|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
170-694 |
1.31e-155 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 480.43 E-value: 1.31e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 170 SEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAD 249
Cdd:COG1132 58 SALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 250 QMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFG 329
Cdd:COG1132 138 GLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 330 GEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSV--IVGALN- 406
Cdd:COG1132 218 REERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLS-GSLTVGDLVAFILYLlrLFGPLRq 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 407 LGNAspcLEAFATGRAAATSIFETIDRKPIIDCmSEDGYKLDRIKGEIEFHNVTFHYPsrPEVKILNDLNMAIKPGEMTA 486
Cdd:COG1132 297 LANV---LNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 487 LVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAA 566
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAA 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 567 KEANAYNFIMDLPQQFDTLVgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIIS 646
Cdd:COG1132 451 KAAQAHEFIEALPDGYDTVVgergvnlsggqrqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIV 530
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2462578034 647 VAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQG 694
Cdd:COG1132 531 IAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
52-1289 |
2.38e-149 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 489.54 E-value: 2.38e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 52 KEQKKISNNNN---------------DKKSRLQDEKKGDGVRVGFFQLFRFSSSTDIWLMFVGSLCAFLHGIAQPGVLLI 116
Cdd:PTZ00265 3 KDQRQKKDNNSgggnlsikdevekelNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 117 FGtmtdvfidydvelqelqipgkacvnntIVWTNSSLNQNMTNgtrcgllniesemIKFASYYAGIAVAVL--ITGYiqi 194
Cdd:PTZ00265 83 FG---------------------------VIMKNMNLGENVND-------------IIFSLVLIGIFQFILsfISSF--- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 195 CFWVIAAarQIQKMRKFYFRRIMRMEIGWFDCNSVG-ELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGW 273
Cdd:PTZ00265 120 CMDVVTT--KILKTLKLEFLKSVFYQDGQFHDNNPGsKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 274 KLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKG 353
Cdd:PTZ00265 198 RLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKAN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 354 IVMGFFTGFVWCLIFLCYALAFWYGSTLVLDE-------GEYTPGTLVQIFLSVIVGALNLGNASPCLEAFATGRAAATS 426
Cdd:PTZ00265 278 FMESLHIGMINGFILASYAFGFWYGTRIIISDlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNS 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 427 IFETIDRKPIIDcMSEDGYKLDRIKgEIEFHNVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFY 506
Cdd:PTZ00265 358 LYEIINRKPLVE-NNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 507 DPCEGMVTV-DGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYG-------------------------------- 553
Cdd:PTZ00265 436 DPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscr 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 554 -----------------------REDATMED--IVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALI 608
Cdd:PTZ00265 516 akcagdlndmsnttdsneliemrKNYQTIKDseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAII 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 609 RNPKILLLDMATSALDNESEAMVQEVLSKIQHGH---TIIsVAHRLSTVRAADTI------------------------- 660
Cdd:PTZ00265 596 RNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnriTII-IAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdn 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 661 ----------------------IGFEHGTAVERGTHEELLERK-GVYFTLVTLQS-QGNQALNEEDIKDATEDDMLARTF 716
Cdd:PTZ00265 675 kennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKvSSKKSSNNDNDKDSDMKSSAYKDS 754
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 717 SRGSYQDSLRASIRQRSKSqlsylvhepplaVVDHKSTYEEDRKDKDIPVQEEVepAPVRRILKfSAPEWPYML------ 790
Cdd:PTZ00265 755 ERGYDPDEMNGNSKHENES------------ASNKKSCKMSDENASENNAGGKL--PFLRNLFK-RKPKAPNNLrivyre 819
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 791 ---------VGSVGAAVNGTVTPLYAFLFSQILGT-FSIPDKEEQRSQINgvclLFVAMGCVSLF-TQFLQGYAFAKSGE 859
Cdd:PTZ00265 820 ifsykkdvtIIALSILVAGGLYPVFALLYAKYVSTlFDFANLEANSNKYS----LYILVIAIAMFiSETLKNYYNNVIGE 895
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 860 LLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVIL 939
Cdd:PTZ00265 896 KVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLT 975
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 940 -CFFPFLALSgATQTRmLTGFASRDKQALEMVGQI----------------TNEALSNIRTVAGIGKERRFIEALETELE 1002
Cdd:PTZ00265 976 gTYFIFMRVF-AIRAR-LTANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAID 1053
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1003 KPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISA 1082
Cdd:PTZ00265 1054 YSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSF 1133
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1083 ARFFQLLDRQPPISVYNTAGEKWDN---FQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL 1159
Cdd:PTZ00265 1134 EKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSL 1213
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1160 LERFYD------------------------------------------------------PDQGKVMIDGHDSKKVNVQF 1185
Cdd:PTZ00265 1214 LMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKD 1293
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIVSQEPVLFACSIMDNIKYGdnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIAR 1265
Cdd:PTZ00265 1294 LRNLFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIAR 1371
|
1450 1460
....*....|....*....|....
gi 2462578034 1266 AIVRDPKILLLDEATSALDTESEK 1289
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEK 1395
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
779-1095 |
2.45e-132 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 408.76 E-value: 2.45e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 779 LKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSG 858
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 859 ELLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVI 938
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 939 LCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFC 1018
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 1019 FAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPI 1095
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
773-1290 |
6.37e-131 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 414.95 E-value: 6.37e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 773 APVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPdkeEQRSQINGVCLLFVAMGCVSLFTQFLQGY 852
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG---GDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 853 AFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSW 932
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 933 KLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKA 1012
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1013 NIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQ 1092
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1093 PPISVYNTAGEKwDNFQGKIDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVM 1172
Cdd:COG1132 322 PEIPDPPGAVPL-PPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1173 IDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQ 1252
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR--PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 2462578034 1253 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
454-691 |
5.79e-128 |
|
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: 393.83 E-value: 5.79e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKI 613
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
180-691 |
2.11e-124 |
|
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: 401.90 E-value: 2.11e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQIC-FWVIA-AARQIQ-KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDdINKINDAIADQMALFIQ 256
Cdd:COG2274 200 IGLLLALLFEGLLRLLrSYLLLrLGQRIDlRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 257 RMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVE 336
Cdd:COG2274 279 DLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 337 RYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV--QIFLSVIVGAL-NLGNAspc 413
Cdd:COG2274 359 RWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVID-GQLTLGQLIafNILSGRFLAPVaQLIGL--- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 414 LEAFATGRAAATSIFETIDRKPiiDCMSEDGYK-LDRIKGEIEFHNVTFHYPSRpEVKILNDLNMAIKPGEMTALVGPSG 492
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPP--EREEGRSKLsLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 493 AGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAY 572
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLH 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 573 NFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLS 652
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
|
490 500 510
....*....|....*....|....*....|....*....
gi 2462578034 653 TVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
199-688 |
9.43e-115 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 375.98 E-value: 9.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 199 IAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLV 278
Cdd:TIGR00958 227 YTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 279 IISVSPLIGIGAATIGlsvsKFTDYELK----AYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGI 354
Cdd:TIGR00958 307 TLINLPLVFLAEKVFG----KRYQLLSEelqeAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKAL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 355 VmgfFTGFVWC------LIFLcyaLAFWYGSTLVLdEGEYTPGTLVqiflSVIVGALNLGNASPCLEAFATGR----AAA 424
Cdd:TIGR00958 383 A---YAGYLWTtsvlgmLIQV---LVLYYGGQLVL-TGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSGMmqavGAS 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 425 TSIFETIDRKPiidCMSEDG-YKLDRIKGEIEFHNVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQ 503
Cdd:TIGR00958 452 EKVFEYLDRKP---NIPLTGtLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 504 RFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFD 583
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYD 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 584 TLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEvlSKIQHGHTIISVAHRLSTVRAADTIIGF 663
Cdd:TIGR00958 609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVL 686
|
490 500
....*....|....*....|....*
gi 2462578034 664 EHGTAVERGTHEELLERKGVYFTLV 688
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
96-427 |
1.43e-111 |
|
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: 352.16 E-value: 1.43e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 96 MFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVELQELQipgkacvnntivwtnsslnqnmtngtrcgllNIESEMIKF 175
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPD-------------------------------EFLDDVNKY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 176 ASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFI 255
Cdd:cd18577 50 ALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 256 QRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREV 335
Cdd:cd18577 130 QSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 336 ERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVIVGALNLGNASPCLE 415
Cdd:cd18577 210 KRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRD-GEISPGDVLTVFFAVLIGAFSLGQIAPNLQ 288
|
330
....*....|..
gi 2462578034 416 AFATGRAAATSI 427
Cdd:cd18577 289 AFAKARAAAAKI 300
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
164-691 |
1.73e-109 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 357.09 E-value: 1.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 164 GLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIA-AARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINK 242
Cdd:TIGR02204 48 GFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWlGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 243 INDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSM 322
Cdd:TIGR02204 128 LQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 323 RTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQ-IFLSVI 401
Cdd:TIGR02204 208 RTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVI-AGKMSAGTLGQfVFYAVM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 402 VGAlNLGNASPCLEAFATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIKGEIEFHNVTFHYPSRPEVKILNDLNMAIKP 481
Cdd:TIGR02204 287 VAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 482 GEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMED 561
Cdd:TIGR02204 366 GETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 562 IVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHG 641
Cdd:TIGR02204 446 VEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKG 525
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2462578034 642 HTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:TIGR02204 526 RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
181-691 |
4.87e-103 |
|
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: 339.39 E-value: 4.87e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 181 GIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTS 260
Cdd:TIGR02203 62 GLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 261 TICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEK 340
Cdd:TIGR02203 142 VIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 341 NLVFAQRWGIRKGIVMGFFTGFVWCLIFLcyALAFWYGSTLVL-DEGEYTPGTLVQIFLSVIVGALNLGNASPCLEAFAT 419
Cdd:TIGR02203 222 VSNRNRRLAMKMTSAGSISSPITQLIASL--ALAVVLFIALFQaQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 420 GRAAATSIFETIDRKPIIDcmsEDGYKLDRIKGEIEFHNVTFHYPSRpEVKILNDLNMAIKPGEMTALVGPSGAGKSTAL 499
Cdd:TIGR02203 300 GLAAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 500 QLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGR-EDATMEDIVQAAKEANAYNFIMDL 578
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 579 PQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAAD 658
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535
|
490 500 510
....*....|....*....|....*....|...
gi 2462578034 659 TIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1112-1290 |
1.04e-99 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 317.56 E-value: 1.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1191
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVLFACSIMDNIKYGDNtkEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDP 1271
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP--DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170
....*....|....*....
gi 2462578034 1272 KILLLDEATSALDTESEKQ 1290
Cdd:cd03249 159 KILLLDEATSALDAESEKL 177
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
324-697 |
1.50e-98 |
|
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: 327.93 E-value: 1.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 324 TVAAFGGEKREVERYEKNLvfaQRW---GIRKGIVMGFFtGFVWCLIF-LCYALAFWYGSTLVLDeGEYTPGTLVQI--F 397
Cdd:COG5265 230 TVKYFGNEAREARRYDEAL---ARYeraAVKSQTSLALL-NFGQALIIaLGLTAMMLMAAQGVVA-GTMTVGDFVLVnaY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 398 LSVIVGALN-LGNAspcleaFATGRAAATSI---FETIDRKP-IIDcmSEDGYKLDRIKGEIEFHNVTFHY-PSRPevkI 471
Cdd:COG5265 305 LIQLYIPLNfLGFV------YREIRQALADMermFDLLDQPPeVAD--APDAPPLVVGGGEVRFENVSFGYdPERP---I 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIR 551
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIA 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 552 YGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMV 631
Cdd:COG5265 454 YGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVgerglklsggekqRVAIARTLLKNPPILIFDEATSALDSRTERAI 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 632 QEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQA 697
Cdd:COG5265 534 QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
454-687 |
4.56e-97 |
|
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: 310.32 E-value: 4.56e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEvKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKI 613
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTL 687
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
767-1288 |
1.79e-96 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 325.52 E-value: 1.79e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 767 QEEVEPAP-VRRILKFSAPEWPYMLVGSVG---AAVNGTVTPLY-AFLFSQILGTFSIPDkeeQRSQINGVCLLFVAmgc 841
Cdd:TIGR00958 140 QGQSETADlLFRLLGLSGRDWPWLISAFVFltlSSLGEMFIPFYtGRVIDTLGGDKGPPA---LASAIFFMCLLSIA--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 842 vSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVT 921
Cdd:TIGR00958 214 -SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 922 VAMIIAFSFSWKLSLVILCFFPFLALSG---ATQTRMLtgfASRDKQALEMVGQITNEALSNIRTVAGIGKE----RRFI 994
Cdd:TIGR00958 291 GLLGFMLWLSPRLTMVTLINLPLVFLAEkvfGKRYQLL---SEELQEAVAKANQVAEEALSGMRTVRSFAAEegeaSRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 995 EALETELEKPFKTAIQKAniyGFCFAFAQCIMFIANSASYrYGGYLI-----SNEGLhfsyvfrviSAVVLSATALGRAF 1069
Cdd:TIGR00958 368 EALEETLQLNKRKALAYA---GYLWTTSVLGMLIQVLVLY-YGGQLVltgkvSSGNL---------VSFLLYQEQLGEAV 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1070 SYT----PSYAKAKISAARFFQLLDRQPPISvyNTAGEKWDNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAF 1145
Cdd:TIGR00958 435 RVLsyvySGMMQAVGASEKVFEYLDRKPNIP--LTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVAL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1146 VGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKeiPMERVIAA 1225
Cdd:TIGR00958 513 VGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDT--PDEEIMAA 590
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 1226 AKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 1288
Cdd:TIGR00958 591 AKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
188-691 |
3.27e-94 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 315.42 E-value: 3.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 188 ITGYIQ-ICF-WViaAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIndAIADQMALF-IQRMTSTICG 264
Cdd:PRK11176 80 ITSFISsYCIsWV--SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQV--ASSSSGALItVVREGASIIG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 265 -FLLGFFRGWKLTLVIISVSPLIGIgaaTIGLsVSK-FTDYELKAYAKAGVV---ADEVISSMRTVAAFGGEKREVERYE 339
Cdd:PRK11176 156 lFIMMFYYSWQLSLILIVIAPIVSI---AIRV-VSKrFRNISKNMQNTMGQVttsAEQMLKGHKEVLIFGGQEVETKRFD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 340 KNLVFAQRWGIRKGIVMGFFTGFVWCLIFLcyALAF-WYGSTLVLDEGEYTPGTLVQIFLSVIvgAL-----NLGNASpc 413
Cdd:PRK11176 232 KVSNRMRQQGMKMVSASSISDPIIQLIASL--ALAFvLYAASFPSVMDTLTAGTITVVFSSMI--ALmrplkSLTNVN-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 414 lEAFATGRAAATSIFETIDRKPIIDcmsEDGYKLDRIKGEIEFHNVTFHYPSRpEVKILNDLNMAIKPGEMTALVGPSGA 493
Cdd:PRK11176 306 -AQFQRGMAACQTLFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGS 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 494 GKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDA-TMEDIVQAAKEANAY 572
Cdd:PRK11176 381 GKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAM 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 573 NFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLS 652
Cdd:PRK11176 461 DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS 540
|
490 500 510
....*....|....*....|....*....|....*....
gi 2462578034 653 TVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:PRK11176 541 TIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
96-427 |
8.86e-94 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 304.20 E-value: 8.86e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 96 MFVGSLCAFLHGIAQPGVLLIFGTMTDVFIdydvelqelqipgkacvnnTIVWTNSSLNQNMTNGTRCGLLNIESEMIKF 175
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFT-------------------NGGMTNITGNSSGLNSSAGPFEKLEEEMTLY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 176 ASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFI 255
Cdd:cd18558 62 AYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 256 QRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREV 335
Cdd:cd18558 142 QNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 336 ERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDEgEYTPGTLVQIFLSVIVGALNLGNASPCLE 415
Cdd:cd18558 222 TRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQ-EYSIGEVLTVFFSVLIGAFSAGQQVPSIE 300
|
330
....*....|..
gi 2462578034 416 AFATGRAAATSI 427
Cdd:cd18558 301 AFANARGAAYHI 312
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
767-1290 |
6.97e-92 |
|
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: 312.54 E-value: 6.97e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 767 QEEVEPAPVRRILKFSAPEWPYM---LVGSVGAAVNGTVTPLyaflFSQILGTFSIPDKeeQRSQINGVCLLFVAMGCVS 843
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLlqvLLASLLINLLALATPL----FTQVVIDRVLPNQ--DLSTLWVLAIGLLLALLFE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 844 LFTQFLQGYAFAKSGELLTKRL-RKFgFRAMLGQDIAWFDdlRNSPGALTTRLaTDASQVQGAAGSQIGMIVNSFTNVTV 922
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLsSRF-FRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 923 AMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLtgfASRDKQALEMVGQITN---EALSNIRTVAGIGKERRFIEALET 999
Cdd:COG2274 286 FLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL---RRLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWEN 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1000 ELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHF-------SYVFRVISAVvlsatalGRAFSYT 1072
Cdd:COG2274 363 LLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLgqliafnILSGRFLAPV-------AQLIGLL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1073 PSYAKAKISAARFFQLLDrQPPISVYNTAGEKWDNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCG 1152
Cdd:COG2274 436 QRFQDAKIALERLDDILD-LPPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1153 KSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLH 1232
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEAARLAGLH 591
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 1233 DFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAI 649
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
454-691 |
2.42e-85 |
|
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: 277.96 E-value: 2.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKI 613
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
452-682 |
5.49e-85 |
|
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: 276.41 E-value: 5.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYpsRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 611
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 612 KILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
176-682 |
5.49e-84 |
|
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: 285.88 E-value: 5.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 176 ASYYAGIAVAVL---ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADQMA 252
Cdd:COG4988 58 LPLLGLLLAVLLlraLLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV----EALDGYFA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 253 LFI-QRM-TSTICGFLLG--FFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAK-AGVVADeVISSMRTVAA 327
Cdd:COG4988 134 RYLpQLFlAALVPLLILVavFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARlSGHFLD-RLRGLTTLKL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 328 FGGEKREVERYEKNlvfAQRWgiRKgIVMG-----FFTGFVwcLIFlcyalaFWYGST-LVLdegeytpgtlVQIFLSVI 401
Cdd:COG4988 213 FGRAKAEAERIAEA---SEDF--RK-RTMKvlrvaFLSSAV--LEF------FASLSIaLVA----------VYIGFRLL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 402 VGALNLGNA------SPclEAF-------------ATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIkGEIEFHNVTFH 462
Cdd:COG4988 269 GGSLTLFAAlfvlllAP--EFFlplrdlgsfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGP-PSIELEDVSFS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 463 YPSRPEVkiLNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLF 542
Cdd:COG4988 346 YPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLF 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 STTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVgegggqmsggqkqRVAIARALIRNPKILLLDMATSA 622
Cdd:COG4988 424 AGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLgeggrglsggqaqRLALARALLRDAPLLLLDEPTAH 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 623 LDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:COG4988 504 LDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
454-691 |
1.29e-78 |
|
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: 258.96 E-value: 1.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHY-PSRPEvkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQI 532
Cdd:cd03252 1 ITFEHVRFRYkPDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPK 612
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 613 ILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
776-1301 |
1.12e-76 |
|
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: 265.43 E-value: 1.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 776 RRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQIL-GTFSipdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAF 854
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFG----GRDRSVLWWVPLVVIGLAVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 855 AKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKL 934
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 935 SLVILCFFPFLALSGATQTRMLTGFaSRDKQalEMVGQITN---EALSNIRTVAGIGKE----RRFIEALETELEKPFKT 1007
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRI-SKEIQ--NSMGQVTTvaeETLQGYRVVKLFGGQayetRRFDAVSNRNRRLAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1008 AiQKANIYGfcfAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQ 1087
Cdd:TIGR02203 234 T-SAGSISS---PITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1088 LLDRQPPIsvyNTAGEKWDNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD 1167
Cdd:TIGR02203 310 LLDSPPEK---DTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1168 QGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVG 1247
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 1248 SQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK--QPCCDHLDKSHT 1301
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERlvQAALERLMQGRT 520
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
447-691 |
1.39e-76 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 265.67 E-value: 1.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 447 LDRIKGEIEFHNVTFHYP-SRPEVKilnDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI 525
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 526 QWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIAR 605
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYF 685
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
....*.
