260 171 ALDP-ISTAKIEELIAE---LKKEyTIVIVTHN---MQQaarvADRTAFLLNGRLVEFGP 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
628-828 |
3.99e-21 |
|
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: 91.54 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 628 TIHSGTFTWAQdlPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHmkgsvayvpqqawiqnctlqe 707
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 nvLFGKALNPKRYQQTLEACALLadlemlpggDQteigekginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH--- 784
Cdd:cd00267 58 --IDGKDIAKLPLEELRRRIGYV---------PQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAsre 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9955970 785 -VAKHIFDHVIGpegvlaGKTRVLVTHGISFL-PQTDFIIVLADGQ 828
Cdd:cd00267 118 rLLELLRELAEE------GRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
644-841 |
6.95e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 93.20 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV------------HMKGSVAYVPQQAWI-QNCTLQENVL 710
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvardpaEVRRRIGYVPQEPALyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 F-------GKALNPKRYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS 783
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 784 HVAKHIFDHVIGpegvLA--GKTRVLVTHGISFLPQT-DFIIVLADGQVSEMGPYPALLQR 841
Cdd:COG1131 165 EARRELWELLRE----LAaeGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
626-841 |
7.32e-21 |
|
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: 98.44 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 626 AITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLG---EMEKLEGKVHMKG------------- 689
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGrdllelsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 690 SVAYVPQQAWIQNC--TLQENVLFG-KALNPKRYQQTLEACALLADLEMLPGGDQtEIGEkginLSGGQRQRVSLARAVY 766
Cdd:COG1123 84 RIGMVFQDPMTQLNpvTVGDQIAEAlENLGLSRAEARARVLELLEAVGLERRLDR-YPHQ----LSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 767 SDADIFLLDDPLSAVDSHVAKHIFDHvIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGPYPALLQR 841
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDL-LRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1289-1501 |
1.55e-20 |
|
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: 91.78 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLD--LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDL---- 1362
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1363 RSQLTIIPQD----PILfsgTLRMN----LDPFGSYSEEDIWWALEL-------SHLHTFVSsqpagldfqcseggeNLS 1427
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENvelpLLLAGVPKKERRERAEELlervglgDRLNHYPS---------------ELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 1428 VGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIR--TQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVV 1501
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
644-831 |
1.66e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.03 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSaLLGEMEKL-EGKVHMKG-----------------SVAYVPQQA-WIQNCT 704
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarlrrrHIGFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLFGKALNPKRYQQTLE-ACALLADLEM------LPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:COG1136 103 ALENVALPLLLAGVSRKERRErARELLERVGLgdrldhRPS-----------QLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 778 LSAVDSHVAKHIFDhvigpegVLA------GKTRVLVTHGISFLPQTDFIIVLADGQVSE 831
Cdd:COG1136 172 TGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
644-840 |
1.75e-20 |
|
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: 92.18 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV--------HMKGS--------VAYVPQQ-AWIQNCTLQ 706
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisGLSEAelyrlrrrMGMLFQSgALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFG----KALNPKRYQQ----TLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPL 778
Cdd:cd03261 96 ENVAFPlrehTRLSEEEIREivleKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 779 SAVDShVAKHIFDHVIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQVSEMGPYPALLQ 840
Cdd:cd03261 165 AGLDP-IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1289-1508 |
2.36e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPI-LFSGTLRMNLDPFG------SYSE--EDIWWALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQLVCLARA 1439
Cdd:PRK13635 86 VFQNPDnQFVGATVQDDVAFGlenigvPREEmvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1440 LLRKSRILVLDEATAAIDLETDNLIQATIRTQFD--TCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPA 1508
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1289-1498 |
3.89e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 89.14 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVrYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGlnvadiglhdlRS 1364
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSS----LFRALaglwPWGSGRIGMPE-----------GE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1365 QLTIIPQDPILFSGTLRMNLdpfgSYSeediwWALELSHlhtfvssqpagldfqcseggenlsvGQRQLVCLARALLRKS 1444
Cdd:cd03223 65 DLLFLPQRPYLPLGTLREQL----IYP-----WDDVLSG-------------------------GEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 1445 RILVLDEATAAIDLETDNLIQATIRTQFdtCTVLTIAHR--LNTImdYTRVLVLDK 1498
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHRpsLWKF--HDRVLDLDG 162
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
644-810 |
4.75e-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: 89.85 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG------------SVAYVPQQ-AWIQNCTLQENVL 710
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHAdGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 F-----GKALNPKRYQQTLEACALlADLEMLPGGdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH- 784
Cdd:COG4133 98 FwaalyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAg 166
|
170 180
....*....|....*....|....*....
gi 9955970 785 ---VAKHIFDHvigpegVLAGKTRVLVTH 810
Cdd:COG4133 167 valLAELIAAH------LARGGAVLLTTH 189
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
644-834 |
4.78e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.67 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGemekLE----GKVHMKG------------SVAYVPQQ-AWIQNCTLQ 706
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGrdlftnlpprerRVGFVFQHyALFPHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFG---KALNPKRYQQTLEACALLADLEML----PGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:COG1118 94 ENIAFGlrvRPPSKAEIRARVEELLELVQLEGLadryPS-----------QLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 780 AVDSHVAK-------HIFDHVigpegvlaGKTRVLVTH------GISflpqtDFIIVLADGQVSEMGP 834
Cdd:COG1118 163 ALDAKVRKelrrwlrRLHDEL--------GGTTVFVTHdqeealELA-----DRVVVMNQGRIEQVGT 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1289-1503 |
4.95e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.50 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADI---GLHDLRSQ 1365
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQD-PILFSGTLRMN----LDPFGsYSEEDIWW----ALELSHLHTFVSSQPagldfqcseggENLSVGQRQLVCL 1436
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENvalpLRVTG-KSRKEIRRrvreVLDLVGLSDKAKALP-----------HELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1437 ARALLRKSRILVLDEATAAIDLET-DNLIQAtirtqFDT-----CTVLtIA-HRLNTIMDY-TRVLVLDKGVVAE 1503
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETsWEIMEL-----LEEinrrgTTVL-IAtHDLELVDRMpKRVLELEDGRLVR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1289-1512 |
5.00e-20 |
|
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: 90.64 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAD---IGLHDLRSQ 1365
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQDPILFSG-TLRMN----LDPFGSYSEEDIwWALELSHLHTfvssqpAGLdfqcsEGGEN-----LSVGQRQLVC 1435
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENvafpLREHTRLSEEEI-REIVLEKLEA------VGL-----RGAEDlypaeLSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1436 LARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDT--CTVLTIAHRLNTIM---DytRVLVLDKGVVAEFDSPANL 1510
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDLDTAFaiaD--RIAVLYDGKIVAEGTPEEL 224
|
..
gi 9955970 1511 IA 1512
Cdd:cd03261 225 RA 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
627-833 |
2.78e-19 |
|
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: 88.90 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAqDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAY 693
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 694 VPQQAWI-QNCTLQENV-LFGKALNPKRYQQTLEACALLADLEMLPGG------DQteigekginLSGGQRQRVSLARAV 765
Cdd:cd03295 80 VIQQIGLfPHMTVEENIaLVPKLLKWPKEKIRERADELLALVGLDPAEfadrypHE---------LSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 766 YSDADIFLLDDPLSAVDSHVAKHIFDHVIGPEGVLaGKTRVLVTHGI-SFLPQTDFIIVLADGQVSEMG 833
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVG 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
644-833 |
2.84e-19 |
|
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: 88.33 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG----------------SVAYVPQQAwiqnctlqe 707
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQDP--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 nvlfGKALNP----------------KRYQQTLEACALLADLEMLPGGDQ------TEigekginLSGGQRQRVSLARAV 765
Cdd:cd03257 92 ----MSSLNPrmtigeqiaeplrihgKLSKKEARKEAVLLLLVGVGLPEEvlnrypHE-------LSGGQRQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 766 YSDADIFLLDDPLSAVDSHVAKHIFDhvigpegVLA------GKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMG 833
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
636-833 |
4.70e-19 |
|
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: 87.08 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 636 WAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQN 702
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 CTLQENvlfgkaLNPKRYQQTLEACALLadlemlpggdqtEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:cd03369 96 GTIRSN------LDPFDEYSDEEIYGAL------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 783 SHvAKHIFDHVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMG 833
Cdd:cd03369 158 YA-TDALIQKTIREE--FTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
638-829 |
7.09e-19 |
|
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: 87.14 E-value: 7.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 638 QDLPPTLHSldiqvpkGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS-------------VAYVPQQAWIQNCT 704
Cdd:cd03248 31 QDVSFTLHP-------GEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLFGKALNP----KRYQQTLEACALLADLEMlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:cd03248 104 LQDNIAYGLQSCSfecvKEAAQKAHAHSFISELAS---GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9955970 781 VD--SHVAKH--IFDhviGPEgvlaGKTRVLVTHGISFLPQTDFIIVLADGQV 829
Cdd:cd03248 181 LDaeSEQQVQqaLYD---WPE----RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
642-834 |
7.39e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.13 E-value: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGemekLE----GKVHMKG-----------SVAYVPQQ-AWIQNCTL 705
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG----LEdptsGEILIGGrdvtdlppkdrNIAMVFQSyALYPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 706 QENVLFG----KALNPKRYQQTLEACALLaDLEML----PGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:COG3839 93 YENIAFPlklrKVPKAEIDRRVREAAELL-GLEDLldrkPK-----------QLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 778 LSAVDshvAKhifdhvigpegvLAGKTR--------------VLVTHGisflpQT------DFIIVLADGQVSEMGP 834
Cdd:COG3839 161 LSNLD---AK------------LRVEMRaeikrlhrrlgtttIYVTHD-----QVeamtlaDRIAVMNDGRIQQVGT 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
644-829 |
1.15e-18 |
|
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: 85.14 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV------------HMKGSVAYVPQQA-WIQNCTLQENvl 710
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikkepeEVKRRIGYLPEEPsLYENLTVREN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 fgkalnpkryqqtleacalladlemlpggdqteigekgINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIF 790
Cdd:cd03230 94 --------------------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9955970 791 DHVIgpEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQV 829
Cdd:cd03230 136 ELLR--ELKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
624-849 |
1.19e-18 |
|
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: 87.27 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 624 GYAITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAWIQN 702
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 CT--LQENVLFGKA----LNPK------RYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDAD 770
Cdd:cd03288 97 LSiiLQDPILFSGSirfnLDPEckctddRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 771 IFLLDDPLSAVDShVAKHIFDHVIgpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALL-QRNGSFANFL 849
Cdd:cd03288 177 ILIMDEATASIDM-ATENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
643-829 |
1.23e-18 |
|
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: 85.77 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 643 TLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG----------SVAYVPQQAWIQ--NCTLQENVL 710
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDYQlfTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FGKALNPKRYQQTLEacaLLADLEMLPGGDQTEIgekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIF 790
Cdd:cd03226 95 LGLKELDAGNEQAET---VLKDLDLYALKERHPL-----SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9955970 791 DhVIGpEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQV 829
Cdd:cd03226 167 E-LIR-ELAAQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1292-1503 |
1.30e-18 |
|
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: 86.72 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1292 RNYSVRYRpGLdLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDlRSQLTIIP- 1370
Cdd:cd03219 4 RGLTKRFG-GL-VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1371 -QDPILFSG-TLRMNLD---------------PFGSYSE--EDIWWALELSHLHTfVSSQPAGldfqcseggeNLSVGQR 1431
Cdd:cd03219 81 fQIPRLFPElTVLENVMvaaqartgsglllarARREEREarERAEELLERVGLAD-LADRPAG----------ELSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1432 QLVCLARALLRKSRILVLDEATAAIDL-ETDNLIQATIRTQFDTCTVLTIAHRLNTIMDY-TRVLVLDKG-VVAE 1503
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGrVIAE 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
642-843 |
2.83e-18 |
|
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: 86.06 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG------------SVAYVPQQAWI-QNCTLQEN 708
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLyDRLTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGKALNPKRYQQTLEACALLAD-LEMLPGGDQTeIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDShVAK 787
Cdd:COG4555 95 IRYFAELYGLFDEELKKRIEELIElLGLEEFLDRR-VGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MAR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 788 HIF-DHVIGpegvLA--GKTRVLVTHGISFLPQT-DFIIVLADGQVSEMGPYPALLQRNG 843
Cdd:COG4555 169 RLLrEILRA----LKkeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
633-834 |
4.26e-18 |
|
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: 85.08 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 633 TFTWAQDlPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAW 699
Cdd:COG1122 7 SFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 700 IQ--NCTLQENVLFG---KALNP----KRYQQTLEACALladlemlpggdqTEIGEKGI-NLSGGQRQRVSLARAVYSDA 769
Cdd:COG1122 86 DQlfAPTVEEDVAFGpenLGLPReeirERVEEALELVGL------------EHLADRPPhELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 770 DIFLLDDPLSAVDSHVAKHIFDHVIGpegvL--AGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGP 834
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKR----LnkEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
644-828 |
4.98e-18 |
|
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: 83.39 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG---------------SVAYVPQQ-AWIQNCTLQE 707
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDfALFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 NVLFGkalnpkryqqtleacalladlemlpggdqteigekginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAK 787
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9955970 788 HIFDHVigpEGVLA--GKTRVLVTHGISFLPQ-TDFIIVLADGQ 828
Cdd:cd03229 138 EVRALL---KSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1289-1505 |
6.40e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrPGLdLVLRDLSLHVHGGEKVGIVGRTGAGKSsmTL--CLFRILEAAKGEIRIDGLNVADIGLHD-LRSQ 1365
Cdd:COG1129 5 LEMRGISKSF-GGV-KALDGVSLELRPGEVHALLGENGAGKS--TLmkILSGVYQPDSGEILLDGEPVRFRSPRDaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQDPILF-----------------SGTL---RMNLDpfgsyseediwwALELshLHTFvssqpaGLDFQCSEGGEN 1425
Cdd:COG1129 81 IAIIHQELNLVpnlsvaeniflgreprrGGLIdwrAMRRR------------AREL--LARL------GLDIDPDTPVGD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1426 LSVGQRQLVCLARALLRKSRILVLDEATAAIDL-ETDNLIqATIRT-QFDTCTVLTIAHRLNTIMDYT-RVLVL-DKGVV 1501
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTErEVERLF-RIIRRlKAQGVAIIYISHRLDEVFEIAdRVTVLrDGRLV 219
|
....
gi 9955970 1502 AEFD 1505
Cdd:COG1129 220 GTGP 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1289-1504 |
1.07e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 85.88 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLV--LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEA---AKGEIRIDGLNVADIGLHDLR 1363
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 ----SQLTIIPQDPilfsgtlrMN-LDP--------------FGSYSEEDIW----WALELSHLHT---FVSSQPagldF 1417
Cdd:COG0444 82 kirgREIQMIFQDP--------MTsLNPvmtvgdqiaeplriHGGLSKAEAReraiELLERVGLPDperRLDRYP----H 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1418 QcseggenLSVGQRQLVCLARALLRKSRILVLDEATAAIDLetdnLIQATI-------RTQFDTcTVLTIAHrlntimdy 1490
Cdd:COG0444 150 E-------LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQIlnllkdlQRELGL-AILFITH-------- 209
|
250
....*....|....
gi 9955970 1491 trvlvlDKGVVAEF 1504
Cdd:COG0444 210 ------DLGVVAEI 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
633-841 |
1.19e-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: 84.08 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 633 TFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWiQNCTLQenVLF- 711
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA-FRRRVQ--MVFq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 --GKALNP-KRYQQTLEACALLADL--------EMLpggDQTEIGE-----KGINLSGGQRQRVSLARAVYSDADIFLLD 775
Cdd:COG1124 87 dpYASLHPrHTVDRILAEPLRIHGLpdreeriaELL---EQVGLPPsfldrYPHQLSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 776 DPLSAVDSHVAKHIFDhvigpegVLA------GKTRVLVTHG---ISFLpqTDFIIVLADGQVSEMGPYPALLQR 841
Cdd:COG1124 164 EPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHDlavVAHL--CDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1289-1501 |
1.39e-17 |
|
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: 83.23 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADigLHD-----LR 1363
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSD--LRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 SQLTIIPQDPILFSgtlrmNLDPFgsyseEDIWWALELS-HLHTFVSSQ-PAGLDFQCSEGGEN-----LSVGQRQLVCL 1436
Cdd:cd03292 78 RKIGVVFQDFRLLP-----DRNVY-----ENVAFALEVTgVPPREIRKRvPAALELVGLSHKHRalpaeLSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 1437 ARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYT--RVLVLDKGVV 1501
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTrhRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
642-833 |
1.82e-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: 83.54 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-----------SVAYVPQQ-AWIQNCTLQENV 709
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 710 LFGKALNPKRY----QQTLEACALLADLEMLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHV 785
Cdd:cd03296 96 AFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQ----LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 786 AKH-------IFDHVigpegvlaGKTRVLVTHGIS-FLPQTDFIIVLADGQVSEMG 833
Cdd:cd03296 172 RKElrrwlrrLHDEL--------HVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
643-833 |
2.13e-17 |
|
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: 82.69 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 643 TLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-----------SVAYVPQQ-AWIQNCTLQENVL 710
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FGKALN--PKRY--QQTLEACALLaDLEMLpggdqteIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVA 786
Cdd:cd03301 95 FGLKLRkvPKDEidERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9955970 787 KHIFDHVIGPEGVLaGKTRVLVTHG-ISFLPQTDFIIVLADGQVSEMG 833
Cdd:cd03301 167 VQMRAELKRLQQRL-GTTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
642-840 |
3.86e-17 |
|
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: 82.10 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--------------VAYVPQ-QAWIQNCTLQ 706
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFG-KALNPKRYQQTLE-ACALLADL-EMLpggdqteiGEKGINLSGGQRQRVSLARAVYSDADIFLLDDP---LSA 780
Cdd:cd03224 94 ENLLLGaYARRRAKRKARLErVYELFPRLkERR--------KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 781 VdshVAKHIFDHV--IGPEGVlagkTRVLVTHGISF-LPQTDFIIVLADGQVSEMGPYPALLQ 840
Cdd:cd03224 166 K---IVEEIFEAIreLRDEGV----TILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1289-1511 |
3.88e-17 |
|
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: 82.38 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRpglDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGlnvADI-GLHDLRSQLT 1367
Cdd:cd03299 1 LKVENLSKDWK---EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDItNLPPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPILFSGT---------LRMNLDPFGSYSEE--DIWWALELSHLhtfVSSQPagldfqcseggENLSVGQRQLVCL 1436
Cdd:cd03299 75 YVPQNYALFPHMtvykniaygLKKRKVDKKEIERKvlEIAEMLGIDHL---LNRKP-----------ETLSGGEQQRVAI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 1437 ARALLRKSRILVLDEATAAIDLET-DNLIQ--ATIRTQFDTcTVLTIAHRLNTI-MDYTRVLVLDKGVVAEFDSPANLI 1511
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDVRTkEKLREelKKIRKEFGV-TVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1275-1513 |
3.98e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 86.66 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1275 EGSRPPEGWPPRGEV--EFRNYSVRY-------RPGLDLV--LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRiLEAA 1343
Cdd:COG4172 260 EPRGDPRPVPPDAPPllEARDLKVWFpikrglfRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1344 KGEIRIDGLNVADIG---LHDLRSQLTIIPQDPilFsGTL--RMN-----------LDPFGSYSEED--IWWALELSHL- 1404
Cdd:COG4172 339 EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLspRMTvgqiiaeglrvHGPGLSAAERRarVAEALEEVGLd 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1405 --------HTFvssqpagldfqcseggenlSVGQRQLVCLARALLRKSRILVLDEATAAIDLetdnLIQATI-------- 1468
Cdd:COG4172 416 paarhrypHEF-------------------SGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQAQIldllrdlq 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1469 -RTQFdtcTVLTIAHRLN---TIMDytRVLVLDKGVVAE-------FDSPAN-----LIAA 1513
Cdd:COG4172 473 rEHGL---AYLFISHDLAvvrALAH--RVMVMKDGKVVEqgpteqvFDAPQHpytraLLAA 528
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
644-829 |
6.68e-17 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 82.03 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG----------------SVAYVPQQ-AWIQNCTLQ 706
Cdd:COG3638 19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrrRIGMIFQQfNLVPRLSVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFG--------KALNPKRYQQTLE-ACALLADLEMLPGGDQteigeKGINLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:COG3638 99 TNVLAGrlgrtstwRSLLGLFPPEDRErALEALERVGLADKAYQ-----RADQLSGGQQQRVAIARALVQEPKLILADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 778 LSAVDSHVAKHIFDhvigpegVLA------GKTRVLVTHGISFLPQ-TDFIIVLADGQV 829
Cdd:COG3638 174 VASLDPKTARQVMD-------LLRriaredGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
644-841 |
7.92e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 7.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWI-QNCTLQENV 709
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTpEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 710 LFGKA--------LNPK---RYQQTLEACALladlemlpggdqTEIGEKGI-NLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:PRK11231 98 AYGRSpwlslwgrLSAEdnaRVNQAMEQTRI------------NHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 778 LSAVD-SHVAKhifdhVIGPEGVL--AGKTRVLVTHGISflpQT----DFIIVLADGQVSEMG-PY----PALLQR 841
Cdd:PRK11231 166 TTYLDiNHQVE-----LMRLMRELntQGKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGtPEevmtPGLLRT 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1308-1508 |
8.00e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.63 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1308 DLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIG---LHDLRSQLTIIPQDPilfSGTL--RM 1382
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnpRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1383 N--------LDPFGSYSEED----IWWALEL-----SHL----HTFvssqpagldfqcseggenlSVGQRQLVCLARALL 1441
Cdd:COG4608 113 TvgdiiaepLRIHGLASKAErrerVAELLELvglrpEHAdrypHEF-------------------SGGQRQRIGIARALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1442 RKSRILVLDEATAAIDLEtdnlIQATI-------RTQFDtCTVLTIAHRLNT---IMDytRVLVLDKGVVAE-------F 1504
Cdd:COG4608 174 LNPKLIVCDEPVSALDVS----IQAQVlnlledlQDELG-LTYLFISHDLSVvrhISD--RVAVMYLGKIVEiaprdelY 246
|
....
gi 9955970 1505 DSPA 1508
Cdd:COG4608 247 ARPL 250
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1289-1507 |
8.56e-17 |
|
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: 80.98 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLD--LVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVADIGlhdl 1362
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKST----LLRIIagleRPTSGEVLVDGEPVTGPG---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1363 rSQLTIIPQDPILFS----------GtLRMNLDPFGSYSEEdiwwALELshLHTFvssqpaGLdfqcsEGGEN-----LS 1427
Cdd:cd03293 73 -PDRGYVFQQDALLPwltvldnvalG-LELQGVPKAEARER----AEEL--LELV------GL-----SGFENayphqLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1428 VGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATI-----RTQFdtcTVLTIAHRLN-TIMDYTRVLVLDKG-- 1499
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTHDIDeAVFLADRVVVLSARpg 210
|
....*....
gi 9955970 1500 -VVAEFDSP 1507
Cdd:cd03293 211 rIVAEVEVD 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1289-1507 |
9.12e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.54 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRIL---EAAKGEIRIDGLNVADIGLHDLRSQ 1365
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQDPIlfsgtlrmnlDPF-GSYSEEDIWWALE-----LSHLHTFVS---SQPAGLDFQCSEGgENLSVGQRQLVCL 1436
Cdd:PRK13640 86 VGIVFQNPD----------NQFvGATVGDDVAFGLEnravpRPEMIKIVRdvlADVGMLDYIDSEP-ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1437 ARALLRKSRILVLDEATAAIDLETDNLIQATIR--TQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSP 1507
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1284-1505 |
9.61e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 81.67 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1284 PPRGEVEFRNYSVRYRPGLD--LVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVADI 1357
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIagleKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1358 GlhdlrSQLTIIPQDPILFsgtlrmnldP---------FG--------SYSEEDIWWALELSHLHTFVSSQPAgldfqcs 1420
Cdd:COG1116 79 G-----PDRGVVFQEPALL---------PwltvldnvaLGlelrgvpkAERRERARELLELVGLAGFEDAYPH------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1421 eggeNLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQ---ATIRTQFDTcTVLTIAH------RLNtimdyT 1491
Cdd:COG1116 138 ----QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQdelLRLWQETGK-TVLFVTHdvdeavFLA-----D 207
|
250
....*....|....*..
gi 9955970 1492 RVLVLDKG---VVAEFD 1505
Cdd:COG1116 208 RVVVLSARpgrIVEEID 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1289-1502 |
1.20e-16 |
|
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: 81.28 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSS-MTLCLFRILEAAKGEIRI-----DGLNVAD----IG 1358
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTlLSLITGDLPPTYGNDVRLfgerrGGEDVWElrkrIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1359 L------HDLRSQLTIIpqDPIL--FSGTLrmnlDPFGSYSEEDI----WW--ALELSHLhtfvssqpAGLDFQcsegge 1424
Cdd:COG1119 82 LvspalqLRFPRDETVL--DVVLsgFFDSI----GLYREPTDEQRerarELleLLGLAHL--------ADRPFG------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1425 NLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRT--QFDTCTVLTIAHRLNTIMD-YTRVLVLDKG-V 1500
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLLLKDGrV 221
|
..
gi 9955970 1501 VA 1502
Cdd:COG1119 222 VA 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
644-829 |
1.29e-16 |
|
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: 81.08 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS----------------VAYVPQQ-AWIQNCTLQ 706
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFGKA-----------LNPKryQQTLEACALLADLEMLPGGDQteigeKGINLSGGQRQRVSLARAVYSDADIFLLD 775
Cdd:cd03256 97 ENVLSGRLgrrstwrslfgLFPK--EEKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 776 DPLSAVDSHVAKHIFDhvigpegVLA------GKTRVLVTHGISF-LPQTDFIIVLADGQV 829
Cdd:cd03256 170 EPVASLDPASSRQVMD-------LLKrinreeGITVIVSLHQVDLaREYADRIVGLKDGRI 223
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
311-602 |
1.33e-16 |
|
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: 82.21 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 311 FLISACFKLIQDLLSFINPQLLSILIRFIsnPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFV-TGVKFRTGIMGVI 389
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV--IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAArLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 390 YRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLA-PFLNLLWSAPLQIILAIYFL----WQnlgpsvLAGVAFmvLLIP 464
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVsSGLLQLLSDVLTLIGALVILfylnWK------LTLVAL--LLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 465 LNGAVAV----KMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPS----FLKQVEGIRQGELQLLRTAAYLHTTTT 536
Cdd:cd07346 151 LYVLILRyfrrRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 537 FTWMCSPFLVtlitLWVYVYVDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd07346 231 LLTALGTALV----LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1289-1503 |
1.55e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 80.47 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLV--LRDLSLHVHGGEKVGIVGRTGAGKSsmTL--CLFRILEAAKGEIRIDGLNVADIG---LHD 1361
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKS--TLlnILGGLDRPTSGEVLIDGQDISSLSereLAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 LRSQ-LTIIPQDPILFSGT-----LRMNLDPFGSYSEEDIWWALEL-------SHLHTFVSSqpagldfqcseggenLSV 1428
Cdd:COG1136 83 LRRRhIGFVFQFFNLLPELtalenVALPLLLAGVSRKERRERARELlervglgDRLDHRPSQ---------------LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1429 GQRQLVCLARALLRKSRILVLDEATAAIDLET-DNLIQ--ATIRTQFDTcTVLTIAH--RLNTIMDytRVLVLDKGVVAE 1503
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLEllRELNRELGT-TIVMVTHdpELAARAD--RVIRLRDGRIVS 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
626-834 |
1.71e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 626 AITIHSGTFTWaQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS----------VAYVP 695
Cdd:PRK15056 6 GIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 696 QQA---WIQNCTLQENVLFGK------ALNPKRYQQTLEACALlADLEMLPGgDQTEIGEkginLSGGQRQRVSLARAVY 766
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwLRRAKKRDRQIVTAAL-ARVDMVEF-RHRQIGE----LSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 767 SDADIFLLDDPLSAVDSHVAKHIFDHVigPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGP 834
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLL--RELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGP 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
641-783 |
2.71e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.68 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 641 PPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSV--------AYVPQQ----AWIqncTLQEN 708
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPWL---NVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGKALN--PK--RYQQTLEACAL--LADLEmlpggdQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:COG4525 97 VAFGLRLRgvPKaeRRARAEELLALvgLADFA------RRRIWQ----LSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
.