gi 2462578034 686 TLVTLQ 691
Cdd:PRK13657 565 ALLRAQ 570
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
200-690 |
3.51e-75 |
|
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: 261.24 E-value: 3.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 200 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADqmaLFIqR---------MTSTICGFLLGFF 270
Cdd:COG4987 82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV----DALDN---LYL-RvllpllvalLVILAAVAFLAFF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 271 rGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAyAKAGVVAD--EVISSMRTVAAFGGEKREVERY---EKNLVFA 345
Cdd:COG4987 154 -SPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAA-ARAALRARltDLLQGAAELAAYGALDRALARLdaaEARLAAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 346 QRwgiRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSV-----IVGALNLGnaspcLEAFATG 420
Cdd:COG4987 232 QR---RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAA-GALSGPLLALLVLAAlalfeALAPLPAA-----AQHLGRV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 421 RAAATSIFETIDRKPIIDcMSEDGYKLDRiKGEIEFHNVTFHYPSRPEvKILNDLNMAIKPGEMTALVGPSGAGKSTALQ 500
Cdd:COG4987 303 RAAARRLNELLDAPPAVT-EPAEPAPAPG-GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 501 LIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQ 580
Cdd:COG4987 380 LLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPD 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 581 QFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTI 660
Cdd:COG4987 460 GLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRI 539
|
490 500 510
....*....|....*....|....*....|
gi 2462578034 661 IGFEHGTAVERGTHEELLERKGVYFTLVTL 690
Cdd:COG4987 540 LVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
92-437 |
3.56e-74 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 249.68 E-value: 3.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 92 DIWLMFVGSLCAFLHGIAQPGVLLIFGTMTDVFidydvelqelqipgkacvnntivwtnsslnqnmtngTRCGLLNIESE 171
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVF------------------------------------SLPDDDELRSE 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 172 MIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFD--CNSVGELNTRFSDDINKINDAIAD 249
Cdd:cd18578 51 ANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 250 QMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFG 329
Cdd:cd18578 131 RLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 330 GEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVIVGALNLGN 409
Cdd:cd18578 211 LEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVAN-GEYTFEQFFIVFMALIFGAQSAGQ 289
|
330 340
....*....|....*....|....*...
gi 2462578034 410 ASPCLEAFATGRAAATSIFETIDRKPII 437
Cdd:cd18578 290 AFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
789-1084 |
4.16e-72 |
|
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: 243.15 E-value: 4.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTFS-----IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTK 863
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 864 RLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFP 943
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 944 FLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQ 1023
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 1024 CIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAAR 1084
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAK 299
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1112-1301 |
9.35e-72 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 239.44 E-value: 9.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1191
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVLFACSIMDNIKYGdnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDP 1271
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG--RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190
....*....|....*....|....*....|..
gi 2462578034 1272 KILLLDEATSALDTESEK--QPCCDHLDKSHT 1301
Cdd:cd03251 158 PILILDEATSALDTESERlvQAALERLMKNRT 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1112-1290 |
1.67e-71 |
|
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: 238.67 E-value: 1.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1191
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVLFACSIMDNIKYGD-NTKEipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRD 1270
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRpDATD---EEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180
....*....|....*....|
gi 2462578034 1271 PKILLLDEATSALDTESEKQ 1290
Cdd:cd03253 156 PPILLLDEATSALDTHTERE 175
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
448-666 |
9.49e-71 |
|
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: 236.21 E-value: 9.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 448 DRIKGEIEFHNVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW 527
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 528 LRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARAL 607
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 608 IRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHG 666
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
454-666 |
4.77e-70 |
|
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: 231.89 E-value: 4.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEvKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFSTTIAENIRYGREdatmedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03228 80 YVPQDPFLFSGTIRENILSGGQ------------------------RQ------------------RIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHG 666
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1110-1289 |
8.03e-70 |
|
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: 233.66 E-value: 8.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1110 GKIDFVDCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN 1189
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1190 IGIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVR 1269
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180
....*....|....*....|
gi 2462578034 1270 DPKILLLDEATSALDTESEK 1289
Cdd:cd03254 157 DPKILILDEATSNIDTETEK 176
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1106-1297 |
2.20e-69 |
|
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: 232.36 E-value: 2.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1106 DNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF 1185
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIVSQEPVLFACSIMDNIKYGDNTKeiPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIAR 1265
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSC--SFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190
....*....|....*....|....*....|..
gi 2462578034 1266 AIVRDPKILLLDEATSALDTESEKQPCCDHLD 1297
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYD 195
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1084-1289 |
1.18e-68 |
|
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: 243.19 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1084 RFFQLLDRQPPISVYNTAGE-KWDnfQGKIDFVDCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLER 1162
Cdd:COG5265 331 RMFDLLDQPPEVADAPDAPPlVVG--GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1163 FYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNtkEIPMERVIAAAKQAQLHDFVMSLPEKY 1242
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP--DASEEEVEAAARAAQIHDFIESLPDGY 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462578034 1243 ETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK 1289
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
861-1290 |
8.29e-67 |
|
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: 236.97 E-value: 8.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 861 LTKRLRKFGFRAMLGQDIAWFDDLRNspGALTTRLATDASQVQGA-------AGSQIGMIVnsftnvtVAMIIAFSFSWK 933
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLRS--GDLLNRLVADVDALDNLylrvllpLLVALLVIL-------AAVAFLAFFSPA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 934 LSLVILCFFPFLALSGATQTRMLTGFASRDKQAL--EMVGQITnEALSNIRTVAGIGKERRF---IEALETELekpfkTA 1008
Cdd:COG4987 157 LALVLALGLLLAGLLLPLLAARLGRRAGRRLAAAraALRARLT-DLLQGAAELAAYGALDRAlarLDAAEARL-----AA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1009 IQK--ANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYvfrvISAVVLSA-------TALGRAFSYTPSYAKAk 1079
Cdd:COG4987 231 AQRrlARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPL----LALLVLAAlalfealAPLPAAAQHLGRVRAA- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1080 isAARFFQLLDRQPPISvyNTAGEKWDNFQGKIDFVDCKFTYPSRPdSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL 1159
Cdd:COG4987 306 --ARRLNELLDAPPAVT--EPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1160 LERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNtkEIPMERVIAAAKQAQLHDFVMSLP 1239
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAALP 458
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 1240 EKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA 509
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
789-1082 |
1.39e-65 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 224.85 E-value: 1.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTF-------------SIPDK----EEQRSQINGVCLLFVAMGCVSLFTQFLQG 851
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnssGLNSSagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 852 YAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFS 931
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 932 WKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQK 1011
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 1012 ANIYGFCFAFAQCIMFIANSASYRYGGYLI-SNEGLHFSYVFRVISAVVLSATALGRAFSYTPsYAKAKISA 1082
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVtQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAA 309
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
215-691 |
2.93e-63 |
|
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: 229.46 E-value: 2.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 215 RIMRMEIGWFDCNSVGELNTRfSDDINKINDAIADqmALFIQRMTSTICGFLLG--FFRGWKLTLVIISVSPLIGIGAAT 292
Cdd:TIGR03797 218 RLLRLPVSFFRQYSTGDLASR-AMGISQIRRILSG--STLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 293 IGLsvsKFTDYELKAYAKAGVVADEV------ISSMRTVAAfggEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCL 366
Cdd:TIGR03797 295 LGL---LQVRKERRLLELSGKISGLTvqlingISKLRVAGA---ENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 367 IFLCYALAFWYGSTLvLDEGEYTPGTLV---QIFLSVIVGALNLGNAspcleafATGRAAATSIFETIdrKPIIDCMSE- 442
Cdd:TIGR03797 369 PVLTSAALFAAAISL-LGGAGLSLGSFLafnTAFGSFSGAVTQLSNT-------LISILAVIPLWERA--KPILEALPEv 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 443 DGYKLD--RIKGEIEFHNVTFHY-PSRPevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHD 519
Cdd:TIGR03797 439 DEAKTDpgKLSGAIEVDRVTFRYrPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 520 IRSLNIQWLRDQIGIVEQEPVLFSTTIAENIrYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQ 599
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK--VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
490
....*....|..
gi 2462578034 680 RKGVYFTLVTLQ 691
Cdd:TIGR03797 674 REGLFAQLARRQ 685
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
212-688 |
3.46e-63 |
|
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: 229.83 E-value: 3.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 212 YFRRIMRMEIGWFDCNSVGELNTRFSddinkINDAIADQMAlfiQRMTSTICGFLLGFFRG-------WKLTLVIISvsp 284
Cdd:TIGR03796 233 FLWHILRLPVRFFAQRHAGDIASRVQ-----LNDQVAEFLS---GQLATTALDAVMLVFYAllmllydPVLTLIGIA--- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 285 LIGIGAATIGLSVSKFTDYELKA---YAKAGVVADEVISSMRTVAAFGGEKREVER---YEKNLVFAQRwgiRKGIVMGF 358
Cdd:TIGR03796 302 FAAINVLALQLVSRRRVDANRRLqqdAGKLTGVAISGLQSIETLKASGLESDFFSRwagYQAKLLNAQQ---ELGVLTQI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 359 FTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV------QIFLSVIVGALNLGNASPCLEA----------FATGRA 422
Cdd:TIGR03796 379 LGVLPTLLTSLNSALILVVGGLRVME-GQLTIGMLVafqslmSSFLEPVNNLVGFGGTLQELEGdlnrlddvlrNPVDPL 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 423 AatsifetIDRKPIIDCMSEDGykldRIKGEIEFHNVTFHYpSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLI 502
Cdd:TIGR03796 458 L-------EEPEGSAATSEPPR----RLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLV 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 503 QRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGreDATM--EDIVQAAKEANAYNFIMDLPQ 580
Cdd:TIGR03796 526 AGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLW--DPTIpdADLVRACKDAAIHDVITSRPG 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 581 QFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSkiQHGHTIISVAHRLSTVRAADTI 660
Cdd:TIGR03796 604 GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEI 681
|
490 500
....*....|....*....|....*...
gi 2462578034 661 IGFEHGTAVERGTHEELLERKGVYFTLV 688
Cdd:TIGR03796 682 IVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
37-690 |
4.41e-63 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 236.85 E-value: 4.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 37 TRRGENKSRTSWSSFKEQKKISNNNNDKKSRLQDEKKGDGVRVGFFQ-LFR----------------FSSSTDIWLMFVG 99
Cdd:PTZ00265 754 SERGYDPDEMNGNSKHENESASNKKSCKMSDENASENNAGGKLPFLRnLFKrkpkapnnlrivyreiFSYKKDVTIIALS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 100 SLCAflhGIAQPGVLLIFGTMTDVFIDYdvelqelqipgkacvnntivwtnsslnqnmtngtrcglLNIESEMIKFASYY 179
Cdd:PTZ00265 834 ILVA---GGLYPVFALLYAKYVSTLFDF--------------------------------------ANLEANSNKYSLYI 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFD--CNSVGELNTRFSDDINKINDAIADQMALFIQR 257
Cdd:PTZ00265 873 LVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHF 952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 258 MTSTICGFLLGFFRgWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVV----------------ADEVISS 321
Cdd:PTZ00265 953 IVLFLVSMVMSFYF-CPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYN 1031
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 322 MRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVldegeyTPGT-LVQIFLSV 400
Cdd:PTZ00265 1032 MNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLI------RRGTiLVDDFMKS 1105
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 401 IVGALNLGNASPCLEAFATGRAAATSIFET----IDRKPIIDCMSEDGYKL---DRIKGEIEFHNVTFHYPSRPEVKILN 473
Cdd:PTZ00265 1106 LFTFLFTGSYAGKLMSLKGDSENAKLSFEKyyplIIRKSNIDVRDNGGIRIknkNDIKGKIEIMDVNFRYISRPNVPIYK 1185
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 474 DLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYD---------------------------------------------- 507
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 508 --------PCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLP 579
Cdd:PTZ00265 1266 sgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLP 1345
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 580 QQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAA 657
Cdd:PTZ00265 1346 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRS 1425
|
730 740 750
....*....|....*....|....*....|....*....
gi 2462578034 658 DTIIGFEH----GTAVE-RGTHEELLE-RKGVYFTLVTL 690
Cdd:PTZ00265 1426 DKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
776-1290 |
3.29e-62 |
|
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: 223.10 E-value: 3.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 776 RRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIpdKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFA 855
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLII--GGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 856 KSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIA-FSFSWKL 934
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLR--GKSTGELATLLTEGVEALDGYFARYLPQLFLAAL-VPLLILVAvFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 935 SLVILCFFP----FLALSG-ATQTRMltgfasrDKQALEMvgqitnEALSN--IRTVAGI------GKERRFIEALETEL 1001
Cdd:COG4988 161 GLILLVTAPliplFMILVGkGAAKAS-------RRQWRAL------ARLSGhfLDRLRGLttlklfGRAKAEAERIAEAS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1002 EKpFKTA------IQKANIYGFCFAFAQCIMFIANSASYRYggyliSNEGLHFsyvFRVISAVVLSA------TALGRAF 1069
Cdd:COG4988 228 ED-FRKRtmkvlrVAFLSSAVLEFFASLSIALVAVYIGFRL-----LGGSLTL---FAALFVLLLAPefflplRDLGSFY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1070 sytpsYAKAK-ISAA-RFFQLLDRQPPISVYNTAGEKWDNfQGKIDFVDCKFTYPSRPdsQVLNGLSVSISPGQTLAFVG 1147
Cdd:COG4988 299 -----HARANgIAAAeKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1148 SSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAK 1227
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALE 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 1228 QAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:COG4988 449 AAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
96-405 |
1.79e-60 |
|
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: 208.65 E-value: 1.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 96 MFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVelqelqipgkacvnntivwtnsslnqnmtngtrcgllNIESEMIKF 175
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD-------------------------------------PETQALNVY 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 176 ASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFI 255
Cdd:pfam00664 44 SLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 256 QRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREV 335
Cdd:pfam00664 124 QSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYEL 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 336 ERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQI--FLSVIVGAL 405
Cdd:pfam00664 204 EKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVIS-GELSVGDLVAFlsLFAQLFGPL 274
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1081-1288 |
1.64e-59 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 215.98 E-value: 1.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1081 SAAR---FFQLLDRQPPISVYNTAGEKwDNFQGKIDFVDCKFTYPSRpdSQVLNGLSVSISPGQTLAFVGSSGCGKSTSI 1157
Cdd:PRK13657 302 AAPKleeFFEVEDAVPDVRDPPGAIDL-GRVKGAVEFDDVSFSYDNS--RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1158 QLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYG--DNTKEipmeRVIAAAKQAQLHDFV 1235
Cdd:PRK13657 379 NLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGrpDATDE----EMRAAAERAQAHDFI 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 1236 MSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 1288
Cdd:PRK13657 455 ERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
180-661 |
2.04e-59 |
|
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: 214.07 E-value: 2.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADQMALFI-QRM 258
Cdd:TIGR02857 51 ALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGV----EALDGYFARYLpQLV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 259 TSTICGFLLG---FFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAK-AGVVADeVISSMRTVAAFGGEKRE 334
Cdd:TIGR02857 127 LAVIVPLAILaavFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRlSGHFLD-RLRGLPTLKLFGRAKAQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 335 VER-YEKNLVFAQRwgirkgiVMGfftgfVWCLIFLcyalafwygSTLVLdegEY-----TPGTLVQIFLSVIVGALNLG 408
Cdd:TIGR02857 206 AAAiRRSSEEYRER-------TMR-----VLRIAFL---------SSAVL---ELfatlsVALVAVYIGFRLLAGDLDLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 409 NASPCL----EAF-------------ATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIkgEIEFHNVTFHYPSRPEVki 471
Cdd:TIGR02857 262 TGLFVLllapEFYlplrqlgaqyharADGVAAAEALFAVLDAAPRPLAGKAPVTAAPAS--SLEFSGVSVAYPGRRPA-- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIR 551
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 552 YGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMV 631
Cdd:TIGR02857 418 LARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
490 500 510
....*....|....*....|....*....|
gi 2462578034 632 QEVLSKIQHGHTIISVAHRLSTVRAADTII 661
Cdd:TIGR02857 498 LEALRALAQGRTVLLVTHRLALAALADRIV 527
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1112-1289 |
2.72e-59 |
|
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: 203.87 E-value: 2.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYpsRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNI 1190
Cdd:cd03252 1 ITFEHVRFRY--KPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1191 GIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRD 1270
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170
....*....|....*....
gi 2462578034 1271 PKILLLDEATSALDTESEK 1289
Cdd:cd03252 157 PRILIFDEATSALDYESEH 175
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
805-1289 |
2.27e-58 |
|
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: 214.99 E-value: 2.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 805 LYAFLFSQILGTFS------IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQG---YAFAKSGELLTKRLRKFGFRAMLG 875
Cdd:TIGR01846 145 LLISLALQLFALVTpllfqvVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGlrtYLFAHLTSRIDVELGARLYRHLLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 876 QDIAWFDDLRNspGALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIAFSFSWKLSLVILCFFPFLAL-----SGA 950
Cdd:TIGR01846 225 LPLGYFESRRV--GDTVARVRELEQIRNFLTGSALTVVLDLLF-VVVFLAVMFFYSPTLTGVVIGSLVCYALlsvfvGPI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 951 TQTRMLTGFaSRDKQALEMVgqitNEALSNIRTVAGIGKERRFIEALETELEKPFKT---AIQKANIYGFCFAFAQCIMF 1027
Cdd:TIGR01846 302 LRKRVEDKF-ERSAAATSFL----VESVTGIETIKATATEPQFQNRWDRQLAAYVAAsfrVTNLGNIAGQAIELIQKLTF 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1028 IAN---SASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTpsyakaKISAARFFQLLDRqpPISVYNTAGEK 1104
Cdd:TIGR01846 377 AILlwfGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQT------GIALERLGDILNS--PTEPRSAGLAA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1105 WDNFQGKIDFVDCKFTYpsRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV 1183
Cdd:TIGR01846 449 LPELRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADP 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1184 QFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAI 1263
Cdd:TIGR01846 527 AWLRRQMGVVLQENVLFSRSIRDNIALCN--PGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAI 604
|
490 500
....*....|....*....|....*.
gi 2462578034 1264 ARAIVRDPKILLLDEATSALDTESEK 1289
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEA 630
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
182-710 |
2.51e-57 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 209.18 E-value: 2.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 182 IAVAVLITGYIQIcFWVIAAARQIQ-KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIN-----------DAIAD 249
Cdd:PRK10789 45 IAVVVYLLRYVWR-VLLFGASYQLAvELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVfaagegvltlvDSLVM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 250 QMALFIQrMTSTIcgfllgffrGWKLTLVIISVSPLIGIGAATIGLSV-SKFTDYElKAYAKAGVVADEVISSMRTVAAF 328
Cdd:PRK10789 124 GCAVLIV-MSTQI---------SWQLTLLALLPMPVMAIMIKRYGDQLhERFKLAQ-AAFSSLNDRTQESLTSIRMIKAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 329 GGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQ--IFLSVIVGaln 406
Cdd:PRK10789 193 GLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVVN-GSLTLGQLTSfvMYLGLMIW--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 407 lgnasPCLeAFA-------TGRAAATSIFETIDRKPIIDcmseDGYK-LDRIKGEIEFHNVTFHYPSRpEVKILNDLNMA 478
Cdd:PRK10789 269 -----PML-ALAwmfniveRGSAAYSRIRAMLAEAPVVK----DGSEpVPEGRGELDVNIRQFTYPQT-DHPALENVNFT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 479 IKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDAT 558
Cdd:PRK10789 338 LKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDAT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 559 MEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI 638
Cdd:PRK10789 418 QQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 639 QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQsQGNQALNEEDIKDATEDD 710
Cdd:PRK10789 498 GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ-QLEAALDDAPEIREEAVD 568
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
443-688 |
7.35e-57 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 208.20 E-value: 7.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 443 DGYKLDRIKGEIEFHNVTFHYPSRPEVkiLNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRS 522
Cdd:TIGR01192 324 DAPELPNVKGAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 523 LNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVA 602
Cdd:TIGR01192 402 VTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:TIGR01192 482 IARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDG 561
|
....*.