gi 9955970 783 S 783
Cdd:COG4525 167 A 167
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1289-1512 |
2.74e-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: 80.04 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVlRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSG-TLRMN--LDP-FGSYSEEDI-WWALELSHLhtfVSSQPAGL-DFQCSEggenLSVGQRQLVCLARALLR 1442
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIrERADELLAL---VGLDPAEFaDRYPHE----LSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1443 KSRILVLDEATAAIDLET-DNLIQATIRTQFDTC-TVLTIAHRLN-TIMDYTRVLVLDKGVVAEFDSPANLIA 1512
Cdd:cd03295 153 DPPLLLMDEPFGALDPITrDQLQEEFKRLQQELGkTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1289-1511 |
2.94e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.14 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAD--IGLHDLR--- 1363
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 ----SQLTIIPQ----DPILFsGTLRMNldpfGSYSEEDIWWALEL-------SHLHTFVSSqpagldfqcseggenLSV 1428
Cdd:PRK09493 80 gmvfQQFYLFPHltalENVMF-GPLRVR----GASKEEAEKQARELlakvglaERAHHYPSE---------------LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1429 GQRQLVCLARALLRKSRILVLDEATAAIDLEtdnLIQATIRTQFDTC----TVLTIAHRLNTIMDY-TRVLVLDKGVVAE 1503
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKVMQDLAeegmTMVIVTHEIGFAEKVaSRLIFIDKGRIAE 216
|
....*...
gi 9955970 1504 FDSPANLI 1511
Cdd:PRK09493 217 DGDPQVLI 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1289-1505 |
3.16e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrPGLdLVLRDLSLHVHGGEKVGIVGRTGAGKSsmTL--CLFRILEAAKGEIRIDG--LNVAD-------- 1356
Cdd:COG3845 6 LELRGITKRF-GGV-VANDDVSLTVRPGEIHALLGENGAGKS--TLmkILYGLYQPDSGEILIDGkpVRIRSprdaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1357 IGLhdlrsqltiIPQDPILFsgtlrmnlDPF--------GSysEEDIWWALELSHLHTFVS--SQPAGLDFQCSEGGENL 1426
Cdd:COG3845 82 IGM---------VHQHFMLV--------PNLtvaenivlGL--EPTKGGRLDRKAARARIRelSERYGLDVDPDAKVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1427 SVGQRQLVCLARALLRKSRILVLDEATAAI-DLETDNLIqATIRtQF--DTCTVLTIAHRLNTIMDYT-RVLVLDKG-VV 1501
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELF-EILR-RLaaEGKSIIFITHKLREVMAIAdRVTVLRRGkVV 220
|
....
gi 9955970 1502 AEFD 1505
Cdd:COG3845 221 GTVD 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
648-849 |
3.73e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.41 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 648 DIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGsvayvpqqawiQNCT------------LQENVLF---- 711
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG-----------QDLTalppaerpvsmlFQENNLFphlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 -----GKALNPK-RY---QQTLEACAL----LADLEM-LPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:COG3840 88 vaqniGLGLRPGlKLtaeQRAQVEQALervgLAGLLDrLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 778 LSAVD-----------SHVAKHifdhvigpegvlAGKTRVLVTHGIS-FLPQTDFIIVLADGQVSEMGPYPALLQRNGS- 844
Cdd:COG3840 157 FSALDpalrqemldlvDELCRE------------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGEPPp 224
|
....*.
gi 9955970 845 -FANFL 849
Cdd:COG3840 225 aLAAYL 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
644-834 |
3.83e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.89 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGKVHMKGSVAYVPQQAWIQ----------------N 702
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 CTLQENVLFGKALN---------PKRYQQTLEACALLADLemlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDADIFL 773
Cdd:PRK14267 100 LTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 774 LDDPLSAVDSHVAKHIfdhvigPEGVLAGK---TRVLVTHGISFLPQ-TDFIIVLADGQVSEMGP 834
Cdd:PRK14267 173 MDEPTANIDPVGTAKI------EELLFELKkeyTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGP 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
644-834 |
4.16e-16 |
|
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: 83.41 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG----------------SVAYVPQQAWIQ-NC--T 704
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDPYSSlNPrmT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLFG----KALNP----KRYQQTLEACALLAD-LEMLPGGdqteigekginLSGGQRQRVSLARAVYSDADIFLLD 775
Cdd:COG1123 361 VGDIIAEPlrlhGLLSRaerrERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 776 DPLSAVDSHVAKHIFDhvigpegVLA------GKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGP 834
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1290-1454 |
4.30e-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: 79.26 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDL-RSQLTI 1368
Cdd:COG0410 5 EVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSG-TLRMNLD------PFGSYSEEDIWWALEL-SHLHTFvSSQPAGldfqcseggeNLSVGQRQLVCLARAL 1440
Cdd:COG0410 83 VPEGRRIFPSlTVEENLLlgayarRDRAEVRADLERVYELfPRLKER-RRQRAG----------TLSGGEQQMLAIGRAL 151
|
170
....*....|....
gi 9955970 1441 LRKSRILVLDEATA 1454
Cdd:COG0410 152 MSRPKLLLLDEPSL 165
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1306-1484 |
4.97e-16 |
|
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: 78.91 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQ----LTIIPQDPILFSGTLR 1381
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1382 MNLdPFGS-YSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLE- 1459
Cdd:cd03290 97 ENI-TFGSpFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180
....*....|....*....|....*..
gi 9955970 1460 TDNLIQATIRT--QFDTCTVLTIAHRL 1484
Cdd:cd03290 176 SDHLMQEGILKflQDDKRTLVLVTHKL 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
642-826 |
5.04e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.68 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEME---KLEGKVHMKGS-----------VAYVPQQAWI-QNCTLQ 706
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRrltalpaeqrrIGILFQDDLLfPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFGKALNPKRYQQTLEACALLADLEMlpggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHV 785
Cdd:COG4136 95 ENLAFALPPTIGRAQRRARVEQALEEAGL------AGFADRDPAtLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9955970 786 AKHI----FDHVigpegvlagKTR----VLVTHGISFLPQTDFIIVLAD 826
Cdd:COG4136 169 RAQFrefvFEQI---------RQRgipaLLVTHDEEDAPAAGRVLDLGN 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
642-839 |
5.19e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.20 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQ-NCTLQE 707
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLSfEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 NVLFGKALNPKRYQQTLEACALLADlEMLPGGDQTEIGEKGI-NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVA 786
Cdd:PRK09536 97 VVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9955970 787 KHIFDHVigPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGPYPALL 839
Cdd:PRK09536 176 VRTLELV--RRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1305-1503 |
7.99e-16 |
|
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: 78.93 E-value: 7.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDL------RS-QLT---------- 1367
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlgiaRTfQNPrlfpeltvle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 --IIPQDPILFSGTLRMNLDPFGSYSEED-----IWWALELSHLHTfVSSQPAGldfqcseggeNLSVGQRQLVCLARAL 1440
Cdd:COG0411 99 nvLVAAHARLGRGLLAALLRLPRARREERearerAEELLERVGLAD-RADEPAG----------NLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1441 LRKSRILVLDEATAAIDL-ETDNLIQ--ATIRTQFDTcTVLTIAHRLNTIMDYT-RVLVLDKG-VVAE 1503
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPeETEELAEliRRLRDERGI-TILLIEHDMDLVMGLAdRIVVLDFGrVIAE 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
645-877 |
9.39e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 80.54 E-value: 9.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 645 HSLDI--QVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-----------------SVAYVPQQAWI-QNCT 704
Cdd:TIGR02142 12 FSLDAdfTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLFG--KALNPKRYQQTLEACALLAD---LEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:TIGR02142 92 VRGNLRYGmkRARPSERRISFERVIELLGIghlLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 780 AVDSHVAKHIFDHVigpeGVLAGKTR---VLVTHGIS-FLPQTDFIIVLADGQVSEMGPyPALLQRNGSFanflcNYAPD 855
Cdd:TIGR02142 161 ALDDPRKYEILPYL----ERLHAEFGipiLYVSHSLQeVLRLADRVVVLEDGRVAAAGP-IAEVWASPDL-----PWLAR 230
|
250 260
....*....|....*....|..
gi 9955970 856 EDQGHLEDSwtALEGAEDKEAL 877
Cdd:TIGR02142 231 EDQGSLIEG--VVAEHDQHYGL 250
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1289-1503 |
9.83e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 80.51 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLV--LRDLSLHVHGGEKVGIVGRTGAGKSsmTL--CLFRiLEAA-KGEIRIDGLNVADI---GLH 1360
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS--TLirCINL-LERPtSGSVLVDGVDLTALserELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1361 DLRSQLTIIPQDPILFSG-TLRMNldpfgsyseedIWWALELSH------------LHTFV------SSQPAgldfqcse 1421
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAEN-----------VALPLEIAGvpkaeirkrvaeLLELVglsdkaDAYPS-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1422 ggeNLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETD----NLIQaTIRTQFDTcTVLTIAHRLN---TIMDytRVL 1494
Cdd:COG1135 140 ---QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLK-DINRELGL-TIVLITHEMDvvrRICD--RVA 212
|
....*....
gi 9955970 1495 VLDKGVVAE 1503
Cdd:COG1135 213 VLENGRIVE 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
644-837 |
1.05e-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: 78.24 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGemekLE----GKVHMKG-----------------SVAYVpQQAW--I 700
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAG----LDrptsGTVRLAGqdlfaldedararlrarHVGFV-FQSFqlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 701 QNCTLQENV-----LFGKALNPKRYQQTLEACALLADLEMLPGGdqteigekginLSGGQRQRVSLARAVYSDADIFLLD 775
Cdd:COG4181 103 PTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 776 DPLSAVDSHVAKHIFDhvigpegvL-------AGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPA 837
Cdd:COG4181 172 EPTGNLDAATGEQIID--------LlfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
644-829 |
1.20e-15 |
|
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: 78.11 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV----------------HMKGSVAYVPQQ-AWIQNCTLQ 706
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIllegtditklrgkklrKLRRRIGMIFQHyNLIERLTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFG---------KALNPKRYQQTLEACALLADLEMLPGGDQteigeKGINLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:TIGR02315 98 ENVLHGrlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQ-----RADQLSGGQQQRVAIARALAQQPDLILADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 778 LSAVDSHVAKHIFDHV--IGPEgvlAGKTRVLVTHGISFLPQ-TDFIIVLADGQV 829
Cdd:TIGR02315 173 IASLDPKTSKQVMDYLkrINKE---DGITVIINLHQVDLAKKyADRIVGLKAGEI 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1310-1514 |
1.55e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.49 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1310 SLHVHGGEKVGIVGRTGAGKSsmTLcLFRI---LEAAKGEIRIDGLNVADIGLHDlRSqLTIIPQDPILFSG-TLRMN-- 1383
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS--TL-LNLIagfLPPDSGRILWNGQDLTALPPAE-RP-VSMLFQENNLFPHlTVAQNig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1384 --LDPFGSYSEED---IWWALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQLVCLARALLRKSRILVLDEATAAID- 1457
Cdd:COG3840 94 lgLRPGLKLTAEQraqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDp 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1458 ---LETDNLIQaTIRTQFDTcTVLTIAHRLNTIMDYT-RVLVLDKGVVAEFDSPANLIAAR 1514
Cdd:COG3840 163 alrQEMLDLVD-ELCRERGL-TVLMVTHDPEDAARIAdRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
645-829 |
1.72e-15 |
|
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: 76.95 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 645 HSLDIQ-VPKGALVAVVGPVGCGKSSLVSALLGeMEKLEG---------------KVHM---KGSVAYVPQQ-AWIQNCT 704
Cdd:cd03297 13 FTLKIDfDLNEEVTGIFGASGAGKSTLLRCIAG-LEKPDGgtivlngtvlfdsrkKINLppqQRKIGLVFQQyALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLFG---KALNPKRYQQTleacalladlEMLPGGDQTEIGEKGI-NLSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:cd03297 92 VRENLAFGlkrKRNREDRISVD----------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9955970 781 VDSHVAKHIFDHVigpEGVLA--GKTRVLVTHGISFLPQ-TDFIIVLADGQV 829
Cdd:cd03297 162 LDRALRLQLLPEL---KQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
644-829 |
1.82e-15 |
|
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: 76.80 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQ----------------NCTLQE 707
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 NVLFG--KALNPKRYQQTLEACALLADLEMLPGGDQteigeKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHV 785
Cdd:cd03262 96 NITLApiKVKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9955970 786 AKHIFDHVIGpegvLA--GKTRVLVTHGISFLPQ-TDFIIVLADGQV 829
Cdd:cd03262 171 VGEVLDVMKD----LAeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
647-833 |
2.48e-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: 76.38 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAWIQNCTLQENVLF---------GKALN 716
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLFahltveqnvGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 717 PKRY-----QQTLEACAL---LADLEM-LPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAK 787
Cdd:cd03298 97 PGLKltaedRQAIEVALArvgLAGLEKrLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9955970 788 HIFDHVIGPEGVlAGKTRVLVTHGIS-FLPQTDFIIVLADGQVSEMG 833
Cdd:cd03298 166 EMLDLVLDLHAE-TKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1292-1509 |
2.54e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1292 RNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVADIGLHDLRSQLT 1367
Cdd:PRK13548 6 RNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKST----LLRALsgelSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPIL-FSGT----LRMNLDPFGSYSEED---IWWALE---LSHLhtfvssqpAGLDFQcseggeNLSVGQRQLVCL 1436
Cdd:PRK13548 80 VLPQHSSLsFPFTveevVAMGRAPHGLSRAEDdalVAAALAqvdLAHL--------AGRDYP------QLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1437 ARALLR------KSRILVLDEATAAIDL----ETDNLIQAtiRTQFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVAEFD 1505
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERGLAVIVVLHDLNLAARYAdRIVLLHQGRLVADG 223
|
....
gi 9955970 1506 SPAN 1509
Cdd:PRK13548 224 TPAE 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1291-1508 |
2.64e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1291 FRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADI---GLHDLRSQLT 1367
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPI-----------LFSGTLR--MNLDPfgsysEEDIWWALELSHLhtfVSSQPAGLDfQCSEggeNLSVGQRQLV 1434
Cdd:PRK10419 93 MVFQDSIsavnprktvreIIREPLRhlLSLDK-----AERLARASEMLRA---VDLDDSVLD-KRPP---QLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1435 CLARALLRKSRILVLDEATAAIDLetdnLIQATI-------RTQFDTCTVLtIAHRLNTIMDY-TRVLVLDKGVVAE--- 1503
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDL----VLQAGVirllkklQQQFGTACLF-ITHDLRLVERFcQRVMVMDNGQIVEtqp 235
|
250
....*....|.
gi 9955970 1504 ------FDSPA 1508
Cdd:PRK10419 236 vgdkltFSSPA 246
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
648-833 |
2.72e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.44 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 648 DIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAWIQNCTLQENVLF---------GKALNP 717
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqSHTGLAPYQRPVSMLFQENNLFahltvrqniGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 718 -----KRYQQTLEACAL---LAD-LEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKH 788
Cdd:TIGR01277 98 glklnAEQQEKVVDAAQqvgIADyLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9955970 789 IFDhVIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQVSEMG 833
Cdd:TIGR01277 167 MLA-LVKQLCSERQRTLLMVTHHLSDARAIaSQIAVVSQGKIKVVS 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
659-833 |
2.90e-15 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 78.69 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 659 VVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQ-----------AWIQNCTLQENVLFG----KALNPKRYQQ 722
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGeDVTNVPPHlrhinmvfqsyALFPHMTVEENVAFGlkmrKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 723 TLEAcalladLEMLPGGDQTEigEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGPEGVLaG 802
Cdd:TIGR01187 81 VLEA------LRLVQLEEFAD--RKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL-G 151
|
170 180 190
....*....|....*....|....*....|..
gi 9955970 803 KTRVLVTHGIS-FLPQTDFIIVLADGQVSEMG 833
Cdd:TIGR01187 152 ITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIG 183
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1289-1460 |
3.83e-15 |
|
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: 76.03 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAD--IGLHDLRSQL 1366
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSgtlrmNLDPFGSYSEEDIW---------WALELSHLhtfvssQPAGLDFQCSEGGENLSVGQRQLVCLA 1437
Cdd:cd03262 79 GMVFQQFNLFP-----HLTVLENITLAPIKvkgmskaeaEERALELL------EKVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180
....*....|....*....|...
gi 9955970 1438 RALLRKSRILVLDEATAAIDLET 1460
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPEL 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
640-858 |
3.96e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.56 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 640 LPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSAL--LGEMEKLE-----------GKVHMKGSVAYVPQQAWIQNCTLQ 706
Cdd:PLN03232 1248 LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALfrIVELEKGRimiddcdvakfGLTDLRRVLSIIPQSPVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVA 786
Cdd:PLN03232 1328 FNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 787 KHIfDHVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGS-FANFLCNYAPDEDQ 858
Cdd:PLN03232 1408 SLI-QRTIREE--FKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFRMVHSTGPANAQ 1477
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1289-1507 |
4.45e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPilfsgtlrmnLDPF-GSYSEEDIWWALE---LSH--LHTFVS---SQPAGLDFQCSEgGENLSVGQRQLVCLARA 1439
Cdd:PRK13648 88 VFQNP----------DNQFvGSIVKYDVAFGLEnhaVPYdeMHRRVSealKQVDMLERADYE-PNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1440 LLRKSRILVLDEATAAIDLET-DNLIQATIRTQFD-TCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSP 1507
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDArQNLLDLVRKVKSEhNITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
644-829 |
4.79e-15 |
|
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: 74.39 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGsvayvpqqawiqnctlqENVLFgkaLNPKRyqqt 723
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------KEVSF---ASPRD---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 724 leacALLADLEMLPggdQteigekginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVigpeGVLA-- 801
Cdd:cd03216 72 ----ARRAGIAMVY---Q---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RRLRaq 131
|
170 180
....*....|....*....|....*....
gi 9955970 802 GKTRVLVTHGISFLPQT-DFIIVLADGQV 829
Cdd:cd03216 132 GVAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1289-1512 |
6.12e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIG-LHDLRSQLT 1367
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPilfsgtlrmNLDPFGSYSEEDIWWA-----LELSHLHTFVSSQPA--GLDFQCSEGGENLSVGQRQLVCLARAL 1440
Cdd:PRK13644 81 IVFQNP---------ETQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRALAeiGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1441 LRKSRILVLDEATAAIDLETDNLIQATIRTQFDTC-TVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIA 1512
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1306-1502 |
6.63e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.01 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAD--IGLHDLRSQLTIIPQDP--ILFSGTLR 1381
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1382 MNLdPFG----SYSEEDIwwalelsHLHTFVSSQPAGLDFQCSEGGE--NLSVGQRQLVCLARALLRKSRILVLDEATAA 1455
Cdd:PRK13637 103 KDI-AFGpinlGLSEEEI-------ENRVKRAMNIVGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9955970 1456 IDLETDNLIQATIRTQFD--TCTVLTIAHRLNTIMDY-TRVLVLDKGVVA 1502
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKGKCE 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
644-847 |
7.30e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.94 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALlGEMEKLE------GKVHMKGSVAYVPQQAWIQNC-------------- 703
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEagtirvGDITIDTARSLSQQKGLIRQLrqhvgfvfqnfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 704 ---TLQENVLFGKALNPK--RYQQTLEACALLADLEMlpGGDQTEIGEKginLSGGQRQRVSLARAVYSDADIFLLDDPL 778
Cdd:PRK11264 98 phrTVLENIIEGPVIVKGepKEEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 779 SAVDSHVAKHIFDHVIGpegvLA--GKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGPYPALlqrngsFAN 847
Cdd:PRK11264 173 SALDPELVGEVLNTIRQ----LAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL------FAD 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1291-1501 |
8.48e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 8.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1291 FRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRILeaaKGEIRIDGLNVAdiglhdLRSQLTI-- 1368
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKIL---AGELEPDSGEVS------IPKGLRIgy 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDPILFSG-----TLRMNLDPFG-------------SYSEEDIwwaLELSHLHTFVSSQPA------------GLDFQ 1418
Cdd:COG0488 66 LPQEPPLDDDltvldTVLDGDAELRaleaeleeleaklAEPDEDL---ERLAELQEEFEALGGweaearaeeilsGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1419 CSEGG---ENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQfdTCTVLTIAH-R--LNTIMdyTR 1492
Cdd:COG0488 143 EEDLDrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--PGTVLVVSHdRyfLDRVA--TR 218
|
....*....
gi 9955970 1493 VLVLDKGVV 1501
Cdd:COG0488 219 ILELDRGKL 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
644-834 |
9.00e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 77.83 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGeMEKL-EGKVHMKG-----------SVAYVPQQ-AWIQNCTLQENVL 710
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPdSGRILLDGrdvtglppekrNVGMVFQDyALFPHLTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FG-KALN-PK--RYQQTLEACAL--LADLEmlpggdQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH 784
Cdd:COG3842 100 FGlRMRGvPKaeIRARVAELLELvgLEGLA------DRYPHQ----LSGGQQQRVALARALAPEPRVLLLDEPLSALDAK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 785 VA-------KHIFDHVigpegvlaGKTRVLVTH------GISflpqtDFIIVLADGQVSEMGP 834
Cdd:COG3842 170 LReemreelRRLQREL--------GITFIYVTHdqeealALA-----DRIAVMNDGRIEQVGT 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
641-831 |
1.32e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 74.70 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 641 PPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEmEKL-EGKVHMKG---------SVAY-------VPQQAW-IQN 702
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERPtSGQVLVNGqdlsrlkrrEIPYlrrrigvVFQDFRlLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 CTLQENVLF-----GKalNPKRYQQTLEAcAL----LADLE-MLPggdqteigekgINLSGGQRQRVSLARAVYSDADIF 772
Cdd:COG2884 94 RTVYENVALplrvtGK--SRKEIRRRVRE-VLdlvgLSDKAkALP-----------HELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 773 LLDDPLSAVDSHVAKHIFDHvigpegvL-----AGKTRVLVTHGISFLPQTDF-IIVLADGQVSE 831
Cdd:COG2884 160 LADEPTGNLDPETSWEIMEL-------LeeinrRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1287-1510 |
1.87e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 76.65 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1287 GEVEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVADIGLHDl 1362
Cdd:COG3839 2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIagleDPTSGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1363 RSqLTIIPQDPILF-SGTLRMNLDpFG----SYSEEDI-----WWA--LELSHLhtfvssqpagLDFQCSEggenLSVGQ 1430
Cdd:COG3839 75 RN-IAMVFQSYALYpHMTVYENIA-FPlklrKVPKAEIdrrvrEAAelLGLEDL----------LDRKPKQ----LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1431 RQLVCLARALLRKSRILVLDEATAAIDletdnliqATIRTQfdtcTVLTIA---HRLNTIMDY------------TRVLV 1495
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLD--------AKLRVE----MRAEIKrlhRRLGTTTIYvthdqveamtlaDRIAV 206
|
250
....*....|....*
gi 9955970 1496 LDKGVVAEFDSPANL 1510
Cdd:COG3839 207 MNDGRIQQVGTPEEL 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1299-1511 |
2.03e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1299 RPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLR-----------SQLT 1367
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPILFSGTLRMNLDpfGSYSEEDIWWALElshlhtfvSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRIL 1447
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELA--GINAEERREKALD--------ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1448 VLDEATAAID--LET---DNLIQATIRTQFdtcTVLTIAHRLNTIMDY-TRVLVLDKGVVAEFDSPANLI 1511
Cdd:PRK10070 187 LMDEAFSALDplIRTemqDELVKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1305-1496 |
2.19e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.04 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLnvADIGLhdLRSQLTIIPQDPILFSGTLRMNL 1384
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAY--VPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1385 ----DPFGSYSEED---IWWALELSHLHTFvssqpAGLDFQcseggeNLSVGQRQLVCLARALLRKSRILVLDEATAAID 1457
Cdd:NF040873 83 warrGLWRRLTRDDraaVDDALERVGLADL-----AGRQLG------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9955970 1458 LETDNLIQATIRTQFDT-CTVLTIAHRLNTIMDYTRVLVL 1496
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
647-837 |
3.28e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQvpKGALVAVVGPVGCGKSSLVSALLGemekLE---------GKVHM------KGSVAYVPQQ-AWIQNCTLQENVL 710
Cdd:PRK11000 24 LDIH--EGEFVVFVGPSGCGKSTLLRMIAG----LEditsgdlfiGEKRMndvppaERGVGMVFQSyALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FG-------KALNPKRYQQTLEACALLADLEMLPGGdqteigekginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD- 782
Cdd:PRK11000 98 FGlklagakKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDa 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 783 ----------SHVAKHIfdhvigpegvlaGKTRVLVTHG-ISFLPQTDFIIVLADGQVSEMGP------YPA 837
Cdd:PRK11000 167 alrvqmrieiSRLHKRL------------GRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKplelyhYPA 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
644-849 |
3.37e-14 |
|
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: 73.91 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS-----------VAYVPQQ-AWIQNCTLQENVLF 711
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 G--KALNPK--RYQQTLEACALLADLEMLpggdqteiGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAK 787
Cdd:cd03299 95 GlkKRKVDKkeIERKVLEIAEMLGIDHLL--------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 788 HIFDHV--IGPEgvlAGKTRVLVTHGIS-FLPQTDFIIVLADGQVSEMGPYPALLQR--NGSFANFL 849
Cdd:cd03299 167 KLREELkkIRKE---FGVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVFKKpkNEFVAEFL 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1288-1502 |
3.46e-14 |
|
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: 72.58 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1288 EVEFRN--YSVRYRPGLD--LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCL--FRILEAAKGEIRIDGLNvadIGLHD 1361
Cdd:cd03213 3 TLSFRNltVTVKSSPSKSgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 LRSQLTIIPQDPILFsGTLRMnldpfgsysEEDIWWALELShlhtfvssqpagldfqcseggeNLSVGQRQLVCLARALL 1441
Cdd:cd03213 80 FRKIIGYVPQDDILH-PTLTV---------RETLMFAAKLR----------------------GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1442 RKSRILVLDEATAAIDLETDNLIQATIRTQFDT-CTVLTIAHRLNTIMDYT--RVLVLDKGVVA 1502
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSEIFELfdKLLLLSQGRVI 191
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1291-1498 |
4.20e-14 |
|
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: 74.51 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1291 FRNYSVRYRPgldlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGlnvadiglhdlrsQLTIIP 1370
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1371 QDPILFSGTLRMNLdPFG-SYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVL 1449
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGvSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9955970 1450 DEATAAIDLETDNLIqatirtqFDTCTVLTIAHRlntimdyTRVLVLDK 1498
Cdd:cd03291 184 DSPFGYLDVFTEKEI-------FESCVCKLMANK-------TRILVTSK 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
644-782 |
4.66e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.00 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQ-NCTLQENV 709
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHSSLAfPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 710 LFGKA---LNPKRYQQTLEACALLADLEMLPGGDQTEigekginLSGGQRQRVSLARA-------VYSDADIFLLDDPLS 779
Cdd:COG4559 97 ALGRAphgSSAAQDRQIVREALALVGLAHLAGRSYQT-------LSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTS 169
|
...