gi 2462578034 683 VYFTLV 688
Cdd:TIGR01192 562 RFYKLL 567
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
834-1301 |
1.26e-54 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 201.40 E-value: 1.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 834 LLFVAMGCVSLFTQFLQGYAFA-KSGELLTkRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGM 912
Cdd:PRK11176 69 LVVIGLMILRGITSFISSYCISwVSGKVVM-TMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALIT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 913 IVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS-GATQTRmltgFASRDKQALEMVGQITNEA---LSNIRTVAGIG 988
Cdd:PRK11176 146 VVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVVSKR----FRNISKNMQNTMGQVTTSAeqmLKGHKEVLIFG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 989 ----KERRFIEALETELEKPFKTAIQKAniygfcfAFAQCIMFIAnSASYRYGGYLISneglhFSYVFRVISA----VVL 1060
Cdd:PRK11176 222 gqevETKRFDKVSNRMRQQGMKMVSASS-------ISDPIIQLIA-SLALAFVLYAAS-----FPSVMDTLTAgtitVVF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1061 SAT-ALGRAF----SYTPSYAKAKISAARFFQLLDRQPPIsvyNTAGEKWDNFQGKIDFVDCKFTYPSRpDSQVLNGLSV 1135
Cdd:PRK11176 289 SSMiALMRPLksltNVNAQFQRGMAACQTLFAILDLEQEK---DEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1136 SISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGdNTK 1215
Cdd:PRK11176 365 KIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYA-RTE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1216 EIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK--QPCC 1293
Cdd:PRK11176 444 QYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERaiQAAL 523
|
....*...
gi 2462578034 1294 DHLDKSHT 1301
Cdd:PRK11176 524 DELQKNRT 531
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1112-1290 |
1.29e-53 |
|
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: 184.89 E-value: 1.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1191
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVLFACSIMDNIkygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDP 1271
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170
....*....|....*....
gi 2462578034 1272 KILLLDEATSALDTESEKQ 1290
Cdd:cd03228 116 PILILDEATSALDPETEAL 134
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
452-672 |
1.34e-53 |
|
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: 187.03 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYPSRpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 611
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 612 KILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 672
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
452-673 |
4.00e-52 |
|
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: 182.69 E-value: 4.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYpsRPEVK-ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 530
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFSTTIAENIrygreD----ATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARA 606
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL-----DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 607 LIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 673
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
789-1043 |
1.45e-51 |
|
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: 183.23 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTFsIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 868
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-LPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 869 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 948
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 949 GATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFI 1028
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250
....*....|....*
gi 2462578034 1029 ANSASYRYGGYLISN 1043
Cdd:pfam00664 238 SYALALWFGAYLVIS 252
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1110-1290 |
5.32e-51 |
|
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: 179.32 E-value: 5.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1110 GKIDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN 1189
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1190 IGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVR 1269
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180
....*....|....*....|.
gi 2462578034 1270 DPKILLLDEATSALDTESEKQ 1290
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEER 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
429-1288 |
1.25e-50 |
|
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: 197.09 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 429 ETIDRKPIIDcmsEDGYKldrikgeIEFHNVTFHYpSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDP 508
Cdd:TIGR00957 622 DSIERRTIKP---GEGNS-------ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 509 CEGMVTVDGhdirslniqwlrdQIGIVEQEPVLFSTTIAENIRYGRedATMEDIVQAAKEANAynFIMDL---PQQFDTL 585
Cdd:TIGR00957 691 VEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACA--LLPDLeilPSGDRTE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 586 VGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE-SEAMVQEVLSK--IQHGHTIISVAHRLSTVRAADTIIG 662
Cdd:TIGR00957 754 IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIV 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 663 FEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQALNEEDI---------KDA--TEDDMLARTFSRGSYQDSLRASirq 731
Cdd:TIGR00957 834 MSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSwtalvsgegKEAklIENGMLVTDVVGKQLQRQLSAS--- 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 732 rSKSQLSYLVHEPPLAVVDHKSTYEEDRKdkdipvQEEVEPAPVRRIlKFSApEWPYMlvgsvgAAVNGTVTPLYAFLF- 810
Cdd:TIGR00957 911 -SSDSGDQSRHHGSSAELQKAEAKEETWK------LMEADKAQTGQV-ELSV-YWDYM------KAIGLFITFLSIFLFv 975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 811 --------SQILGTFSIPDKEEQRSQINGVCLLFV--AMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAW 880
Cdd:TIGR00957 976 cnhvsalaSNYWLSLWTDDPMVNGTQNNTSLRLSVygALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSF 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 881 FDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVIlcffPFLALSGATQTRMLTGfA 960
Cdd:TIGR00957 1056 FE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVII----PPLGLLYFFVQRFYVA-S 1128
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 961 SRDKQALEMVGQIT-----NEALSNIRTVAGIGKERRFIEALETELEkpfktAIQKAniygfcfafaqCIMFIANSASYR 1035
Cdd:TIGR00957 1129 SRQLKRLESVSRSPvyshfNETLLGVSVIRAFEEQERFIHQSDLKVD-----ENQKA-----------YYPSIVANRWLA 1192
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1036 YGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYT-------------PSYAKAKISAA---RFFQLLDRQPPISVYN 1099
Cdd:TIGR00957 1193 VRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSlqvtfylnwlvrmSSEMETNIVAVerlKEYSETEKEAPWQIQE 1272
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1100 TAG-EKWDNfQGKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD 1177
Cdd:TIGR00957 1273 TAPpSGWPP-RGRVEFRNYCLRY--REDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1178 SKKVNVQFLRSNIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGE 1257
Cdd:TIGR00957 1350 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQ 1426
|
890 900 910
....*....|....*....|....*....|.
gi 2462578034 1258 KQRIAIARAIVRDPKILLLDEATSALDTESE 1288
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
188-689 |
9.19e-50 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 189.57 E-value: 9.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 188 ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDdINKINDAIADQM-ALFIQRMTSTICGFL 266
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTIlSLFLDMWILVIVGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 267 LGFfRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKrevERY-------- 338
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEA---ERYskidsefg 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 339 ---EKNLVFAQRWGIRKGIVMGFftgfvwCLIFLCYALafWYGSTLVLdEGEYTPGTLV--QIFLSVIVGAL-NLGNASP 412
Cdd:TIGR01193 366 dylNKSFKYQKADQGQQAIKAVT------KLILNVVIL--WTGAYLVM-RGKLTLGQLItfNALLSYFLTPLeNIINLQP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 413 CLEAfatGRAAATSIFETIdrkpIIDCMSEDGYKLD---RIKGEIEFHNVTFHYPSRPEvkILNDLNMAIKPGEMTALVG 489
Cdd:TIGR01193 437 KLQA---ARVANNRLNEVY----LVDSEFINKKKRTelnNLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 490 PSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYG-REDATMEDIVQAAKE 568
Cdd:TIGR01193 508 MSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEI 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 569 ANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHgHTIISVA 648
Cdd:TIGR01193 588 AEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVA 666
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2462578034 649 HRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVT 689
Cdd:TIGR01193 667 HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1110-1290 |
3.66e-46 |
|
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: 165.36 E-value: 3.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1110 GKIDFVDCKFTYpsRPDSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 1188
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 NIGIVSQEPVLFACSIMDNI----KYGDntkeipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIA 1264
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180
....*....|....*....|....*.
gi 2462578034 1265 RAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDAL 177
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
180-696 |
1.08e-45 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 174.91 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITG-------YIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA 252
Cdd:PRK10790 65 AGLAAAYVGLQllaaglhYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 253 LFIqRMTSTICGFLLGFFR-GWKLTLVIISVSPLIgIGAATIGLSVSKFTDYELKAYakagvVAD------EVISSM--- 322
Cdd:PRK10790 145 TVL-RSAALIGAMLVAMFSlDWRMALVAIMIFPAV-LVVMVIYQRYSTPIVRRVRAY-----LADindgfnEVINGMsvi 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 323 ---RTVAAFGGEKREVER--YEKNLVFAQRWGIRKGIVMGFFTGFVWC-LIFLcyalaFWYGSTLVLDEGeytpgtLVQI 396
Cdd:PRK10790 218 qqfRQQARFGERMGEASRshYMARMQTLRLDGFLLRPLLSLFSALILCgLLML-----FGFSASGTIEVG------VLYA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 397 FLSVIvGALNlgnaSPCLEaFATGRA-------AATSIFETIDRkpiidcmSEDGYKLDRI---KGEIEFHNVTFHYpsR 466
Cdd:PRK10790 287 FISYL-GRLN----EPLIE-LTTQQSmlqqavvAGERVFELMDG-------PRQQYGNDDRplqSGRIDIDNVSFAY--R 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 467 PEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTI 546
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 547 AENIRYGReDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE 626
Cdd:PRK10790 432 LANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 627 SEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQ 696
Cdd:PRK10790 511 TEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
378-680 |
2.51e-45 |
|
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: 173.40 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 378 GSTLVLdEGEYTPGTLvqIFLSVIVG-ALnlgnaSPcLE-------AFATGRAAATSIFETIDRKPiidcMSEDGYKLDR 449
Cdd:COG4618 260 GAYLVI-QGEITPGAM--IAASILMGrAL-----AP-IEqaiggwkQFVSARQAYRRLNELLAAVP----AEPERMPLPR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 450 IKGEIEFHNVTFHYPSRPEVkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRslniQWLR 529
Cdd:COG4618 327 PKGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 530 DQ----IGIVEQEPVLFSTTIAENI-RYGreDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIA 604
Cdd:COG4618 402 EElgrhIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 605 RALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
328-687 |
6.91e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 172.32 E-value: 6.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 328 FGGEKR---EVERYEKNLVFAQRwgirkgiVMGFFTGFVWCLIFLCYALA----FWYGSTLVldEGEYTPGTLVQIF--- 397
Cdd:PRK11160 216 FGAEDRyrqQLEQTEQQWLAAQR-------RQANLTGLSQALMILANGLTvvlmLWLAAGGV--GGNAQPGALIALFvfa 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 398 -------LSVIVGA-LNLGNaspCLeafatgrAAATSIFETIDRKPIIDCMSEDGYKLDRikGEIEFHNVTFHYPSRPEv 469
Cdd:PRK11160 287 alaafeaLMPVAGAfQHLGQ---VI-------ASARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 470 KILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAEN 549
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDN 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 550 IRYGREDATMEDIVQAAKEANAYNFIMDlPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEA 629
Cdd:PRK11160 434 LLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETER 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 630 MVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTL 687
Cdd:PRK11160 513 QILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
787-1290 |
8.14e-45 |
|
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: 170.93 E-value: 8.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 787 PYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDkeEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLR 866
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAG--EPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 867 KFGFRAMLGQDIAWFddLRNSPGALTTRLATDASQVQG-AAGSQIGMIVNSFtnVTVAMIIA-FSFSWKLSLVILCFFP- 943
Cdd:TIGR02857 81 ERLLEAVAALGPRWL--QGRPSGELATLALEGVEALDGyFARYLPQLVLAVI--VPLAILAAvFPQDWISGLILLLTAPl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 944 ---FLALSG-ATQTRmltgfASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELE-------KPFKTAIQKA 1012
Cdd:TIGR02857 157 ipiFMILIGwAAQAA-----ARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEeyrertmRVLRIAFLSS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1013 NIYGFcFAfAQCIMFIANSASYRY-GGYLISNEGLhfsYVFRVISAVVLSATALGRAFSYTpsyAKAKISAARFFQLLDR 1091
Cdd:TIGR02857 232 AVLEL-FA-TLSVALVAVYIGFRLlAGDLDLATGL---FVLLLAPEFYLPLRQLGAQYHAR---ADGVAAAEALFAVLDA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1092 QPPIsVYNTAGEKWDNFQGkIDFVDCKFTYPSRPdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV 1171
Cdd:TIGR02857 304 APRP-LAGKAPVTAAPASS-LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1172 MIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGS 1251
Cdd:TIGR02857 380 AVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGA 457
|
490 500 510
....*....|....*....|....*....|....*....
gi 2462578034 1252 QLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAE 496
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
454-677 |
1.22e-43 |
|
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: 158.50 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQ-- 526
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 527 WLRDQIGIVEQEPVLFSTTIAENIRYG------REDATMEDIVQAAKEanaynfIMDLP----------------QQfdt 584
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALR------KAALWdevkdrlhalglsggqQQ--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 585 lvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGF 663
Cdd:cd03260 149 ---------------RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFL 213
|
250
....*....|....
gi 2462578034 664 EHGTAVERGTHEEL 677
Cdd:cd03260 214 LNGRLVEFGPTEQI 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
200-651 |
1.55e-43 |
|
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: 167.15 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 200 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADqmaLFIQRMTSTICGFLLG-------FFRG 272
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADV----DALQD---LYVRVIVPAGVALVVGaaavaaiAVLS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 273 WKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAyaKAGVVADEVISSMRTVA---AFGGEKREVERYEKnlvfAQRWG 349
Cdd:TIGR02868 153 VPAALILAAGLLLAGFVAPLVSLRAARAAEQALAR--LRGELAAQLTDALDGAAelvASGALPAALAQVEE----ADREL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 350 IRKGIVMGFFTGFVWCLIFLCYALAFWygSTLVLDEGEYTPGTLVQIFLSVIV-GALNLGNA----SPCLEAFATGRAAA 424
Cdd:TIGR02868 227 TRAERRAAAATALGAALTLLAAGLAVL--GALWAGGPAVADGRLAPVTLAVLVlLPLAAFEAfaalPAAAQQLTRVRAAA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 425 TSIFETIDRKPIIDCMS---EDGYKLDRIKgeIEFHNVTFHYPSRPEVkiLNDLNMAIKPGEMTALVGPSGAGKSTALQL 501
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSapaAGAVGLGKPT--LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 502 IQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQ 581
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDG 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 582 FDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRL 651
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
916-1288 |
3.88e-43 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 167.37 E-value: 3.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 916 SFTNVTVAMIIAFSFSWKLSLVILCF-FPFLALSGATQTRMLTGFASRDKQALEMVGQITnEALSNIRTVAGIGKERRFI 994
Cdd:TIGR01192 140 TFVALFLLIPTAFAMDWRLSIVLMVLgILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVS-DSISNVSVVHSYNRIEAET 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 995 EALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHfsyVFRVISAVVLSATALGR-----AF 1069
Cdd:TIGR01192 219 SALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELS---VGEVIAFIGFANLLIGRldqmsGF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1070 SYTPSYAKAKISaaRFFQLLDRQPPISVYNTAGEkWDNFQGKIDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSS 1149
Cdd:TIGR01192 296 ITQIFEARAKLE--DFFDLEDSVFQREEPADAPE-LPNVKGAVEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1150 GCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKEipMERVIAAAKQA 1229
Cdd:TIGR01192 371 GAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGAT--DEEVYEAAKAA 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 1230 QLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 1288
Cdd:TIGR01192 449 AAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETE 507
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
467-693 |
1.51e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 165.40 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 467 PEVKILND-LNMAIKPGEMTALVGPSGAGKSTALQLIQRFYdPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTT 545
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 546 IAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDN 625
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 626 ESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQ 693
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
454-681 |
7.42e-42 |
|
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: 153.64 E-value: 7.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPV--LFSTTIAENI-----RYGREDATMEDIV-QAAKEANAYNF----IMDLP---QQfdtlvgegggqmsggqk 598
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVafgpeNLGLPREEIRERVeEALELVGLEHLadrpPHELSggqKQ----------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 599 qRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEE 676
Cdd:COG1122 142 -RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPRE 220
|
....*
gi 2462578034 677 LLERK 681
Cdd:COG1122 221 VFSDY 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1081-1290 |
1.44e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 162.30 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1081 SAARFFQLLDRQPPISVYNTAGEKWDnfQGKIDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL 1160
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1161 ERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSlPE 1240
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPN--ASDEALIEVLQQVGLEKLLED-DK 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1241 KYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQ 513
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
174-424 |
2.27e-41 |
|
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: 154.26 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 174 KFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMAL 253
Cdd:cd18557 37 ELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 254 FIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKR 333
Cdd:cd18557 117 LLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 334 EVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQIFLSVIVGALNLGNASPC 413
Cdd:cd18557 197 EIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVL-SGQLTVGELTSFILYTIMVASSVGGLSSL 275
|
250
....*....|.
gi 2462578034 414 LEAFATGRAAA 424
Cdd:cd18557 276 LADIMKALGAS 286
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
454-668 |
2.57e-41 |
|
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: 149.67 E-value: 2.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFSTTIAENIRYGREdatmediVQaakeanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03246 80 YLPQDDELFSGSIAENILSGGQ-------RQ-----------------------------------RLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 614 LLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRAADTIIGFEHGTA 668
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1130-1281 |
2.88e-41 |
|
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: 148.95 E-value: 2.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLF-ACSIMDNI 1208
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 1209 KYGdntkeIPMERVIAAAKQAQLHDFV--MSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1281
Cdd:pfam00005 81 RLG-----LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1129-1289 |
3.15e-41 |
|
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: 161.07 E-value: 3.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 1208
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1209 -KYGDntkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1287
Cdd:COG4618 427 aRFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
..
gi 2462578034 1288 EK 1289
Cdd:COG4618 503 EA 504
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
775-1289 |
3.58e-41 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 161.42 E-value: 3.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 775 VRRILKFSAPeWP-------YMLVGSVGAAVNGTVtpLYAFLFSQILGTFSIPDKeeqrsQINGVCLLFVAMGCVSLFTQ 847
Cdd:PRK10790 11 LKRLLAYGSP-WRkplglavLMLWVAAAAEVSGPL--LISYFIDNMVAKGNLPLG-----LVAGLAAAYVGLQLLAAGLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 848 FLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlrNSP-GALTTRLATDASQVQGAAGSQIGMIVNSFTNVtVAMII 926
Cdd:PRK10790 83 YAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD---TQPvGQLISRVTNDTEVIRDLYVTVVATVLRSAALI-GAMLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 927 A-FSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPF 1005
Cdd:PRK10790 159 AmFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1006 KTAIQKANIYGFC--------FAFAQCIMFIAnsasyrYGgylISNEGlhfsyvfrVISAVVLSA--TALGRA------- 1068
Cdd:PRK10790 239 MARMQTLRLDGFLlrpllslfSALILCGLLML------FG---FSASG--------TIEVGVLYAfiSYLGRLnepliel 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1069 FSYTPSYAKAKISAARFFQLLDRqpPISVYNTAGEKWDnfQGKIDFVDCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGS 1148
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFELMDG--PRQQYGNDDRPLQ--SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGH 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1149 SGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGdntKEIPMERVIAAAKQ 1228
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALET 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 1229 AQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK 1289
Cdd:PRK10790 453 VQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1053-1290 |
9.24e-41 |
|
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: 159.06 E-value: 9.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1053 RVISAVVLSATALGRAFSYTP----SYAKAKISAARFFQLLDRQPPISVYNTAGEKwDNFQGKIDFV--DCKFTYPsrPD 1126
Cdd:TIGR02868 271 VTLAVLVLLPLAAFEAFAALPaaaqQLTRVRAAAERIVEVLDAAGPVAEGSAPAAG-AVGLGKPTLElrDLSAGYP--GA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1127 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMD 1206
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1207 NIKYGdnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1286
Cdd:TIGR02868 428 NLRLA--RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
....