gi 9955970 780 AVD 782
Cdd:COG4559 170 ALD 172
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1289-1502 |
5.43e-14 |
|
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: 72.79 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRP--GLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLhDLRSQL 1366
Cdd:cd03266 2 ITADALTKRFRDvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSG-TLRMNLDPFGSYseediwWALELSHLHTFVSSQPAGLDFQ--CSEGGENLSVGQRQLVCLARALLRK 1443
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGL------YGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1444 SRILVLDEATAAIDLETDNLIQATIRTQFDT-CTVLTIAHRLNTIMDYT-RVLVLDKGVVA 1502
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCdRVVVLHRGRVV 215
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1049-1260 |
5.69e-14 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 74.36 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1049 LHNKI-RSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTP---LFTVVILPLAVLYTL 1124
Cdd:cd18547 84 LFEKLqRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPlltLIVLVTVPLSLLVTK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1125 V-----QRFYAATSRQLKRLEsvsrspiySHFSETVTGASVIRAYNR----SRDFEIISDTKVDANQRScypYIISNrwl 1195
Cdd:cd18547 164 FiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNReeeaIEEFDEINEELYKASFKA---QFYSG--- 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1196 SIG--VEFVGN----CVVLFAALFAVIGRSSLnpGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERV 1260
Cdd:cd18547 230 LLMpiMNFINNlgyvLVAVVGGLLVINGALTV--GVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
644-782 |
5.72e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.65 E-value: 5.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------------SVAYVPQQAWIQ-NCTLQENV 709
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLSfPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 710 LFGKA---LNPKRYQQTLEACALLADLEMLPGGDQTEigekginLSGGQRQRVSLARA---VYSDAD---IFLLDDPLSA 780
Cdd:PRK13548 98 AMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqLWEPDGpprWLLLDEPTSA 170
|
..
gi 9955970 781 VD 782
Cdd:PRK13548 171 LD 172
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
648-849 |
6.56e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.69 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 648 DIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGsvayvpqqawiQNCT------------LQENVLF---- 711
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-----------QDHTttppsrrpvsmlFQENNLFshlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 -----GKALNP---------KRYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:PRK10771 88 vaqniGLGLNPglklnaaqrEKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 778 LSAVDSHVAKHIFDHVigpEGVLAGK--TRVLVTHGIS----FLPQTdfiIVLADGQVSEMGPYPALLQRNGSFANFL 849
Cdd:PRK10771 157 FSALDPALRQEMLTLV---SQVCQERqlTLLMVSHSLEdaarIAPRS---LVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
642-783 |
6.93e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVP---------QQAWIQNCTLQENVLFG 712
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 713 KAL----NPKRYQQTLEACALLaDLEmlpGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS 783
Cdd:PRK11248 95 LQLagveKMQRLEIAHQMLKKV-GLE---GAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
629-820 |
7.03e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 629 IHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALlGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQ-- 706
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVNLNrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 -------------------ENVLFGKAL---NPK-RYQQTLEACALLADL--EMlpggdQTEIGEKGINLSGGQRQRVSL 761
Cdd:PRK14258 87 rrqvsmvhpkpnlfpmsvyDNVAYGVKIvgwRPKlEIDDIVESALKDADLwdEI-----KHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 762 ARAVYSDADIFLLDDPLSAVDShVAKHIFDHVIGPEGVLAGKTRVLVTHGisfLPQ----TDF 820
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDP-IASMKVESLIQSLRLRSELTMVIVSHN---LHQvsrlSDF 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1293-1503 |
7.63e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 7.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1293 NYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQD 1372
Cdd:PRK11231 7 NLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1373 PILFSG-TLR----------MNLdpFGSYSEED---IWWALELSHLHTFVsSQPAgldfqcseggENLSVGQRQLVCLAR 1438
Cdd:PRK11231 85 HLTPEGiTVRelvaygrspwLSL--WGRLSAEDnarVNQAMEQTRINHLA-DRRL----------TDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1439 ALLRKSRILVLDEATAAIDL----ETDNLIQatiRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKG--VVAE 1503
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDInhqvELMRLMR---ELNTQGKTVVTVLHDLNQASRYCDHLVVLANghVMAQ 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
644-833 |
8.29e-14 |
|
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: 72.65 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVP----------QQ-AWIQNCTLQENVLF 711
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPphkrpvntvfQNyALFPHLTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 GKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKH--- 788
Cdd:cd03300 96 GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDmql 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9955970 789 ----IFDHVigpegvlaGKTRVLVTHGIS-FLPQTDFIIVLADGQVSEMG 833
Cdd:cd03300 172 elkrLQKEL--------GITFVFVTHDQEeALTMSDRIAVMNKGKIQQIG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1289-1510 |
9.78e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.36 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSsmTLClfRIL----EAAKGEIRIDGLNVADIGLHDlRs 1364
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKT--TLL--RMIagfeTPDSGRILLDGRDVTGLPPEK-R- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1365 QLTIIPQDPILFsgtlrmnldP---------FG----SYSEEDI----WWALELSHLHTFVSSQPAgldfqcseggeNLS 1427
Cdd:COG3842 78 NVGMVFQDYALF---------PhltvaenvaFGlrmrGVPKAEIrarvAELLELVGLEGLADRYPH-----------QLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1428 VGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRT---QFDTCTV---------LTIAHrlntimdytRVLV 1495
Cdd:COG3842 138 GGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqrELGITFIyvthdqeeaLALAD---------RIAV 208
|
250
....*....|....*
gi 9955970 1496 LDKGVVAEFDSPANL 1510
Cdd:COG3842 209 MNDGRIEQVGTPEEI 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1305-1502 |
9.83e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPIL---FSG--T 1379
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVrqV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1380 LRMNLDP----FGSYSEED---IWWALELSHLHTFVsSQPAgldfqcseggENLSVGQRQLVCLARALLRKSRILVLDEA 1452
Cdd:PRK09536 98 VEMGRTPhrsrFDTWTETDraaVERAMERTGVAQFA-DRPV----------TSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1453 TAAIDLETDNLIQATIRTQFDTC-TVLTIAHRLNTIMDY--TRVLVLDKGVVA 1502
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDGkTAVAAIHDLDLAARYcdELVLLADGRVRA 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1298-1469 |
1.02e-13 |
|
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: 71.62 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1298 YRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAdiglhdlrsQLTIIPQDPILFS 1377
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------EQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1378 G---------TLRMNLD---PFGSYSEEDIWWALELSHLHTFvSSQPAGldfqcseggeNLSVGQRQLVCLARALLRKSR 1445
Cdd:TIGR01189 79 GhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRP 147
|
170 180
....*....|....*....|....
gi 9955970 1446 ILVLDEATAAIDLETDNLIQATIR 1469
Cdd:TIGR01189 148 LWILDEPTTALDKAGVALLAGLLR 171
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1284-1499 |
1.31e-13 |
|
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: 70.54 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1284 PPRGEVefRNYSVRYRpgldlvLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLR 1363
Cdd:cd03215 2 EPVLEV--RGLSVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 SQ-LTIIPQDPilfsgtLRMNLdpFGSYSeedIWWALELSHLhtfvssqpagldfqcseggenLSVGQRQLVCLARALLR 1442
Cdd:cd03215 74 RAgIAYVPEDR------KREGL--VLDLS---VAENIALSSL---------------------LSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1443 KSRILVLDEATAAIDLETDNLIQATIRTQFDT-CTVLTIAHRLNTIM---DytRVLVLDKG 1499
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLglcD--RILVMYEG 180
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
623-833 |
1.47e-13 |
|
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: 72.68 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 623 PGYAITIHSGTFTWAQDLPPT-----LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-------- 689
Cdd:cd03294 14 PQKAFKLLAKGKSKEEILKKTgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 690 ---------SVAYVPQQ-AWIQNCTLQENVLFG-------KALNPKRYQQTLEACALLADLEMLPGgdqteigekgiNLS 752
Cdd:cd03294 94 kelrelrrkKISMVFQSfALLPHRTVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 753 GGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGPEGVLaGKTRVLVTHG-ISFLPQTDFIIVLADGQVSE 831
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAEL-QKTIVFITHDlDEALRLGDRIAIMKDGRLVQ 241
|
..
gi 9955970 832 MG 833
Cdd:cd03294 242 VG 243
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
644-829 |
1.70e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.35 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLG----------EMEKLEGKVHMKGSVA-----------YVPQQAWIQN 702
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirksrantgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 -CTLQENVLFG------------KALNPKRYQQTLEAcalLADLEMLPGGDQteigeKGINLSGGQRQRVSLARAVYSDA 769
Cdd:PRK09984 100 rLSVLENVLIGalgstpfwrtcfSWFTREQKQRALQA---LTRVGMVHFAHQ-----RVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 770 DIFLLDDPLSAVDSHVAKHIFD--HVIGPEGvlaGKTRVLVTHGISF-LPQTDFIIVLADGQV 829
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDtlRDINQND---GITVVVTLHQVDYaLRYCERIVALRQGHV 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1308-1518 |
1.71e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.61 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1308 DLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILeAAKGEI----RIDG---LNVADIGLHDLRS-QLTIIPQDPIlfsgt 1379
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGreiLNLPEKELNKLRAeQISMIFQDPM----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1380 lrMNLDPFGSYSEEdiwwALELSHLHTFVSSQPAgldFQCS----------EGGENL-------SVGQRQLVCLARALLR 1442
Cdd:PRK09473 108 --TSLNPYMRVGEQ----LMEVLMLHKGMSKAEA---FEESvrmldavkmpEARKRMkmyphefSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1443 KSRILVLDEATAAIDLEtdnlIQATIRT-------QFDTcTVLTIAHRLNT---IMDytRVLVLDKGVVAEFDSpanlia 1512
Cdd:PRK09473 179 RPKLLIADEPTTALDVT----VQAQIMTllnelkrEFNT-AIIMITHDLGVvagICD--KVLVMYAGRTMEYGN------ 245
|
....*.
gi 9955970 1513 ARGIFY 1518
Cdd:PRK09473 246 ARDVFY 251
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
644-840 |
1.77e-13 |
|
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: 71.93 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAWI----------QNC------TLQ 706
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrrigmlfQGGalfdslTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFG----KALNPKRYQQ----TLEACALLADLEMLPGgdqteigEkginLSGGQRQRVSLARAVYSDADIFLLDDPL 778
Cdd:COG1127 101 ENVAFPlrehTDLSEAEIRElvleKLELVGLPGAADKMPS-------E----LSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 779 SAVDShVAKHIFDHVIgpegvLA-----GKTRVLVTHGISFLPQT-DFIIVLADGQVSEMGPYPALLQ 840
Cdd:COG1127 170 AGLDP-ITSAVIDELI-----RElrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1012-1260 |
1.78e-13 |
|
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: 72.97 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1012 LGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLL 1091
Cdd:cd07346 42 ALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1092 NSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFE 1171
Cdd:cd07346 122 SDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1172 IISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVLFAALFAV--IGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSD 1249
Cdd:cd07346 202 ERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGylVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQ 281
|
250
....*....|.
gi 9955970 1250 LESNIVAVERV 1260
Cdd:cd07346 282 LQQALASLERI 292
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
646-849 |
1.83e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.60 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 646 SLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSvaYVPQQAwIQN---C------------TLQENVL 710
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHRS-IQQrdiCmvfqsyalfphmSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FG-KALN-PK--RYQQTLEACALLaDLEmlpgG------DQteigekginLSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:PRK11432 101 YGlKMLGvPKeeRKQRVKEALELV-DLA----GfedryvDQ---------ISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 781 VDSHVAKHIFDHVIGPEGVLaGKTRVLVTHGIS-FLPQTDFIIVLADGQVSEMGPYPALLQRNGS--FANFL 849
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQF-NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASrfMASFM 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
646-787 |
2.07e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.58 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 646 SLDIqvPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS-----------VAYVPQQ-AWIQNCTLQENVLFGK 713
Cdd:PRK10851 22 SLDI--PSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 714 ALNPKRYQQTLEAC--ALLADLEMLpggDQTEIGEK-GINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAK 787
Cdd:PRK10851 100 TVLPRRERPNAAAIkaKVTQLLEMV---QLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
613-810 |
2.16e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 613 PQSVERKTISPGYAItihsGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SV 691
Cdd:PRK11607 8 PQAKTRKALTPLLEI----RNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 692 AYVP-----------QQAWIQNCTLQENVLFG-KALNPKRYQQTLEACALLADLEMlpggdQTEIGEKGINLSGGQRQRV 759
Cdd:PRK11607 84 SHVPpyqrpinmmfqSYALFPHMTVEQNIAFGlKQDKLPKAEIASRVNEMLGLVHM-----QEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9955970 760 SLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGP-EGVlaGKTRVLVTH 810
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDIlERV--GVTCVMVTH 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1305-1505 |
2.43e-13 |
|
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: 71.02 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGL-HDLRSQLTIIpqDPILFSGTLrMN 1383
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGFNPELTGR--ENIYLNGRL-LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1384 LDP-FGSYSEEDIWwalELSHLHTFVsSQPAGldfqcseggeNLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDN 1462
Cdd:cd03220 114 LSRkEIDEKIDEII---EFSELGDFI-DLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9955970 1463 LIQATIRTQFDTC-TVLTIAHRLNTIMDY-TRVLVLDKGVVAEFD 1505
Cdd:cd03220 180 KCQRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1289-1503 |
2.57e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.91 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLV--LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVA---DIGLHDLR 1363
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 SQLTIIPQDPILFSG-------TLRMNLDpfgSYSEEDIWWALE-------LSHLHtfvSSQPAgldfqcseggeNLSVG 1429
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrtvfdnvALPLELA---GTPKAEIKARVTellelvgLSDKA---DRYPA-----------QLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1430 QRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQ---ATIRTQFDTcTVLTIAHRlntiMDYT-----RVLVLDKGVV 1501
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILellKDINRELGL-TIVLITHE----MDVVkricdRVAVIDAGRL 219
|
..
gi 9955970 1502 AE 1503
Cdd:PRK11153 220 VE 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
633-834 |
2.91e-13 |
|
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: 71.69 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 633 TFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAW---------IQN- 702
Cdd:TIGR04520 7 SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvgmvFQNp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 ------CTLQENVLFG---KALNP----KRYQQTLEACALLADLEMLPggdqteigekgINLSGGQRQRVSLARAVYSDA 769
Cdd:TIGR04520 87 dnqfvgATVEDDVAFGlenLGVPReemrKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 770 DIFLLDDPLSAVDshvakhifdhvigPEG---VLA---------GKTRVLVTHGISFLPQTDFIIVLADGQVSEMGP 834
Cdd:TIGR04520 156 DIIILDEATSMLD-------------PKGrkeVLEtirklnkeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1305-1499 |
3.09e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 71.66 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRI----LEAAKGEIRIDGLNVADIGLHDlRSQLtI--IPQDPI---- 1374
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAiagsLPPDSGSILIDGKDVTKLPEYK-RAKY-IgrVFQDPMmgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1375 --------------------LFSGTLRMNLDPFGSYSEEdiwwaLELS---HLHTfvssqPAGLdfqcseggenLSVGQR 1431
Cdd:COG1101 95 psmtieenlalayrrgkrrgLRRGLTKKRRELFRELLAT-----LGLGlenRLDT-----KVGL----------LSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 1432 QLVCLARALLRKSRILVLDEATAAID-------LE-TDNLIQAtirtqfDTCTVLTIAHRLNTIMDY-TRVLVLDKG 1499
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDYgNRLIMMHEG 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
642-829 |
3.35e-13 |
|
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: 70.51 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV--------HMKGS-VAYVPQQ--------AWIQNCT 704
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsDLRGRaIPYLRRKigvvfqdfRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLF-------GKALNPKRYQQTLEACALLADLEMLPGGdqteigekginLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:cd03292 95 VYENVAFalevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9955970 778 LSAVDSHVAKHIFDHVigpEGV-LAGKTRVLVTHGISFLPQTDF-IIVLADGQV 829
Cdd:cd03292 164 TGNLDPDTTWEIMNLL---KKInKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1290-1510 |
3.46e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYrPGLdLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVA--------DI 1357
Cdd:PRK11288 6 SFDGIGKTF-PGV-KALDDISFDCRAGQVHALMGENGAGKST----LLKILsgnyQPDAGSILIDGQEMRfasttaalAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1358 GLHDLRSQLTIIPQDPI---LFSGTLrmnldP--FGSYSEEDI--WWALELSHLhtfvssqpaGLDFQCSEGGENLSVGQ 1430
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVaenLYLGQL-----PhkGGIVNRRLLnyEAREQLEHL---------GVDIDPDTPLKYLSIGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1431 RQLVCLARALLRKSRILVLDEATAAIDL-ETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYT-RVLVLDKG-VVAEFDSP 1507
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIFALCdAITVFKDGrYVATFDDM 225
|
...
gi 9955970 1508 ANL 1510
Cdd:PRK11288 226 AQV 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1289-1510 |
3.51e-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: 70.73 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVADIGLHdlRS 1364
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLIagfeTPTSGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1365 QLTIIPQDPILF---------SGTLRMNLDPfGSYSEEDIWWALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQLVC 1435
Cdd:cd03300 73 PVNTVFQNYALFphltvfeniAFGLRLKKLP-KAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1436 LARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTC--TVLTIAHRLN---TIMDytRVLVLDKGVVAEFDSPANL 1510
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEealTMSD--RIAVMNKGKIQQIGTPEEI 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
648-841 |
3.72e-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: 72.83 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 648 DIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSV-----------------AYVPQQAwiqncTL----- 705
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQEA-----RLfphls 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 706 -QENVLFG--KALNPKRYQQTLEACALL---ADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:COG4148 94 vRGNLLYGrkRAPRAERRISFDEVVELLgigHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 780 AVDsHVAKH--------IFDHVIGPegVLagktrvLVTHGISFLPQ-TDFIIVLADGQVSEMGPYPALLQR 841
Cdd:COG4148 163 ALD-LARKAeilpylerLRDELDIP--IL------YVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1259-1505 |
4.50e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1259 RVKEYSKTETEAPWVVEGS---RPPEGwPPRGE--VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmt 1333
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTveiRFPPP-ERLGKkvLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKST-- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1334 lcLFRIL----EAAKGEIRIdGLNVaDIG-----LHDLRSQLTII-------PQDPILFSGTL--RMNLDPfgsyseEDI 1395
Cdd:COG0488 357 --LLKLLagelEPDSGTVKL-GETV-KIGyfdqhQEELDPDKTVLdelrdgaPGGTEQEVRGYlgRFLFSG------DDA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1396 WwalelshlhTFVSSqpagldfqcseggenLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTqFDTc 1475
Cdd:COG0488 427 F---------KPVGV---------------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG- 480
|
250 260 270
....*....|....*....|....*....|...
gi 9955970 1476 TVLTIAH-R--LNTIMDytRVLVLDKGVVAEFD 1505
Cdd:COG0488 481 TVLLVSHdRyfLDRVAT--RILEFEDGGVREYP 511
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
644-834 |
5.04e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 70.41 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGemekLE----GKVHMKG---------------SVAYVPQQ------- 697
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL----LEepdsGTITVDGedltdskkdinklrrKVGMVFQQfnlfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 698 -AwIQNCTL-QENVLfGKalnPKRyqqtlEACALlAdLEMLpggDQTEIGEKG----INLSGGQRQRVSLARAVYSDADI 771
Cdd:COG1126 93 tV-LENVTLaPIKVK-KM---SKA-----EAEER-A-MELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 772 FLLDDPLSAVDshvakhifdhvigPE---GVLA--------GKTRVLVTHGISFLPQT-DFIIVLADGQVSEMGP 834
Cdd:COG1126 158 MLFDEPTSALD-------------PElvgEVLDvmrdlakeGMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGP 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
642-834 |
5.16e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.50 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAWIQNCTL--QEN---------- 708
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGlDVATTPSRELAKRLAIlrQENhinsrltvre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 -VLFGK------ALNPKRYQQTLEACALLaDLEmlpggdqtEIGEKGIN-LSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:COG4604 95 lVAFGRfpyskgRLTAEDREIIDEAIAYL-DLE--------DLADRYLDeLSGGQRQRAFIAMVLAQDTDYVLLDEPLNN 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 781 VDSHVAKHIFDHVIGpegvLA---GKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGP 834
Cdd:COG4604 166 LDMKHSVQMMKLLRR----LAdelGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGT 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1288-1510 |
5.38e-13 |
|
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: 70.45 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1288 EVEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRI---LEAA-KGEIRIDGLNVADIGLHDlr 1363
Cdd:cd03296 2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTT----LLRLiagLERPdSGTILFGGEDATDVPVQE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 SQLTIIPQDPILFSG-TLRMNLdPFG--------SYSEEDIWWA----LELSHLHTFVSSQPAgldfqcseggeNLSVGQ 1430
Cdd:cd03296 74 RNVGFVFQHYALFRHmTVFDNV-AFGlrvkprseRPPEAEIRAKvhelLKLVQLDWLADRYPA-----------QLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1431 RQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTI--AHRLNTIMDYT-RVLVLDKGVVAEFDSP 1507
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEVAdRVVVMNKGRIEQVGTP 221
|
...
gi 9955970 1508 ANL 1510
Cdd:cd03296 222 DEV 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1295-1501 |
5.42e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1295 SVRYRPGlDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAdiglHDLRSQL-TIIPQD- 1372
Cdd:PRK15056 13 TVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLvAYVPQSe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1373 ------PILFSGTLRMnldpfGSYSEEDiWWALELSHLHTFVSSQPAG---LDFQCSEGGEnLSVGQRQLVCLARALLRK 1443
Cdd:PRK15056 88 evdwsfPVLVEDVVMM-----GRYGHMG-WLRRAKKRDRQIVTAALARvdmVEFRHRQIGE-LSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 1444 SRILVLDEATAAIDLETDNLIQATIRTQFDT-CTVLTIAHRLNTIMDYTRVLVLDKGVV 1501
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
643-810 |
7.21e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.19 E-value: 7.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 643 TLHSLDIQVPKGALVAVVGPVGCGKSSLVSALlGEMEKLEGKVHMKGSVAY---------------------VPQQAWIQ 701
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 702 NCTLQENVLFGKALNPKRYQQTLEAcALLADLEMLPGGDQTE--IGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|..
gi 9955970 780 AVDSHVAKHIFDHVIGpegvLAGK-TRVLVTH 810
Cdd:PRK14239 178 ALDPISAGKIEETLLG----LKDDyTMLLVTR 205
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1289-1512 |
7.22e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.89 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDL-VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLT 1367
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPilfsgtlrmNLDPFGSYSEEDIWWALELSHL--HTFVSSQPAG------LDFQCSEGGEnLSVGQRQLVCLARA 1439
Cdd:PRK13642 85 MVFQNP---------DNQFVGATVEDDVAFGMENQGIprEEMIKRVDEAllavnmLDFKTREPAR-LSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1440 LLRKSRILVLDEATAAIDLETDNLIQATIRTQFDT--CTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIA 1512
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1304-1497 |
1.15e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1304 LVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVADIGlHDLRSQLtiipqdpiLFSG- 1378
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTS----LLRILaglaRPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1379 ------------TLRMNLDPFGSYSEEDIWWALELSHLHTFvssqpagLDFQCSeggeNLSVGQRQLVCLARALLRKSRI 1446
Cdd:PRK13538 82 qpgikteltaleNLRFYQRLHGPGDDEALWEALAQVGLAGF-------EDVPVR----QLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1447 LVLDEATAAIDLETDNLIQATIR--TQFDTCTVLTIAHRLNTIMDYTRVLVLD 1497
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAqhAEQGGMVILTTHQDLPVASDKVRKLRLG 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1289-1514 |
1.18e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLV---LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDG----LNVADIGLHD 1361
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 LRSQLTIIPQDP--ILFSGTLRMNLDpFG----SYSEED-----IWWALELSHLHTFVSSQPagldFQcseggenLSVGQ 1430
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVE-FGpknfGFSEDEakekaLKWLKKVGLSEDLISKSP----FE-------LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1431 RQLVCLARALLRKSRILVLDEATAAIDLET-DNLIQATIRTQFDTCTVLTIAHRLNTIMDYTR-VLVLDKGVVAEFDSPA 1508
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADdVLVLEHGKLIKHASPK 230
|
....*.
gi 9955970 1509 NLIAAR 1514
Cdd:PRK13641 231 EIFSDK 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
644-833 |
1.44e-12 |
|
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: 67.96 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLG--EMEKLEGKVHMKG----------SVAYVPQQ-AWIQNCTLQENVL 710
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGrpldkrsfrkIIGYVPQDdILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FGKALnpkryqqtleacalladlemlpggdqteigeKGInlSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIF 790
Cdd:cd03213 105 FAAKL-------------------------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 791 DHVIGpegvLA--GKTRVLVTHGIS------FlpqtDFIIVLADGQVSEMG 833
Cdd:cd03213 152 SLLRR----LAdtGRTIICSIHQPSseifelF----DKLLLLSQGRVIYFG 194
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1289-1501 |
1.49e-12 |
|
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: 68.46 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPglDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHD------- 1361
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 --LRSQLTIIPQdpILFSGTLRmNLDPFGSYSEEDIWW-ALELSHLHtfvssqpagldfqcSEGGENLSVGQRQLVCLAR 1438
Cdd:cd03269 79 rgLYPKMKVIDQ--LVYLAQLK-GLKKEEARRRIDEWLeRLELSEYA--------------NKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1439 ALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDT-CTVLTIAHRLNTIMDY-TRVLVLDKGVV 1501
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
644-834 |
1.61e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.13 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAWIQNCTLQ-----------ENVLF 711
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTVFQsyalfphmtvfENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 G----KALNPKRYQQTLEACALLaDLEMLpggdqteIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAK 787
Cdd:PRK09452 110 GlrmqKTPAAEITPRVMEALRMV-QLEEF-------AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9955970 788 HIFDHVIGPEGVLaGKTRVLVTHGI-SFLPQTDFIIVLADGQVSEMGP 834
Cdd:PRK09452 182 QMQNELKALQRKL-GITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1259-1511 |
1.82e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1259 RVKEYSKTETEAPWVVEGSRPPEGWPPRGEVEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFR 1338
Cdd:PRK13536 12 RRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1339 ILEAAKGEIRIDGLNVADIGlHDLRSQLTIIPQ-DPILFSGTLRMNLDPFGSY-------SEEDIWWALELSHLHTFVSS 1410
Cdd:PRK13536 90 MTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLEFARLESKADA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1411 QPAgldfqcseggeNLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTC-TVLTIAHrlntIMD 1489
Cdd:PRK13536 169 RVS-----------DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTH----FME 233
|
250 260
....*....|....*....|....*...
gi 9955970 1490 YT-----RVLVLDKGV-VAEfDSPANLI 1511
Cdd:PRK13536 234 EAerlcdRLCVLEAGRkIAE-GRPHALI 260
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1289-1505 |
1.85e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.38 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDP--ILFSGT---------LRMNLDPfgSYSEEDIWWALELSHLHTFVSSQPagldfqcseggENLSVGQRQLVCLA 1437
Cdd:PRK13647 84 VFQDPddQVFSSTvwddvafgpVNMGLDK--DEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1438 RALLRKSRILVLDEATAAIDLETdnliQATIRTQFDTC-----TVLTIAHRLNTIMDYT-RVLVLDKG-VVAEFD 1505
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRG----QETLMEILDRLhnqgkTVIVATHDVDLAAEWAdQVIVLKEGrVLAEGD 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1289-1491 |
2.45e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.91 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAaKGEIRIDG------LNVAD--IGLH 1360
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1361 DLRSQLTIIPQDPILFSGTLRMNLdpfgSYSEEDIWWALELsHLHTFVSSQPAGLDF------QCSEGGENLSVGQRQLV 1434
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVGWRPKL-EIDDIVESALKDADLwdeikhKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1435 CLARALLRKSRILVLDEATAAID----LETDNLIQA-TIRTQFDTCTVLTIAHRLNTIMDYT 1491
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSELTMVIVSHNLHQVSRLSDFT 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
644-782 |
2.48e-12 |
|
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: 68.34 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG--------------SVAYVPQQAWI-QNCTLQEN 708
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 709 VL-FGKALNPKRYQQTLEACALLADLEMLPGGDQteigeKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:cd03218 96 ILaVLEIRGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1305-1457 |
2.74e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 67.84 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRID----GLNVADIG---LHDLR-------SQ-LTII 1369
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRrrtigyvSQfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1370 PQ--------DPILFSGT-------------LRMNLDpfgsyseEDIWwalelsHL--HTFvssqpagldfqcsEGGEnl 1426
Cdd:COG4778 106 PRvsaldvvaEPLLERGVdreearararellARLNLP-------ERLW------DLppATF-------------SGGE-- 157
|
170 180 190
....*....|....*....|....*....|.
gi 9955970 1427 svgqRQLVCLARALLRKSRILVLDEATAAID 1457
Cdd:COG4778 158 ----QQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
644-777 |
2.80e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMkGS---VAYVPQQawiQ-----NCTLQENVlfgKAL 715
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQH---QeeldpDKTVLDEL---RDG 403
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 716 NPKRYQQtlEACALLADLeMLPGGDQ-TEIGekgiNLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:COG0488 404 APGGTEQ--EVRGYLGRF-LFSGDDAfKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
651-789 |
2.85e-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: 68.07 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 651 VPKGALVAVVGPVGCGKSSLVSALLGEMEK---LEGKV----------HMKGSVAYVPQQ-AWIQNCTLQENVLF----- 711
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQIlfngqprkpdQFQKCVAYVRQDdILLPGLTVRETLTYtailr 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 712 GKALNPKRYQQTLEACALLADLEMLPGGdqteiGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHI 789
Cdd:cd03234 110 LPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
654-784 |
3.24e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 654 GALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG----------SVAYV-PQQAWIQNCTLQENVLFGKALNPKRYQQ 722
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFWAAFLGGEELD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 723 TLEA-CAL-LADLEMLPGGdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH 784
Cdd:PRK13539 108 IAAAlEAVgLAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
644-777 |
3.60e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG--SVAYVPQQAWI-QNCTLQENVLFGkalNPKRY 720
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLdDDLTVLDTVLDG---DAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 721 QQTLEACALLADLEMlPGGDQTEIGEK-----------------------GI----------NLSGGQRQRVSLARAVYS 767
Cdd:COG0488 91 ALEAELEELEAKLAE-PDEDLERLAELqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLS 169
|
170
....*....|
gi 9955970 768 DADIFLLDDP 777
Cdd:COG0488 170 EPDLLLLDEP 179
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
644-849 |
3.95e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.73 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSAL-LGEMEKlEGKVHMKGS-------------------VAYVPQQ--AWiQ 701
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQynLW-P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 702 NCTLQENVLFG--KALNPKRYQQTLEACALLADLEMLPGGDQTEIgekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:PRK11124 96 HLTVQQNLIEApcRVLGLSKDQALARAEKLLERLRLKPYADRFPL-----HLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 780 AVDSHVAKHIFDhvIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQVSEMGPYPALLQ-RNGSFANFL 849
Cdd:PRK11124 171 ALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGDASCFTQpQTEAFKNYL 240
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1056-1260 |
4.19e-12 |
|
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: 68.57 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1056 PQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTP---LFTVVILPLAVLytlVQRFYAAT 1132
Cdd:cd18544 88 PLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWrlaLISLLVLPLLLL---ATYLFRKK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1133 SRQLKRLESVSRSPIYSHFSETVTGASVIRAYNR----SRDFEIISDTKVDANQRScypyIISNRWLSIGVEFVGNcvVL 1208
Cdd:cd18544 165 SRKAYREVREKLSRLNAFLQESISGMSVIQLFNRekreFEEFDEINQEYRKANLKS----IKLFALFRPLVELLSS--LA 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1209 FAALFAVIGRSSLNpGLVGLSVSYslqvTFaLNWM------IRMMSD----LESNIVAVERV 1260
Cdd:cd18544 239 LALVLWYGGGQVLS-GAVTLGVLY----AF-IQYIqrffrpIRDLAEkfniLQSAMASAERI 294
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
598-782 |
4.46e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 598 SLKRIQQF---LSQEELDPQSVERKTISPGYAITIHSGTFTwaqdLP---PTLHSLDIQVPKGALVAVVGPVGCGKSSLV 671
Cdd:COG4178 331 TVDRLAGFeeaLEAADALPEAASRIETSEDGALALEDLTLR----TPdgrPLLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 672 SALLGemekL----EGKVHM--KGSVAYVPQQAWIQNCTLQENVLF---GKALNPKRYQQTLEACALLADLEMLpggDQT 742
Cdd:COG4178 407 RAIAG----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGHLAERL---DEE 479
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9955970 743 EIGEKGinLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:COG4178 480 ADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1274-1513 |
4.56e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1274 VEGSRPPEGwPPRGEV--EFRNYSVRYRpgldlvLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDG 1351
Cdd:COG1129 241 LEDLFPKRA-AAPGEVvlEVEGLSVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1352 -----LNVAD-----IGL--HDlRSQLTIIPQDPILFSGTLrMNLDPFGSYSEedIWWALELSHLHTFVSS---QPAGLD 1416
Cdd:COG1129 314 kpvriRSPRDairagIAYvpED-RKGEGLVLDLSIRENITL-ASLDRLSRGGL--LDRRRERALAEEYIKRlriKTPSPE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1417 FQCSeggeNLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCT-----------VLTIAHrln 1485
Cdd:COG1129 390 QPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKavivisselpeLLGLSD--- 462
|
250 260 270
....*....|....*....|....*....|...
gi 9955970 1486 timdytRVLVLDKG-VVAEFD----SPANLIAA 1513
Cdd:COG1129 463 ------RILVMREGrIVGELDreeaTEEAIMAA 489
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
631-834 |
5.12e-12 |
|
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: 67.22 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 631 SGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGeMEK-LEGKVHMKG----------------SVAY 693
Cdd:cd03258 8 SKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERpTSGSVLVDGtdltllsgkelrkarrRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 694 VPQQ-AWIQNCTLQENVLF-------GKALNPKRYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAV 765
Cdd:cd03258 87 IFQHfNLLSSRTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 766 YSDADIFLLDDPLSAVDSHVAKHIFD--HVIGPEgvlAGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGP 834
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILAllRDINRE---LGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1293-1504 |
5.21e-12 |
|
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: 66.83 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1293 NYSVRYRPGLdlVLRDLSLHVHGGeKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGlHDLRSQLTIIPQD 1372
Cdd:cd03264 5 NLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1373 PILFSG-TLRMNLDPFG-------SYSEEDIWWALELSHLHTFVSSQPAGLdfqcseggenlSVGQRQLVCLARALLRKS 1444
Cdd:cd03264 81 FGVYPNfTVREFLDYIAwlkgipsKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1445 RILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMD-YTRVLVLDKGVVAEF 1504
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
644-829 |
5.75e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGeMEKLEGKVHMKGSVayvPQQAWIQNCTL--QE-----------NVL 710
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTA---PLAEAREDTRLmfQDarllpwkkvidNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FGKALNPK-RYQQTLEACALlADlemlpggdqtEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDShVAKHI 789
Cdd:PRK11247 104 LGLKGQWRdAALQALAAVGL-AD----------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRIE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9955970 790 FDHVIGPEGVLAGKTRVLVTHGIS-FLPQTDFIIVLADGQV 829
Cdd:PRK11247 172 MQDLIESLWQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1305-1502 |
6.16e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGlHDLRSQLTI--IPQDPILFSG-TLR 1381
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1382 MNLdPFGSYSEEDiwwalELSHLHTFVSSQPAGLDFQCSEGgeNLSVGQRQLVCLARALLRKSRILVLDEATAAID-LET 1460
Cdd:PRK15439 105 ENI-LFGLPKRQA-----SMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9955970 1461 DNLIQATIRTQFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVA 1502
Cdd:PRK15439 177 ERLFSRIRELLAQGVGIVFISHKLPEIRQLAdRISVMRDGTIA 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
642-841 |
6.72e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.04 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALlGEMEKLEG------KVHMKGSVA----------YVPQQAWI-QNCT 704
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSgdlivdGLKVNDPKVderlirqeagMVFQQFYLfPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLFGkalnPKRYQQTLEACALLADLEMLpggDQTEIGEKG----INLSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:PRK09493 94 ALENVMFG----PLRVRGASKEEAEKQARELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 781 VDSHVaKHifdHVIGPEGVLA--GKTRVLVTHGISFLPQT-DFIIVLADGQVSEMGPYPALLQR 841
Cdd:PRK09493 167 LDPEL-RH---EVLKVMQDLAeeGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
644-834 |
6.88e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.25 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGKVHMKGS----------------VAYVPQQawIQN 702
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQdifkmdvielrrrvqmVFQIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 CTLQENVLFGKALN---------PKRYQQTLEACALLADLemlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDADIFL 773
Cdd:PRK14247 97 LSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 774 LDDPLSAVDSHVAKHIfdhvigPEGVLAGK---TRVLVTHgisFLPQ----TDFIIVLADGQVSEMGP 834
Cdd:PRK14247 170 ADEPTANLDPENTAKI------ESLFLELKkdmTIVLVTH---FPQQaariSDYVAFLYKGQIVEWGP 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
694-845 |
7.21e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 694 VPQQAWIQNCTLQENVLFGKAlNPKRyQQTLEACALLAD---LEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDAD 770
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKE-DATR-EDVKRACKFAAIdefIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 771 IFLLDDPLSAVDSHVAKHIFDHVIGPEGVlAGKTRVLVTHGISFLPQTDFIIVLADGqvsemgpypallQRNGSF 845
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVDIKDK-ADKTIITIAHRIASIKRSDKIVVFNNP------------DRTGSF 1440
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
644-849 |
7.41e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSAL-LGEMEKlEGKVHMKGS-------------------VAYVPQQ--AWiQ 701
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD-SGQLNIAGHqfdfsqkpsekairllrqkVGMVFQQynLW-P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 702 NCTLQENVLFG--KALNPKRYQQTLEACALLADLEMLPGGDQTEIgekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:COG4161 96 HLTVMENLIEApcKVLGLSKEQAREKAMKLLARLRLTDKADRFPL-----HLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 780 AVDSHVAKHIFDhvIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQVSEMGPYPALLQ-RNGSFANFL 849
Cdd:COG4161 171 ALDPEITAQVVE--IIRELSQTGITQVIVTHEVEFARKVaSQVVYMEKGRIIEQGDASHFTQpQTEAFAHYL 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1301-1470 |
7.67e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1301 GLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRI----LEAAKGEIRIDGlnvADIGLHDLRSQLTII-PQDPIL 1375
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTT----LLRLiaglLPPAAGTIKLDG---GDIDDPDVAEACHYLgHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1376 FSGTLRMNL----DPFGSySEEDIWWALE---LSHL-HTfvssqPAGldfqcseggeNLSVGQRQLVCLARALLRKSRIL 1447
Cdd:PRK13539 86 PALTVAENLefwaAFLGG-EELDIAAALEavgLAPLaHL-----PFG----------YLSAGQKRRVALARLLVSNRPIW 149
|
170 180
....*....|....*....|...
gi 9955970 1448 VLDEATAAIDLETDNLIQATIRT 1470
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRA 172
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
647-810 |
7.68e-12 |
|
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: 65.98 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNC-------------TLQENVLFGK 713
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylghapgikttlSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 714 ALNPKryQQTLEACAL--LADLEMLPGGdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFD 791
Cdd:cd03231 99 ADHSD--EQVEEALARvgLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*....
gi 9955970 792 HVIGPEGvlAGKTRVLVTH 810
Cdd:cd03231 167 AMAGHCA--RGGMVVLTTH 183
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1289-1470 |
9.08e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNysVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHdLRSQLTI 1368
Cdd:PRK13537 8 IDFRN--VEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQ----DPILfsgTLRMNLDPFGSY-------SEEDIWWALELSHLHTfvssqpaGLDFQCSEggenLSVGQRQLVCLA 1437
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLEN-------KADAKVGE----LSGGMKRRLTLA 150
|
170 180 190
....*....|....*....|....*....|...
gi 9955970 1438 RALLRKSRILVLDEATAAIDLETDNLIQATIRT 1470
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRS 183
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
646-792 |
1.27e-11 |
|
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: 69.39 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 646 SLDIQVPKGALVAVVGPVGCGKSSLVSaLLGEMEKLEGKVHMK---GSVAYVPQQAWIQNCTLQENVLFgkalnPKRYQQ 722
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKpakGKLFYVPQRPYMTLGTLRDQIIY-----PDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 723 TLEACALLADLE-MLPGGDQTEIGEKGIN----------LSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFD 791
Cdd:TIGR00954 544 MKRRGLSDKDLEqILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
.
gi 9955970 792 H 792
Cdd:TIGR00954 624 L 624
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1289-1513 |
1.32e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.26 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLD--------------------LVLRDLSLHVHGGEKVGIVGRTGAGKSsmTLC--LFRILEAAKGE 1346
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKS--TLLklIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1347 IRIDG-----LNVAdIGLHdlrSQLTIIpqDPILFSGTLrMNLdpfgsySEEDIwwalelSHLHTFVssqpagLDFqcSE 1421
Cdd:COG1134 83 VEVNGrvsalLELG-AGFH---PELTGR--ENIYLNGRL-LGL------SRKEI------DEKFDEI------VEF--AE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1422 GGE-------NLSVGQRqlvclAR-----ALLRKSRILVLDEATAAIDLE----TDNLIQATIRtqfDTCTVLTIAHRLN 1485
Cdd:COG1134 136 LGDfidqpvkTYSSGMR-----ARlafavATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSHSMG 207
|
250 260
....*....|....*....|....*....
gi 9955970 1486 TIMDY-TRVLVLDKGVVAEFDSPANLIAA 1513
Cdd:COG1134 208 AVRRLcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
642-824 |
1.50e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS-VAYVPQQAWIQN---CTlQENVLFGKA--- 714
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLKPEIYRQQvsyCA-QTPTLFGDTvyd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 715 --LNPkrYQ---QTLEACALLADLEM--LPggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHvA 786
Cdd:PRK10247 100 nlIFP--WQirnQQPDPAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-N 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 9955970 787 KHIFDHVIgPEGVLAGKTRVL-VTHGISFLPQTDFIIVL 824
Cdd:PRK10247 173 KHNVNEII-HRYVREQNIAVLwVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
627-833 |
1.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 66.70 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMK----------------GS 690
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNnqaitddnfeklrkhiGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 691 VAYVPQQAWIQNcTLQENVLFGKALNPKRYQQTLEACA-LLADLEMLPGGDqteigEKGINLSGGQRQRVSLARAVYSDA 769
Cdd:PRK13648 88 VFQNPDNQFVGS-IVKYDVAFGLENHAVPYDEMHRRVSeALKQVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 770 DIFLLDDPLSAVDSHVAKHIFDHVigpEGVLAGK--TRVLVTHGISFLPQTDFIIVLADGQVSEMG 833
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLV---RKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1289-1505 |
1.93e-11 |
|
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: 65.35 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHD------- 1361
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 ----LRSQLTIIpqDPILFSGTLRmnldpfgSYSEEDI----WWALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQL 1433
Cdd:cd03301 79 qnyaLYPHMTVY--DNIAFGLKLR-------KVPKDEIdervREVAELLQIEHLLDRKPK-----------QLSGGQRQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1434 VCLARALLRKSRILVLDEATAAID--------LETDNLIQ----ATIRTQFDTCTVLTIAhrlntimdyTRVLVLDKGVV 1501
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDaklrvqmrAELKRLQQrlgtTTIYVTHDQVEAMTMA---------DRIAVMNDGQI 209
|
....
gi 9955970 1502 AEFD 1505
Cdd:cd03301 210 QQIG 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1305-1503 |
1.93e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILeAAKGEIRIDGLNVADIG---LHDLRSQLTIIPQDPilfSGTL- 1380
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1381 -RMNLdpfgsysEEDIWWALELSHLHTFVSSQPA---------GLDFQC-----SEggenLSVGQRQLVCLARALLRKSR 1445
Cdd:PRK15134 377 pRLNV-------LQIIEEGLRVHQPTLSAAQREQqviavmeevGLDPETrhrypAE----FSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1446 ILVLDEATAAIdletDNLIQATIRT------QFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVAE 1503
Cdd:PRK15134 446 LIILDEPTSSL----DKTVQAQILAllkslqQKHQLAYLFISHDLHVVRALChQVIVLRQGEVVE 506
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1289-1514 |
2.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.41 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDG--LNVADIGLHDLRSQL 1366
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDP--ILFSGTLR-------MNLDPFGSYSEEDIWWALE---LSHLhtfvSSQPAgldfqcseggENLSVGQRQLV 1434
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKrtgIEHL----KDKPT----------HCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1435 CLARALLRKSRILVLDEATAAID-LETDNLIQATIRTQFDTCTVLTIA-HRLNTIMDYT-RVLVLDKGVVAEFDSPANLI 1511
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKELGLTIIIAtHDIDIVPLYCdNVFVMKEGRVILQGNPKEVF 230
|
...
gi 9955970 1512 AAR 1514
Cdd:PRK13636 231 AEK 233
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
982-1451 |
2.44e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 68.29 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 982 SAAAIGANVWLSAWTNDAMADSRQNNTSLrLGVYAALGILqgFLVmlaamAMAAGGIQAARVLHQALLH------NKIR- 1054
Cdd:COG4615 22 GLLSGLANAGLIALINQALNATGAALARL-LLLFAGLLVL--LLL-----SRLASQLLLTRLGQHAVARlrlrlsRRILa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1055 SPQSFFDTTPSGRILNCFSKDIyvvdEVLAPVILMLLNSFFNAISTLVVI--MA--STPLFTVVILPLAVLYTLVQRFYA 1130
Cdd:COG4615 94 APLERLERIGAARLLAALTEDV----RTISQAFVRLPELLQSVALVLGCLayLAwlSPPLFLLTLVLLGLGVAGYRLLVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1131 ATSRQLKRLeSVSRSPIYSHFSETVTGASVIRaYNRSR-------DFEIISDTKVDANQRSCYPYIISNRWlsigvefvG 1203
Cdd:COG4615 170 RARRHLRRA-REAEDRLFKHFRALLEGFKELK-LNRRRrraffdeDLQPTAERYRDLRIRADTIFALANNW--------G 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1204 NCVVLFA---ALFAVIGRSSLNPGLVglsVSYSLQVTF---ALNWMIRMMSDLESNIVAVERVKEYSKTETEAPWVVEGS 1277
Cdd:COG4615 240 NLLFFALiglILFLLPALGWADPAVL---SGFVLVLLFlrgPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1278 RPPEGWPPRGEVEFRNYSVRYRPGLD---LVLRDLSLHVHGGEKVGIVGRTGAGKS--SMTLC-LFRileAAKGEIRIDG 1351
Cdd:COG4615 317 AAPPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKStlAKLLTgLYR---PESGEILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1352 LNVADIGLHDLRSQLTIIPQDPILFSGTLrmNLDPFGSYSEEDIWWA-LELSHLHTFvssqpagldfqcsEGGE----NL 1426
Cdd:COG4615 394 QPVTADNREAYRQLFSAVFSDFHLFDRLL--GLDGEADPARARELLErLELDHKVSV-------------EDGRfsttDL 458
|
490 500
....*....|....*....|....*
gi 9955970 1427 SVGQRQLVCLARALLRKSRILVLDE 1451
Cdd:COG4615 459 SQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1308-1502 |
3.02e-11 |
|
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: 64.44 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1308 DLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAdiGLHDLRSQLTIIPQDPILFSG-TLRMNLD- 1385
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1386 ---PFGSYSEED---IWWALELSHLHTFVSSQPagldfqcseggENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLE 1459
Cdd:cd03298 94 glsPGLKLTAEDrqaIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9955970 1460 TDNLIQATIRT--QFDTCTVLTIAHRLNTIMD-YTRVLVLDKGVVA 1502
Cdd:cd03298 163 LRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
738-839 |
3.28e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 738 GGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDhvIGPEGVLAGKTRVLVTHGISFLPQ 817
Cdd:PRK10619 140 GIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARH 217
|
90 100
....*....|....*....|...
gi 9955970 818 -TDFIIVLADGQVSEMGPYPALL 839
Cdd:PRK10619 218 vSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
645-810 |
3.74e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 645 HSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG------------SVAYVPQQAWIQN-CTLQENVLF 711
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTeLTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 GKAL-NPKRYQQTLEACAL--LADLEMLPGGdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH---- 784
Cdd:PRK13538 98 YQRLhGPGDDEALWEALAQvgLAGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgvar 167
|
170 180
....*....|....*....|....*.
gi 9955970 785 VAKHIFDHvigpegVLAGKTRVLVTH 810
Cdd:PRK13538 168 LEALLAQH------AEQGGMVILTTH 187
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
644-829 |
3.92e-11 |
|
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: 64.16 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSV------------AYVPQQAWIQNCTLQENVLF 711
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealrrigALIEAPGFYPNLTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 GKALNPKRYQQTLEAcalladLEMLpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDshvakhifd 791
Cdd:cd03268 96 LARLLGIRKKRIDEV------LDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD--------- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9955970 792 hvigPEGVLA-----------GKTRVLVTHGISFLPQT-DFIIVLADGQV 829
Cdd:cd03268 159 ----PDGIKElrelilslrdqGITVLISSHLLSEIQKVaDRIGIINKGKL 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1306-1489 |
4.14e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNV----------ADIGLhdLRSQLTIIPQDPI- 1374
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeAGIGI--IHQELNLIPQLTIa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1375 --LFSGtlRMNLDPFGS------YSEEDIWWA-LELSHlhtfVSSQPAGldfqcseggeNLSVGQRQLVCLARALLRKSR 1445
Cdd:PRK10762 98 enIFLG--REFVNRFGRidwkkmYAEADKLLArLNLRF----SSDKLVG----------ELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9955970 1446 ILVLDEATAAI-DLETDNLIQATIRTQFDTCTVLTIAHRLNTIMD 1489
Cdd:PRK10762 162 VIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIFE 206
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1305-1514 |
5.03e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.94 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSsMTLclfRI---LEAA-KGEIRIDGlNVADIGLHDLRSQLTIIPQDPILFsgtl 1380
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKT-TLL---RIiagLETPdSGRIVLNG-RDLFTNLPPRERRVGFVFQHYALF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1381 rmnldP---------FG----SYSEEDI------WwaLELSHLHTFVSSQPAgldfqcseggeNLSVGQRQLVCLARALL 1441
Cdd:COG1118 88 -----PhmtvaeniaFGlrvrPPSKAEIrarveeL--LELVQLEGLADRYPS-----------QLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1442 RKSRILVLDEATAAID------LEtDNLIQATIRTQFdtcTVLTIAHRLNTIMDYT-RVLVLDKGVVAE-------FDSP 1507
Cdd:COG1118 150 VEPEVLLLDEPFGALDakvrkeLR-RWLRRLHDELGG---TTVFVTHDQEEALELAdRVVVMNQGRIEQvgtpdevYDRP 225
|
....*..
gi 9955970 1508 ANLIAAR 1514
Cdd:COG1118 226 ATPFVAR 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1310-1512 |
5.47e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.22 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1310 SLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNvadiglHDL----RSQLTIIPQDPILFSG-TLRMN- 1383
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppsRRPVSMLFQENNLFSHlTVAQNi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1384 ---LDPfgsyseediwwALELSH--------------LHTFVSSQPAgldfqcseggeNLSVGQRQLVCLARALLRKSRI 1446
Cdd:PRK10771 93 glgLNP-----------GLKLNAaqreklhaiarqmgIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1447 LVLDEATAAID----LETDNLIQATIRTQfdTCTVLTIAHRLNTIMDY-TRVLVLDKGVVAEFDSPANLIA 1512
Cdd:PRK10771 151 LLLDEPFSALDpalrQEMLTLVSQVCQER--QLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1292-1513 |
5.68e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1292 RNYSVRYRPG--LDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAA-----KGEIRIDG---LNVADIGLHD 1361
Cdd:PRK15134 9 ENLSVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGeslLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 LR-SQLTIIPQDPILfsgtlrmNLDPFGSYSEEdiwwALELSHLHTFVSSQPA-GLDFQCSE--GGEN-----------L 1426
Cdd:PRK15134 89 VRgNKIAMIFQEPMV-------SLNPLHTLEKQ----LYEVLSLHRGMRREAArGEILNCLDrvGIRQaakrltdyphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1427 SVGQRQLVCLARALLRKSRILVLDEATAAIDLEtdnlIQATIRT------QFDTCTVLTIAHRLNTIMDYT-RVLVLDKG 1499
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVS----VQAQILQllrelqQELNMGLLFITHNLSIVRKLAdRVAVMQNG 233
|
250
....*....|....
gi 9955970 1500 VVAEFDSPANLIAA 1513
Cdd:PRK15134 234 RCVEQNRAATLFSA 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
627-828 |
6.04e-11 |
|
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: 62.08 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDlpPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV--HMKGSVAYVPQqawiqnct 704
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtwGSTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 lqenvlfgkalnpkryqqtleacalladlemlpggdqteigekginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH 784
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9955970 785 VAKHIFDHVIGPEGVLagktrVLVTHGISFLPQ-TDFIIVLADGQ 828
Cdd:cd03221 105 SIEALEEALKEYPGTV-----ILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
644-839 |
6.47e-11 |
|
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: 64.34 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEM------------EKLeGKVHM---KGSVAYV-P--QQAWIQNCTL 705
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygndvrlfgERR-GGEDVwelRKRIGLVsPalQLRFPRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 706 QENVL---FGKALNPKRY--QQTLEACALLADLEMLPGGDQTeIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:COG1119 98 LDVVLsgfFDSIGLYREPtdEQRERARELLELLGLAHLADRP-FGT----LSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 781 VDSHvAKHIFDHVIgpeGVLAG---KTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGPYPALL 839
Cdd:COG1119 173 LDLG-ARELLLALL---DKLAAegaPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
653-833 |
6.83e-11 |
|
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: 64.35 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 653 KGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAWIQNCTLQENVLFGKAlnPKRYQQTLEACALLA 731
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSIT--KDFYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 732 DLEMLPGGDQtEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH-------VAKHIFDHvigpegvlAGKT 804
Cdd:cd03237 102 PLQIEQILDR-EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmaskVIRRFAEN--------NEKT 168
|
170 180 190
....*....|....*....|....*....|
gi 9955970 805 RVLVTHGISFLPQ-TDFIIVLaDGQVSEMG 833
Cdd:cd03237 169 AFVVEHDIIMIDYlADRLIVF-EGEPSVNG 197
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1286-1503 |
7.53e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.16 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1286 RGEVEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAKGEIRIDGLNVADIGLH 1360
Cdd:PRK14247 1 MNKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1361 DLRSQLTIIPQDP-------ILFSGTLRMNLDPFGSYS---EEDIWWALELSHLHTFVSSQ---PAGldfqcseggeNLS 1427
Cdd:PRK14247 79 ELRRRVQMVFQIPnpipnlsIFENVALGLKLNRLVKSKkelQERVRWALEKAQLWDEVKDRldaPAG----------KLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 1428 VGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAH---RLNTIMDYtrVLVLDKGVVAE 1503
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVE 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1289-1457 |
1.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGlDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDG--LNVADIGLHDLRSQL 1366
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDP--ILFSGTLR-------MNLDPFGSYSEEDIWWALELSHLHTFVSSQPagldfqcseggENLSVGQRQLVCLA 1437
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIA 149
|
170 180
....*....|....*....|
gi 9955970 1438 RALLRKSRILVLDEATAAID 1457
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLD 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1290-1514 |
1.25e-10 |
|
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: 65.86 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYR--PGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEA----AKGEIRIDGLNVADIGLHDLR 1363
Cdd:COG4172 8 SVEDLSVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1364 ----SQLTIIPQDPilfsgtlrMN-LDPFgsYS-EEDIWWALElshLHTFVSSQPA-----------GLD---------- 1416
Cdd:COG4172 88 rirgNRIAMIFQEP--------MTsLNPL--HTiGKQIAEVLR---LHRGLSGAAAraralellervGIPdperrldayp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1417 FQcseggenLSVGQRQLVCLARALLRKSRILVLDEATAAIDLeTdnlIQATI-------RTQFDTcTVLTIAHRLNTIMD 1489
Cdd:COG4172 155 HQ-------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV-T---VQAQIldllkdlQRELGM-ALLLITHDLGVVRR 222
|
250 260 270
....*....|....*....|....*....|....*...