gi 2462578034 1287 SEKQ 1290
Cdd:TIGR02868 506 TADE 509
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
791-1288 |
1.16e-38 |
|
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: 152.89 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 791 VGSVGAAVN--GTVTPLYAF-LFSQILGTFSIPdkeeqrsqingvCLLFVAMGCVSLFT-----QFLQGYAFAKSGELLT 862
Cdd:TIGR01842 11 VGLFSFVINilMLAPPLYMLqVYDRVLTSGSVP------------TLLMLTVLALGLYLflgllDALRSFVLVRIGEKLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 863 KRLRKFGFRAMLGQDiawfddLRNSPGalttrlatDASQvqgaagsqigmIVNSFTNV----TVAMIIAF-SFSWKLSLV 937
Cdd:TIGR01842 79 GALNQPIFAASFSAT------LRRGSG--------DGLQ-----------ALRDLDQLrqflTGPGLFAFfDAPWMPIYL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 938 ILCF-----FPFLALSGAT---QTRMLTGFASRD--KQALEMVGQITNEALSNIR------TVAGIGKERRFIEALETEL 1001
Cdd:TIGR01842 134 LVCFllhpwIGILALGGAVvlvGLALLNNRATKKplKEATEASIRANNLADSALRnaevieAMGMMGNLTKRWGRFHSKY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1002 EKPFKTAIQKANIYGfcfAFAQCIMFIANSASYRYGGYL-ISNE---GLhfsyvfrVISAVVLSATALG---RAFSYTPS 1074
Cdd:TIGR01842 214 LSAQSAASDRAGMLS---NLSKYFRIVLQSLVLGLGAYLaIDGEitpGM-------MIAGSILVGRALApidGAIGGWKQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1075 YAKAKISAARFFQLLDRQPPisvyNTAGEKWDNFQGKIDfVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKS 1154
Cdd:TIGR01842 284 FSGARQAYKRLNELLANYPS----RDPAMPLPEPEGHLS-VENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKS 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1155 TSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI-KYGDNTKEipmERVIAAAKQAQLHD 1233
Cdd:TIGR01842 359 TLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFGENADP---EKIIEAAKLAGVHE 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 1234 FVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 1288
Cdd:TIGR01842 436 LILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1126-1287 |
1.40e-38 |
|
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: 143.86 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD-----PDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1198
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFACSIMDNIKYGDN-----TKEIPMERVIAAAKQAQLHDfvmslpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKI 1273
Cdd:cd03260 92 PFPGSIYDNVAYGLRlhgikLKEELDERVEEALRKAALWD---------EVKDRLHALGLSGGQQQRLCLARALANEPEV 162
|
170
....*....|....
gi 2462578034 1274 LLLDEATSALDTES 1287
Cdd:cd03260 163 LLLDEPTSALDPIS 176
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
454-649 |
4.22e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.88 E-value: 4.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFSTTIAENI----RYGREDATMEDIVQAAKEANAYNFIMDLP--------QQfdtlvgegggqmsggqkqRV 601
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPverlsggeRQ------------------RL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462578034 602 AIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 649
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSH 189
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
178-394 |
5.63e-38 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 144.22 E-value: 5.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 178 YYAGIAVAVLITGYIQ-ICFWvIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQ 256
Cdd:cd18572 41 LLLLLSVLSGLFSGLRgGCFS-YAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 257 RMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVE 336
Cdd:cd18572 120 NLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREAR 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 337 RYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLV 394
Cdd:cd18572 200 RYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVL-SGRMSAGQLV 256
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
454-667 |
6.31e-38 |
|
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: 140.40 E-value: 6.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW--LRDQ 531
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFST-TIAENIRYGredatmedivqaakeanaynfimdLP---QQfdtlvgegggqmsggqkqRVAIARAL 607
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG------------------------LSggqQQ------------------RVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 608 IRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGT 667
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
179-393 |
2.28e-37 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 142.77 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 179 YAGIAVAVLITGYiqiCFwVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRM 258
Cdd:cd18780 52 VLIGSIATFLRSW---LF-TLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 259 TSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERY 338
Cdd:cd18780 128 VQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 339 EKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTL 393
Cdd:cd18780 208 SEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVID-GELTTGLL 261
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
454-680 |
5.08e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 147.36 E-value: 5.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRP--EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWL 528
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 529 RDQIGIVEQEPV--LF-STTIAENIRYG---REDATMEDIVQAAKE-----------ANAYnfimdlPQQFdtlvgeggg 591
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEllervglppdlADRY------PHELsgg------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 592 qmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTA 668
Cdd:COG1123 409 -----qrqRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250
....*....|..
gi 2462578034 669 VERGTHEELLER 680
Cdd:COG1123 484 VEDGPTEEVFAN 495
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
455-667 |
5.28e-37 |
|
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: 138.75 E-value: 5.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 455 EFHNVTFHYPSRPEvKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGI 534
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 535 VEQEP--VLFSTTIAENIRYGREDATM--EDIVQAAKEANAYNFIMDLP-----------QQfdtlvgegggqmsggqkq 599
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLpeEEIEERVEEALELVGLEGLRdrspftlsggqKQ------------------ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRA-ADTIIGFEHGT 667
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
454-672 |
2.15e-36 |
|
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: 135.90 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEvKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIG 533
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFSTTIAENIryGREDATMEdivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--GRRFSGGE-------------------RQ------------------RLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 672
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
884-1290 |
3.07e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 146.01 E-value: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 884 LRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFT-NVTVAMIIAFSFSWKLSLVILCFFPFLALsgaTQTRMLTGFASR 962
Cdd:PRK10789 88 LRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVmGCAVLIVMSTQISWQLTLLALLPMPVMAI---MIKRYGDQLHER 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 963 DKQALEMVGQITN---EALSNIRTVAGIGKE----RRFIEALETELEKPFKTAIQKA----NIYgfcFAFAqcimfIANS 1031
Cdd:PRK10789 165 FKLAQAAFSSLNDrtqESLTSIRMIKAFGLEdrqsALFAADAEDTGKKNMRVARIDArfdpTIY---IAIG-----MANL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1032 ASYRYGGYLISNEGLHF----SYVFrVISAVVLSATALGRAFSYTpsyakAKISAA--RFFQLLDRQPpisVYNTAGEKW 1105
Cdd:PRK10789 237 LAIGGGSWMVVNGSLTLgqltSFVM-YLGLMIWPMLALAWMFNIV-----ERGSAAysRIRAMLAEAP---VVKDGSEPV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1106 DNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF 1185
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIVSQEPVLFACSIMDNIKYG--DNTKEipmeRVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAI 1263
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALGrpDATQQ----EIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISI 462
|
410 420
....*....|....*....|....*..
gi 2462578034 1264 ARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQ 489
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
454-661 |
7.08e-36 |
|
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: 136.06 E-value: 7.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSR-PEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlrDQI 532
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLFS-TTIAENIRYGREDATM-----EDIVQAAKE-------ANAYnfimdlP-------QQfdtlvgegggq 592
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVpkaeaRERAEELLElvglsgfENAY------PhqlsggmRQ----------- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 593 msggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTII 661
Cdd:cd03293 139 -------RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVV 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
454-678 |
7.17e-36 |
|
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: 137.10 E-value: 7.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVL-FSTTIAENIRYGR---------EDATMEDIVQAA-KEANAYNFIMdlpQQFDTLvgegggqmsggqkqRVA 602
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAVEEAlERTGLEHLAD---RPVDELsgg--------erqRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 603 IARALIRNPKILLLDMATSALD--NESEAMvqEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEEL 677
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlaHQLEVL--ELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 2462578034 678 L 678
Cdd:COG1120 226 L 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
455-667 |
8.58e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 133.52 E-value: 8.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 455 EFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGI 534
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 535 VEQepvlFSttiaeniryGREdatmedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKIL 614
Cdd:cd00267 78 VPQ----LS---------GGQ------------------------RQ------------------RVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 615 LLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGT 667
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
806-1043 |
1.07e-35 |
|
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: 137.69 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 806 YAFLFSQILGTFSIP-------D---KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLG 875
Cdd:cd18557 2 LLFLLISSAAQLLLPyligrliDtiiKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 876 QDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRM 955
Cdd:cd18557 82 QEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 956 LTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYR 1035
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLW 239
|
....*...
gi 2462578034 1036 YGGYLISN 1043
Cdd:cd18557 240 YGGYLVLS 247
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
454-678 |
1.43e-35 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 135.40 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLR 529
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 530 DQIGIVEQEPVLFST-TIAENIRYGREDATMEDIVQAAK------------EANAYnfimdlPQQFdtlvgegggqmSGG 596
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERvlellelvgledKADAY------PAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 597 QKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGT 673
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....*
gi 2462578034 674 HEELL 678
Cdd:cd03258 225 VEEVF 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
452-673 |
1.75e-35 |
|
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: 134.46 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHY-PSRPEVkiLNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 530
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFSTTIAENI-RYGREDAtmEDIVQAAKEANAYNfimDLPQQFDTLVgegggqmsggqkqrvAIARALIR 609
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYSD--EEIYGALRVSEGGL---NLSQGQRQLL---------------CLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 610 NPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 673
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1129-1287 |
1.94e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.17 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 1208
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1209 KYGDNTKEIP--MERVIAAAKQAQLHDFVMslpekyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1286
Cdd:COG4619 95 PFPFQLRERKfdRERALELLERLGLPPDIL------DKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
.
gi 2462578034 1287 S 1287
Cdd:COG4619 165 N 165
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
454-670 |
4.96e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 133.63 E-value: 4.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPS-RPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLI---QRfydPCEGMVTVDGHDIRSLNI---- 525
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSErela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 526 QWLRDQIGIVEQEPVLFST-TIAENI----RYGREDAtmEDIVQAAKEA--------NAYNFIMDLP---QQfdtlvgeg 589
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENValplLLAGVSR--KERRERARELlervglgdRLDHRPSQLSggqQQ-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 590 ggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:COG1136 152 ----------RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGR 221
|
...
gi 2462578034 668 AVE 670
Cdd:COG1136 222 IVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
454-666 |
5.14e-35 |
|
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: 133.38 E-value: 5.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPE-VKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQWL 528
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 529 RDQIGIVEQEPVLFST-TIAENIRY-----GREDATMEDIVQAAKE-----ANAYNFIMDLP---QQfdtlvgegggqms 594
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELLErvglgDRLNHYPSELSggqQQ------------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 595 ggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAADTIIGFEHG 666
Cdd:cd03255 148 -----RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
472-621 |
8.99e-35 |
|
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: 130.08 E-value: 8.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFS-TTIAENI 550
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 551 RYGREdatMEDIVQAAKEANAYNFI--MDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATS 621
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
454-682 |
1.14e-34 |
|
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: 133.44 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqWLRDQIG 533
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST-TIAENIRYgreDATMEDIVQAAKEANAYNFI--MDLPQQFDTLVgeggGQMSGGQKQRVAIARALIRN 610
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIelLGLEEFLDRRV----GELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 611 PKILLLDMATSALDNES-EAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:COG4555 151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
454-680 |
1.17e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.20 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI--RSLNIQWLRDQ 531
Cdd:COG1126 2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFS-TTIAENIRYG--------REDAT---ME--DIVQAAKEANAYnfimdlP-------QQfdtlvgegg 590
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvkkmsKAEAEeraMEllERVGLADKADAY------PaqlsggqQQ--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 591 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQH----GHTIISVAHRLSTVR-AADTIIGFEH 665
Cdd:COG1126 144 ---------RVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDVMRDlakeGMTMVVVTHEMGFAReVADRVVFMDG 211
|
250
....*....|....*
gi 2462578034 666 GTAVERGTHEELLER 680
Cdd:COG1126 212 GRIVEEGPPEEFFEN 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
454-678 |
5.01e-34 |
|
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: 131.27 E-value: 5.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFS-TTIAENI-------RYGRedatmEDIVQAAKEANAynfIMDLPQQfdTLVGEGGGQMSGGQKQRVAIAR 605
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkllKWPK-----EKIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRL-STVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
454-680 |
6.17e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 130.95 E-value: 6.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRdQIG 533
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST-TIAENIR-----YGREDATMEDIVQAAKEAnaynfiMDLPQQFDTLVgegggqmsggqKQ-------R 600
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEARERIDELLEL------FGLTDAADRKV-----------GTlsggmkqR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 601 VAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 678
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELK 219
|
..
gi 2462578034 679 ER 680
Cdd:COG1131 220 AR 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
454-670 |
7.98e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.17 E-value: 7.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQE-PVLFSTTIAENIRY-----GREDATMEDIVQAA--------KeanAYNFIMDLP---QQfdtlvgegggqm 593
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVldlvglsdK---AKALPHELSggeQQ------------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 594 sggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADT-IIGFEHGTAVE 670
Cdd:COG2884 145 ------RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
454-672 |
1.34e-33 |
|
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: 129.55 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD-- 530
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 -QIGIVEQEPvlFST-----TIAENIRYGREDATMEDIVQAAKEANAYNFI-MDLP---------------QQfdtlvge 588
Cdd:cd03257 82 kEIQMVFQDP--MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPeevlnryphelsggqRQ------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 589 gggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEH 665
Cdd:cd03257 153 -----------RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeeLGLTLLFITHDLGVVAKiADRVAVMYA 221
|
....*..
gi 2462578034 666 GTAVERG 672
Cdd:cd03257 222 GKIVEEG 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
454-672 |
1.39e-33 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 129.18 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDqIG 533
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRN-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST-TIAENIRYGREDATM--EDIVQAAKEANAynfIMDLP--------------QQfdtlvgegggqmsgg 596
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEgllnryphelsggqQQ--------------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 597 qkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHGTAVERG 672
Cdd:cd03259 138 ---RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1110-1288 |
2.42e-33 |
|
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: 128.30 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1110 GKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 1188
Cdd:cd03369 5 GEIEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 NIGIVSQEPVLFACSIMDNI----KYGDntkeipmERVIAAAKqaqlhdfvmslpekyetnVGSQGSQLSRGEKQRIAIA 1264
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdpfdEYSD-------EEIYGALR------------------VSEGGLNLSQGQRQLLCLA 137
|
170 180
....*....|....*....|....
gi 2462578034 1265 RAIVRDPKILLLDEATSALDTESE 1288
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATD 161
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1112-1284 |
2.49e-33 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 128.74 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflrsnI 1190
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1191 GIVSQEPVLFA-CSIMDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIAR 1265
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKaearERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170
....*....|....*....
gi 2462578034 1266 AIVRDPKILLLDEATSALD 1284
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALD 163
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
454-679 |
3.13e-33 |
|
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: 128.94 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFST-TIAENIRYG-RE-----DATMEDIVQAAKEAnaynfiMDLPQQFDTLvgegggqmsggqkqRVAI 603
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREhtdlsEAEIRELVLEKLEL------VGLPGAADKMpsels----ggmrkRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 679
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1126-1284 |
3.18e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.39 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD--PDQ---GKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1198
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDiyDPDVDVVELRRRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFACSIMDNIKYG-----DNTKEIPMERVIAAAKQAQLHDFVmslpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKI 1273
Cdd:COG1117 103 PFPKSIYDNVAYGlrlhgIKSKSELDEIVEESLRKAALWDEV-------KDRLKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170
....*....|.
gi 2462578034 1274 LLLDEATSALD 1284
Cdd:COG1117 176 LLMDEPTSALD 186
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
454-1288 |
3.22e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 140.11 E-value: 3.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVdghdirslniqwLRDQIG 533
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFSTTIAENIRYGrEDATMEDIVQAAkEANAYNFIMDL-PQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPK 612
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFG-SDFESERYWRAI-DVTALQHDLDLlPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 613 ILLLDMATSALDNESEAMVQEvlSKIQH---GHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVT 689
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFD--SCMKDelkGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 690 lqsqgNQALNEEDIKDATEDDMLARTFSRGSYQDSLR--ASIRQrSKSQLSYLVHepplavvdhkstyeedrkdkdipvQ 767
Cdd:PLN03232 839 -----NAGKMDATQEVNTNDENILKLGPTVTIDVSERnlGSTKQ-GKRGRSVLVK------------------------Q 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 768 EEVEPAPVrrilkfsapEWPYMLvgSVGAAVNG--TVTPLYA-FLFSQILGTFSIP------DKEEQRSQINGVCLLFVA 838
Cdd:PLN03232 889 EERETGII---------SWNVLM--RYNKAVGGlwVVMILLVcYLTTEVLRVSSSTwlsiwtDQSTPKSYSPGFYIVVYA 957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 839 M-GCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSF 917
Cdd:PLN03232 958 LlGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKDIGDIDRNVANLMNMFMNQL 1035
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 918 -----TNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQ--------TR---------MLTGFAS-RDKQALEMVGQIT 974
Cdd:PLN03232 1036 wqllsTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSRevrrldsvTRspiyaqfgeALNGLSSiRAYKAYDRMAKIN 1115
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 975 NEAL-SNIR-TVAGIGKERRFIEALETelekpfktaiqkanIYGFCFAFAQCIMFIANSASYRYGGYlISNEGLHFSY-- 1050
Cdd:PLN03232 1116 GKSMdNNIRfTLANTSSNRWLTIRLET--------------LGGVMIWLTATFAVLRNGNAENQAGF-ASTMGLLLSYtl 1180
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1051 --------VFRVISAVVLSATALGRAFSYT--PSYAKAKISAARffqlldrqPPISvyntagekWDNfQGKIDFVDCKFT 1120
Cdd:PLN03232 1181 nittllsgVLRQASKAENSLNSVERVGNYIdlPSEATAIIENNR--------PVSG--------WPS-RGSIKFEDVHLR 1243
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1121 YpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL 1199
Cdd:PLN03232 1244 Y--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL 1321
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 FACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:PLN03232 1322 FSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
....*....
gi 2462578034 1280 TSALDTESE 1288
Cdd:PLN03232 1399 TASVDVRTD 1407
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1128-1290 |
3.52e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 128.24 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGHD----SKKVNVQFLRSNIGIVSQE---- 1196
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDisslSERELARLRRRHIGFVFQFfnll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 PVLfacSIMDNI----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPK 1272
Cdd:COG1136 99 PEL---TALENValplLLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQRVAIARALVNRPK 164
|
170
....*....|....*...
gi 2462578034 1273 ILLLDEATSALDTESEKQ 1290
Cdd:COG1136 165 LILADEPTGNLDSKTGEE 182
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
807-1290 |
3.74e-33 |
|
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: 138.33 E-value: 3.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 807 AFLFSQILGTFsIPDKEEQRSQINGVCLLFVAMgcVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRN 886
Cdd:TIGR01193 176 SYYLQKIIDTY-IPHKMMGTLGIISIGLIIAYI--IQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRT 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 887 spGALTTRLaTDASQVQGAAGSqigMIVNSFTNVTVAMIIAFSFSW---KLSLVILCFFPFLALSGATQTRMLTGFASRD 963
Cdd:TIGR01193 253 --GEIVSRF-TDASSIIDALAS---TILSLFLDMWILVIVGLFLVRqnmLLFLLSLLSIPVYAVIIILFKRTFNKLNHDA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 964 KQALEMVGQITNEALSNIRTVAGIGKERRFIEALETE----LEKPFKTAIQKANIYgfcfAFAQCIMFIANSASYRYGGY 1039
Cdd:TIGR01193 327 MQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEfgdyLNKSFKYQKADQGQQ----AIKAVTKLILNVVILWTGAY 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1040 LISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQ--LLDRQPPISVYNTAGEkwdNFQGKIDFVDC 1117
Cdd:TIGR01193 403 LVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEFINKKKRTELN---NLNGDIVINDV 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1118 KFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP 1197
Cdd:TIGR01193 480 SYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEP 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1198 VLFACSIMDNIKYGDNTKeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLD 1277
Cdd:TIGR01193 558 YIFSGSILENLLLGAKEN-VSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
490
....*....|...
gi 2462578034 1278 EATSALDTESEKQ 1290
Cdd:TIGR01193 637 ESTSNLDTITEKK 649
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1126-1287 |
4.67e-33 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 127.64 E-value: 4.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSI 1204
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYG-----DNTKEIPmERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:cd03259 90 AENIAFGlklrgVPKAEIR-ARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLDEP 157
|
....*...