gi 9955970 1490 YT-RVLVLDKGVVAE-------FDSPAN-----LIAAR 1514
Cdd:COG4172 223 FAdRVAVMRQGEIVEqgptaelFAAPQHpytrkLLAAE 260
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1305-1512 |
1.37e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.87 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDG--LNVADIGLHDLRSQLTIIPQDP---ILFS-- 1377
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqqIFYTdi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1378 -GTLRMNLDPFGSYSEE---DIWWALELSHLHTFvSSQPagldFQCseggenLSVGQRQLVCLARALLRKSRILVLDEAT 1453
Cdd:PRK13638 96 dSDIAFSLRNLGVPEAEitrRVDEALTLVDAQHF-RHQP----IQC------LSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1454 AAIDLETDNLIQATIRTQFDTCTVLTI-AHRLNTIMDYT-RVLVLDKGVVAEFDSPANLIA 1512
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEISdAVYVLRQGQILTHGAPGEVFA 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
644-841 |
1.41e-10 |
|
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: 62.87 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVP---QQAWIQN------CTLQENVlfgka 714
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNysllpwLTVRENI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 715 lnpkryqqtleACALLADLEMLPGGDQTEIGEKGINL--------------SGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:TIGR01184 76 -----------ALAVDRVLPDLSKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 781 VDSHVAKHIFDHV--IGPEgvlAGKTRVLVTHGIS---FLpqTDFIIVLADGQVSEMG-----PYPALLQR 841
Cdd:TIGR01184 145 LDALTRGNLQEELmqIWEE---HRVTVLMVTHDVDealLL--SDRVVMLTNGPAANIGqilevPFPRPRDR 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1316-1502 |
1.48e-10 |
|
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: 62.70 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1316 GEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGlnvadIGLHDLRSQLTIIPQD---PILFSG-------TLRMNLD 1385
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-----TVLFDSRKKINLPPQQrkiGLVFQQyalfphlNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1386 pFG---------SYSEEDIWWALELSHLhtfVSSQPAGLdfqcseggenlSVGQRQLVCLARALLRKSRILVLDEATAAI 1456
Cdd:cd03297 98 -FGlkrkrnredRISVDELLDLLGLDHL---LNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9955970 1457 DLETDNLIQATIR---TQFDTcTVLTIAHRLNTIMDYT-RVLVLDKGVVA 1502
Cdd:cd03297 163 DRALRLQLLPELKqikKNLNI-PVIFVTHDLSEAEYLAdRIVVMEDGRLQ 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1289-1457 |
1.57e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.52 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSsmTL--CLFRILE-----AAKGEIRIDGLNV--ADIGL 1359
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKS--TLlrCLNRMNDlipgaRVEGEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1360 HDLRSQLTIIPQDPILFSGT--------LRMNldpfGSYSEEDI----WWALELSHLHTFVS---SQPAGldfqcsegge 1424
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSiydnvaygLRLH----GIKSKSELdeivEESLRKAALWDEVKdrlKKSAL---------- 153
|
170 180 190
....*....|....*....|....*....|...
gi 9955970 1425 NLSVGQRQLVCLARALLRKSRILVLDEATAAID 1457
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
644-833 |
1.78e-10 |
|
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: 62.21 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGaLVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS------------VAYVPQQ-AWIQNCTLQENVL 710
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEfGVYPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FGKAL---NPKRYQQtlEACALLADLEMLPGGDQtEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDShVAK 787
Cdd:cd03264 95 YIAWLkgiPSKEVKA--RVDEVLELVNLGDRAKK-KIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EER 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9955970 788 HIFDHVIGpeGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQVSEMG 833
Cdd:cd03264 167 IRFRNLLS--ELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1305-1499 |
1.83e-10 |
|
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: 62.74 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGL--------NVADIGL-HDLRSQL--TIIPQDp 1373
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkrrkkFLRRIGVvFGQKTQLwwDLPVID- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1374 ilfsgTLRMN-----LDPFgSYSE--EDIWWALELSH-LHTFVssqpagldfqcseggENLSVGQRQLVCLARALLRKSR 1445
Cdd:cd03267 115 -----SFYLLaaiydLPPA-RFKKrlDELSELLDLEElLDTPV---------------RQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1446 ILVLDEATAAIDLETDNLIQATIRT---QFDTcTVLTIAHRLNTIMDY-TRVLVLDKG 1499
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEynrERGT-TVLLTSHYMKDIEALaRRVLVIDKG 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1306-1472 |
1.94e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.11 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEA---AKGEIRIDGLNVADIGLHdlRSQLTIIPQDPILFS----- 1377
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1378 GTLRMNLDPFGSYSE--EDIWWALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQLVCLARALLRKSRILVLDEATAA 1455
Cdd:COG4136 95 ENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170
....*....|....*..
gi 9955970 1456 IDletdnliqATIRTQF 1472
Cdd:COG4136 164 LD--------AALRAQF 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1289-1498 |
2.13e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAKGEIRIDGLNV--ADIGLHD 1361
Cdd:PRK14267 5 IETVNLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 LRSQLTIIPQDPILFS----------GTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQpagldfqCSEGGENLSVGQR 1431
Cdd:PRK14267 83 VRREVGMVFQYPNPFPhltiydnvaiGVKLNGLVKSKKELDERVEWALKKAALWDEVKDR-------LNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1432 QLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAH---RLNTIMDYTRVLVLDK 1498
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYLGK 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
646-789 |
2.14e-10 |
|
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: 65.19 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 646 SLDI---QVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLFGKalNPKRYQQ 722
Cdd:COG1245 355 SLEVeggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEFLRSA--NTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 723 TLEacalladlemlpggdQTEIGEK-GI---------NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS----HVAKH 788
Cdd:COG1245 433 SYY---------------KTEIIKPlGLeklldknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKA 497
|
.
gi 9955970 789 I 789
Cdd:COG1245 498 I 498
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
647-842 |
2.23e-10 |
|
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: 62.45 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVP-------------QQAWI-QNCTLQENVLF 711
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPpheiarlgigrtfQIPRLfPELTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 G------KALNPKRYQQTLEACALLADlEMLpggDQTEIGEKG----INLSGGQRQRVSLARAVYSDADIFLLDDP---L 778
Cdd:cd03219 99 AaqartgSGLLLARARREEREARERAE-ELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEPaagL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 779 SAVDSHVAKHIFDHVigpegVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGPyPALLQRN 842
Cdd:cd03219 175 NPEETEELAELIREL-----RERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT-PDEVRNN 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
624-784 |
2.51e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.08 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 624 GYAITIHSGTFTWAQDLpptlhslDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGsvAYVPQQA----- 698
Cdd:PRK10253 10 GEQLTLGYGKYTVAENL-------TVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG--EHIQHYAskeva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 699 -----WIQNCTLQENVLFGKALNPKRY-QQTLEACALLADLEMLPGGDQ----TEIGEKGIN-LSGGQRQRVSLARAVYS 767
Cdd:PRK10253 81 rriglLAQNATTPGDITVQELVARGRYpHQPLFTRWRKEDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLAQ 160
|
170
....*....|....*...
gi 9955970 768 DADIFLLDDPLSAVD-SH 784
Cdd:PRK10253 161 ETAIMLLDEPTTWLDiSH 178
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1295-1501 |
2.51e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1295 SVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRILEaakgeiridGLNVADIG--------LHDLRSQL 1366
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLA---------GLETPSAGellagtapLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1367 TIIPQDPILFSgtLRMNLDPFGSYSEEDiWWALELSHLHTfvssqpAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRI 1446
Cdd:PRK11247 84 RLMFQDARLLP--WKKVIDNVGLGLKGQ-WRDAALQALAA------VGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1447 LVLDEATAAID----LETDNLIQATIRTQ-FdtcTVLTIAHRLN---TIMDytRVLVLDKGVV 1501
Cdd:PRK11247 155 LLLDEPLGALDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeavAMAD--RVLLIEEGKI 212
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
627-845 |
2.96e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 62.95 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLgEMEKLEGKVHMKG-------------SVAY 693
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 694 VPQQAWIQNCTLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFL 773
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 774 LDDP---LSAVDSHVAKHIFDHvigpegVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSF 845
Cdd:cd03289 162 LDEPsahLDPITYQVIRKTLKQ------AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
644-833 |
3.02e-10 |
|
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: 61.61 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQA---------------WIqncTLQE 707
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEArrrlgfvsdstglydRL---TARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 NVLFGKALnpkryqQTLEACALLADLEMLpgGDQTEIGE----KGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS 783
Cdd:cd03266 98 NLEYFAGL------YGLKGDELTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 784 HVAKHIFDHVigPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMG 833
Cdd:cd03266 170 MATRALREFI--RQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
626-782 |
3.34e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.49 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 626 AITIHSGTFTWAQDLpptlhSLDIqvPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGKVHMKGSVAYVP----- 695
Cdd:PRK14243 15 NLNVYYGSFLAVKNV-----WLDI--PKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPdvdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 696 ----------QQAWIQNCTLQENVLFGKALNPKR------YQQTLEACALLADLemlpggdQTEIGEKGINLSGGQRQRV 759
Cdd:PRK14243 88 evrrrigmvfQKPNPFPKSIYDNIAYGARINGYKgdmdelVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRL 160
|
170 180
....*....|....*....|...
gi 9955970 760 SLARAVYSDADIFLLDDPLSAVD 782
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALD 183
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
647-829 |
3.63e-10 |
|
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: 61.75 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG------------SVAYVPQqawiqnctlqENVLFgKA 714
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQ----------FDALF-DE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 715 LNPKryqQTLEACALL-------ADLEMLPGGDQTEIGEKG----INLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS 783
Cdd:cd03263 90 LTVR---EHLRFYARLkglpkseIKEEVELLLRVLGLTDKAnkraRTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9955970 784 HVAKHIFDHVigpEGVLAGKTRVLVTHG---ISFLpqTDFIIVLADGQV 829
Cdd:cd03263 167 ASRRAIWDLI---LEVRKGRSIILTTHSmdeAEAL--CDRIAIMSDGKL 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
644-782 |
4.00e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.98 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSAL--LGEME---KLEGKVHMKG---------------SVAYVPQQAwiqN- 702
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIpgaRVEGEILLDGediydpdvdvvelrrRVGMVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 --CTLQENVLFGKALN---PKRY-----QQTLEACALLADLEmlpggDQteIGEKGINLSGGQRQRVSLARAVYSDADIF 772
Cdd:COG1117 104 fpKSIYDNVAYGLRLHgikSKSEldeivEESLRKAALWDEVK-----DR--LKKSALGLSGGQQQRLCIARALAVEPEVL 176
|
170
....*....|
gi 9955970 773 LLDDPLSAVD 782
Cdd:COG1117 177 LMDEPTSALD 186
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
644-789 |
4.21e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.03 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQ---AWI----QN-----C---TLQE 707
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkraKYIgrvfQDpmmgtApsmTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 NVL----------FGKALNPKRYQQTLEacaLLADLEM-LPGGDQTEIGekgiNLSGGQRQRVSLARAVYSDADIFLLDD 776
Cdd:COG1101 102 NLAlayrrgkrrgLRRGLTKKRRELFRE---LLATLGLgLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170
....*....|...
gi 9955970 777 PLSAVDSHVAKHI 789
Cdd:COG1101 175 HTAALDPKTAALV 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
644-793 |
4.43e-10 |
|
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: 59.86 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHM--KGSVAYVPQQAWIQNCTLQENVLFgkalnpkryq 721
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGTLREQLIY---------- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 722 qtleacalladlemlPGGDqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHV 793
Cdd:cd03223 87 ---------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
644-833 |
4.66e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAWI--------------QNCTLQEN 708
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIkpvrkkvgvvfqfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGKALNPKRYQQTLEACALLA--DLEMLpgGDQTEIGEKG-INLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHV 785
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAaeKLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9955970 786 ---AKHIFDHVIGpegvlAGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMG 833
Cdd:PRK13643 180 rieMMQLFESIHQ-----SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1289-1513 |
4.72e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYS--VRYRPGL------DLVlRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAdIGLH 1360
Cdd:PRK15112 5 LEVRNLSktFRYRTGWfrrqtvEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1361 DLRSQ-LTIIPQDPI-----------LFSGTLRMNLDPFGSYSEEDIWWAL-ELSHLHTFVSSQPagldfqcseggENLS 1427
Cdd:PRK15112 83 SYRSQrIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYP-----------HMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1428 VGQRQLVCLARALLRKSRILVLDEATAAIDLET-DNLIQATIRTQ--FDTCTVLTIAH--RLNTIMDytRVLVLDKGVVA 1502
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMrSQLINLMLELQekQGISYIYVTQHlgMMKHISD--QVLVMHQGEVV 229
|
250
....*....|.
gi 9955970 1503 EFDSPANLIAA 1513
Cdd:PRK15112 230 ERGSTADVLAS 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
633-834 |
4.90e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 633 TFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVaYVPQQAW---------IQN- 702
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvgmvFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 ------CTLQENVLFGKALN--P-----KRYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDA 769
Cdd:PRK13635 91 dnqfvgATVQDDVAFGLENIgvPreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 770 DIFLLDDPLSAVDShvakhifdhvIGPEGVLA---------GKTRVLVTHGISFLPQTDFIIVLADGQVSEMGP 834
Cdd:PRK13635 160 DIIILDEATSMLDP----------RGRREVLEtvrqlkeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
625-842 |
5.17e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.06 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 625 YAITIHSGTFTWaQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQN-- 702
Cdd:PRK13647 3 NIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 -------------CTLQENVLFG---KALNPKRYQQTLEACALLADLEmlpggdqtEIGEKG-INLSGGQRQRVSLARAV 765
Cdd:PRK13647 82 glvfqdpddqvfsSTVWDDVAFGpvnMGLDKDEVERRVEEALKAVRMW--------DFRDKPpYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 766 YSDADIFLLDDPLSAVDSHvakhifdhviGPEGVLA--------GKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGPYP 836
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPR----------GQETLMEildrlhnqGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKS 223
|
....*.
gi 9955970 837 ALLQRN 842
Cdd:PRK13647 224 LLTDED 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
644-810 |
5.36e-10 |
|
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: 60.76 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSvayvPQQAWIQNctlqenvLFG-----KALNPK 718
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----PLDIAARN-------RIGylpeeRGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 719 ryQQTLEACALLADLEMLPGGD----------QTEIGEKGI----NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSh 784
Cdd:cd03269 85 --MKVIDQLVYLAQLKGLKKEEarrridewleRLELSEYANkrveELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP- 161
|
170 180
....*....|....*....|....*.
gi 9955970 785 VAKHIFDHVIGpEGVLAGKTRVLVTH 810
Cdd:cd03269 162 VNVELLKDVIR-ELARAGKTVILSTH 186
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1299-1512 |
5.59e-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: 61.89 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1299 RPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIG---LHDLRSQ--------LT 1367
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPILFSGTLRMNLDPFGSYS-EEDIWWALELSHLHTFVSSQPagldfqcsegGEnLSVGQRQLVCLARALLRKSRI 1446
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAErEERAAEALELVGLEGWEHKYP----------DE-LSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1447 LVLDEATAAIdletDNLIQATIRTQFDTC------TVLTIAHRLNTIM---DytRVLVLDKGVVAEFDSPANLIA 1512
Cdd:cd03294 182 LLMDEAFSAL----DPLIRREMQDELLRLqaelqkTIVFITHDLDEALrlgD--RIAIMKDGRLVQVGTPEEILT 250
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
644-831 |
6.18e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG---SVAYVPQQAWIQNCTLQ-------------- 706
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKAELRNQKLGfiyqfhhllpdfta 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 -ENV----LFGKAlNPKRYQQTLeacalladLEMLPG-GDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:PRK11629 105 lENVamplLIGKK-KPAEINSRA--------LEMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 781 VDSHVAKHIFDhVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSE 831
Cdd:PRK11629 176 LDARNADSIFQ-LLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
642-810 |
6.50e-10 |
|
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: 64.26 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG------------SVAYVPQQAWI-QNCTLQEN 708
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGKALNPKRYQQT-LEACALLADLemlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAK 787
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAqLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180
....*....|....*....|...
gi 9955970 788 HIFDHVIGPEgvlAGKTRVLVTH 810
Cdd:TIGR01257 1099 SIWDLLLKYR---SGRTIIMSTH 1118
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1289-1499 |
7.41e-10 |
|
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: 58.61 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRILEaakGEIRIDglnvadiglhdlrsqlti 1368
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKST----LLKLIA---GELEPD------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 ipqdpilfSGTLRmnldpFGSyseediwwALELSHLhtfvssqpagldfqcseggENLSVGQRQLVCLARALLRKSRILV 1448
Cdd:cd03221 54 --------EGIVT-----WGS--------TVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1449 LDEATAAIDLETDNLIQATIRtQFDtCTVLTIAH-R--LNTIMdyTRVLVLDKG 1499
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALK-EYP-GTVILVSHdRyfLDQVA--TKIIELEDG 143
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1289-1497 |
8.27e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRidglnvadiglHDLRSQLTI 1368
Cdd:PRK09544 5 VSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQ----DPILFSGTLR-MNLDPfgSYSEEDIWWALE---LSHLHtfvsSQPAgldfqcseggENLSVGQRQLVCLARAL 1440
Cdd:PRK09544 72 VPQklylDTTLPLTVNRfLRLRP--GTKKEDILPALKrvqAGHLI----DAPM----------QKLSGGETQRVLLARAL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1441 LRKSRILVLDEATAAID----LETDNLIQaTIRTQFDtCTVLTIAHRLNTIMDYT-RVLVLD 1497
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDvngqVALYDLID-QLRRELD-CAVLMVSHDLHLVMAKTdEVLCLN 195
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1275-1483 |
8.73e-10 |
|
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: 63.23 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1275 EGSRPPEGWPPRGEVEFRNYSVRYR------PGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRILeaakGE-- 1346
Cdd:TIGR00954 431 EGGRNSNLVPGRGIVEYQDNGIKFEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS----LFRIL----GElw 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1347 -IRIDGLNVadiglhDLRSQLTIIPQDPILFSGTLR------MNLDPF--GSYSEEDIWWALELSHLHTFVSSQpAGLDF 1417
Cdd:TIGR00954 503 pVYGGRLTK------PAKGKLFYVPQRPYMTLGTLRdqiiypDSSEDMkrRGLSDKDLEQILDNVQLTHILERE-GGWSA 575
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1418 QCsEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAI--DLEtDNLIQATIRTQFdtcTVLTIAHR 1483
Cdd:TIGR00954 576 VQ-DWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVsvDVE-GYMYRLCREFGI---TLFSVSHR 638
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
644-829 |
8.93e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.25 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG--------SVAYVPQQAWI--QNC-------TLQ 706
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTVGIvfQNPddqlfapTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFGkALN--------PKRYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPL 778
Cdd:PRK13639 98 EDVAFG-PLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9955970 779 SAVDSHVAKHIFD--HVIGPEGVlagkTRVLVTHGISFLP-QTDFIIVLADGQV 829
Cdd:PRK13639 166 SGLDPMGASQIMKllYDLNKEGI----TIIISTHDVDLVPvYADKVYVMSDGKI 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
599-810 |
9.77e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.16 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 599 LKRIQQFLSQEELDPQSVERKTISPGYAITIHSGTF-TWAQDL---------PPTLHSLDIQVPKGALVAVVGPVGCGKS 668
Cdd:PRK13536 2 LTRAVAEEAPRRLELSPIERKHQGISEAKASIPGSMsTVAIDLagvsksygdKAVVNGLSFTVASGECFGLLGPNGAGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 669 SLVSALLGEMEKLEGKVHMKGsvAYVPQQAWI---------------QNCTLQENVL-FGKALNPKryQQTLEAC-ALLA 731
Cdd:PRK13536 82 TIARMILGMTSPDAGKITVLG--VPVPARARLararigvvpqfdnldLEFTVRENLLvFGRYFGMS--TREIEAViPSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 732 DLEMLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHvAKH-IFDHVigpEGVLA-GKTRVLVT 809
Cdd:PRK13536 158 EFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHlIWERL---RSLLArGKTILLTT 229
|
.
gi 9955970 810 H 810
Cdd:PRK13536 230 H 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
647-789 |
1.28e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 59.68 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNC-------------TLQENVLFGK 713
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylghlpglkpelSALENLHFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 714 ALNPKRYQQTLEACAL--LADLEMLPGGdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD--------S 783
Cdd:TIGR01189 99 AIHGGAQRTIEDALAAvgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagvallaG 168
|
....*.
gi 9955970 784 HVAKHI 789
Cdd:TIGR01189 169 LLRAHL 174
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
642-782 |
2.68e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.63 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSV-----------AYVpqqawIQN------CT 704
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadrdiAMV-----FQNyalyphMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLFG-------KALNPKRYQqtlEACALLadlemlpggdqtEIGE----KGINLSGGQRQRVSLARAVYSDADIFL 773
Cdd:PRK11650 93 VRENMAYGlkirgmpKAEIEERVA---EAARIL------------ELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
....*....
gi 9955970 774 LDDPLSAVD 782
Cdd:PRK11650 158 FDEPLSNLD 166
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
626-843 |
2.75e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.20 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 626 AITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSS---LVSALLGEMEKLEGKVHMKGsVAYVPQQAW--- 699
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWdir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 700 ------IQN-------CTLQENVLFG---KALnPKRYQQTLEAcALLADLEMLpggdqTEIGEKGINLSGGQRQRVSLAR 763
Cdd:PRK13640 84 ekvgivFQNpdnqfvgATVGDDVAFGlenRAV-PRPEMIKIVR-DVLADVGML-----DYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 764 AVYSDADIFLLDDPLSAVDSHVAKHIFDhVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQV------SEMGPYPA 837
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILK-LIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLlaqgspVEIFSKVE 235
|
....*.
gi 9955970 838 LLQRNG 843
Cdd:PRK13640 236 MLKEIG 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
641-841 |
2.81e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 641 PPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEM----EKLEGKVHMKGsVAYVPQQA-WIQNCTLQENVLfgKAL 715
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDG-KPVAPCALrGRKIATIMQNPR--SAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 716 NPKRY-----QQTLEACALLADLEMLP--------GGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:PRK10418 93 NPLHTmhthaRETCLALGKPADDATLTaaleavglENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 783 SHVAKHIFD------HVIGPeGVLagktrvLVTHGISFLPQ-TDFIIVLADGQVSEMGPYPALLQR 841
Cdd:PRK10418 173 VVAQARILDllesivQKRAL-GML------LVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1289-1510 |
2.91e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDLVLR---DLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIG----LHD 1361
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 LRSQLTIIPQDP--ILFSGTLRMNL----DPFGSYSEEDIWWALELSHLhtfvssqpAGLDFQCSEGGE-NLSVGQRQLV 1434
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEM--------VGLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1435 CLARALLRKSRILVLDEATAAID----LETDNLIQATIRTqfdTCTVLTIAHRLNTIMDYTR-VLVLDKGVVAEFDSPAN 1509
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS---GQTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSD 230
|
.
gi 9955970 1510 L 1510
Cdd:PRK13643 231 V 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1306-1501 |
2.96e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.64 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAK---GEIRIDGLNVADIG-----LHDLRSQLTIIPQDPILFS 1377
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGrlardIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1378 GTLRMNLDPFGSYSEEDIW-----WALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEA 1452
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWrtcfsWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1453 TAAIDLETDNLIQATIR--TQFDTCTVLTIAHRLNTIMDY-TRVLVLDKGVV 1501
Cdd:PRK09984 180 IASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
644-831 |
3.01e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-----------------SVAYVPQQ-AWIQNCTL 705
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 706 QENV-----LFGKALNPKRYQ--QTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPL 778
Cdd:PRK10584 106 LENVelpalLRGESSRQSRNGakALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9955970 779 SAVDSHVAKHIFDHVIGPEGVLAgKTRVLVTHGISFLPQTDFIIVLADGQVSE 831
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHG-TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1305-1503 |
3.02e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 58.31 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKS--SMTLCLFRILEAAKGEIRIDGLNVADIGLHDlRSQ--LTIIPQDPILFSGtl 1380
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKStlAKTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1381 rmnldpfgsyseediwwaLELSHLHTFVssqpagldfqcsegGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLET 1460
Cdd:cd03217 92 ------------------VKNADFLRYV--------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9955970 1461 DNLIQATIRTQFD-TCTVLTIAHRLNtIMDY---TRVLVLDKGVVAE 1503
Cdd:cd03217 140 LRLVAEVINKLREeGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVK 185
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
635-782 |
3.02e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.71 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 635 TWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS----------VAYVPQ-QAWIQNC 703
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHlPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 704 TLQENVLFGKALNPKRYQQTL-EACALLAdlemLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQMPgSALAIVG----LAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
627-838 |
3.09e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.10 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLPPTLHSLD---IQVPKGALVAVVGPVGCGKSSLV---SALL--------------------GEMEK 680
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDnvsVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtgtiewifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 681 LEGKVHMKGS--------------VAYVPQQAWIQ--NCTLQENVLFGkalnPKRYQQT-LEACALLADLEMLPGGDQTE 743
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikeirrrVGVVFQFAEYQlfEQTIEKDIIFG----PVSMGVSkEEAKKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 744 IGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDhvIGPEGVLAGKTRVLVTHGI-SFLPQTDFII 822
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTI 236
|
250
....*....|....*..
gi 9955970 823 VLADGQVSEMG-PYPAL 838
Cdd:PRK13651 237 FFKDGKIIKDGdTYDIL 253
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
626-829 |
3.10e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.62 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 626 AITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG------SVAYVPQQAW 699
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 700 I--QN-------CTLQENVLFG---KALNPKRYQQTLEACALLADLEMLpggdqteIGEKGINLSGGQRQRVSLARAVYS 767
Cdd:PRK13632 87 IifQNpdnqfigATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 768 DADIFLLDDPLSAVDSHVAKHI--FDHVIGPEGvlaGKTRVLVTHGISFLPQTDFIIVLADGQV 829
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIkkIMVDLRKTR---KKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1304-1501 |
3.21e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.72 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1304 LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIG-LHDLRSQLTIIPQDP--------- 1373
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivativ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1374 ---ILFsGTLRMNLDPFGSYSEEDiwWALELSHLHTFVSSQPagldfqcseggENLSVGQRQLVCLARALLRKSRILVLD 1450
Cdd:PRK13633 104 eedVAF-GPENLGIPPEEIRERVD--ESLKKVGMYEYRRHAP-----------HLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1451 EATAAIDLETDNLIQATIR--TQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVV 1501
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1306-1507 |
3.25e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGL--------NVADIGL---HdlRSQL--TIIPQD 1372
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvpfkrrkeFARRIGVvfgQ--RSQLwwDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1373 pilfsgTLRMN-----LDP------FGSYSEediwwALELSH-LHTFVssqpagldfqcseggENLSVGQRQLVCLARAL 1440
Cdd:COG4586 116 ------SFRLLkaiyrIPDaeykkrLDELVE-----LLDLGElLDTPV---------------RQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1441 LRKSRILVLDEATAAIDLETDNLIQATIRT---QFDTcTVLTIAHRLNTIMDY-TRVLVLDKGVVAeFDSP 1507
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEynrERGT-TILLTSHDMDDIEALcDRVIVIDHGRII-YDGS 238
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
647-810 |
3.40e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKvhmkgSVAYVPQQAWIQNCTLQENVLfgkalnpkRYQQTLEA 726
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA-----GCVDVPDNQFGREASLIDAIG--------RKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 727 CALLADLemlpggdqteigekGIN-----------LSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKhIFDHVIG 795
Cdd:COG2401 116 VELLNAV--------------GLSdavlwlrrfkeLSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK-RVARNLQ 180
|
170
....*....|....*
gi 9955970 796 PEGVLAGKTRVLVTH 810
Cdd:COG2401 181 KLARRAGITLVVATH 195
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
640-829 |
3.63e-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: 57.83 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 640 LPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--------------VAYVP----QQAWIQ 701
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 702 NCTLQENVLfgkalnpkryqqtleacalLADLemlpggdqteigekginLSGGQRQRVSLARAVYSDADIFLLDDPLSAV 781
Cdd:cd03215 92 DLSVAENIA-------------------LSSL-----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9955970 782 DSHVAKHIFDHVIgpEGVLAGKTRVLVThgiSFLPQ----TDFIIVLADGQV 829
Cdd:cd03215 136 DVGAKAEIYRLIR--ELADAGKAVLLIS---SELDEllglCDRILVMYEGRI 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1308-1499 |
3.90e-09 |
|
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: 60.99 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1308 DLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAA-KGEIRIDGLNVaDIG--LHDLRSQLTIIPQD-------PILFS 1377
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV-DIRnpAQAIRAGIAMVPEDrkrhgivPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1378 G---TLRMnLDPFGSYSEED-------IWWALELSHLHTFVSSQPAGldfqcseggeNLSVGQRQLVCLARALLRKSRIL 1447
Cdd:TIGR02633 357 GkniTLSV-LKSFCFKMRIDaaaelqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 1448 VLDEATAAIDL----ETDNLIQATIRtqfDTCTVLTIAHRLNTIMDYT-RVLVLDKG 1499
Cdd:TIGR02633 426 ILDEPTRGVDVgakyEIYKLINQLAQ---EGVAIIVVSSELAEVLGLSdRVLVIGEG 479
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1049-1172 |
3.97e-09 |
|
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: 59.74 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1049 LHNKI-RSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTP---LFTVVILPLAVLytL 1124
Cdd:cd18552 78 LFDKLlRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWkltLIALVVLPLAAL--P 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1125 VQRFyaatSRQLKRL-----ESVSRspIYSHFSETVTGASVIRAYNRsRDFEI 1172
Cdd:cd18552 156 IRRI----GKRLRKIsrrsqESMGD--LTSVLQETLSGIRVVKAFGA-EDYEI 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
654-834 |
4.20e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 654 GALVAVVGPVGCGKSSLVSALLGEMEK---------LEGKV----HMKGSVAYVPQQ-AWIQNCTLQENVLFGKALNPKR 719
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkgsgsvlLNGMPidakEMRAISAYVQQDdLFIPTLTVREHLMFQAHLRMPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 720 Y----QQTLEACALLADLEMLPGGDqTEIGEKGI--NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHV 793
Cdd:TIGR00955 131 RvtkkEKRERVDEVLQALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9955970 794 IGpegvLA--GKTRVLVTHGIS--FLPQTDFIIVLADGQVSEMGP 834
Cdd:TIGR00955 210 KG----LAqkGKTIICTIHQPSseLFELFDKIILMAEGRVAYLGS 250
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1306-1488 |
4.52e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRILEAA------KGEIRIDG--LNVADI------GLHDLRSQLTIIPQ 1371
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKST----LMKVLSGVyphgtyEGEIIFEGeeLQASNIrdteraGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1372 DPIL---FSGTL-----RMNLDPFgsYSEEDIWwaleLSHLHTFVS-SQPAGldfqcseggeNLSVGQRQLVCLARALLR 1442
Cdd:PRK13549 97 LSVLeniFLGNEitpggIMDYDAM--YLRAQKL----LAQLKLDINpATPVG----------NLGLGQQQLVEIAKALNK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9955970 1443 KSRILVLDEATAAI-DLETDNL--IQATIRTQFDTCtvLTIAHRLNTIM 1488
Cdd:PRK13549 161 QARLLILDEPTASLtESETAVLldIIRDLKAHGIAC--IYISHKLNEVK 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1305-1503 |
4.71e-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: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLfRILEAAK------GEIRIDG---LNVADIGLHDLRSQLTIIPQDPIL 1375
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEagtirvGDITIDTarsLSQQKGLIRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1376 FSGtlRMNLD-----PF---GSYSEEDIWWALELShlhtfvssQPAGLdfqcsEGGEN-----LSVGQRQLVCLARALLR 1442
Cdd:PRK11264 97 FPH--RTVLEniiegPVivkGEPKEEATARARELL--------AKVGL-----AGKETsyprrLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1443 KSRILVLDEATAAIDLETDNLIQATIRT-QFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVAE 1503
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDVAdRAIFMDQGRIVE 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
647-810 |
4.76e-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: 58.15 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG------------SVAYVPQQAWIQN-CTLQENV-LFG 712
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDeLTGWENLyIHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 713 KALNPKRYQQTLEACALLADLEMLPGGDqteigEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDH 792
Cdd:cd03265 99 RLYGVPGAERRERIDELLDFVGLLEAAD-----RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
170 180
....*....|....*....|
gi 9955970 793 VigpEGVLA--GKTRVLVTH 810
Cdd:cd03265 174 I---EKLKEefGMTILLTTH 190
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
644-791 |
4.76e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVH--------------MKGSVAYVPQQAWI-QNCTLQEN 708
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfdgkditdwqtakiMREAVAIVPEGRRVfSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGKAL-NPKRYQQTLEACalladLEMLPGGDQTEIGEKGiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAK 787
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWV-----YELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
....
gi 9955970 788 HIFD 791
Cdd:PRK11614 175 QIFD 178
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
646-780 |
5.14e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 646 SLDI---QVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQ----------QAWIQNCTlqenvlfg 712
Cdd:PRK13409 354 SLEVeggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyikpdydgtvEDLLRSIT-------- 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 713 KALNPKRYQQtleacalladlEMLPGGDQTEIGEKGIN-LSGGQRQRVSLARAVYSDADIFLLDDPlSA 780
Cdd:PRK13409 426 DDLGSSYYKS-----------EIIKPLQLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
644-829 |
5.84e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.42 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--------------VAYVPQQ-AWIQNCTLQEN 708
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQElNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFGK------ALNPKR-YQQTLEACALLaDLEMLPggdQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAV 781
Cdd:COG1129 100 IFLGReprrggLIDWRAmRRRARELLARL-GLDIDP---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9955970 782 DSHVAKHIFDHVigpeGVLA--GKTRVLVTHgisFLPQ----TDFIIVLADGQV 829
Cdd:COG1129 172 TEREVERLFRII----RRLKaqGVAIIYISH---RLDEvfeiADRVTVLRDGRL 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1305-1509 |
6.31e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGL------NVADIGLHDLRSQLTIIPQDPILFS- 1377
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1378 ----GTLRMNLDPFGSYSEEDIWWALELS--------HLHTFVSSqPAgldfqcseggENLSVGQRQLVCLARALLRKSR 1445
Cdd:PRK14246 105 lsiyDNIAYPLKSHGIKEKREIKKIVEEClrkvglwkEVYDRLNS-PA----------SQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1446 ILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAH---RLNTIMDYtrVLVLDKGVVAE-------FDSPAN 1509
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEwgssneiFTSPKN 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
644-841 |
6.34e-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: 60.47 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGeMEKLEGKVHMKG-SVAYVPQQAW------IQnctlqenVLF----G 712
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQ-------VVFqdpfG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 713 kALNP-------------------KRYQQTLEACALLADLEMLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFL 773
Cdd:COG4172 374 -SLSPrmtvgqiiaeglrvhgpglSAAERRARVAEALEEVGLDPAARHRYPHE----FSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 774 LDDPLSAVDSHVAKHIFDhvigpegVLAGKTRvlvTHGISFLpqtdFI--------------IVLADGQVSEMGPYPALL 839
Cdd:COG4172 449 LDEPTSALDVSVQAQILD-------LLRDLQR---EHGLAYL----FIshdlavvralahrvMVMKDGKVVEQGPTEQVF 514
|
..
gi 9955970 840 QR 841
Cdd:COG4172 515 DA 516
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1277-1454 |
7.42e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1277 SRPPEGWPprgEVEFRNYSVRYrPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAD 1356
Cdd:PRK10522 314 PQAFPDWQ---TLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1357 IGLHDLRSQLTIIPQDPILFSGTlrmnLDPFGSYSEE---DIWWA-LELSHLHTFVSSQPAGLdfqcseggeNLSVGQRQ 1432
Cdd:PRK10522 390 EQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPalvEKWLErLKMAHKLELEDGRISNL---------KLSKGQKK 456
|
170 180
....*....|....*....|..
gi 9955970 1433 LVCLARALLRKSRILVLDEATA 1454
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAA 478
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
647-810 |
8.19e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.05 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV------------HMKGSVAYVPQQAWIQ-NCTLQENVL-FG 712
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepvpsrarHARQRVGVVPQFDNLDpDFTVRENLLvFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 713 kalnpkRY-----QQTLEACALLADLEMLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHvAK 787
Cdd:PRK13537 106 ------RYfglsaAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-AR 174
|
170 180
....*....|....*....|....*
gi 9955970 788 H-IFDHVigpEGVLA-GKTRVLVTH 810
Cdd:PRK13537 175 HlMWERL---RSLLArGKTILLTTH 196
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1289-1512 |
8.96e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.64 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDL---VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVA----DIGLHD 1361
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 LRSQLTIIPQDP------------ILFS-GTLRMNLDPFGSYSEEDIwwaLELSHLHTFVSSQPagldFQcseggenLSV 1428
Cdd:PRK13646 83 VRKRIGMVFQFPesqlfedtvereIIFGpKNFKMNLDEVKNYAHRLL---MDLGFSRDVMSQSP----FQ-------MSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1429 GQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRT-QFD-TCTVLTIAHRLNTIMDYT-RVLVLDKGVVAEFD 1505
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDeNKTIILVSHDMNEVARYAdEVIVMKEGSIVSQT 228
|
....*..
gi 9955970 1506 SPANLIA 1512
Cdd:PRK13646 229 SPKELFK 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1287-1499 |
9.00e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1287 GEV--EFRNYSV-----RYRPGLDlvlrDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAK-GEIRIDGLNVaDIG 1358
Cdd:PRK13549 256 GEVilEVRNLTAwdpvnPHIKRVD----DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPV-KIR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1359 --LHDLRSQLTIIPQD-------PILFSG---TLrMNLDPFGSYSEEDIwwALELSHLHTFV-------SS--QPAGldf 1417
Cdd:PRK13549 331 npQQAIAQGIAMVPEDrkrdgivPVMGVGkniTL-AALDRFTGGSRIDD--AAELKTILESIqrlkvktASpeLAIA--- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1418 qcseggeNLSVGQRQLVCLARALLRKSRILVLDEATAAIDL----ETDNLIQATIRTQFdtcTVLTIAHRLNTIMDYT-R 1492
Cdd:PRK13549 405 -------RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQLVQQGV---AIIVISSELPEVLGLSdR 474
|
....*..
gi 9955970 1493 VLVLDKG 1499
Cdd:PRK13549 475 VLVMHEG 481
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
648-782 |
9.78e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 57.73 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 648 DIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--------------VAYVPQQAWI-QNCTLQEN---V 709
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIfRKLTVEDNilaV 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 710 LFGKALNPKRYQQTLEAcaLLADLEMLPGGDQteigeKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:COG1137 103 LELRKLSKKEREERLEE--LLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
644-829 |
1.14e-08 |
|
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: 57.74 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAwI---------QN------CTLQE 707
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrDITGLPPHR-IarlgiartfQNprlfpeLTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 NVL-----------FGKALNPKRYQQTLEACALLADlEMLpggDQTEIGEK-----GiNLSGGQRQRVSLARAVYSDADI 771
Cdd:COG0411 99 NVLvaaharlgrglLAALLRLPRARREEREARERAE-ELL---ERVGLADRadepaG-NLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 772 FLLDDPLSAVDSHVAKHIFDHVIGpegvLA---GKTRVLVTH------GISflpqtDFIIVLADGQV 829
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRR----LRderGITILLIEHdmdlvmGLA-----DRIVVLDFGRV 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1296-1512 |
1.29e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.67 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1296 VRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDG------------LNVADIG-LHDL 1362
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqLKVADKNqLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1363 RSQLTIIPQdpilfsgtlRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPA-------GLDfQCSEGG--ENLSVGQRQL 1433
Cdd:PRK10619 91 RTRLTMVFQ---------HFNLWSHMTVLENVMEAPIQVLGLSKQEARERAvkylakvGID-ERAQGKypVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1434 VCLARALLRKSRILVLDEATAAIDLEtdnLIQATIRTQFDTC----TVLTIAHRlntiMDYTR-----VLVLDKGVVAEF 1504
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQLAeegkTMVVVTHE----MGFARhvsshVIFLHQGKIEEE 233
|
....*...
gi 9955970 1505 DSPANLIA 1512
Cdd:PRK10619 234 GAPEQLFG 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1308-1523 |
1.62e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1308 DLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHdlRSQLTIIPQDPILFSG-TLRMNLdP 1386
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQNI-A 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1387 FG------------SYSEEdiwwALELSHLHTFVSSQPagldfqcseggENLSVGQRQLVCLARALLRKSRILVLDEATA 1454
Cdd:PRK11607 114 FGlkqdklpkaeiaSRVNE----MLGLVHMQEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1455 AIDLETDNLIQATIRTQFD----TCTVLTiaHRLNTIMDYT-RVLVLDKGVVAEFDSP------------ANLIAARGIF 1517
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILErvgvTCVMVT--HDQEEAMTMAgRIAIMNRGKFVQIGEPeeiyehpttrysAEFIGSVNVF 256
|
....*.
gi 9955970 1518 YGMARD 1523
Cdd:PRK11607 257 EGVLKE 262
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1306-1513 |
1.72e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.10 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGL-------NVADIG------LHDLR-SQLTIIPQ 1371
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrQVIELSeqsaaqMRHVRgADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1372 DPIlfsgtlrMNLDPFGSYSEEdiwwALELSHLHTFVSSQPAGLDFQ--------------CSEGGENLSVGQRQLVCLA 1437
Cdd:PRK10261 112 EPM-------TSLNPVFTVGEQ----IAESIRLHQGASREEAMVEAKrmldqvripeaqtiLSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 1438 RALLRKSRILVLDEATAAIDLETDNLIQATIRT--QFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVAEFDSPANLIAA 1513
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVlqKEMSMGVIFITHDMGVVAEIAdRVLVMYQGEAVETGSVEQIFHA 259
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1305-1512 |
1.97e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.83 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHD-LRSQLTIIPQDPILFS------ 1377
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1378 ---GTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQpagldfqcsegGENLSVGQRQLVCLARALLRKSRILVLDEATA 1454
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1455 AIDLETDNLIQATIRTQFDT-CTVLTIAHRLNTIMDY-TRVLVLDKGVVAEFDSPANLIA 1512
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1299-1525 |
2.10e-08 |
|
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: 58.19 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1299 RPGLDLvlrDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRI---LE-AAKGEIRIDG---------LNVAdigLHdlRSQ 1365
Cdd:COG4148 11 RGGFTL---DVDFTLPGRGVTALFGPSGSGKTT----LLRAiagLErPDSGRIRLGGevlqdsargIFLP---PH--RRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQDPILFSG-TLRMNLDpFG---------SYSEEDIWWALELSHLhtfVSSQPAgldfqcseggeNLSVGQRQLVC 1435
Cdd:COG4148 79 IGYVFQEARLFPHlSVRGNLL-YGrkrapraerRISFDEVVELLGIGHL---LDRRPA-----------TLSGGERQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1436 LARALLRKSRILVLDEATAAIDLETDNLIQ---ATIRTQFDTcTVLTIAHRLNTIM---DytRVLVLDKGVVAEFDSPAN 1509
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDELDI-PILYVSHSLDEVArlaD--HVVLLEQGRVVASGPLAE 220
|
250
....*....|....*..
gi 9955970 1510 LIAARGIF-YGMARDAG 1525
Cdd:COG4148 221 VLSRPDLLpLAGGEEAG 237
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
998-1183 |
2.16e-08 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 57.42 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 998 DAMADsrQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLhQALLHNKI-----RSPQSFFDTTPSGRILNCF 1072
Cdd:cd18541 27 DALTA--GTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRI-EYDLRNDLfahllTLSPSFYQKNRTGDLMARA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1073 SKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFT-VVILPLAVLYTLVQRFyaatSRQL-KRLESVSRSpiYSH 1150
Cdd:cd18541 104 TNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTlIALLPLPLLALLVYRL----GKKIhKRFRKVQEA--FSD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9955970 1151 FS----ETVTGASVIRAYNR----SRDFEIISDTKVDANQR 1183
Cdd:cd18541 178 LSdrvqESFSGIRVIKAFVQeeaeIERFDKLNEEYVEKNLR 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1289-1512 |
2.17e-08 |
|
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: 58.66 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRY---RPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEI--------------RIDG 1351
Cdd:TIGR03269 280 IKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1352 LNVAD--IGLhdLRSQLTIIPQDPILFSGTLRMNLD-PFgsyseediwwalELSHLHTFVSSQPAGLDFQCSEG-----G 1423
Cdd:TIGR03269 360 RGRAKryIGI--LHQEYDLYPHRTVLDNLTEAIGLElPD------------ELARMKAVITLKMVGFDEEKAEEildkyP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1424 ENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATI---RTQFDTcTVLTIAHRLNTIMDYT-RVLVLDKG 1499
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVCdRAALMRDG 504
|
250
....*....|...
gi 9955970 1500 VVAEFDSPANLIA 1512
Cdd:TIGR03269 505 KIVKIGDPEEIVE 517
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
644-833 |
2.60e-08 |
|
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: 56.00 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQ-QAWIQ-NCTLQENVLFG---KALNPK 718
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNpELTGRENIYLNgrlLGLSRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 719 RYQQTLEACALLADLEmlpggdqtEIGEKGI-NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSH----VAKHIFDHV 793
Cdd:cd03220 118 EIDEKIDEIIEFSELG--------DFIDLPVkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRELL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9955970 794 IGpegvlaGKTRVLVTHGISFLPQT-DFIIVLADGQVSEMG 833
Cdd:cd03220 190 KQ------GKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
640-830 |
3.00e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 640 LPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--------------VAYVP----QQAWIQ 701
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 702 NCTLQENVL------FGKA--LNPKRYQQTLEAcaLLADLEMLPGGDQTEIGekgiNLSGGQRQRVSLARAVYSDADIFL 773
Cdd:COG1129 344 DLSIRENITlasldrLSRGglLDRRRERALAEE--YIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 774 LDDPLSAVDshV-AKH-IFDHVIGpegvLA--GKTRVLVThgiSFLPQ----TDFIIVLADGQVS 830
Cdd:COG1129 418 LDEPTRGID--VgAKAeIYRLIRE----LAaeGKAVIVIS---SELPEllglSDRILVMREGRIV 473
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1305-1496 |
3.06e-08 |
|
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: 55.58 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNL 1384
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1385 DPFGSY-SEEDIWWALELSHLHTFvSSQPAGldfqcseggeNLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNL 1463
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 9955970 1464 IQATIR--TQFDTCTVLTIAHRLNTIMDYTRVLVL 1496
Cdd:cd03231 164 FAEAMAghCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1305-1511 |
3.19e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.76 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAA--------KGEIRIDGLNVADIG---LHDLRSQLTIIPQDP 1373
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1374 ILFSGTLRMNLDPF------GSYSEED---IWWALELSHLHTFVssqpaGLDFQCSEGGENLSVG-QRQLVCL--ARALL 1441
Cdd:PRK13547 96 FAFSAREIVLLGRYpharraGALTHRDgeiAWQALALAGATALV-----GRDVTTLSGGELARVQfARVLAQLwpPHDAA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1442 RKSRILVLDEATAAIDLETDNLIQATIR--TQFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVAEFDSPANLI 1511
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRrlARDWNLGVLAIVHDPNLAARHAdRIAMLADGAIVAHGAPADVL 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
647-777 |
3.32e-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: 58.02 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSV--AYVPQqawiqnctlqenvlFGKALNPKR--YQq 722
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVklAYVDQ--------------SRDALDPNKtvWE- 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 723 tleacalladlEMLPGGDQTEIGEKGIN---------------------LSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:TIGR03719 406 -----------EISGGLDIIKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1289-1512 |
3.66e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHD-LRSQLT 1367
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPILFSG-TLRMNLDPFGSYSEED-----IWWALELSHLHTFVSSQPAGldfqcseggeNLSVGQRQLVCLARALL 1441
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDqfqerIKWVYELFPRLHERRIQRAG----------TMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1442 RKSRILVLDEATAAidletdnLIQATIRTQFDTC--------TVLTIAHRLNTIMDYT-RVLVLDKGVVAEFDSPANLIA 1512
Cdd:PRK11614 154 SQPRLLLLDEPSLG-------LAPIIIQQIFDTIeqlreqgmTIFLVEQNANQALKLAdRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1301-1520 |
3.95e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.15 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1301 GLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTL 1380
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1381 RMNLDPFGSYSEEDIW--WALELSHLHTfVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDL 1458
Cdd:PRK10253 98 VQELVARGRYPHQPLFtrWRKEDEEAVT-KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 1459 ETD----NLIQATIRTQfdTCTVLTIAHRLNTIMDY-TRVLVLDKGVVAEFDSPANLIAARGI--FYGM 1520
Cdd:PRK10253 177 SHQidllELLSELNREK--GYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIVTAELIerIYGL 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
627-833 |
4.68e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLP---PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLG------------------------EME 679
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGliisetgqtivgdyaipanlkkikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 680 KLEGKVhmkGSVAYVPQQAWIQNcTLQENVLFGKALNPKRYQQTLEACALLADLEMLPggdQTEIGEKGINLSGGQRQRV 759
Cdd:PRK13645 87 RLRKEI---GLVFQFPEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP---EDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 760 SLARAVYSDADIFLLDDPLSAVDSHvAKHIFDHVIGPEGVLAGKTRVLVTHGI-SFLPQTDFIIVLADGQVSEMG 833
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIG 233
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
642-789 |
5.07e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.96 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSAL---LGEMEKLEGKVHMKG------------SVAYVPQQAW-IQNCTL 705
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaekypgEIIYVSEEDVhFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 706 QenvlfgkalnpkryqQTLEACALLADLEMLPGgdqteigekginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHV 785
Cdd:cd03233 101 R---------------ETLDFALRCKGNEFVRG------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
....
gi 9955970 786 AKHI 789
Cdd:cd03233 154 ALEI 157
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1305-1457 |
6.06e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.43 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDL----RSQLTIIPQDPILFSG-T 1379
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1380 LRMNLD-P---FGSYSEEDIWWALELSH---LHTFVSSQPAgldfqcseggeNLSVGQRQLVCLARALLRKSRILVLDEA 1452
Cdd:PRK10535 103 AAQNVEvPavyAGLERKQRLLRAQELLQrlgLEDRVEYQPS-----------QLSGGQQQRVSIARALMNGGQVILADEP 171
|
....*
gi 9955970 1453 TAAID 1457
Cdd:PRK10535 172 TGALD 176
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
649-833 |
7.30e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.58 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 649 IQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-----------------SVAYVPQQ-AWIQNCTLQENVL 710
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSfALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 FGKALN----PKRYQQTLEACALLAdLEMLPGGDQTEigekginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVA 786
Cdd:PRK10070 129 FGMELAginaEERREKALDALRQVG-LENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9955970 787 KHIFDHVIGPEGVlAGKTRVLVTHGI-SFLPQTDFIIVLADGQVSEMG 833
Cdd:PRK10070 201 TEMQDELVKLQAK-HQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVG 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
627-829 |
7.54e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.51 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLP-PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSvAYVPQQAW------ 699
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 700 ---IQN-------CTLQENVLFG---KALNPK----RYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLA 762
Cdd:PRK13650 84 gmvFQNpdnqfvgATVEDDVAFGlenKGIPHEemkeRVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 763 RAVYSDADIFLLDDPLSAVDshvakhifdhvigPEGVLA------------GKTRVLVTHGISFLPQTDFIIVLADGQV 829
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1296-1457 |
9.21e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1296 VRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPIL 1375
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1376 FSGTLRMNLD-PF---GSYSEEDIWwaleLSHLHTFvssqpaGLDFQCSEGGEN-LSVGQRQLVCLARALLRKSRILVLD 1450
Cdd:PRK10247 93 FGDTVYDNLIfPWqirNQQPDPAIF----LDDLERF------ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLD 162
|
....*..
gi 9955970 1451 EATAAID 1457
Cdd:PRK10247 163 EITSALD 169
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
642-784 |
1.03e-07 |
|
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: 54.65 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTL---QENVLF------- 711
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvfgQKTQLWwdlpvid 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 712 GKALN-------PKRYQQTLEACAlladlEMLpggDQTEIGEKGI-NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS 783
Cdd:cd03267 115 SFYLLaaiydlpPARFKKRLDELS-----ELL---DLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
.
gi 9955970 784 H 784
Cdd:cd03267 187 V 187
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
653-829 |
1.16e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.76 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 653 KGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVhmkgsvayvpqqawiqnctlqenvlfgKALNPKRYQQTLEACALlad 732
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------------IYIDGEDILEEVLDQLL--- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 733 lemlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGPEGVLA---GKTRVLVT 809
Cdd:smart00382 51 --------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLkseKNLTVILT 122
|
170 180
....*....|....*....|
gi 9955970 810 HGISFLPQTDFIIVLADGQV 829
Cdd:smart00382 123 TNDEKDLGPALLRRRFDRRI 142
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1305-1460 |
1.31e-07 |
|
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: 54.36 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRI---LEAA-KGEIRIDGLNVADI---GLHDLRSQLT-IIPQD-PIL 1375
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKST----LLGLlagLDRPtSGTVRLAGQDLFALdedARARLRARHVgFVFQSfQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1376 FSGT----------LRMNLDPFGSYSEEdiwwaLE---LSHLHTFVSSQpagldfqcseggenLSVGQRQLVCLARALLR 1442
Cdd:COG4181 103 PTLTalenvmlpleLAGRRDARARARAL-----LErvgLGHRLDHYPAQ--------------LSGGEQQRVALARAFAT 163
|
170
....*....|....*...
gi 9955970 1443 KSRILVLDEATAAIDLET 1460
Cdd:COG4181 164 EPAILFADEPTGNLDAAT 181
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1044-1260 |
1.31e-07 |
|
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: 54.87 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1044 LHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYT 1123
Cdd:cd18557 71 LRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1124 LVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRdFEIIS-DTKVDANQRSCYPYIISNRWLSIGVEFV 1202
Cdd:cd18557 151 IASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEE-KEIRRySEALDRSYRLARKKALANALFQGITSLL 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1203 GNcVVLFAALF---AVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERV 1260
Cdd:cd18557 230 IY-LSLLLVLWyggYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1316-1458 |
1.39e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1316 GEKVGIVGRTGAGKSSMTLCLFRILEAAKGEI-----RIDGLnvADIGLHDLRSQLTIIPQDPIlfsgtlrMNLDPF--- 1387
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqRIDTL--SPGKLQALRRDIQFIFQDPY-------ASLDPRqtv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1388 ---------------GSYSEEDIWWALELshlhtfVSSQPAgldfQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEA 1452
Cdd:PRK10261 421 gdsimeplrvhgllpGKAAAARVAWLLER------VGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
....*.
gi 9955970 1453 TAAIDL 1458
Cdd:PRK10261 491 VSALDV 496
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
644-829 |
1.41e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSaLLGEMEK-LEGKVHMKGS-VAYVPQQAWIQ-----------------NCT 704
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQdVATLDADALAQlrrehfgfifqryhllsHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENV-----LFGKAlnpkRYQQTLEACALLADLemlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:PRK10535 103 AAQNVevpavYAGLE----RKQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 780 AVDSHVAkhifdhvigpEGVLA--------GKTRVLVTHGISFLPQTDFIIVLADGQV 829
Cdd:PRK10535 174 ALDSHSG----------EEVMAilhqlrdrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
644-840 |
1.43e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS-------------VAYVPQQ-AWIQNCTLQENV 709
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 710 LFGK-----ALNpkRY-----QQTLEACALladlemlpggdqteIGEKGI------NLSGGQRQRVSLARAVYSDADIFL 773
Cdd:PRK10575 107 AIGRypwhgALG--RFgaadrEKVEEAISL--------------VGLKPLahrlvdSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 774 LDDPLSAVDshVAKHIfdhvigpeGVLA---------GKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGPYPALLQ 840
Cdd:PRK10575 171 LDEPTSALD--IAHQV--------DVLAlvhrlsqerGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
651-833 |
1.46e-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: 52.96 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 651 VPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQawiqnctlqenvlfgkalnpkryqqtleacal 729
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 730 ladlemlpggdqteigekgINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS----HVA---KHIFDHvigpegvlAG 802
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAAraiRRLSEE--------GK 122
|
170 180 190
....*....|....*....|....*....|.