gi 2462578034 1280 TSALDTES 1287
Cdd:cd03259 158 LSALDAKL 165
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1125-1290 |
4.85e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 136.51 E-value: 4.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1125 PDSQVLNG-LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACS 1203
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1204 IMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1283
Cdd:PRK11174 439 LRDNVLLGN--PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
....*..
gi 2462578034 1284 DTESEKQ 1290
Cdd:PRK11174 517 DAHSEQL 523
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
454-680 |
5.50e-33 |
|
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: 135.42 E-value: 5.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGHDIRSLNIQWLRD 530
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEP--VLFSTTIAENIRYGRE--DATMEDIVQAAKEANAYNFIMDL----PQQFdtlvgegggqmSGGQKQRVA 602
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVLELLEAVGLERRldryPHQL-----------SGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLE 679
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 2462578034 680 R 680
Cdd:COG1123 233 A 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1112-1290 |
6.18e-33 |
|
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: 125.89 E-value: 6.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQfLRSNIG 1191
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVLFACSIMDNIkygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqGSQLSRGEKQRIAIARAIVRDP 1271
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170
....*....|....*....
gi 2462578034 1272 KILLLDEATSALDTESEKQ 1290
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQ 136
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
173-424 |
6.32e-33 |
|
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: 129.59 E-value: 6.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 173 IKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA 252
Cdd:cd07346 39 LWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 253 LFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEK 332
Cdd:cd07346 119 QLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 333 REVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV------QIFLSVIVGALN 406
Cdd:cd07346 199 REIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQ-GSLTIGELVaflaylGMLFGPIQRLAN 277
|
250
....*....|....*...
gi 2462578034 407 LGNaspcleAFATGRAAA 424
Cdd:cd07346 278 LYN------QLQQALASL 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
180-404 |
8.94e-33 |
|
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: 129.14 E-value: 8.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18576 43 LGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYE 339
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 340 KNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQ-IFLSVIVGA 404
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLA-GELTAGDLVAfLLYTLFIAG 267
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
454-677 |
1.18e-32 |
|
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: 127.30 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL---NIQWLRD 530
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFS-TTIAENIRYGREDA-----------TMEDIVQAAKEANAYNFIMDLPQQFDTLvgegggqmSGGQK 598
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRrstwrslfglfPKEEKQRALAALERVGLLDKAYQRADQL--------SGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 599 QRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHE 675
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 2462578034 676 EL 677
Cdd:cd03256 231 EL 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1112-1290 |
1.47e-32 |
|
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: 126.68 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1191
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPV--LFACSIMDNIKYG----DNTKEIPMERVIAAAKQAQLHDFvmslpekYETNVgsqgSQLSRGEKQRIAIAR 1265
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlGLPREEIRERVEEALELVGLEHL-------ADRPP----HELSGGQKQRVAIAG 147
|
170 180
....*....|....*....|....*
gi 2462578034 1266 AIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRE 172
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
454-680 |
2.11e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.83 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIG 533
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFS-TTIAENIRYG----------REDATME--DIVQAAKEANAYnfIMDLP---QQfdtlvgegggqmsggq 597
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrmrgvpkaeIRARVAEllELVGLEGLADRY--PHQLSggqQQ---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 598 kqRVAIARALIRNPKILLLDMATSALDNES-EAMVQEvLSKIQH--GHTIISVAHRLS---TVraADTIIGFEHGTAVER 671
Cdd:COG3842 143 --RVALARALAPEPRVLLLDEPLSALDAKLrEEMREE-LRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQV 217
|
....*....
gi 2462578034 672 GTHEELLER 680
Cdd:COG3842 218 GTPEEIYER 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
454-649 |
7.39e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.59 E-value: 7.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniqwLRDQI 532
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLFS-TTIAENIRYGREDATM-----EDIVQAAKE-------ANAYnfimdlP-------QQfdtlvgegggq 592
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVpkaerRERARELLElvglagfEDAY------PhqlsggmRQ----------- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 593 msggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 649
Cdd:COG1116 146 -------RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH 197
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1114-1290 |
8.90e-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: 123.73 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1114 FVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIV 1193
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1194 SQEP--VLFACSIMDNIKYG-----DNTKEIPmERVIAAAKQAQLHDFvmslpEKYETnvgsqgSQLSRGEKQRIAIARA 1266
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGlenlgLPEEEIE-ERVEEALELVGLEGL-----RDRSP------FTLSGGQKQRVAIAGV 148
|
170 180
....*....|....*....|....
gi 2462578034 1267 IVRDPKILLLDEATSALDTESEKQ 1290
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRE 172
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1126-1286 |
1.48e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 123.95 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLF 1200
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1201 A-CSIMDNIKYG---------DNTKEIPME---RViaaakqaQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAI 1267
Cdd:COG1126 90 PhLTVLENVTLApikvkkmskAEAEERAMElleRV-------GLADKADAYP-----------AQLSGGQQQRVAIARAL 151
|
170
....*....|....*....
gi 2462578034 1268 VRDPKILLLDEATSALDTE 1286
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPE 170
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
199-393 |
1.82e-31 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 125.70 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 199 IAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLV 278
Cdd:cd18573 67 IAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 279 IISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGF 358
Cdd:cd18573 147 MLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGL 226
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462578034 359 F---TGFVWCLIFLCyalAFWYGSTLVLdEGEYTPGTL 393
Cdd:cd18573 227 FfgsTGFSGNLSLLS---VLYYGGSLVA-SGELTVGDL 260
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
789-1046 |
2.07e-31 |
|
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: 125.36 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTFsIPDKeeQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 868
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV-IPAG--DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 869 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 948
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 949 GATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFI 1028
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250
....*....|....*...
gi 2462578034 1029 ANSASYRYGGYLISNEGL 1046
Cdd:cd07346 236 GTALVLLYGGYLVLQGSL 253
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
454-666 |
2.10e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.01 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFS-TTIAENI----------------RYGREDatmediVQAAKEANAynfIMDLP-------------- 579
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagrlgrtstwrsllgLFPPED------RERALEALE---RVGLAdkayqradqlsggq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 580 QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA- 656
Cdd:COG3638 152 QQ------------------RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRy 213
|
250
....*....|
gi 2462578034 657 ADTIIGFEHG 666
Cdd:COG3638 214 ADRIIGLRDG 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
454-681 |
3.15e-31 |
|
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: 124.08 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL-NIQWLRDQI 532
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEP--VLFSTTIAENIRYGRED-----ATMEDIVQ-AAKEANAYNFIMDLPQ-------Qfdtlvgegggqmsggq 597
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgvprEEMRKRVDeALKLVGMEDFRDREPHllsggqkQ---------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 598 kqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHE 675
Cdd:TIGR04520 144 --RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
....*.
gi 2462578034 676 ELLERK 681
Cdd:TIGR04520 222 EIFSQV 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
454-680 |
3.17e-31 |
|
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: 123.37 E-value: 3.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPE-VKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQI 532
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVL-----FS--TTIAENIRYGREDATMEDIVQAAKEanaynfiMDLP---------------QQfdtlvgegg 590
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRIHGLPDREERIAELLEQ-------VGLPpsfldryphqlsggqRQ--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 591 gqmsggqkqRVAIARALIRNPKILLLDMATSALDneseAMVQ----EVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGF 663
Cdd:COG1124 146 ---------RVAIARALILEPELLLLDEPTSALD----VSVQaeilNLLKDLReeRGLTYLFVSHDLAVVaHLCDRVAVM 212
|
250
....*....|....*..
gi 2462578034 664 EHGTAVERGTHEELLER 680
Cdd:COG1124 213 QNGRIVEELTVADLLAG 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
454-678 |
4.96e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 125.58 E-value: 4.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD-- 530
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 -QIGIVEQEPVLFST-TIAENIRYGREDATM--EDIVQAAKE----------ANAYnfimdlP-------QQfdtlvgeg 589
Cdd:COG1135 82 rKIGMIFQHFNLLSSrTVAENVALPLEIAGVpkAEIRKRVAEllelvglsdkADAY------PsqlsggqKQ-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 590 ggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHG 666
Cdd:COG1135 148 ----------RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInrELGLTIVLITHEMDVVRRiCDRVAVLENG 217
|
250
....*....|..
gi 2462578034 667 TAVERGTHEELL 678
Cdd:COG1135 218 RIVEQGPVLDVF 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
147-694 |
7.33e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 132.79 E-value: 7.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 147 VWTNSSLNQNMtngtRCGLLNIESEMIKFASyyagiaVAVLITGyiqiCFWVIAAARQIQK-MRKFYFRRIMRMEIGWFD 225
Cdd:PLN03232 937 IWTDQSTPKSY----SPGFYIVVYALLGFGQ------VAVTFTN----SFWLISSSLHAAKrLHDAMLNSILRAPMLFFH 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 226 CNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLgffRGWKLTLVIISVSPLIGIGAATIGLSVSkfTDYEL 305
Cdd:PLN03232 1003 TNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFAL---IGTVSTISLWAIMPLLILFYAAYLYYQS--TSREV 1077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 306 K---------AYAKAGVvADEVISSMRTVAAFGGEKREVERY-EKNLVF------AQRW-GIRKGIVMGFftgfvwcLIF 368
Cdd:PLN03232 1078 RrldsvtrspIYAQFGE-ALNGLSSIRAYKAYDRMAKINGKSmDNNIRFtlantsSNRWlTIRLETLGGV-------MIW 1149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 369 LCYALA-FWYGSTlvldEGEYTPGTLVQIFLSVIVgalnlgNASPCLEAFATGRAAATSIFETIDR-KPIIDCMSE--DG 444
Cdd:PLN03232 1150 LTATFAvLRNGNA----ENQAGFASTMGLLLSYTL------NITTLLSGVLRQASKAENSLNSVERvGNYIDLPSEatAI 1219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 445 YKLDR------IKGEIEFHNVTFHYpsRPEVK-ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG 517
Cdd:PLN03232 1220 IENNRpvsgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD 1297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 518 HDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGRE--DAtmeDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSG 595
Cdd:PLN03232 1298 CDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEhnDA---DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSV 1374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 596 GQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHE 675
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQ 1454
|
570 580
....*....|....*....|
gi 2462578034 676 ELLERKG-VYFTLVtlQSQG 694
Cdd:PLN03232 1455 ELLSRDTsAFFRMV--HSTG 1472
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
454-677 |
7.74e-31 |
|
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: 121.84 E-value: 7.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLF-STTIAENIRYG-RE-----DATMEDIVQAAKEAnaynfiMDLPQQFDTLVgeggGQMSGGQKQRVAI 603
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPlREhtrlsEEEIREIVLEKLEA------VGLRGAEDLYP----AELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 677
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1128-1284 |
1.01e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 121.71 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQfLRSNIGIVSQEPVLFA-CSIMD 1206
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVPQEPALYPdLTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1207 NIK-----YGDNTKEIPmERVIAAAKQAQLHDFvmslpekYETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATS 1281
Cdd:COG1131 93 NLRffarlYGLPRKEAR-ERIDELLELFGLTDA-------ADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
...
gi 2462578034 1282 ALD 1284
Cdd:COG1131 161 GLD 163
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1111-1284 |
1.06e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 122.51 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1111 KIDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFLRSN 1189
Cdd:COG1116 7 ALELRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1190 IGIVSQEPVLFA-CSIMDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIA 1264
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKaerrERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIA 150
|
170 180
....*....|....*....|
gi 2462578034 1265 RAIVRDPKILLLDEATSALD 1284
Cdd:COG1116 151 RALANDPEVLLMDEPFGALD 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1112-1287 |
1.12e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.93 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN---VQFLRS 1188
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 NIGIVSQE-PVLFACSIMDNIKY-----GDNTKEIpMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIA 1262
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEI-RRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180
....*....|....*....|....*
gi 2462578034 1263 IARAIVRDPKILLLDEATSALDTES 1287
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPET 172
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1112-1284 |
1.34e-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: 128.10 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDS--QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---SKKVNVQFL 1186
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1187 RSNIGIVSQEPV--LFAC-SIMDNI-----KYGDNTKEIPMERVIAAAKQAQLH-DFVMSLPekyetnvgsqgSQLSRGE 1257
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIaeplrLHGLLSRAERRERVAELLERVGLPpDLADRYP-----------HELSGGQ 409
|
170 180
....*....|....*....|....*..
gi 2462578034 1258 KQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALD 436
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
147-687 |
1.99e-30 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 131.22 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 147 VWTNSSLNQNMTNGTRcgllniESEMIKFASYYA-GIAVAVLITGY-IQICFWVIAAARQIQKMrkfYFRRIMRMEIGWF 224
Cdd:TIGR00957 986 YWLSLWTDDPMVNGTQ------NNTSLRLSVYGAlGILQGFAVFGYsMAVSIGGIQASRVLHQD---LLHNKLRSPMSFF 1056
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 225 DCNSVGELNTRFSDDINKINDAIADQMALFIQrmtsticgfllGFFRGWKLTLVIISVSPLIGIGAATIGLS---VSKF- 300
Cdd:TIGR00957 1057 ERTPSGNLVNRFSKELDTVDSMIPPVIKMFMG-----------SLFNVIGALIVILLATPIAAVIIPPLGLLyffVQRFy 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 301 --TDYELK---AYAKAGVVA--DEVISSMRTVAAFGGEKR-------EVERYEKNL---VFAQRW-GIRKGIVMGfftgf 362
Cdd:TIGR00957 1126 vaSSRQLKrleSVSRSPVYShfNETLLGVSVIRAFEEQERfihqsdlKVDENQKAYypsIVANRWlAVRLECVGN----- 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 363 vwCLIFLCYALAfwygstlVLDEGEYTPGtLVQIFLSV---IVGALN-LGNASPCLEA--FATGRAAATSIFETIDRKPI 436
Cdd:TIGR00957 1201 --CIVLFAALFA-------VISRHSLSAG-LVGLSVSYslqVTFYLNwLVRMSSEMETniVAVERLKEYSETEKEAPWQI 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 437 IDCMSEDGYKLdriKGEIEFHNVTFHYpsRPEVK-ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTV 515
Cdd:TIGR00957 1271 QETAPPSGWPP---RGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 516 DGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENI----RYGREDATMedivqAAKEANAYNFIMDLPQQFDTLVGEGGG 591
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEVWW-----ALELAHLKTFVSALPDKLDHECAEGGE 1420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 592 QMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVER 671
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
570
....*....|....*.
gi 2462578034 672 GTHEELLERKGVYFTL 687
Cdd:TIGR00957 1501 GAPSNLLQQRGIFYSM 1516
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
452-688 |
2.49e-30 |
|
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: 121.17 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYPS--RPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLR 529
Cdd:cd03288 18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 530 DQIGIVEQEPVLFSTTIAENIRYGREdATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIR 609
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 610 NPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERK-GVYFTLV 688
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1112-1286 |
4.75e-30 |
|
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: 119.05 E-value: 4.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDS---KKVNVQFLRS 1188
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 NIGIVSQE-PVLFACSIMDNIKY-----GDNTKEIPmERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIA 1262
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFalevtGVPPREIR-KRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVA 146
|
170 180
....*....|....*....|....
gi 2462578034 1263 IARAIVRDPKILLLDEATSALDTE 1286
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPD 170
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1120-1290 |
5.31e-30 |
|
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: 119.15 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL---RSNIGIVSQ 1195
Cdd:cd03257 10 SFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1196 EPvlFAC-----SIMDNIK-----YGDNTKEipmerviAAAKQAQLHDFV-MSLPEKYETnvgSQGSQLSRGEKQRIAIA 1264
Cdd:cd03257 90 DP--MSSlnprmTIGEQIAeplriHGKLSKK-------EARKEAVLLLLVgVGLPEEVLN---RYPHELSGGQRQRVAIA 157
|
170 180
....*....|....*....|....*.
gi 2462578034 1265 RAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQ 183
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
454-677 |
5.78e-30 |
|
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: 119.71 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFS-TTIAENIRYGREDA-----------TMEDIvQAAKEANAYNFIMDLP-QQFDTLvgegggqmSGGQ 597
Cdd:TIGR02315 80 RIGMIFQHYNLIErLTVLENVLHGRLGYkptwrsllgrfSEEDK-ERALSALERVGLADKAyQRADQL--------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 598 KQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTH 674
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkEDGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAP 230
|
...
gi 2462578034 675 EEL 677
Cdd:TIGR02315 231 SEL 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
454-679 |
6.13e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 6.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniqwLRDQIG 533
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVL---FSTTIAENI------------RYGREDatmEDIVQAA-KEANAYNF----IMDLP---QQfdtlvgegg 590
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgrygrrglfrRPSRAD---REAVDEAlERVGLEDLadrpIGELSggqQQ--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 591 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTII-----GF 663
Cdd:COG1121 147 ---------RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLllnrgLV 217
|
250
....*....|....*.
gi 2462578034 664 EHGTAVERGTHEELLE 679
Cdd:COG1121 218 AHGPPEEVLTPENLSR 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
440-680 |
6.87e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.76 E-value: 6.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 440 MSEDGYKLDRIkgeIEFHNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYD--P---CEGMVT 514
Cdd:COG1117 1 MTAPASTLEPK---IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 515 VDGHDI--RSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYG------REDATMEDIVQAA-KEA------------NAyn 573
Cdd:COG1117 75 LDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlRKAalwdevkdrlkkSA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 574 fiMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR 650
Cdd:COG1117 153 --LGLSggqQQ------------------RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|.
gi 2462578034 651 LS-TVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:COG1117 213 MQqAARVSDYTAFFYLGELVEFGPTEQIFTN 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1112-1290 |
6.96e-30 |
|
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: 119.22 E-value: 6.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQ---LLERfydPDQGKVMIDGHDSKKVN---VQ 1184
Cdd:cd03258 2 IELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1185 FLRSNIGIVSQEPVLFAC-SIMDNIKY-----GDNTKEIPmERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEK 1258
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIE-ERVLELLELVGLEDKADAYP-----------AQLSGGQK 146
|
170 180 190
....*....|....*....|....*....|..
gi 2462578034 1259 QRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQS 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1119-1289 |
7.15e-30 |
|
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: 116.93 E-value: 7.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYP--SRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQE 1196
Cdd:cd03246 8 FRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 PVLFACSIMDNIkygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170
....*....|...
gi 2462578034 1277 DEATSALDTESEK 1289
Cdd:cd03246 121 DEPNSHLDVEGER 133
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
455-672 |
7.42e-30 |
|
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: 117.15 E-value: 7.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 455 EFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGI 534
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 535 VEqepvlfsttiaenirygredatmedivQAAKEANAYNFIMdlpQQFDTLvgegggqmsggqkqRVAIARALIRNPKIL 614
Cdd:cd03214 78 VP---------------------------QALELLGLAHLAD---RPFNELsgg--------erqRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 615 LLDMATSALD--NESEAMvqEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERG 672
Cdd:cd03214 120 LLDEPTSHLDiaHQIELL--ELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
454-666 |
1.08e-29 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 118.02 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI--RSLNIQWLRDQ 531
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFS-TTIAENIRYG--------REDAT---ME--DIVQAAKEANAYnfimdlP-------QQfdtlvgegg 590
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLApikvkgmsKAEAEeraLEllEKVGLADKADAY------PaqlsggqQQ--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 591 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKI----QHGHTIISVAHRLSTVR-AADTIIGFEH 665
Cdd:cd03262 143 ---------RVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVMkdlaEEGMTMVVVTHEMGFAReVADRVIFMDD 210
|
.