gi 9955970 803 KTRVLVTHGISFLPQTDFIIVLADGQVSEMG 833
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFEGEPGVYG 153
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1301-1503 |
1.56e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1301 GLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMtLCLFRILEAAK-GEIRIDGL------NVADIGLHDLRSQLTIIPQD- 1372
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLEMPRsGTLNIAGNhfdfskTPSDKAIRELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1373 ---PILfsgTLRMNL--DP---FGSYSEEDIWWALELS---HLHTFVSSQPAgldfqcseggeNLSVGQRQLVCLARALL 1441
Cdd:PRK11124 92 nlwPHL---TVQQNLieAPcrvLGLSKDQALARAEKLLerlRLKPYADRFPL-----------HLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1442 RKSRILVLDEATAAIDLETDNLIQATIRTQFDT-CTVLTIAHRLNTIMDY-TRVLVLDKGVVAE 1503
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTaSRVVYMENGHIVE 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1290-1499 |
1.75e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.23 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1290 EFRNYSVRYrPGLdLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHD-------- 1361
Cdd:PRK11300 7 SVSGLMMRF-GGL-LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarmgvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 ------LRSQLTII-----PQDPILFSGTLR--MNLDPFGSYSEEDIWWA---LELSHLhTFVSSQPAGldfqcseggeN 1425
Cdd:PRK11300 85 tfqhvrLFREMTVIenllvAQHQQLKTGLFSglLKTPAFRRAESEALDRAatwLERVGL-LEHANRQAG----------N 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1426 LSVGQRQLVCLARALLRKSRILVLDEATAAID-LETDNLIQ--ATIRTQFDTcTVLTIAHRLNTIMDYT-RVLVLDKG 1499
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEHNV-TVLLIEHDMKLVMGISdRIYVVNQG 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1284-1513 |
1.80e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1284 PPRGEVEFRNYSVRYR-PGLDLvLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDL 1362
Cdd:PRK10575 5 TNHSDTTFALRNVSFRvPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1363 RSQLTIIPQD-PILFSGTLRM-----------NLDPFGSYSEEDIWWALELSHL----HTFVSSqpagldfqcseggenL 1426
Cdd:PRK10575 84 ARKVAYLPQQlPAAEGMTVRElvaigrypwhgALGRFGAADREKVEEAISLVGLkplaHRLVDS---------------L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1427 SVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIR--TQFDTCTVLTIAHRLNTIMDYTRVLVLDKG--VVA 1502
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHrlSQERGLTVIAVLHDINMAARYCDYLVALRGgeMIA 228
|
250
....*....|.
gi 9955970 1503 EfDSPANLIAA 1513
Cdd:PRK10575 229 Q-GTPAELMRG 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1305-1512 |
1.84e-07 |
|
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: 55.58 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMtLCLFRIL---EAAKGEI---------------------------------R 1348
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRIiyhvalcekcgyverpskvgepcpvcggtlepeE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1349 IDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRM------NLDPFGSYSEEDIWWALEL------SHLHTFVSsqpagld 1416
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVldnvleALEEIGYEGKEAVGRAVDLiemvqlSHRITHIA------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1417 fqcseggENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRT---QFDTCTVLTiAHRLNTIMDYT-R 1492
Cdd:TIGR03269 167 -------RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkASGISMVLT-SHWPEVIEDLSdK 238
|
250 260
....*....|....*....|
gi 9955970 1493 VLVLDKGVVAEFDSPANLIA 1512
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVA 258
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
646-782 |
1.93e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.74 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 646 SLDIqvPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG-SVAYVPQQAW------IQnctlqenVLF----GkA 714
Cdd:COG4608 38 SFDI--RRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDITGLSGRELrplrrrMQ-------MVFqdpyA-S 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 715 LNP-KRYQQTLEAcALLAdLEMLPGGDQTEIGEK-----GIN----------LSGGQRQRVSLARAVYSDADIFLLDDPL 778
Cdd:COG4608 108 LNPrMTVGDIIAE-PLRI-HGLASKAERRERVAEllelvGLRpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
....
gi 9955970 779 SAVD 782
Cdd:COG4608 186 SALD 189
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1013-1260 |
2.28e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 54.41 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1013 GVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLN 1092
Cdd:cd18540 46 LLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVW 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1093 SFFNAISTLVVIMASTP---LFTVVILP-LAVLYTLVQRFYAATSRQLKRLESVsrspIYSHFSETVTGASVIRAYNR-- 1166
Cdd:cd18540 126 GITYMIGILIVMLILNWklaLIVLAVVPvLAVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITGAKTTKTLVRee 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1167 --SRDFEIISDTKVDANQRSCypyIISNRWLSIgVEFVGNCVVLFAALFAviGRSSLNPGL-VG-LSV--SYSLQVTFAL 1240
Cdd:cd18540 202 knLREFKELTEEMRRASVRAA---RLSALFLPI-VLFLGSIATALVLWYG--GILVLAGAItIGtLVAfiSYATQFFEPI 275
|
250 260
....*....|....*....|
gi 9955970 1241 NWMIRMMSDLESNIVAVERV 1260
Cdd:cd18540 276 QQLARVLAELQSAQASAERV 295
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1308-1496 |
2.47e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.33 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1308 DLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDG---LNVADIGLHDLRSQLTIIPQDPiLFSGTLRMNL 1384
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1385 -----DPFGSY----SEEDI-----WWALELSHLHTFVSSQPagldfqcseggENLSVGQRQLVCLARALLRKSRILVLD 1450
Cdd:PRK15079 118 geiiaEPLRTYhpklSRQEVkdrvkAMMLKVGLLPNLINRYP-----------HEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1451 EATAAIDLETD----NLIQATIRTQfdTCTVLTIAHRLNT---IMDytRVLVL 1496
Cdd:PRK15079 187 EPVSALDVSIQaqvvNLLQQLQREM--GLSLIFIAHDLAVvkhISD--RVLVM 235
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
642-782 |
2.61e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS------VAYVPQQAWI-------QNCTLQEN 708
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVghrsginPYLTLREN 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 709 VLFGKALNPKRYQQTlEACAL--LADLEMLPGGdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:PRK13540 95 CLYDIHFSPGAVGIT-ELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1056-1260 |
2.85e-07 |
|
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: 53.99 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1056 PQSFFDTTPSGRILNCFSkDIYVVDEVLAPVILMLLNSFFNAISTLVVIMA-STPLFTVVILPLaVLYTLVQRFYAATSR 1134
Cdd:cd18570 89 PLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFyNWKLFLITLLII-PLYILIILLFNKPFK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1135 QLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPY---IISNRWLSIGVEFVGNCVVLFAA 1211
Cdd:cd18570 167 KKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLgklSNLQSSIKGLISLIGSLLILWIG 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9955970 1212 LFAVIgRSSLNPG-LVGLsvsYSLQVTF--ALNWMIRMMSDLESNIVAVERV 1260
Cdd:cd18570 247 SYLVI-KGQLSLGqLIAF---NALLGYFlgPIENLINLQPKIQEAKVAADRL 294
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1289-1457 |
3.57e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.18 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAKGEIRIDGLNVADIGLHD--- 1361
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAENrhv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1362 --------LRSQLTIIpqDPILFSgtLRMNLDPFgSYSEEDIWWALELSHLHTFVSSQPAgldfqcseggeNLSVGQRQL 1433
Cdd:PRK09452 89 ntvfqsyaLFPHMTVF--ENVAFG--LRMQKTPA-AEITPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQR 152
|
170 180
....*....|....*....|....
gi 9955970 1434 VCLARALLRKSRILVLDEATAAID 1457
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALD 176
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
644-834 |
3.98e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 53.93 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGemekLE----GKVHMKG----------------SVAYVPQQ-AWIQN 702
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL----LErptsGSVLVDGvdltalserelraarrKIGMIFQHfNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 703 CTLQENVLF-------GKALNPKRYQQTLEacalLADLEmlpggdqteigEKG----INLSGGQRQRVSLARAVYSDADI 771
Cdd:COG1135 97 RTVAENVALpleiagvPKAEIRKRVAELLE----LVGLS-----------DKAdaypSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 772 FLLDDPLSAVDshvakhifdhvigPE---GVLA---------GKTRVLVTHgisflpQTDFI--I-----VLADGQVSEM 832
Cdd:COG1135 162 LLCDEATSALD-------------PEttrSILDllkdinrelGLTIVLITH------EMDVVrrIcdrvaVLENGRIVEQ 222
|
..
gi 9955970 833 GP 834
Cdd:COG1135 223 GP 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1426-1524 |
4.50e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.18 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1426 LSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYT--RVLVLDKGVVAE 1503
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISdrAALFFDGRLVEE 243
|
90 100
....*....|....*....|....*....
gi 9955970 1504 ------FDSPANLIAARGI--FYGMARDA 1524
Cdd:PRK14271 244 gpteqlFSSPKHAETARYVagLSGDVKDA 272
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
654-809 |
4.95e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 654 GALVAVVGPVGCGKSSLVSALLGEMEK--LEGKVHMKGS---------VAYVPQQAWI-QNCTLQENVLFGKALN-PK-- 718
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRkptkqilkrTGFVTQDDILyPHLTVRETLVFCSLLRlPKsl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 719 -RYQQTLEACALLADLEMLPGGDqTEIGEKGIN-LSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGp 796
Cdd:PLN03211 174 tKQEKILVAESVISELGLTKCEN-TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS- 251
|
170
....*....|...
gi 9955970 797 egvLAGKTRVLVT 809
Cdd:PLN03211 252 ---LAQKGKTIVT 261
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
647-782 |
5.17e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 53.52 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLG---EMEKLEGKVHMKGS-----------------VAYVPQQAwiqnctlq 706
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQDP-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 envlfGKALNPKR--YQQTLEAcalLADLEMLPGGDQTEIGEK-----GIN------------LSGGQRQRVSLARAVYS 767
Cdd:COG0444 96 -----MTSLNPVMtvGDQIAEP---LRIHGGLSKAEARERAIEllervGLPdperrldrypheLSGGMRQRVMIARALAL 167
|
170
....*....|....*
gi 9955970 768 DADIFLLDDPLSAVD 782
Cdd:COG0444 168 EPKLLIADEPTTALD 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
627-833 |
5.20e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 53.24 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 627 ITIHSGTFTWAQDLP---PTLHSLDIQVPKGALVAVVGPVGCGKSSLV---SALL----GEMEKLEGKVHMK-------- 688
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIqniNALLkpttGTVTVDDITITHKtkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 689 -----GSVAYVPQQAWIQNcTLQENVLFGkalnPKRYQQTLE-----ACALLADLemlpGGDQTEIGEKGINLSGGQRQR 758
Cdd:PRK13646 83 vrkriGMVFQFPESQLFED-TVEREIIFG----PKNFKMNLDevknyAHRLLMDL----GFSRDVMSQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 759 VSLARAVYSDADIFLLDDPLSAVDSHvAKHIFDHVIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMG 833
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQT 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
641-782 |
6.25e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.04 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 641 PPTLHSLD---IQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLFGK---A 714
Cdd:PRK11308 25 ERLVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpygS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 715 LNP-KRYQQTLEA-----CALLAD------LEMLPG-GDQTEIGEKGINL-SGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:PRK11308 105 LNPrKKVGQILEEpllinTSLSAAerrekaLAMMAKvGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
..
gi 9955970 781 VD 782
Cdd:PRK11308 185 LD 186
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1255-1505 |
6.69e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1255 VAVERVKEYSKTE-------TEAPWVVEgsRPPegwPPRGEV--EFRNYSVRYRPGLDlVLRDLSLHVHGGEKVGIVGRT 1325
Cdd:COG3845 220 VGTVDTAETSEEElaelmvgREVLLRVE--KAP---AEPGEVvlEVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1326 GAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQ-LTIIPQDP-----ILfSGTLRMNL-------DPFGSyse 1392
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrglVP-DMSVAENLilgryrrPPFSR--- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1393 ediWWALELSHLHTFVSS-------QPAGLDFQCSeggeNLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQ 1465
Cdd:COG3845 370 ---GGFLDRKAIRAFAEElieefdvRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIH 442
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 9955970 1466 ATIRTQFDT-CTVLTIAHRLNTIMDYT-RVLVLDKG-VVAEFD 1505
Cdd:COG3845 443 QRLLELRDAgAAVLLISEDLDEILALSdRIAVMYEGrIVGEVP 485
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1306-1499 |
7.63e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLN--------VADIGLHDLRSQLTIIPQDPI--- 1374
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhklAAQLGIGIIYQELSVIDELTVlen 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1375 LFSGTL---RMNLDPFGSYSEEDIWWALELSHLhtfvssqpaGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDE 1451
Cdd:PRK09700 101 LYIGRHltkKVCGVNIIDWREMRVRAAMMLLRV---------GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9955970 1452 ATAAI-DLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDY-TRVLVLDKG 1499
Cdd:PRK09700 172 PTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
644-829 |
7.86e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.52 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLV---SALL----GEME----------------KLEGKVhmkGSVAYVPQQAWI 700
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTITiagyhitpetgnknlkKLRKKV---SLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 701 QNcTLQENVLFGkalnPKRYQQTLEACALLADLEMLPGGDQTEIGEKG-INLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:PRK13641 100 EN-TVLKDVEFG----PKNFGFSEDEAKEKALKWLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 780 AVDSHVAKHIFDhvIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQV 829
Cdd:PRK13641 175 GLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
649-782 |
9.54e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.82 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 649 IQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV------------HMKG--SVAYVPQQAWI-QNCTLQENVL--- 710
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARArrGIGYLPQEASIfRRLSVYDNLMavl 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 711 -FGKALNPKryQQTLEACALLADLEMLPGGDQTeigekGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:PRK10895 104 qIRDDLSAE--QREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
650-777 |
1.16e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 650 QVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHM--KGSVAYVPQ--QAWIQNCTLQENVLFGKalnpkryqQTLE 725
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtKLEVAYFDQhrAELDPEKTVMDNLAEGK--------QEVM 412
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 726 -------ACALLADLEMLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDP 777
Cdd:PRK11147 413 vngrprhVLGYLQDFLFHPKRAMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
644-833 |
1.24e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAW-IQNCTLQENV-LFGKALNP---- 717
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFqIDAIKLRKEVgMVFQQPNPfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 718 ----------------------KRYQQTLEACALLADLemlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLD 775
Cdd:PRK14246 106 siydniayplkshgikekreikKIVEECLRKVGLWKEV-------YDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 776 DPLSAVDSHVAKHIFDHVIGPEGVLagkTRVLVTHGisflPQ-----TDFIIVLADGQVSEMG 833
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEI---AIVIVSHN----PQqvarvADYVAFLYNGELVEWG 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1289-1510 |
1.34e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.41 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYrpGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMtLCLFRILEA-AKGEIRIDGLNVADIGLHdlRSQLT 1367
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTV-LRLVAGLEKpTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1368 IIPQDPILFSGT---------LRMnldpFGSYSEE---DIWWALELSHLhtfvssqpagldfqcsEGGEN-----LSVGQ 1430
Cdd:PRK11432 82 MVFQSYALFPHMslgenvgygLKM----LGVPKEErkqRVKEALELVDL----------------AGFEDryvdqISGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1431 RQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIR---TQFDTcTVLTIAHrlntimDYTR-------VLVLDKGV 1500
Cdd:PRK11432 142 QQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQFNI-TSLYVTH------DQSEafavsdtVIVMNKGK 214
|
250
....*....|
gi 9955970 1501 VAEFDSPANL 1510
Cdd:PRK11432 215 IMQIGSPQEL 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
644-782 |
1.34e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.27 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--VAYVPQQAWIqNCTLQENVLFGKALNPK-RY 720
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYL-DTTLPLTVNRFLRLRPGtKK 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9955970 721 QQTLEACALLADLEMLPGGDQteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:PRK09544 99 EDILPALKRVQAGHLIDAPMQ--------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1271-1502 |
1.44e-06 |
|
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: 51.12 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1271 PWVVEGSRPPEGWPPRgevefrnysvryrpgldLVLRDLSLHVHGGEKVGIVGRTGAGKSSM---TLCLFRILEAAKGEI 1347
Cdd:cd03234 5 PWWDVGLKAKNWNKYA-----------------RILNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1348 RIDGlnvADIGLHDLRSQLTIIPQDPILFSG-TLRmnldpfgsyseEDIWWALELSHLHTFVSSQPAGLDFQCSE----- 1421
Cdd:cd03234 68 LFNG---QPRKPDQFQKCVAYVRQDDILLPGlTVR-----------ETLTYTAILRLPRKSSDAIRKKRVEDVLLrdlal 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1422 ---GG---ENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIR-TQFDTCTVLTIAH--RLNTIMDYTR 1492
Cdd:cd03234 134 triGGnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSqLARRNRIVILTIHqpRSDLFRLFDR 213
|
250
....*....|
gi 9955970 1493 VLVLDKGVVA 1502
Cdd:cd03234 214 ILLLSSGEIV 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
644-833 |
1.55e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.56 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMK--------------------GSVAYVPQQAWIQNc 703
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkknkklkplrkkvGIVFQFPEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 704 TLQENVLFGkalnPKRYQQTLEACALLADlEM--LPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAV 781
Cdd:PRK13634 102 TVEKDICFG----PMNFGVSEEDAKQKAR-EMieLVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 782 DSHVAKHIFD--HVIGPEGvlaGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMG 833
Cdd:PRK13634 177 DPKGRKEMMEmfYKLHKEK---GLTTVLVTHSMEDAARyADQIVVMHKGTVFLQG 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1288-1512 |
1.80e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.56 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1288 EVEFRNYSVRYRPGL---DLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIdGLNVADIG-----L 1359
Cdd:PRK13634 2 DITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1360 HDLRSQLTIIPQDP--ILFSGTLR-------MNldpFGSYSEEDIWWALELSHLhtfvssqpAGLDFQCSEGGE-NLSVG 1429
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEkdicfgpMN---FGVSEEDAKQKAREMIEL--------VGLPEELLARSPfELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1430 QRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQ---ATIRTQFDTCTVLtIAHRLNTIMDYT-RVLVLDKGVVAEFD 1505
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHKEKGLTTVL-VTHSMEDAARYAdQIVVMHKGTVFLQG 228
|
....*..
gi 9955970 1506 SPANLIA 1512
Cdd:PRK13634 229 TPREIFA 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1306-1484 |
1.84e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAKGEIRIDGLNV----ADIglHDLRSQLTIIPQDPILF 1376
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysprTDT--VDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1377 SGT--------LRMN-------LDPF--GSYSEEDIWWALElSHLHtfvssqpagldfqcsEGGENLSVGQRQLVCLARA 1439
Cdd:PRK14239 99 PMSiyenvvygLRLKgikdkqvLDEAveKSLKGASIWDEVK-DRLH---------------DSALGLSGGQQQRVCIARV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9955970 1440 LLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRL 1484
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
645-834 |
1.93e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.80 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 645 HSLDI--QVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSV-----------------AYVPQQAWI-QNCT 704
Cdd:PRK11144 13 LCLTVnlTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLFGkaLNPKRYQQTLEACALLAD---LEMLPggdqteigekgINLSGGQRQRVSLARAVYSDADIFLLDDPLSAV 781
Cdd:PRK11144 93 VRGNLRYG--MAKSMVAQFDKIVALLGIeplLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 782 D-----------SHVAKHIfdhvigpegvlagKTRVL-VTHGI-SFLPQTDFIIVLADGQVSEMGP 834
Cdd:PRK11144 160 DlprkrellpylERLAREI-------------NIPILyVSHSLdEILRLADRVVVLEQGKVKAFGP 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1292-1489 |
2.32e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1292 RNYSVR----YRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAD---IGLHDLRS 1364
Cdd:PRK11308 13 KHYPVKrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1365 QLTIIPQDP------------ILfSGTLRMNLDPFGSYSEEDIWWALELSHL---------HTFvssqpagldfqcsegg 1423
Cdd:PRK11308 93 KIQIVFQNPygslnprkkvgqIL-EEPLLINTSLSAAERREKALAMMAKVGLrpehydrypHMF---------------- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 1424 enlSVGQRQLVCLARALLRKSRILVLDEATAAIDLEtdnlIQATIrtqfdtctvltiahrLNTIMD 1489
Cdd:PRK11308 156 ---SGGQRQRIAIARALMLDPDVVVADEPVSALDVS----VQAQV---------------LNLMMD 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
644-833 |
2.52e-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: 52.11 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLG--EMEKLEGKVHMKgsVAYVPQQAWI-------QNCTLQENVL---- 710
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYH--VALCEKCGYVerpskvgEPCPVCGGTLepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 711 --FGKALNPKRY----------QQTLeacALLAD-------LEMLPggdqtEIGEKGI---------------------- 749
Cdd:TIGR03269 94 vdFWNLSDKLRRrirkriaimlQRTF---ALYGDdtvldnvLEALE-----EIGYEGKeavgravdliemvqlshrithi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 750 --NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIgpEGVLAGKTRVLVThgiSFLPQ-----TDFII 822
Cdd:TIGR03269 166 arDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASGISMVLT---SHWPEviedlSDKAI 240
|
250
....*....|.
gi 9955970 823 VLADGQVSEMG 833
Cdd:TIGR03269 241 WLENGEIKEEG 251
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1289-1510 |
2.72e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.96 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTI 1368
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1369 IPQDP--ILFSGTLRMNLdPFG----SYSEEDIWWALElSHLHTFvssqpaGLDFQCSEGGENLSVGQRQLVCLARALLR 1442
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDI-AFGpinlGLDEETVAHRVS-SALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1443 KSRILVLDEATAAIDLETDNLIQATIRTQFDT--CTVLTIAHRLNTI---MDYtrVLVLDKGVVAEFDSPANL 1510
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpemADY--IYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
644-841 |
3.11e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.57 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS-------------VAYVPQQA--WIQNCTLQEN 708
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 709 VLFG-------KALNPKRYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAV 781
Cdd:PRK13652 100 IAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 782 DSHVAKHIFDhVIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVL------ADGQVSEMGPYPALLQR 841
Cdd:PRK13652 169 DPQGVKELID-FLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMdkgrivAYGTVEEIFLQPDLLAR 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
574-832 |
3.94e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 574 LFniLRLPL----NMLPQLISnltqASVSLKRIQQFlsqeELDPQSVERKTISPG---YAITIHSGTFTWaQDLPPTLHS 646
Cdd:PRK10522 273 LF--LRTPLlsavGALPTLLS----AQVAFNKLNKL----ALAPYKAEFPRPQAFpdwQTLELRNVTFAY-QDNGFSVGP 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 647 LDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS-VAYVPQQAWIQnctLQENV-----LFGKALNPKRY 720
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYRK---LFSAVftdfhLFDQLLGPEGK 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 721 QQTLEACAL-LADLEMlpgGDQTEIGE---KGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKhIFDHVIGP 796
Cdd:PRK10522 419 PANPALVEKwLERLKM---AHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR-EFYQVLLP 494
|
250 260 270
....*....|....*....|....*....|....*.
gi 9955970 797 EGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEM 832
Cdd:PRK10522 495 LLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSEL 530
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1013-1217 |
5.36e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 50.18 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1013 GVYAALGILQGFLVmlaamamAAGGIQAARVLHQALLHNKIRS-------PQSFFDTTPSGRILNCFSKDIYVVDEVLAP 1085
Cdd:cd18546 43 AAYLAVVLAGWVAQ-------RAQTRLTGRTGERLLYDLRLRVfahlqrlSLDFHERETSGRIMTRMTSDIDALSELLQT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1086 VILMLLNSFFNAISTLVVIMASTP---LFTVVILPLAVLYTLVQRFYAATSRQLKRlESVSRspIYSHFSETVTGASVIR 1162
Cdd:cd18546 116 GLVQLVVSLLTLVGIAVVLLVLDPrlaLVALAALPPLALATRWFRRRSSRAYRRAR-ERIAA--VNADLQETLAGIRVVQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1163 AYNRSRD----FEIISDTKVDANQRscypyiiSNRWLSI---GVEFVGNC---VVLFAALFAVIG 1217
Cdd:cd18546 193 AFRRERRnaerFAELSDDYRDARLR-------AQRLVAIyfpGVELLGNLataAVLLVGAWRVAA 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1284-1497 |
5.65e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1284 PPRGEVEFRNYsVRYrPGLDLVLRDLSLHVHGG-----EKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDglnvadig 1358
Cdd:PRK13409 330 PPRDESERETL-VEY-PDLTKKLGDFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1359 lhdlrsqLTII--PQ----DpilFSGT----LRMNLDPFG-SYSEEDIWWALELSHLhtfvssqpagLDFQCSEggenLS 1427
Cdd:PRK13409 400 -------LKISykPQyikpD---YDGTvedlLRSITDDLGsSYYKSEIIKPLQLERL----------LDKNVKD----LS 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9955970 1428 VGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDT--CTVLTIAHRLnTIMDY--TRVLVLD 1497
Cdd:PRK13409 456 GGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEreATALVVDHDI-YMIDYisDRLMVFE 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
644-829 |
5.66e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHM-KG-SVAYVPQQAwIQNCTLQENVLFGKA-LNPKRY 720
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGiKLGYFAQHQ-LEFLRADESPLQHLArLAPQEL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 721 QQTLEacalladlEMLPG----GDQ-TEIGEKginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIG 795
Cdd:PRK10636 407 EQKLR--------DYLGGfgfqGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID 475
|
170 180 190
....*....|....*....|....*....|....*
gi 9955970 796 PEGVLagktrVLVTHGISFL-PQTDFIIVLADGQV 829
Cdd:PRK10636 476 FEGAL-----VVVSHDRHLLrSTTDDLYLVHDGKV 505
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
750-834 |
6.20e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 50.18 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 750 NLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDhvigpegVLA------GKTRVLVTHGISFLPQT-DFII 822
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdinrelGLTIVLITHEMDVVKRIcDRVA 212
|
90
....*....|..
gi 9955970 823 VLADGQVSEMGP 834
Cdd:PRK11153 213 VIDAGRLVEQGT 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1304-1457 |
7.57e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1304 LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVaDIGLHDLRSQLTIIPQ----DPILfsgT 1379
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHrsgiNPYL---T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1380 LRMN--LDPFGSYSeediwwALELSHLHTFVSSQPAgLDFQCSEggenLSVGQRQLVCLARALLRKSRILVLDEATAAID 1457
Cdd:PRK13540 91 LRENclYDIHFSPG------AVGITELCRLFSLEHL-IDYPCGL----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1291-1519 |
8.47e-06 |
|
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: 48.41 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1291 FRNYSVRYRPGLD--LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILE---AAKGEIRIDGLNVADIGLHdlrsq 1365
Cdd:cd03233 6 WRNISFTTGKGRSkiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEK----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 ltiiPQDPILFSgtlrmnldpfgsySEEDIwwalelsHLHTFVSSQPagLDFQCS-EGGENL---SVGQRQLVCLARALL 1441
Cdd:cd03233 81 ----YPGEIIYV-------------SEEDV-------HFPTLTVRET--LDFALRcKGNEFVrgiSGGERKRVSIAEALV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1442 RKSRILVLDEATaaidletdnliqatirTQFDTCTVLTIAHRLNTIMDYTRVLVL------DKGVVAEFDSPANLIAARG 1515
Cdd:cd03233 135 SRASVLCWDNST----------------RGLDSSTALEILKCIRTMADVLKTTTFvslyqaSDEIYDLFDKVLVLYEGRQ 198
|
....
gi 9955970 1516 IFYG 1519
Cdd:cd03233 199 IYYG 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1306-1487 |
8.75e-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: 50.21 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1306 LRDLSLHVHGGEKVGIVGRTGAGKSSmtlcLFRILEAA------KGEIRIDGLNVADIGLHD--------LRSQLTIIPQ 1371
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKST----LMKILSGVyphgtwDGEIYWSGSPLKASNIRDteragiviIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1372 DPIL---FSG---TL---RMNlDPFGSYSEEDIWWALELSHLHTfvsSQPAGldfqcseggeNLSVGQRQLVCLARALLR 1442
Cdd:TIGR02633 93 LSVAeniFLGneiTLpggRMA-YNAMYLRAKNLLRELQLDADNV---TRPVG----------DYGGGQQQLVEIAKALNK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9955970 1443 KSRILVLDEATAAI-DLETDNLIQATIRTQFDTCTVLTIAHRLNTI 1487
Cdd:TIGR02633 159 QARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEV 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
642-834 |
8.85e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.05 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--------------VAYVPQQAWI-QNCTLQ 706
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFG---KALNPKRYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDS 783
Cdd:PRK15439 105 ENILFGlpkRQASMQKMKQLLAALGCQLDLDSSAG-----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 784 HVAKHIFDHVigpegvlagktRVLVT--HGISF----LPQ----TDFIIVLADGQVSEMGP 834
Cdd:PRK15439 174 AETERLFSRI-----------RELLAqgVGIVFishkLPEirqlADRISVMRDGTIALSGK 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
654-815 |
9.31e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 654 GALVAVVGPVGCGKSSLVSALLGEMEKLEGKVH-MKG-SVAYVPQQAWI-QNCTLQENVLFG-----KALnpKRY----- 720
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpQPGiKVGYLPQEPQLdPTKTVRENVEEGvaeikDAL--DRFneisa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 721 -------------------QQTLEACA---LLADLEM------LPGGDQteigeKGINLSGGQRQRVSLARAVYSDADIF 772
Cdd:TIGR03719 109 kyaepdadfdklaaeqaelQEIIDAADawdLDSQLEIamdalrCPPWDA-----DVTKLSGGERRRVALCRLLLSKPDML 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9955970 773 LLDDPLSAVDSHVAKHIFDHVIGPEGvlagkTRVLVTHGISFL 815
Cdd:TIGR03719 184 LLDEPTNHLDAESVAWLERHLQEYPG-----TVVAVTHDRYFL 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1308-1522 |
1.09e-05 |
|
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: 48.56 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1308 DLSLHVHGG-----EKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVAdiglhdLRSQlTIIPQDPILFSGTLRM 1382
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------YKPQ-YIKADYEGTVRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1383 NLDPFG--SYSEEDIWWALELSHLhtfvssqpagLDFQCSEggenLSVGQRQLVCLARALLRKSRILVLDEATAAIDLET 1460
Cdd:cd03237 85 ITKDFYthPYFKTEIAKPLQIEQI----------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 1461 DNLIQATIRTQFDTC--TVLTIAHrlNTIM-DYT--RVLVLD--KGVVAEFDSPANLIAargifyGMAR 1522
Cdd:cd03237 151 RLMASKVIRRFAENNekTAFVVEH--DIIMiDYLadRLIVFEgePSVNGVANPPQSLRS------GMNR 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1282-1502 |
1.16e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1282 GWPPR--GEVEFRNYSVRyRPGLDlvlRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNV----- 1354
Cdd:PRK11288 247 GYRPRplGEVRLRLDGLK-GPGLR---EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsp 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1355 -----ADIGL--HDlRSQLTIIP----QDPILFSGtlRMNLDPFGSYSEEDiwWALELSHLH-------TFVSSQPAGld 1416
Cdd:PRK11288 323 rdairAGIMLcpED-RKAEGIIPvhsvADNINISA--RRHHLRAGCLINNR--WEAENADRFirslnikTPSREQLIM-- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1417 fqcseggeNLSVGQRQLVCLARALLRKSRILVLDEATAAIDL----ETDNLIQATIRtqfDTCTVLTIAHRLNTIMDYT- 1491
Cdd:PRK11288 396 --------NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgakhEIYNVIYELAA---QGVAVLFVSSDLPEVLGVAd 464
|
250
....*....|.
gi 9955970 1492 RVLVLDKGVVA 1502
Cdd:PRK11288 465 RIVVMREGRIA 475
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
626-841 |
1.24e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.97 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 626 AITIHSGTFTWAQDLP---PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKV----------------- 685
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstsknkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 686 HMKGSVAYVPQQAWIQncTLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKG-INLSGGQRQRVSLARA 764
Cdd:PRK13649 82 QIRKKVGLVFQFPESQ--LFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNpFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 765 VYSDADIFLLDDPLSAVDSHVAKHIFDhvIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQVSEMGPYPALLQR 841
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1049-1184 |
1.54e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 48.62 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1049 LHNKI-RSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTP---LFTVVILPLAVLYTL 1124
Cdd:cd18545 79 LFSHLqKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVrlaLVTLAVLPLLVLVVF 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1125 V-QRFyaatSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNR----SRDFEIISDTKVDANQRS 1184
Cdd:cd18545 159 LlRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFARedenEEIFDELNRENRKANMRA 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
644-834 |
1.56e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.55 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSvAYVPQQAW---------IQN-------CTLQE 707
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrkigmvFQNpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 NVLFG-------KALNPKRYQQTLEACALLADLEMLPGgdqteigekgiNLSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:PRK13642 102 DVAFGmenqgipREEMIKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9955970 781 VDSHVAKHIFD--HVIGPEGVLagkTRVLVTHGISFLPQTDFIIVLADGQ-VSEMGP 834
Cdd:PRK13642 171 LDPTGRQEIMRviHEIKEKYQL---TVLSITHDLDEAASSDRILVMKAGEiIKEAAP 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1284-1459 |
1.92e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.40 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1284 PPRGEVEFRNYsVRYrPGLDLVLRDLSLHVHGG-----EKVGIVGRTGAGKSSMTlclfRILeaaKGEIRIDGLNVadig 1358
Cdd:COG1245 331 APRREKEEETL-VEY-PDLTKSYGGFSLEVEGGeiregEVLGIVGPNGIGKTTFA----KIL---AGVLKPDEGEV---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1359 lhdlRSQLTI------IPQDpilFSGTLRMNL-----DPFG-SYSEEDIWWALELSHLhtfvssqpagLDFQCSEggenL 1426
Cdd:COG1245 398 ----DEDLKIsykpqyISPD---YDGTVEEFLrsantDDFGsSYYKTEIIKPLGLEKL----------LDKNVKD----L 456
|
170 180 190
....*....|....*....|....*....|...
gi 9955970 1427 SVGQRQLVCLARALLRKSRILVLDEATAAIDLE 1459
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
642-777 |
1.95e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--------------VAYVPQ----QAWIQNC 703
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 704 TLQENVLFGKA----------LNPKRYQQtlEACALLADLEMLPGGDQTEIGekgiNLSGGQRQRVSLARAVYSDADIFL 773
Cdd:COG3845 352 SVAENLILGRYrrppfsrggfLDRKAIRA--FAEELIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLI 425
|
....
gi 9955970 774 LDDP 777
Cdd:COG3845 426 AAQP 429
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
644-839 |
2.14e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGK-------------------VHMKGSVAYVPQQAWIQNCT 704
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvllggrsifnyrdvLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 705 LQENVLFG---KALNPKRYQQTLeACALLADLEMLpGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAV 781
Cdd:PRK14271 117 IMDNVLAGvraHKLVPRKEFRGV-AQARLTEVGLW-DAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 782 DSHVAKHIFDHVIGpegvLAGK-TRVLVTHGISFLPQ-TDFIIVLADGQVSEMGPYPALL 839
Cdd:PRK14271 195 DPTTTEKIEEFIRS----LADRlTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
644-827 |
2.83e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKG----------------SVAYvPQQAWIQNCTLQE 707
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlgiGIIY-QELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 708 NVLFGKALNPK-------RYQQTLEACALLadleMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:PRK09700 100 NLYIGRHLTKKvcgvniiDWREMRVRAAMM----LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9955970 781 VDSHVAKHIFdhVIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLADG 827
Cdd:PRK09700 176 LTNKEVDYLF--LIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
644-781 |
2.88e-05 |
|
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: 48.67 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLG--EMEKLEGKVHMKGS--------------VAYVPQQ-AWIQNCTLQ 706
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 707 ENVLFGKALNPKRY-----QQTLEACALLADLEMLPGGDQTEIGEKGinlsGGQRQRVSLARAVYSDADIFLLDDPLSAV 781
Cdd:TIGR02633 97 ENIFLGNEITLPGGrmaynAMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1289-1499 |
3.54e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNYSVRYRPGLDlVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHD---LRSQ 1365
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQD-PILFSGTLRMNLD-PF--GSYSEEDIwwalelsHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALL 1441
Cdd:PRK10908 81 IGMIFQDhHLLMDRTVYDNVAiPLiiAGASGDDI-------RRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9955970 1442 RKSRILVLDEATAAIDletDNLIQATIR--TQFDT--CTVLTIAHRLNTIMDYT-RVLVLDKG 1499
Cdd:PRK10908 154 NKPAVLLADEPTGNLD---DALSEGILRlfEEFNRvgVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1277-1457 |
3.54e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1277 SRPPEGWPPRGEV--EFRNYSVrYRPgLD---LVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLF------RIleaaKG 1345
Cdd:NF040905 244 DRYPERTPKIGEVvfEVKNWTV-YHP-LHperKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygrNI----SG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1346 EIRIDG-----LNVADIGLHDL------RSQLTIIPQDPILFSGTLrMNLDPFGSYS----EEDIWWALEL-SHLHTFVS 1409
Cdd:NF040905 318 TVFKDGkevdvSTVSDAIDAGLayvtedRKGYGLNLIDDIKRNITL-ANLGKVSRRGvideNEEIKVAEEYrKKMNIKTP 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9955970 1410 S--QPAGldfqcseggeNLSVGQRQLVCLARALLRKSRILVLDEATAAID 1457
Cdd:NF040905 397 SvfQKVG----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
658-819 |
4.68e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 46.75 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 658 AVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGsvayvpqqawiqnCTLQEN----------VLF---GKALNPK-RYQQT 723
Cdd:COG4167 43 AIIGENGSGKSTLAKMLAGIIEPTSGEILING-------------HKLEYGdykyrckhirMIFqdpNTSLNPRlNIGQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 724 LEACALLA-DLE----------------MLPggDQTEIGekgIN-LSGGQRQRVSLARAVYSDADIFLLDDPLSAVD--- 782
Cdd:COG4167 110 LEEPLRLNtDLTaeereerifatlrlvgLLP--EHANFY---PHmLSSGQKQRVALARALILQPKIIIADEALAALDmsv 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 783 ----------------------SH---VAKHIFDHVI----GpEGVLAGKTRVLVTHgisflPQTD 819
Cdd:COG4167 185 rsqiinlmlelqeklgisyiyvSQhlgIVKHISDKVLvmhqG-EVVEYGKTAEVFAN-----PQHE 244
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1309-1501 |
5.74e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.46 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1309 LSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEaAKGEIRIDGLNVADIGLHDL---RSQLTiiPQDPILFSgtlrMnld 1385
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPFA----M--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1386 pfgsyseeDIWWALELshlhtfvsSQPAGLDFQCSEGGEN------------------LSVGQRQLVCLARALLR----- 1442
Cdd:PRK03695 85 --------PVFQYLTL--------HQPDKTRTEAVASALNevaealglddklgrsvnqLSGGEWQRVRLAAVVLQvwpdi 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9955970 1443 --KSRILVLDEATAAIDLETDNLIQATIRtQFdtC----TVLTIAHRLNTIMDY-TRVLVLDKGVV 1501
Cdd:PRK03695 149 npAGQLLLLDEPMNSLDVAQQAALDRLLS-EL--CqqgiAVVMSSHDLNHTLRHaDRVWLLKQGKL 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
644-834 |
5.99e-05 |
|
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: 45.60 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEM--EKLEGKVHMKGSVayvpqqawIQNCTLQENVLFGKAL---NPK 718
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGED--------ITDLPPEERARLGIFLafqYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 719 RYQQtleacalLADLEMLpggdqteigeKGIN--LSGGQRQRVSLARAVYSDADIFLLDDPLSAVD----SHVAKHIfDH 792
Cdd:cd03217 88 EIPG-------VKNADFL----------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalRLVAEVI-NK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9955970 793 VIGPegvlaGKTRVLVTH--GISFLPQTDFIIVLADGQVSEMGP 834
Cdd:cd03217 150 LREE-----GKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1425-1488 |
6.62e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 6.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 1425 NLSVGQRQLVCLARALLRKSRILVLDEATAAIDlETD-----NLIQAtIRTQFDTCTVltIAHRLNTIM 1488
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDsaallDLLLE-LKAQGITSII--ISHKLNEIR 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
642-790 |
7.12e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLD---IQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--------------VAYVPQQA-WIQNC 703
Cdd:PRK10982 9 PGVKALDnvnLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 704 TLQENVLFG----KAL---NPKRYQQTLeacALLADLEMlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDD 776
Cdd:PRK10982 89 SVMDNMWLGryptKGMfvdQDKMYRDTK---AIFDELDI-----DIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170
....*....|....
gi 9955970 777 PLSAVDSHVAKHIF 790
Cdd:PRK10982 161 PTSSLTEKEVNHLF 174
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1049-1260 |
8.91e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 46.27 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1049 LHNKI-RSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTP---LFTVVILPLAVLYTL 1124
Cdd:cd18542 78 LYDHLqRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWkltLISLAIIPFIALFSY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1125 -----VQRFYAATSRQLKRLESVsrspiyshFSETVTGASVIRAYNRsRDFEI-----ISDTKVDANQRSCYpyiISNRW 1194
Cdd:cd18542 158 vffkkVRPAFEEIREQEGELNTV--------LQENLTGVRVVKAFAR-EDYEIekfdkENEEYRDLNIKLAK---LLAKY 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1195 LSIGvEFVGNC----VVLFAALFAVIGRSSLnpG-LVGLSvSYslqvTFALNWMIRMM----SDLESNIVAVERV 1260
Cdd:cd18542 226 WPLM-DFLSGLqivlVLWVGGYLVINGEITL--GeLVAFI-SY----LWMLIWPVRQLgrliNDMSRASASAERI 292
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
653-835 |
9.09e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.38 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 653 KGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMK----------GSVAYVPQQAWIQNC------------------- 703
Cdd:PRK13631 51 KNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKIKNFkelrrrvsmvfqfpeyqlf 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 704 --TLQENVLFGK-ALNPKRYqqtlEACALLAD-LEMLpGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLS 779
Cdd:PRK13631 131 kdTIEKDIMFGPvALGVKKS----EAKKLAKFyLNKM-GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 780 AVDSHVAKHIFDHVIgpEGVLAGKTRVLVTHGI-SFLPQTDFIIVLADGQVSEMG-PY 835
Cdd:PRK13631 206 GLDPKGEHEMMQLIL--DAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGtPY 261
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
644-780 |
1.28e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLDIQVPKGALVAVVGPVGCGKSSLVSALLG-------------EMEKLEGKvHMKGS----VAYVPQQ-AWIQNCTL 705
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifEGEELQAS-NIRDTeragIAIIHQElALVKELSV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 706 QENVLFGKALNPKRY----QQTLEACALLADLEMlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSA 780
Cdd:PRK13549 100 LENIFLGNEITPGGImdydAMYLRAQKLLAQLKL-----DINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1321-1507 |
1.54e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.61 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1321 IVGRTGAGKSSMTLCLFRILEAAKGEIRI-DGLNVADIGLHD---------------LRSQLTIIPQDP--ILFSGTLrm 1382
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVgDIYIGDKKNNHElitnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTI-- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1383 nldpfgsysEEDIWWALELSHLHTFVSSQPA-------GLDFQCSEGGE-NLSVGQRQLVCLARALLRKSRILVLDEATA 1454
Cdd:PRK13631 135 ---------EKDIMFGPVALGVKKSEAKKLAkfylnkmGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1455 AIDLETDN-LIQATIRTQFDTCTVLTIAHRLNTIMDYT-RVLVLDKGVVAEFDSP 1507
Cdd:PRK13631 206 GLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILKTGTP 260
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
642-837 |
1.74e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 642 PTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--VAYVPQQ------AWI------------- 700
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQDglangiVYIsedrkrdglvlgm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 701 ---QN---CTLQENVLFGKALNPKRYQQTLEACALLADLEMlPGGDQTeIGekgiNLSGGQRQRVSLARAVYSDADIFLL 774
Cdd:PRK10762 346 svkENmslTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKT-PSMEQA-IG----LLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 775 DDPLSAVDSHVAKHIFDHV--IGPEGVlagkTRVLVThgiSFLPQ----TDFIIVLADGQVSemGPYPA 837
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLInqFKAEGL----SIILVS---SEMPEvlgmSDRILVMHEGRIS--GEFTR 479
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
720-828 |
2.91e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 720 YQQTLEACALLADLEMLPggdqtEIGEKGIN-LSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVakhifdhVIGPEG 798
Cdd:PLN03073 318 YTAEARAASILAGLSFTP-----EMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA-------VLWLET 385
|
90 100 110
....*....|....*....|....*....|..
gi 9955970 799 VLAG--KTRVLVTHGISFLPQTDFIIVLADGQ 828
Cdd:PLN03073 386 YLLKwpKTFIVVSHAREFLNTVVTDILHLHGQ 417
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
749-829 |
3.19e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.71 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 749 INLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDhvIGPEGVLAGKTRVLVTHGISFLPQTDF-IIVLADG 827
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR--LFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDG 213
|
..
gi 9955970 828 QV 829
Cdd:PRK10908 214 HL 215
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1054-1184 |
5.06e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 44.04 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1054 RSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVIL-PLAVLYTLVQRFYAAT 1132
Cdd:cd18564 99 RLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALaVAPLLLLAARRFSRRI 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 9955970 1133 ---SRQLKRLESVsrspIYSHFSETVTGASVIRAYNR----SRDFEIISDTKVDANQRS 1184
Cdd:cd18564 179 keaSREQRRREGA----LASVAQESLSAIRVVQAFGReeheERRFARENRKSLRAGLRA 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
626-834 |
5.69e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 626 AITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLgEMEKLEGKVHMKGSvayvPQQAWIQNCTL 705
Cdd:PRK15134 284 AFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQ----PLHNLNRRQLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 706 ----QENVLF---GKALNPKRYQQTLEACALLADLEMLPGGDQTE-----IGEKGIN----------LSGGQRQRVSLAR 763
Cdd:PRK15134 359 pvrhRIQVVFqdpNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQqviavMEEVGLDpetrhrypaeFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 764 AVYSDADIFLLDDPLSAVDSHVAKHIfdhvigpegvLAGKTRVLVTHGISFLpqtdFI--------------IVLADGQV 829
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQI----------LALLKSLQQKHQLAYL----FIshdlhvvralchqvIVLRQGEV 504
|
....*
gi 9955970 830 SEMGP 834
Cdd:PRK15134 505 VEQGD 509
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
651-830 |
6.49e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 651 VPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGS--------------VAYVP----QQAWIQNCTLQENV--- 709
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsprdairagIMLCPedrkAEGIIPVHSVADNInis 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 710 ------LFGKALNPKRYQQTleACALLADLEM-LPGGDQteigeKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVD 782
Cdd:PRK11288 356 arrhhlRAGCLINNRWEAEN--ADRFIRSLNIkTPSREQ-----LIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 783 shV-AKHIFDHVIGPegvLA--GKTRVLVThgiSFLPQ----TDFIIVLADGQVS 830
Cdd:PRK11288 429 --VgAKHEIYNVIYE---LAaqGVAVLFVS---SDLPEvlgvADRIVVMREGRIA 475
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1316-1489 |
7.28e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1316 GEKVGIVGRTGAGKSSMTLCLFRILEAA-KGEIRIDGlnvaDIGLHDLRSQLTIIPQDpilfsgtlrmnldpfgsyseed 1394
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDG----EDILEEVLDQLLLIIVG---------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1395 iwwalelshlhtfvssqpagldfqcsEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDT 1474
Cdd:smart00382 56 --------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
170 180
....*....|....*....|..
gi 9955970 1475 -------CTVLTIAHRLNTIMD 1489
Cdd:smart00382 110 llkseknLTVILTTNDEKDLGP 131
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
311-602 |
7.61e-04 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 43.17 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 311 FLISACFKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIY 390
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 391 RKALVITNSVKRASTVGEIVNLMS--VDAQRFMdLAPFLNLLWSAPLQIILAIYF-LWQNLGPSVLAgVAFMVLLIPLNG 467
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATndLNAVRMA-LGPGILYLVDALFLGVLVLVMmFTISPKLTLIA-LLPLPLLALLVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 468 AVAVKM-RAFQVKQMKLKDsriklMS----EILNGIKVLKLYAWEPS----FLKQVEGIRQGELQLLRTAAYLHTTTTFT 538
Cdd:cd18541 159 RLGKKIhKRFRKVQEAFSD-----LSdrvqESFSGIRVIKAFVQEEAeierFDKLNEEYVEKNLRLARVDALFFPLIGLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 539 wmcsPFLVTLITLWV---YVYVDPNNVLDaekaFVS-VSLFNILRLPLNMLPQLISNLTQASVSLKRI 602
Cdd:cd18541 234 ----IGLSFLIVLWYggrLVIRGTITLGD----LVAfNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1054-1217 |
1.40e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 42.47 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1054 RSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTP---LFTVVILPLAVLYTLV--QRF 1128
Cdd:cd18550 84 RMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWrlaLLSLVLLPLFVLPTRRvgRRR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1129 YAATSRQLKRLESVSrspiySHFSET--VTGASVIRAYNRSRD----FEIISDTKVDANQRScypyIISNRWLSIGVEFV 1202
Cdd:cd18550 164 RKLTREQQEKLAELN-----SIMQETlsVSGALLVKLFGREDDeaarFARRSRELRDLGVRQ----ALAGRWFFAALGLF 234
|
170
....*....|....*...
gi 9955970 1203 GNC---VVLFAALFAVIG 1217
Cdd:cd18550 235 TAIgpaLVYWVGGLLVIG 252
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
614-777 |
1.95e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 614 QSVERKTISPGYaitihsgtftwaqDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHM--KGSV 691
Cdd:PRK15064 318 NALEVENLTKGF-------------DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWseNANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 692 AYVPQ---QAWIQNCTLQEnvLFGKALNPKRYQQTLEacALLAdlEMLPGGDqtEIGEKGINLSGGQRQRVSLARAVYSD 768
Cdd:PRK15064 385 GYYAQdhaYDFENDLTLFD--WMSQWRQEGDDEQAVR--GTLG--RLLFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
....*....
gi 9955970 769 ADIFLLDDP 777
Cdd:PRK15064 457 PNVLVMDEP 465
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1292-1362 |
2.10e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.84 E-value: 2.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9955970 1292 RNYSVRYRPGLDLvlRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGlnvADIGLHDL 1362
Cdd:PRK11701 10 RGLTKLYGPRKGC--RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM---RDGQLRDL 75
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1015-1165 |
2.40e-03 |
|
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: 41.69 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1015 YAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSF 1094
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9955970 1095 FNAISTLVVIMASTPLFTVVILPLAVLYTLVqrfYAATSRQLKRLESVSRSpIY----SHFSETVTGASVIRAYN 1165
Cdd:cd18577 133 STFIAGFIIAFIYSWKLTLVLLATLPLIAIV---GGIMGKLLSKYTKKEQE-AYakagSIAEEALSSIRTVKAFG 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1288-1499 |
2.69e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.61 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1288 EVEFRNYSVRYRPGLDL---VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEI--------------RID 1350
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1351 GLNVADI----------GLHDLRSQLTIIPQ--DPILFSGTLRMNLdPFGSYS-----EEDIWWALELSHLhtfvssqpA 1413
Cdd:PRK13651 82 KVLEKLViqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDI-IFGPVSmgvskEEAKKRAAKYIEL--------V 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1414 GLDFQCSEGGE-NLSVGQRQLVCLARALLRKSRILVLDEATAAIDLE-TDNLIQATIRTQFDTCTVLTIAHRLNTIMDYT 1491
Cdd:PRK13651 153 GLDESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWT 232
|
....*....
gi 9955970 1492 -RVLVLDKG 1499
Cdd:PRK13651 233 kRTIFFKDG 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1305-1465 |
3.36e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.22 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGlhdlrSQLTIIPQDPILFsgtlrmnl 1384
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLL-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1385 dPFGSySEEDIWWALELSHLHTFVSSQPAG--LDFQCSEGGEN-----LSVGQRQLVCLARALLRKSRILVLDEATAAID 1457
Cdd:PRK11248 83 -PWRN-VQDNVAFGLQLAGVEKMQRLEIAHqmLKKVGLEGAEKryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
....*...
gi 9955970 1458 LETDNLIQ 1465
Cdd:PRK11248 161 AFTREQMQ 168
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
644-782 |
3.42e-03 |
|
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: 41.20 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 644 LHSLdiQVPK-GALVAVVGPVGCGKSSLVSALLGEMEKLEGKV-----------HMKGS---------------VAYVPQ 696
Cdd:cd03236 17 LHRL--PVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSelqnyftkllegdvkVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 697 qawiqNCTLQENVLFGKALnpkryqQTLEACALLADLEMLPggDQTEIG---EKGI-NLSGGQRQRVSLARAVYSDADIF 772
Cdd:cd03236 95 -----YVDLIPKAVKGKVG------ELLKKKDERGKLDELV--DQLELRhvlDRNIdQLSGGELQRVAIAAALARDADFY 161
|
170
....*....|
gi 9955970 773 LLDDPLSAVD 782
Cdd:cd03236 162 FFDEPSSYLD 171
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1075-1260 |
4.39e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 40.84 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1075 DIYVVDEVLAPVILMLLNSFFNAISTLVVI------MASTPLFTVVILpLAVLYTLVQRFYAATSRQLKRLESVSRSpiy 1148
Cdd:cd18548 105 DVTQVQNFVMMLLRMLVRAPIMLIGAIIMAfrinpkLALILLVAIPIL-ALVVFLIMKKAIPLFKKVQKKLDRLNRV--- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1149 shFSETVTGASVIRAYNRSrDFEIisdTKVD-ANQRSCYPYIISNRWLSI---GVEFVGN----CVVLFAALFAVIGrsS 1220
Cdd:cd18548 181 --VRENLTGIRVIRAFNRE-DYEE---ERFDkANDDLTDTSLKAGRLMALlnpLMMLIMNlaivAILWFGGHLINAG--S 252
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9955970 1221 LNPG-LVGLsVSYSLQVTFALNWMIRMMSDLESNIVAVERV 1260
Cdd:cd18548 253 LQVGdLVAF-INYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
649-677 |
4.48e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 4.48e-03
10 20 30
....*....|....*....|....*....|..
gi 9955970 649 IQVPKGaLVAVVGPVGCGKSSLVSAL---LGE 677
Cdd:TIGR02168 19 INFDKG-ITGIVGPNGCGKSNIVDAIrwvLGE 49
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
654-840 |
4.94e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.38 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 654 GALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQncTLQENVLF-----GKALNPK---------- 718
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQ--ALRRDIQFifqdpYASLDPRqtvgdsimep 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 719 -RYQQTLEACA-------LLADLEMLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIF 790
Cdd:PRK10261 428 lRVHGLLPGKAaaarvawLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9955970 791 DHVIGPEGVLaGKTRVLVTHGISFLPQTDF-IIVLADGQVSEMGPYPALLQ 840
Cdd:PRK10261 504 NLLLDLQRDF-GIAYLFISHDMAVVERISHrVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1053-1172 |
5.71e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 40.54 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1053 IRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAAT 1132
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 9955970 1133 SRQL--KRLESVSRSpiYSHFSETVTGASVIRAYNRSrDFEI 1172
Cdd:cd18576 160 IRKLskKVQDELAEA--NTIVEETLQGIRVVKAFTRE-DYEI 198
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
751-834 |
5.76e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.88 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 751 LSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGpegvLAGKTR---VLVTHGISFLPQT-DFIIVLAD 826
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLE----LQQKENmalVLITHDLALVAEAaHKIIVMYA 229
|
....*...
gi 9955970 827 GQVSEMGP 834
Cdd:PRK11022 230 GQVVETGK 237
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1289-1503 |
6.84e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.13 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1289 VEFRNysVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADI---GLHDLRSQ 1365
Cdd:PRK11831 8 VDMRG--VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1366 LTIIPQdpilfSGTLRMNLDPFgsyseEDIWWAL-ELSHL-----HTFV--SSQPAGLDFQCSEGGENLSVGQRQLVCLA 1437
Cdd:PRK11831 86 MSMLFQ-----SGALFTDMNVF-----DNVAYPLrEHTQLpapllHSTVmmKLEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9955970 1438 RALLRKSRILVLDEATAAIDLET--------DNLIQA----TIRTQFDTCTVLTIAhrlntimDYTRVlVLDKGVVAE 1503
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITmgvlvkliSELNSAlgvtCVVVSHDVPEVLSIA-------DHAYI-VADKKIVAH 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1426-1506 |
7.64e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 40.24 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9955970 1426 LSVGQRQLVCLARALLRKSRILVLDEATAAIDL----ETDNLIQaTIRTQFDTcTVLTIAHRLNTIM---DytRVLVLDK 1498
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLE-RLAREINI-PILYVSHSLDEILrlaD--RVVVLEQ 204
|
....*...
gi 9955970 1499 GVVAEFDS 1506
Cdd:PRK11144 205 GKVKAFGP 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1305-1348 |
7.85e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 7.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 9955970 1305 VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIR 1348
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| |