gi 2462578034 666 G 666
Cdd:cd03262 211 G 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1112-1290 |
1.38e-29 |
|
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: 117.59 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHDSKKVN----V 1183
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSekelA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1184 QFLRSNIGIVSQE----PVLfacSIMDNIkygdntkEIPMErvIAAAKQAQLHDFVMSLPEKyetnVGSQG------SQL 1253
Cdd:cd03255 78 AFRRRHIGFVFQSfnllPDL---TALENV-------ELPLL--LAGVPKKERRERAEELLER----VGLGDrlnhypSEL 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462578034 1254 SRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKE 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
454-661 |
1.44e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 115.96 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRdQIG 533
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST-TIAENIRY--GredatMedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRN 610
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKLsgG-----M--------------------KQ------------------RLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 611 PKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTII 661
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAeRLCDRVA 166
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1123-1287 |
1.92e-29 |
|
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: 116.13 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG--HDSKKVNVQFLRSNIGIVSQEPVLF 1200
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1201 A-CSIMDNIKYGdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:cd03229 89 PhLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
....*...
gi 2462578034 1280 TSALDTES 1287
Cdd:cd03229 128 TSALDPIT 135
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
452-694 |
3.42e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 127.16 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYpsRPEVK-ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 530
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFSTTIAENIRYGRE--DAtmeDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALI 608
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEhnDA---DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 609 RNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLV 688
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
....*.
gi 2462578034 689 tLQSQG 694
Cdd:PLN03130 1471 -VQSTG 1475
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1114-1290 |
3.72e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 114.26 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1114 FVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIV 1193
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1194 sqepvlfacsimdnikygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKI 1273
Cdd:cd00267 79 ---------------------------------------------------------PQLSGGQRQRVALARALLLNPDL 101
|
170
....*....|....*..
gi 2462578034 1274 LLLDEATSALDTESEKQ 1290
Cdd:cd00267 102 LLLDEPTSGLDPASRER 118
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
454-681 |
6.32e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.40 E-value: 6.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEP---VLFSTT---IA---ENIRYGREDatMEDIV-QAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 603
Cdd:PRK13632 87 IIFQNPdnqFIGATVeddIAfglENKKVPPKK--MKDIIdDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
455-661 |
8.42e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 115.32 E-value: 8.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 455 EFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdirsLNIQWLRDQIGI 534
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 535 VEQEPVL---FSTTIAENI------------RYGREDatMEDIVQAAKEANAYNFImdlPQQFDTLvgegggqmSGGQKQ 599
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmglyghkglfrRLSKAD--KAKVDEALERVGLSELA---DRQIGEL--------SGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTII 661
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVL 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
454-666 |
1.54e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 114.81 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFST-TIAENIRYGRE--DATMEDIVQAAKEANAynfIMDLPQQFDTLvgegGGQMSGGQKQRVAIARAL 607
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 608 IRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHG 666
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVdTTRHRVIALERG 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1112-1287 |
1.55e-28 |
|
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: 115.34 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFlRSNIG 1191
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVLFA-CSIMDNIKY-----GDNTKEIPmERVIAAAKQAQLHDFvmsLPEKYETnvgsqgsqLSRGEKQRIAIAR 1265
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYfaelyGLFDEELK-KRIEELIELLGLEEF---LDRRVGE--------LSTGMKKKVALAR 145
|
170 180
....*....|....*....|..
gi 2462578034 1266 AIVRDPKILLLDEATSALDTES 1287
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMA 167
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1126-1284 |
1.99e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSI 1204
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPhLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:COG3842 95 AENVAFGLRMRGVPKaeirARVAELLELVGLEGLADRYP-----------HQLSGGQQQRVALARALAPEPRVLLLDEPL 163
|
....
gi 2462578034 1281 SALD 1284
Cdd:COG3842 164 SALD 167
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1126-1286 |
3.64e-28 |
|
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: 113.39 E-value: 3.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGH--DSKKVNVQFLRSNIGIVSQEPVLF 1200
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLklTDDKKNINELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1201 A-CSIMDNIKYGD-NTKEIPMERVIAAAKQA----QLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKIL 1274
Cdd:cd03262 89 PhLTVLENITLAPiKVKGMSKAEAEERALELlekvGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVM 157
|
170
....*....|..
gi 2462578034 1275 LLDEATSALDTE 1286
Cdd:cd03262 158 LFDEPTSALDPE 169
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1126-1284 |
3.67e-28 |
|
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: 114.26 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSkkVNVQFLRSNIGIVSQEPVLFA-CSI 1204
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:cd03300 90 FENIAFGLRLKKLPKaeikERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
....
gi 2462578034 1281 SALD 1284
Cdd:cd03300 159 GALD 162
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
470-677 |
5.79e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.10 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 470 KILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQW--LRDQIGIVEQEPVLF 542
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 STTIAENIRYG------REDATMEDIVQAA-KEANAYNFIMDlpQQFDTLVGEGGGQMSggqkqRVAIARALIRNPKILL 615
Cdd:PRK14239 99 PMSIYENVVYGlrlkgiKDKQVLDEAVEKSlKGASIWDEVKD--RLHDSALGLSGGQQQ-----RVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 616 LDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEEL 677
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1112-1284 |
7.74e-28 |
|
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: 113.55 E-value: 7.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1191
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVLFA-CSIMDNIKYGDNTKEIPMERVIAAAKQAqLHDfvMSLPEkyETNVGSQGSQLSRGEKQRIAIARAIVRD 1270
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIALVPKLLKWPKEKIRERADEL-LAL--VGLDP--AEFADRYPHELSGGQQQRVGVARALAAD 153
|
170
....*....|....
gi 2462578034 1271 PKILLLDEATSALD 1284
Cdd:cd03295 154 PPLLLMDEPFGALD 167
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
804-1041 |
1.70e-27 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 113.88 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 804 PLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDd 883
Cdd:cd18780 16 PYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 884 lRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRD 963
Cdd:cd18780 95 -VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 964 KQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFcfaFAQCIMFIANSA---SYRYGGYL 1040
Cdd:cd18780 174 QDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGG---FNGFMGAAAQLAivlVLWYGGRL 250
|
.
gi 2462578034 1041 I 1041
Cdd:cd18780 251 V 251
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1126-1290 |
1.92e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.81 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSI 1204
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPhMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:PRK09452 104 FENVAFGLRMQKTPaaeiTPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170
....*....|
gi 2462578034 1281 SALDTESEKQ 1290
Cdd:PRK09452 173 SALDYKLRKQ 182
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1128-1284 |
1.96e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.17 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-ACSIMD 1206
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYpHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1207 NIKYG-----DNTKEIpMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1281
Cdd:COG3839 95 NIAFPlklrkVPKAEI-DRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
...
gi 2462578034 1282 ALD 1284
Cdd:COG3839 163 NLD 165
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1126-1287 |
2.74e-27 |
|
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: 109.41 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPVLFA-CSI 1204
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYEnLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYgdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqlSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:cd03230 91 RENLKL-------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
...
gi 2462578034 1285 TES 1287
Cdd:cd03230 128 PES 130
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1119-1284 |
2.98e-27 |
|
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: 112.06 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPV 1198
Cdd:COG1120 9 VGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 L-FACSIMDNIKYG---------DNTKEipMERVIAAA-KQAQLHDFVmslpekyETNVgsqgSQLSRGEKQRIAIARAI 1267
Cdd:COG1120 86 ApFGLTVRELVALGryphlglfgRPSAE--DREAVEEAlERTGLEHLA-------DRPV----DELSGGERQRVLIARAL 152
|
170
....*....|....*..
gi 2462578034 1268 VRDPKILLLDEATSALD 1284
Cdd:COG1120 153 AQEPPLLLLDEPTSHLD 169
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1120-1284 |
8.08e-27 |
|
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: 110.66 E-value: 8.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSRPDSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP- 1197
Cdd:COG1124 10 SYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1198 ---------------VLFACSIMDNikygdntkeipMERVIAAAKQAQLHDfvmSLPEKYetnvgsqGSQLSRGEKQRIA 1262
Cdd:COG1124 90 aslhprhtvdrilaePLRIHGLPDR-----------EERIAELLEQVGLPP---SFLDRY-------PHQLSGGQRQRVA 148
|
170 180
....*....|....*....|..
gi 2462578034 1263 IARAIVRDPKILLLDEATSALD 1284
Cdd:COG1124 149 IARALILEPELLLLDEPTSALD 170
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
182-410 |
1.17e-26 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 111.63 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 182 IAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIqRMTST 261
Cdd:cd18784 45 LAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFL-RSLVK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 262 ICGFLLGFFR-GWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEK 340
Cdd:cd18784 124 AIGVIVFMFKlSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSE 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 341 NLVFAQRWGIRKGIVMGfftGFVWCLIFLCYALA---FWYGSTLVLdEGEYTPGTLVqiflSVIVGALNLGNA 410
Cdd:cd18784 204 KLKDTYKLKIKEALAYG---GYVWSNELTELALTvstLYYGGHLVI-TGQISGGNLI----SFILYQLELGSC 268
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1106-1284 |
1.59e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.47 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1106 DNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF 1185
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIP---MERVIA-AAKQAQLHDFVMSLPEKyetnvgsqgsqLSRGEKQ 1259
Cdd:PRK13632 81 IRKKIGIIFQNPdnQFIGATVEDDIAFGLENKKVPpkkMKDIIDdLAKKVGMEDYLDKEPQN-----------LSGGQKQ 149
|
170 180
....*....|....*....|....*
gi 2462578034 1260 RIAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLD 174
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
454-680 |
1.63e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.80 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR--SLNIQWLRDQ 531
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFSTTIA-ENIRYG--------REDA-----TMEDIVQAAKEANAYNFIMDLPQQfdtlvgegggqmsggq 597
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGplrvrgasKEEAekqarELLAKVGLAERAHHYPSELSGGQQ---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 598 kQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQ----HGHTIISVAHRLSTVR-AADTIIGFEHGTAVERG 672
Cdd:PRK09493 143 -QRVAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKVMQdlaeEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDG 218
|
....*...
gi 2462578034 673 THEELLER 680
Cdd:PRK09493 219 DPQVLIKN 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1120-1286 |
1.67e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.09 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHDSKKVNVQFL---RSNIGI 1192
Cdd:COG1135 10 TFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELraaRRKIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1193 VSQEPVLF-ACSIMDNIKY-----GDNTKEIPmERViaaakqAQLHDFVmSLPEK---YEtnvgsqgSQLSRGEKQRIAI 1263
Cdd:COG1135 87 IFQHFNLLsSRTVAENVALpleiaGVPKAEIR-KRV------AELLELV-GLSDKadaYP-------SQLSGGQKQRVGI 151
|
170 180
....*....|....*....|...
gi 2462578034 1264 ARAIVRDPKILLLDEATSALDTE 1286
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPE 174
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
453-653 |
3.09e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 107.25 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 453 EIEFHNVTF---HYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLI--QRFYDPCEGMVTVDGHDIRslnIQW 527
Cdd:cd03213 3 TLSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 528 LRDQIGIVEQEPVLFST-TIAENIRYgredatmedivqAAK-------EAnaynfimdlpqqfdtlvgegggqmsggqkQ 599
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMF------------AAKlrglsggER-----------------------------K 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLST 653
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSS 173
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
823-1047 |
4.08e-26 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 109.94 E-value: 4.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 823 EEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQV 902
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 903 qgaaGSQIGMIVNSFTN----VTVAMIIAFSFSWKLSLVILCFFPFLALS----GATQTRMltgfASRDKQALEMVGQIT 974
Cdd:cd18572 107 ----SDPLSTNLNVFLRnlvqLVGGLAFMFSLSWRLTLLAFITVPVIALItkvyGRYYRKL----SKEIQDALAEANQVA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 975 NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLH 1047
Cdd:cd18572 179 EEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMS 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
472-680 |
5.60e-26 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 107.81 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIGIVEQEPVLF-STTIAENI 550
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 551 RYGREdatMEDIVQAAKEANAYNFIMDLpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAM 630
Cdd:cd03299 93 AYGLK---KRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 631 VQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLER 680
Cdd:cd03299 168 LREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
454-680 |
5.90e-26 |
|
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: 107.71 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrsLNIQWLRDQIG 533
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFS-TTIAENIRYG------------REDATMEDIVQAAKEANAYNFIMDLPQQfdtlvgegggqmsggqkQR 600
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrlkklpkaeikERVAEALDLVQLEGYANRKPSQLSGGQQ-----------------QR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 601 VAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 677
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
...
gi 2462578034 678 LER 680
Cdd:cd03300 219 YEE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1112-1290 |
8.53e-26 |
|
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: 113.46 E-value: 8.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQFLRS 1188
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 NIGIVSQEP--VLFACSIMDNI----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIA 1262
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIaealENLGLSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVA 152
|
170 180
....*....|....*....|....*...
gi 2462578034 1263 IARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAE 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1112-1284 |
1.19e-25 |
|
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: 106.82 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV---QFLRS 1188
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 NIGIVSQEPVLF-ACSIMDNI-----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIA 1262
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVafplrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180
....*....|....*....|..
gi 2462578034 1263 IARAIVRDPKILLLDEATSALD 1284
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLD 168
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
454-673 |
1.30e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.89 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYP-SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL---R 529
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 530 DQIGIVEQE-PVLFSTTIAENIRYGREDATME------------DIVQAAKEANAYnfimdlPQQFdtlvgegggqmSGG 596
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALPLELAGTPkaeikarvtellELVGLSDKADRY------PAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 597 QKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGT 673
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
472-679 |
1.30e-25 |
|
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: 107.73 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL----RDQIGIVEQEPVLF-STTI 546
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 547 AENIRYG----------REDATMEDIVQAAKEANAYNFIMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03294 120 LENVAFGlevqgvpraeREERAAEALELVGLEGWEHKYPDELSggmQQ------------------RVGLARALAVDPDI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 614 LLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1125-1290 |
1.33e-25 |
|
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: 107.04 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1125 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CS 1203
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1204 IMDNIKYGDNTKEIPmERVIAAAKQAQLHDFVM-----SLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:cd03296 91 VFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLKlvqldWLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170
....*....|..
gi 2462578034 1279 ATSALDTESEKQ 1290
Cdd:cd03296 163 PFGALDAKVRKE 174
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
454-679 |
1.65e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.53 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEP--VLFSTTIAENIRYGREDAT-----MEDIV-QAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIAR 605
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAvpydeMHRRVsEALKQVDMLERADYEPNALS-----------GGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 606 ALIRNPKILLLDMATSALDNESEA----MVQEVlsKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
453-680 |
1.67e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.47 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 453 EIEFHNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniqWL--RD 530
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLppRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 -QIGIVEQEPVLF-STTIAENIRYG-----------REDAtME--DIVQAAKEANAYnfimdlP-------QQfdtlvge 588
Cdd:COG1118 75 rRVGFVFQHYALFpHMTVAENIAFGlrvrppskaeiRARV-EEllELVQLEGLADRY------PsqlsggqRQ------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 589 gggqmsggqkqRVAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSKIqhGHTIISVAH-RLSTVRAADTIIGF 663
Cdd:COG1118 141 -----------RVALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVM 207
|
250
....*....|....*..
gi 2462578034 664 EHGTAVERGTHEELLER 680
Cdd:COG1118 208 NQGRIEQVGTPDEVYDR 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
454-680 |
3.00e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.61 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkiLNdLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlrDQ-- 531
Cdd:COG3840 2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFS-TTIAENI--------RYGREDAtmEDIVQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsg 595
Cdd:COG3840 73 VSMLFQENNLFPhLTVAQNIglglrpglKLTAEQR--AQVEQALERVGLAGLLDRLPgqlsggqRQ-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 596 gqkqRVAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSkiQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 670
Cdd:COG3840 137 ----RVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAaRIADRVLLVADGRIAA 210
|
250
....*....|
gi 2462578034 671 RGTHEELLER 680
Cdd:COG3840 211 DGPTAALLDG 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1112-1285 |
3.62e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.70 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGHDSKkVNVQFLRS 1188
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLF-TNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 NIGIVSQEPVLFA-CSIMDNIKYGdntkeIPMERVIAAAKQAQlhdfVMSLPEKyetnVGSQG------SQLSRGEKQRI 1261
Cdd:COG1118 76 RVGFVFQHYALFPhMTVAENIAFG-----LRVRPPSKAEIRAR----VEELLEL----VQLEGladrypSQLSGGQRQRV 142
|
170 180
....*....|....*....|....
gi 2462578034 1262 AIARAIVRDPKILLLDEATSALDT 1285
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDA 166
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1129-1285 |
4.65e-25 |
|
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: 105.11 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIMDN 1207
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1208 IKYG-----DNTKEIPmERVIAAAKQAQLHDFvmsLPEKYETnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSA 1282
Cdd:cd03299 92 IAYGlkkrkVDKKEIE-RKVLEIAEMLGIDHL---LNRKPET--------LSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
...
gi 2462578034 1283 LDT 1285
Cdd:cd03299 160 LDV 162
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
454-676 |
4.75e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.67 E-value: 4.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHY-PSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI--RSLNIQWLR 529
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 530 DQIGIVEQEP--VLFSTTIAENIRYGREDATMED--IVQAAKEAnaynfiMDLPQ-QFDTLVGEGGGQMSGGQKQRVAIA 604
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEeeIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 605 RALIRNPKILLLDMATSALDNESEamvQEVLSKIQHGH-----TIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 676
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGR---DEILNKIKELHkeynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1110-1284 |
5.94e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.29 E-value: 5.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1110 GKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 1188
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 NIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIV 1268
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170
....*....|....*.
gi 2462578034 1269 RDPKILLLDEATSALD 1284
Cdd:PLN03130 1391 RRSKILVLDEATAAVD 1406
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1126-1284 |
8.29e-25 |
|
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: 104.68 E-value: 8.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV---QFLRSNIGIVSQEPVLF-A 1201
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFdS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNI-----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:COG1127 97 LTVFENVafplrEHTDLSEAEIRELVLEKLELVGLPGAADKMP-----------SELSGGMRKRVALARALALDPEILLY 165
|
....*...
gi 2462578034 1277 DEATSALD 1284
Cdd:COG1127 166 DEPTAGLD 173
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1129-1284 |
8.90e-25 |
|
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: 103.87 E-value: 8.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkVN-VQFLRSNIGIVSQEPVLFA-CSIMD 1206
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD---VTdLPPKDRDIAMVFQNYALYPhMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1207 NIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1282
Cdd:cd03301 92 NIAFGLKLRKVPKdeidERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
..
gi 2462578034 1283 LD 1284
Cdd:cd03301 161 LD 162
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
793-1043 |
9.22e-25 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 106.06 E-value: 9.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 793 SVGAAVNGTVtPlyaFLFSQILGTFS--IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGF 870
Cdd:cd18573 6 LVSSAVTMSV-P---FAIGKLIDVASkeSGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 871 RAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGA 950
Cdd:cd18573 82 KSILRQDAAFFD--KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 951 TQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQcimFIAN 1030
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTG---FSGN 236
|
250
....*....|....*.
gi 2462578034 1031 SASYR---YGGYLISN 1043
Cdd:cd18573 237 LSLLSvlyYGGSLVAS 252
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1112-1286 |
1.08e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.58 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1191
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEP--VLFACSIMDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIAR 1265
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHeemkERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180
....*....|....*....|.
gi 2462578034 1266 AIVRDPKILLLDEATSALDTE 1286
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPE 174
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1112-1290 |
1.46e-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: 102.93 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDSQ--VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ErfYDPDQGKVmidghdskkvnvqFLR 1187
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1188 SNIGIVSQEPVLFACSIMDNIKYGdntKEIPMERVIAAAKQAQLH-DFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARA 1266
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFG---KPFDEERYEKVIKACALEpDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180
....*....|....*....|....
gi 2462578034 1267 IVRDPKILLLDEATSALDTESEKQ 1290
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRH 165
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
454-679 |
1.72e-24 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 103.28 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN-IQWLRDQI 532
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLFST-TIAENIRYG-------REDATMEDIV-----------QAAK-----EanaynfimdlpQQFdtlvge 588
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGayarrraKRKARLERVYelfprlkerrkQLAGtlsggE-----------QQM------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 589 gggqmsggqkqrVAIARALIRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLSTVRA-ADTIIGF 663
Cdd:cd03224 141 ------------LAIARALMSRPKLLLLDEPSEGL---APKIVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVL 205
|
250
....*....|....*.
gi 2462578034 664 EHGTAVERGTHEELLE 679
Cdd:cd03224 206 ERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
454-680 |
2.71e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.50 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEvKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGHDIRSLNIQWLRD 530
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEP--VLFSTTIAENIRYGRED-----ATMEDIV-QAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVA 602
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENravprPEMIKIVrDVLADVGMLDYIDSEPANLS-----------GGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1129-1288 |
3.03e-24 |
|
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: 103.45 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 1208
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1209 kygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 1288
Cdd:cd03288 116 ---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1119-1284 |
3.04e-24 |
|
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: 100.97 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQepv 1198
Cdd:cd03214 7 VGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 lfacsimdnikygdntkeipmerviaAAKQAQLHDFVmslpekyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:cd03214 81 --------------------------ALELLGLAHLA-------DRPF----NELSGGERQRVLLARALAQEPPILLLDE 123
|
....*.
gi 2462578034 1279 ATSALD 1284
Cdd:cd03214 124 PTSHLD 129
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1130-1284 |
3.15e-24 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 103.88 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN---VQFLRSN-IGIVSQEPVLFA-CSI 1204
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:cd03294 120 LENVAFGLEVQGVPraerEERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
....
gi 2462578034 1281 SALD 1284
Cdd:cd03294 189 SALD 192
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
454-660 |
3.98e-24 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 101.79 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWlRDQIG 533
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST-TIAENIR-----YGReDATMEDIVQAAKEanaynfiMDLPQQFDTLVGEgggqmsggqkqRVAIARAL 607
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVRQlsag----qkrRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 608 IRNPKILLLDMATSALDNESEAMVQEVLSK-IQHGHTIISVAHRLSTVRAADTI 660
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
453-685 |
4.02e-24 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 102.80 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 453 EIEFHNVTFHYPSRPEvkiLNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQI 532
Cdd:cd03296 2 SIEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLFS-TTIAENIRYGREdatMEDIVQAAKEANAYNFIMDLPQ--QFDTLVGEGGGQMSGGQKQRVAIARALIR 609
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGLR---VKPRSERPPEAEIRAKVHELLKlvQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 610 NPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELLERKGVYF 685
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
452-649 |
4.26e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.54 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDq 531
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-DRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLF-STTIAENIRYG----REDAtmEDIVQAAKEANAynfIMDL-------P-------QQfdtlvgegggq 592
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrKVPK--AEIDRRVREAAE---LLGLedlldrkPkqlsggqRQ----------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 593 msggqkqRVAIARALIRNPKILLLDMATSALDNES-EAMVQEvLSKIQH--GHTIISVAH 649
Cdd:COG3839 141 -------RVALGRALVREPKVFLLDEPLSNLDAKLrVEMRAE-IKRLHRrlGTTTIYVTH 192
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
470-675 |
6.07e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 6.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 470 KILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAEN 549
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 550 IRYGREdatmedIVQAAKEANAynFIMDLpQQF---DTLVGEGGGQMSGGQKQRVaiarALIRN----PKILLLDMATSA 622
Cdd:PRK10247 101 LIFPWQ------IRNQQPDPAI--FLDDL-ERFalpDTILTKNIAELSGGEKQRI----SLIRNlqfmPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 623 LDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFE-HGTAVERGTHE 675
Cdd:PRK10247 168 LDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1134-1284 |
6.78e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 101.76 E-value: 6.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1134 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnvqFLRSNIG-----IVSQEPVLFA-CSIMDN 1207
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-------LTALPPAerpvsMLFQENNLFPhLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1208 I--------KYGDNTKEipmeRVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:COG3840 92 IglglrpglKLTAEQRA----QVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEP 156
|
....*
gi 2462578034 1280 TSALD 1284
Cdd:COG3840 157 FSALD 161
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
454-660 |
7.65e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 7.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ-I 532
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLFST-TIAENIRYGRE--------DATMEDivQAAKEANAYNF-------IMDLP---QQFdtlvgegggqm 593
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREprrgglidWRAMRR--RARELLARLGLdidpdtpVGDLSvaqQQL----------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 594 sggqkqrVAIARALIRNPKILLLDMATSALdNESEAmvqEVLSKI-----QHGHTIISVAHRLSTVRA-ADTI 660
Cdd:COG1129 149 -------VEIARALSRDARVLILDEPTASL-TEREV---ERLFRIirrlkAQGVAIIYISHRLDEVFEiADRV 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
454-678 |
1.17e-23 |
|
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: 101.70 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGM-VTVDGHDIRSLNIQWLRDQI 532
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVeqepvlfSTTIAENIrygREDATMEDIV-------------------QAAKEanaynfIMDL-------PQQFDTLv 586
Cdd:COG1119 81 GLV-------SPALQLRF---PRDETVLDVVlsgffdsiglyreptdeqrERARE------LLELlglahlaDRPFGTL- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 587 gegggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLStvraaDTIIGFE 664
Cdd:COG1119 144 -------SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVE-----EIPPGIT 211
|
250 260
....*....|....*....|
gi 2462578034 665 H------GTAVERGTHEELL 678
Cdd:COG1119 212 HvlllkdGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
454-680 |
1.19e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.50 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEP--VLFSTTIAENIRYGREDATM--EDIVQAAKEA----NAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAIAR 605
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIphEEMKERVNEAlelvGMQDFKEREPARL-----------SGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrdDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1120-1284 |
1.76e-23 |
|
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: 102.82 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDP---DQGKVMIDGHD----SKKVNVQFLRSNIG 1191
Cdd:COG0444 10 YFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllklSEKELRKIRGREIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPvlFAC---------SIMDNIKY-GDNTKEIPMERVIAAAKQAQLHDfvmslPEKYetnVGSQGSQLSRGEKQRI 1261
Cdd:COG0444 90 MIFQDP--MTSlnpvmtvgdQIAEPLRIhGGLSKAEARERAIELLERVGLPD-----PERR---LDRYPHELSGGMRQRV 159
|
170 180
....*....|....*....|...
gi 2462578034 1262 AIARAIVRDPKILLLDEATSALD 1284
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALD 182
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1120-1290 |
1.84e-23 |
|
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: 100.72 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---SKKVNVQFLRSNIGIVSQE 1196
Cdd:cd03256 9 TYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 PVLFA-CSIMDNIKYGdNTKEIPMERVIA-----AAKQAQLH--DFVmSLPEKYETNVgsqgSQLSRGEKQRIAIARAIV 1268
Cdd:cd03256 87 FNLIErLSVLENVLSG-RLGRRSTWRSLFglfpkEEKQRALAalERV-GLLDKAYQRA----DQLSGGQQQRVAIARALM 160
|
170 180
....*....|....*....|..
gi 2462578034 1269 RDPKILLLDEATSALDTESEKQ 1290
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQ 182
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
471-678 |
2.10e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.98 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI---RSLN-----IQWLRDQIGIVEQEPVLF 542
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 S-TTIAENIRYG--------REDAT------MEDIVQAAKEaNAYNFIMDLPQQfdtlvgegggqmsggqkQRVAIARAL 607
Cdd:PRK11264 98 PhRTVLENIIEGpvivkgepKEEATararelLAKVGLAGKE-TSYPRRLSGGQQ-----------------QRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 608 IRNPKILLLDMATSALDNEseaMVQEVLSKI----QHGHTIISVAHRLSTVR-AADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPE---LVGEVLNTIrqlaQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALF 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1111-1284 |
2.49e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 101.63 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1111 KIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNI 1190
Cdd:PRK13635 5 IIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1191 GIVSQEP--VLFACSIMDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIA 1264
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFGLENIGVPreemVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIA 152
|
170 180
....*....|....*....|
gi 2462578034 1265 RAIVRDPKILLLDEATSALD 1284
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLD 172
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1126-1284 |
3.64e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD--PD---QGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1198
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFACSIMDNIKYG-----DNTKEIPMERVIAAAKQAQLHDFVMSlpEKYETNVGsqgsqLSRGEKQRIAIARAIVRDPKI 1273
Cdd:PRK14239 97 PFPMSIYENVVYGlrlkgIKDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKI 169
|
170
....*....|.
gi 2462578034 1274 LLLDEATSALD 1284
Cdd:PRK14239 170 ILLDEPTSALD 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
454-680 |
3.87e-23 |
|
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: 102.05 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPC---EGMVTVDGHDIRSLN---IQ 526
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 527 WLR-DQIGIVEQEPvlFS---------TTIAENIRY----GREDAT------MED--IVQAAKEANAYnfimdlPQQFdt 584
Cdd:COG0444 82 KIRgREIQMIFQDP--MTslnpvmtvgDQIAEPLRIhgglSKAEAReraielLERvgLPDPERRLDRY------PHELsg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 585 lvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTII 661
Cdd:COG0444 154 g-----------mrqRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQreLGLAILFITHDLGVVAEiADRVA 222
|
250
....*....|....*....
gi 2462578034 662 GFEHGTAVERGTHEELLER 680
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
182-399 |
4.27e-23 |
|
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: 100.97 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 182 IAVAVL--ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18542 46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSK-FTDYElKAYAKAGVVADEVISSMRTVAAFGGEKREVERY 338
Cdd:cd18542 126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPaFEEIR-EQEGELNTVLQENLTGVRVVKAFAREDYEIEKF 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 339 EK-NLVFAQRWgIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQiFLS 399
Cdd:cd18542 205 DKeNEEYRDLN-IKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVIN-GEITLGELVA-FIS 263
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
182-427 |
5.04e-23 |
|
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: 100.96 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 182 IAVAVL--ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18552 46 IGLFLLrgLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERY- 338
Cdd:cd18552 126 TVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFr 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 339 ---EKNLVFAQRWGIRKGI---VMGFFTGFVwclIflcyALAFWYGSTLVLDeGEYTPGTlvqiFLSVIVGAL------- 405
Cdd:cd18552 206 kanERLRRLSMKIARARALsspLMELLGAIA---I----ALVLWYGGYQVIS-GELTPGE----FISFITALLllyqpik 273
|
250 260
....*....|....*....|..
gi 2462578034 406 NLGNASpclEAFATGRAAATSI 427
Cdd:cd18552 274 RLSNVN---ANLQRGLAAAERI 292
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
454-667 |
6.11e-23 |
|
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: 97.93 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEV--KILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHdirslniqwlrdq 531
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFSTTIAENIRYGRE-DATM-EDIVQA-AKEAnaynfimDLpQQFD----TLVGEGGGQMSGGQKQRVAIA 604
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKAcALEP-------DL-EILPdgdlTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 605 RALIRNPKILLLDMATSALDNESEAMVQE--VLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
471-680 |
1.29e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.95 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWlRDqIGIVEQEPVLFS-TTIAEN 549
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-ICMVFQSYALFPhMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 550 IRYG--REDATMEDIVQAAKEANAynfIMDLPQQFDTLVgeggGQMSGGQKQRVAIARALIRNPKILLLDMATSALD-NE 626
Cdd:PRK11432 99 VGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDaNL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 627 SEAMvQEVLSKIQHGHTIIS--VAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK11432 172 RRSM-REKIRELQQQFNITSlyVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
454-680 |
1.32e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.32 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYP--SRPEVKilnDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:PRK13635 6 IRVEHISFRYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEP--VLFSTTIAENIRYGRE------DATMEDIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 603
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLEnigvprEEMVERVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEamvQEVLSKI-----QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGR---REVLETVrqlkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
..
gi 2462578034 679 ER 680
Cdd:PRK13635 229 KS 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1123-1287 |
1.46e-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: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFlRSNIGIVSQEPVLF-A 1201
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNIK-----YGDntkEIPMERVIAAAKQAQLHDFvMSLPekyetnvgsqGSQLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:COG4133 90 LTVRENLRfwaalYGL---RADREAIDEALEAVGLAGL-ADLP----------VRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170
....*....|.
gi 2462578034 1277 DEATSALDTES 1287
Cdd:COG4133 156 DEPFTALDAAG 166
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1124-1284 |
1.48e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.42 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1124 RPDSQV--LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN---VQFLRSNIGIVSQEPv 1198
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 lFAcSIMDNIKYGD--------NTKEIPMERviaAAKQAQLHDFVMSLPEKYetnvGSQGSQLSRGEKQRIAIARAIVRD 1270
Cdd:PRK11308 102 -YG-SLNPRKKVGQileeplliNTSLSAAER---REKALAMMAKVGLRPEHY----DRYPHMFSGGQRQRIAIARALMLD 172
|
170
....*....|....
gi 2462578034 1271 PKILLLDEATSALD 1284
Cdd:PRK11308 173 PDVVVADEPVSALD 186
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1139-1290 |
1.49e-22 |
|
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: 97.37 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1139 PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG---HDS-KKVNVQFLRSNIGIVSQEPVLFA-CSIMDNIKYGDN 1213
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSrKKINLPPQQRKIGLVFQQYALFPhLNVRENLAFGLK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 1214 TKEiPMERVIAAAKQAQLHDfVMSLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:cd03297 102 RKR-NREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
454-708 |
1.66e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEP--VLFSTTIAENIRYG------REDATMEDIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAIAR 605
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERG-----THEELL 678
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250 260 270
....*....|....*....|....*....|....*
gi 2462578034 679 ERKGVYFTLVT-----LQSQGNQALnEEDIKDATE 708
Cdd:PRK13647 232 EQAGLRLPLVAqifedLPELGQSKL-PLTVKEAVQ 265
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
454-678 |
1.66e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.01 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEP--VLFSTTIAENIRYGREDATM--EDIVQAAKEA----NAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIAR 605
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIprEEMIKRVDEAllavNMLDFKTREPARLS-----------GGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1126-1290 |
1.88e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIM 1205
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1206 DNIKYgdnTKEIPMERVIAAAKQAQLHDFvmSLPEK-YETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK10247 99 DNLIF---PWQIRNQQPDPAIFLDDLERF--ALPDTiLTKNI----AELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
....*.
gi 2462578034 1285 tESEKQ 1290
Cdd:PRK10247 170 -ESNKH 174
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1119-1284 |
2.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.63 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP- 1197
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1198 -VLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKyetnvgsQGSQLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:PRK13642 92 nQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTR-------EPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
....*...
gi 2462578034 1277 DEATSALD 1284
Cdd:PRK13642 165 DESTSMLD 172
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1116-1290 |
2.74e-22 |
|
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: 96.17 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1116 DCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNVQFLRSNIGIVSQ 1195
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1196 EP--VLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKI 1273
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170
....*....|....*..
gi 2462578034 1274 LLLDEATSALDTESEKQ 1290
Cdd:cd03226 148 LIFDEPTSGLDYKNMER 164
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
170-395 |
2.83e-22 |
|
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: 98.64 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 170 SEMIKFASYYAGIAVAVLITGYIQiCFWVIAAARQIQK-MRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIA 248
Cdd:cd18541 37 SQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIEYdLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 249 DQMALFIQrmTSTICGFLLG--FFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVA 326
Cdd:cd18541 116 PGILYLVD--ALFLGVLVLVmmFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIK 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 327 AFGGEKREVER--------YEKNLVFAQrwgirkgiVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQ 395
Cdd:cd18541 194 AFVQEEAEIERfdklneeyVEKNLRLAR--------VDALFFPLIGLLIGLSFLIVLWYGGRLVIR-GTITLGDLVA 261
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
454-680 |
4.82e-22 |
|
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: 101.68 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSR--------PEVKILNDLNMAIKPGEMTALVGPSGAGKST----ALQLIqrfydPCEGMVTVDGHDIR 521
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 522 SLN---IQWLRDQIGIVEQEPvlFST-----TIAENI-------RYGREDATMEDIVQAAKE--------ANAYnfimdl 578
Cdd:COG4172 351 GLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIaeglrvhGPGLSAAERRARVAEALEevgldpaaRHRY------ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 579 PQQFdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA 656
Cdd:COG4172 423 PHEFsgg-----------qrqRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQreHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....*
gi 2462578034 657 -ADTIIGFEHGTAVERGTHEELLER 680
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1116-1290 |
5.23e-22 |
|
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: 95.68 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1116 DCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVnvqflRSNIGIVSQ 1195
Cdd:cd03235 4 DLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1196 EPVL---FACSIMDNIKYGDNTKEIPMERVIAAAKQA--QLHDFV-MSlpEKYETNVGsqgsQLSRGEKQRIAIARAIVR 1269
Cdd:cd03235 76 RRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKvdEALERVgLS--ELADRQIG----ELSGGQQQRVLLARALVQ 149
|
170 180
....*....|....*....|.
gi 2462578034 1270 DPKILLLDEATSALDTESEKQ 1290
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQED 170
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
454-672 |
7.64e-22 |
|
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: 95.34 E-value: 7.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpevKILNDLNMAIKPGeMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 533
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST-TIAENIRY---------GREDATmedIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 603
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkgipsKEVKAR---VDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 672
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
180-427 |
8.55e-22 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 97.12 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18551 43 VALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYE 339
Cdd:cd18551 123 TVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 340 KNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVlDEGEYTPGTLVQIFLSV--IVGAL-NLGNAspcLEA 416
Cdd:cd18551 203 EAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARV-ASGALTVGTLVAFLLYLfqLITPLsQLSSF---FTQ 278
|
250
....*....|.
gi 2462578034 417 FATGRAAATSI 427
Cdd:cd18551 279 LQKALGALERI 289
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
454-669 |
9.99e-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: 93.26 E-value: 9.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ-I 532
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVlfsttiAEnirygredatmedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPK 612
Cdd:cd03216 78 AMVYQLSV------GE-------------------------------RQ------------------MVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 613 ILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 669
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
209-404 |
1.19e-21 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 96.78 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 209 RKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGI 288
Cdd:cd18575 72 RKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 289 GAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERY----EKNLVFAQRW-GIRkgivmGFFTGFV 363
Cdd:cd18575 152 PIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFatavEAAFAAALRRiRAR-----ALLTALV 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462578034 364 WCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQ-IFLSVIVGA 404
Cdd:cd18575 227 IFLVFGAIVFVLWLGAHDVL-AGRMSAGELSQfVFYAVLAAG 267
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
470-672 |
1.75e-21 |
|
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: 94.28 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 470 KILNDLNMAIK---PGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG---HDIR-SLNIQWLRDQIGIVEQEPVLF 542
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 S-TTIAENIRYG-REDATMEDIVQAAKeanaynfIMDLpQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMAT 620
Cdd:cd03297 88 PhLNVRENLAFGlKRKRNREDRISVDE-------LLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 621 SALDNESEAMVQEVLSKIQ---HGHTIIsVAHRLSTV-RAADTIIGFEHGTAVERG 672
Cdd:cd03297 160 SALDRALRLQLLPELKQIKknlNIPVIF-VTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1113-1284 |
2.50e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.10 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1113 DFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGI 1192
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1193 VSQEPVLFA-CSIMDNIKYGDNTKEIPMERVIAAAKQA-QLHDFVmSLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRD 1270
Cdd:PRK11432 83 VFQSYALFPhMSLGENVGYGLKMLGVPKEERKQRVKEAlELVDLA-GFEDRYV-------DQISGGQQQRVALARALILK 154
|
170
....*....|....
gi 2462578034 1271 PKILLLDEATSALD 1284
Cdd:PRK11432 155 PKVLLFDEPLSNLD 168
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
454-681 |
2.85e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.62 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHY-PSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG----HDIRSLNIQW 527
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 528 LRDQIGIVEQ--EPVLFSTTIAENIRYGREDATMEdiVQAAKEaNAYNFIMDLPQQFDTLvGEGGGQMSGGQKQRVAIAR 605
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVKN-YAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1120-1284 |
3.06e-21 |
|
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: 93.72 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSRPdSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPVL 1199
Cdd:cd03263 9 TYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 F-ACSIMDNIKY-----GDNTKEIPMErviaaakQAQLHDfVMSLPEKYETNVGsqgsQLSRGEKQRIAIARAIVRDPKI 1273
Cdd:cd03263 87 FdELTVREHLRFyarlkGLPKSEIKEE-------VELLLR-VLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSV 154
|
170
....*....|.
gi 2462578034 1274 LLLDEATSALD 1284
Cdd:cd03263 155 LLLDEPTSGLD 165
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1133-1284 |
3.42e-21 |
|
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: 93.33 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1133 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIMDNIKYG 1211
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 1212 DNT----KEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:cd03298 95 LSPglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1130-1290 |
3.74e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.41 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHDSKKVNVQFLRS---NIGIVSQEPVLFAC- 1202
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMIFQHFNLLSSr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 SIMDNIKygdntkeIPMErvIAAAKQAQLHDFVMSLPE---------KYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKI 1273
Cdd:PRK11153 98 TVFDNVA-------LPLE--LAGTPKAEIKARVTELLElvglsdkadRYP-------AQLSGGQKQRVAIARALASNPKV 161
|
170
....*....|....*..
gi 2462578034 1274 LLLDEATSALDTESEKQ 1290
Cdd:PRK11153 162 LLCDEATSALDPATTRS 178
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1126-1284 |
3.77e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.11 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEP--VLFA 1201
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNIKYGD-----NTKEIpMERVIAAAKQAQLhdfvmslpeKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:PRK13637 99 ETIEKDIAFGPinlglSEEEI-ENRVKRAMNIVGL---------DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
....*...
gi 2462578034 1277 DEATSALD 1284
Cdd:PRK13637 169 DEPTAGLD 176
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
453-677 |
4.14e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.09 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 453 EIEFHNVTFHY-PSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI----RSLNIQ 526
Cdd:PRK13634 2 DITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 527 WLRDQIGIVEQ--EPVLFSTTIAENIRYGRED--ATMEDIVQAAKEANAynfIMDLPQQfdtLVGEGGGQMSGGQKQRVA 602
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEE---LLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEEL 677
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
789-1009 |
4.44e-21 |
|
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: 95.18 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTFSIpdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 868
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFV---EKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 869 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALs 948
Cdd:cd18552 78 LFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 949 gatqtrmLTGFASR-----DKQALEMVGQITN---EALSNIRTVAGIGKERRFIEALETELEKPFKTAI 1009
Cdd:cd18552 155 -------PIRRIGKrlrkiSRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSM 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1130-1284 |
5.41e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.08 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD-----PDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLFAC 1202
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 SIMDNIKYGD--NTKEIPM-ERVIAAAKQAQLHDFVmslPEKYETNvgsqGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMdELVERSLRQAALWDEV---KDKLKQS----GLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
....*
gi 2462578034 1280 TSALD 1284
Cdd:PRK14243 179 CSALD 183
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
469-676 |
5.55e-21 |
|
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: 93.27 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 469 VKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIGIVE--QEPVLFST-T 545
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 546 IAENIR-----YGREDATMEDIVQAAKEANAYNF----IMDLPQQFDTLVgeggGQMSGGQKQRVAIARALIRNPKILLL 616
Cdd:cd03219 92 VLENVMvaaqaRTGSGLLLARARREEREARERAEelleRVGLADLADRPA----GELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 617 DMATSAL-DNESEAMVqEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEE 676
Cdd:cd03219 168 DEPAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1112-1284 |
5.72e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.37 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL--RSN 1189
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1190 IGIVSQEP--VLFACSIMDNIKYGDNTKEIPME----RVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAI 1263
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEevekRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180
....*....|....*....|.
gi 2462578034 1264 ARAIVRDPKILLLDEATSALD 1284
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLD 169
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
454-681 |
5.85e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.90 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHY-PSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR----SLNIQW 527
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 528 LRDQIGIVEQ--EPVLFSTTIAENIRYGREDATMEDivQAAKEAnAYNFI--MDLPQQfdtLVGEGGGQMSGGQKQRVAI 603
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE--DEAKEK-ALKWLkkVGLSED---LISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 604 ARALIRNPKILLLDMATSALDNES-EAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1126-1286 |
5.93e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.62 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLFA-C 1202
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPKVDERLIRQEAGMVFQQFYLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 SIMDNIKYGdntkeiPMeRVIAAAKqAQLHDFVMSLPEK--YETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:PRK09493 93 TALENVMFG------PL-RVRGASK-EEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
....*.
gi 2462578034 1281 SALDTE 1286
Cdd:PRK09493 165 SALDPE 170
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1123-1284 |
5.98e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 95.57 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQV--LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD----SKKVNVQfLRSNIGIVSQE 1196
Cdd:COG4608 25 GRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitglSGRELRP-LRRRMQMVFQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 PvlFAC-----SIMDNIK-----YGDNTKEIPMERViaaakqAQLHDFVMSLPEKYETNVGsqgsQLSRGEKQRIAIARA 1266
Cdd:COG4608 104 P--YASlnprmTVGDIIAeplriHGLASKAERRERV------AELLELVGLRPEHADRYPH----EFSGGQRQRIGIARA 171
|
170
....*....|....*...
gi 2462578034 1267 IVRDPKILLLDEATSALD 1284
Cdd:COG4608 172 LALNPKLIVCDEPVSALD 189
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
454-683 |
6.59e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 6.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVkiLNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--DIRSLNIQWLRDQ 531
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEP--VLFSTTIAENIRYGREDATM-EDIVQA----AKEANAYNFIMDLPQQFDTLvgegggqmsgGQKQRVAIA 604
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpEDEVRKrvdnALKRTGIEHLKDKPTHCLSF----------GQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 605 RALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEK 233
|
..
gi 2462578034 682 GV 683
Cdd:PRK13636 234 EM 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1119-1284 |
6.91e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.95 E-value: 6.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD-----QGKVMIDGHD--SKKVNVQFLRSNIG 1191
Cdd:PRK14258 15 FYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNiyERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVLFACSIMDNIKYGDNT----KEIPMERVIAAA-KQAQLHDFVmslpekyETNVGSQGSQLSRGEKQRIAIARA 1266
Cdd:PRK14258 92 MVHPKPNLFPMSVYDNVAYGVKIvgwrPKLEIDDIVESAlKDADLWDEI-------KHKIHKSALDLSGGQQQRLCIARA 164
|
170
....*....|....*...
gi 2462578034 1267 IVRDPKILLLDEATSALD 1284
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLD 182
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-666 |
7.74e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.56 E-value: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDI--RSLNIQ 526
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 527 WLRDQIGIVEQEPVLFSTTIAENIRYG------REDATMEDIVQAAKEAnaynfiMDLPQQFDTLVGEGGGQMSGGQKQR 600
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 601 VAIARALIRNPKILLLDMATSALDNESEAMVQEVLS--KIQHGHTIISVAHRLSTVRAADTIIGFEHG 666
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1109-1287 |
8.03e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.44 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1109 QGKIDFVDCKFTYPsrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD--PD---QGKVMIDGHDSKKVNV 1183
Cdd:PRK14247 1 MNKIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1184 QFLRSNIGIVSQEP-VLFACSIMDNIKYG-------DNTKEIpMERVIAAAKQAQLHDFVmslpekyETNVGSQGSQLSR 1255
Cdd:PRK14247 78 IELRRRVQMVFQIPnPIPNLSIFENVALGlklnrlvKSKKEL-QERVRWALEKAQLWDEV-------KDRLDAPAGKLSG 149
|
170 180 190
....*....|....*....|....*....|..
gi 2462578034 1256 GEKQRIAIARAIVRDPKILLLDEATSALDTES 1287
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
454-678 |
8.04e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 93.64 E-value: 8.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG4559 2 LEAENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVL-FSTTIAENIRYGR-----EDATMEDIVQAAKEAnaynfiMDLP--------------QQfdtlvgegggqm 593
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVALGRaphgsSAAQDRQIVREALAL------VGLAhlagrsyqtlsggeQQ------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 594 sggqkqRVAIARALI-------RNPKILLLDMATSALDneseamvqevlskIQHGHTIISVAHRLS-------------- 652
Cdd:COG4559 141 ------RVQLARVLAqlwepvdGGPRWLFLDEPTSALD-------------LAHQHAVLRLARQLArrgggvvavlhdln 201
|
250 260
....*....|....*....|....*..
gi 2462578034 653 -TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:COG4559 202 lAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1127-1286 |
8.54e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1127 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---SKKVN---VQFLRSNIGIVSQE---- 1196
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSdkaIRELRRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 PVLfacSIMDN-----IKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDP 1271
Cdd:PRK11124 95 PHL---TVQQNlieapCRVLGLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEP 160
|
170
....*....|....*
gi 2462578034 1272 KILLLDEATSALDTE 1286
Cdd:PRK11124 161 QVLLFDEPTAALDPE 175
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1124-1290 |
8.86e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.34 E-value: 8.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1124 RPDSQVL-NGLSVSISPGQTLAFVGSSGCGKST--------------SIQLlerfydPDQGKVMidghdskkvnvqFLrs 1188
Cdd:COG4178 372 TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTllraiaglwpygsgRIAR------PAGARVL------------FL-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 nigivSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEkyetnVGSQGSQLSRGEKQRIAIARAIV 1268
Cdd:COG4178 432 -----PQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERLDE-----EADWDQVLSLGEQQRLAFARLLL 501
|
170 180
....*....|....*....|..
gi 2462578034 1269 RDPKILLLDEATSALDTESEKQ 1290
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAA 523
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
464-672 |
1.62e-20 |
|
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: 91.66 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 464 PSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLRDQIGIVEQEPVLFS 543
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 544 -TTIAENIRY-GRedatmediVQAAKEANAYNFIMDLPQQFDT--LVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMA 619
Cdd:cd03266 92 rLTARENLEYfAG--------LYGLKGDELTARLEELADRLGMeeLLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 620 TSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTV-RAADTIIGFEHGTAVERG 672
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
469-676 |
1.68e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 92.41 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 469 VKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiQWLRDQIGIVE--QEPVLFST-T 545
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 546 IAENI--------------------RYGREDATMEDIVQA-------AKEANAYnfIMDLP--QQfdtlvgegggqmsgg 596
Cdd:COG0411 96 VLENVlvaaharlgrgllaallrlpRARREEREARERAEEllervglADRADEP--AGNLSygQQ--------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 597 qkQRVAIARALIRNPKILLLD-----MATSaldnESEAMVqEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTA 668
Cdd:COG0411 159 --RRLEIARALATEPKLLLLDepaagLNPE----ETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
....*...
gi 2462578034 669 VERGTHEE 676
Cdd:COG0411 232 IAEGTPAE 239
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1123-1286 |
1.98e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.00 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQflRSNIGIVSQEPVL 1199
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 FA-CSIMDNIKYG---DNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILL 1275
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 2462578034 1276 LDEATSALDTE 1286
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
454-678 |
2.00e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVL-FSTTIAENIRYGR-----EDATMEDIVQAAKEAN-----AYNFIMDLP---QQfdtlvgegggqmsggqkq 599
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRaphglSRAEDDALVAAALAQVdlahlAGRDYPQLSggeQQ------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 600 RVAIARALIR------NPKILLLDMATSALDneseamvqevlskIQHGHTIISVAHRLS----------------TVRAA 657
Cdd:PRK13548 142 RVQLARVLAQlwepdgPPRWLLLDEPTSALD-------------LAHQHHVLRLARQLAherglavivvlhdlnlAARYA 208
|
250 260
....*....|....*....|.
gi 2462578034 658 DTIIGFEHGTAVERGTHEELL 678
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAEVL 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1119-1290 |
2.06e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVnvqflRSNIGIVSQEPV 1198
Cdd:COG1121 14 VSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 L---FACSIMDNIKYGdNTKEIPM---------ERVIAAAKQAQLHDFVmslpekyetnvGSQGSQLSRGEKQRIAIARA 1266
Cdd:COG1121 86 VdwdFPITVRDVVLMG-RYGRRGLfrrpsradrEAVDEALERVGLEDLA-----------DRPIGELSGGQQQRVLLARA 153
|
170 180
....*....|....*....|....
gi 2462578034 1267 IVRDPKILLLDEATSALDTESEKQ 1290
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEA 177
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
454-681 |
2.07e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPS-RP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL----NIQW 527
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 528 LRDQIGIVEQ--EPVLFSTTIAENIRYGRED--ATMEDIVQAAKEANAYNFIMdlpqqfDTLVGEGGGQMSGGQKQRVAI 603
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGT------HE 675
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKpkdifqDV 236
|
....*.
gi 2462578034 676 ELLERK 681
Cdd:PRK13649 237 DFLEEK 242
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
454-649 |
2.09e-20 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 91.73 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQWL 528
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 529 RDQIGIVEQ-EPVLFSTTIAENI-----RYGREDATmedivQAAKE----------ANAYnfimdlP-------QQfdtl 585
Cdd:COG4181 89 ARHVGFVFQsFQLLPTLTALENVmlpleLAGRRDAR-----ARARAllervglghrLDHY------PaqlsggeQQ---- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 586 vgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 649
Cdd:COG4181 154 --------------RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnrERGTTLVLVTH 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1129-1286 |
2.32e-20 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 91.34 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGHDSKKVN----VQFLRSNIGIVSQE----P 1197
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1198 VLFAcsiMDNIkygdntkEIPMErvIAAAKQAQlhdfvmSLPEKYETNVGSQG------SQLSRGEKQRIAIARAIVRDP 1271
Cdd:COG4181 104 TLTA---LENV-------MLPLE--LAGRRDAR------ARARALLERVGLGHrldhypAQLSGGEQQRVALARAFATEP 165
|
170
....*....|....*
gi 2462578034 1272 KILLLDEATSALDTE 1286
Cdd:COG4181 166 AILFADEPTGNLDAA 180
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1130-1284 |
2.70e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 96.29 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFyDPDQGKVMIDGHD----SKKVNvQFLRSNIGIVSQEPvlFAC--- 1202
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDldglSRRAL-RPLRRRMQVVFQDP--FGSlsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 --SIMDNIKYGDNTKEIPM------ERVIAAAKQAQLHDFVMslpEKYETnvgsqgsQLSRGEKQRIAIARAIVRDPKIL 1274
Cdd:COG4172 378 rmTVGQIIAEGLRVHGPGLsaaerrARVAEALEEVGLDPAAR---HRYPH-------EFSGGQRQRIAIARALILEPKLL 447
|
170
....*....|
gi 2462578034 1275 LLDEATSALD 1284
Cdd:COG4172 448 VLDEPTSALD 457
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
826-1046 |
2.79e-20 |
|
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: 92.55 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 826 RSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNspGALTTRLATDASQVQGA 905
Cdd:cd18576 32 TASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV--GELTSRLSNDVTQIQDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 906 AGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFAsrdKQALEMVGQITN---EALSNIR 982
Cdd:cd18576 110 LTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLS---KKVQDELAEANTiveETLQGIR 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 983 TVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 1046
Cdd:cd18576 187 VVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGEL 250
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
463-1290 |
2.84e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 97.93 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 463 YPSRPEVkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVtvdghdirslniqWLRDQIGIVEQEPVLF 542
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 STTIAENIRYGRED--ATMEDIVQAAK-EANaynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMA 619
Cdd:PTZ00243 734 NATVRGNILFFDEEdaARLADAVRVSQlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 620 TSALDNE-SEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLeRKGVYFTLVTlQSQGNQAL 698
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATLAA-ELKENKDS 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 699 NEEDiKDATEDDMLArtfSRGSYQDSLRASIRQRSKSQLSYLVHEPPlavVDHKSTYEEDRKDKDIPVQEEVE------- 771
Cdd:PTZ00243 888 KEGD-ADAEVAEVDA---APGGAVDHEPPVAKQEGNAEGGDGAALDA---AAGRLMTREEKASGSVPWSTYVAylrfcgg 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 772 -PAPVRRILKFSAPE--------WPYMLvgSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEqrsqingVCLLFVAMGCV 842
Cdd:PTZ00243 961 lHAAGFVLATFAVTElvtvssgvWLSMW--STRSFKLSAATYLYVYLGIVLLGTFSVPLRFF-------LSYEAMRRGSR 1031
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 843 SLFTQFLQGYAFAKsgelltkrlrkfgframlgqdIAWFDdlRNSPGALTTRLATDAsqvqGAAGSQIGMIVNSFTNVTV 922
Cdd:PTZ00243 1032 NMHRDLLRSVSRGT---------------------MSFFD--TTPLGRILNRFSRDI----DILDNTLPMSYLYLLQCLF 1084
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 923 AM---IIAFSFSWKLSLVIL--CFFPFLAL-----SGATQTRMLTGFASRDkqalemVGQITNEALSNIRTVAGIGKERR 992
Cdd:PTZ00243 1085 SIcssILVTSASQPFVLVALvpCGYLYYRLmqfynSANREIRRIKSVAKSP------VFTLLEEALQGSATITAYGKAHL 1158
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 993 FI-EALEtELEKPFKTAIQK--------------ANIYGFCFAFAQCIMFIANSASYRYGgyLIS---------NEGLhf 1048
Cdd:PTZ00243 1159 VMqEALR-RLDVVYSCSYLEnvanrwlgvrveflSNIVVTVIALIGVIGTMLRATSQEIG--LVSlsltmamqtTATL-- 1233
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1049 SYVFRVISAVVLSATALGRAFSYTPSYAKAKISA--ARFFQLLDRQ------------PPISVYNTAGEkwdNFQ-GKID 1113
Cdd:PTZ00243 1234 NWLVRQVATVEADMNSVERLLYYTDEVPHEDMPEldEEVDALERRTgmaadvtgtvviEPASPTSAAPH---PVQaGSLV 1310
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1114 FVDCKFTY----PsrpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN 1189
Cdd:PTZ00243 1311 FEGVQMRYreglP-----LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1190 IGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIV- 1268
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLk 1462
|
890 900
....*....|....*....|..
gi 2462578034 1269 RDPKILLLDEATSALDTESEKQ 1290
Cdd:PTZ00243 1463 KGSGFILMDEATANIDPALDRQ 1484
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
454-672 |
2.95e-20 |
|
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: 90.63 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEvkilnDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIG 533
Cdd:cd03298 1 VRLDKIRFSYGEQPM-----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFS-TTIAENIRYGREDA---TMED---IVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIARA 606
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSPGlklTAEDrqaIEVALARVGLAGLEKRLPGELS-----------GGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 607 LIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 672
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
452-685 |
3.25e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 97.93 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHY-PSRPEVkiLNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 530
Cdd:PTZ00243 1307 GSLVFEGVQMRYrEGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFSTTIAENIRYGREDATMEdiVQAAKE-ANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALI- 608
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAE--VWAALElVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLk 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 609 RNPKILLLDMATS----ALDNESEAMVQEVLSkiqhGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVY 684
Cdd:PTZ00243 1463 KGSGFILMDEATAnidpALDRQIQATVMSAFS----AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSI 1538
|
.
gi 2462578034 685 F 685
Cdd:PTZ00243 1539 F 1539
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
454-649 |
3.25e-20 |
|
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: 90.39 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDqIG 533
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLF-STTIAENIRYG------REDATMEDIVQAAKeanaynfIMDLpqqfDTLVGEGGGQMSGGQKQRVAIARA 606
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAE-------LLQI----EHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462578034 607 LIRNPKILLLDMATSALDNE-SEAMVQEvLSKIQ--HGHTIISVAH 649
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKlRVQMRAE-LKRLQqrLGTTTIYVTH 189
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1144-1287 |
4.16e-20 |
|
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: 93.63 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1144 AFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGH---DSKKVnvQFL---RSNIGIVSQEPVLFA-CSIMDNIKYGdn 1213
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqDSARG--IFLpphRRRIGYVFQEARLFPhLSVRGNLLYG-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1214 tkeipMERVIAAAKQAQLHDfVMSL----------PEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1283
Cdd:COG4148 102 -----RKRAPRAERRISFDE-VVELlgighlldrrPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
....
gi 2462578034 1284 DTES 1287
Cdd:COG4148 165 DLAR 168
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
454-649 |
4.20e-20 |
|
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: 90.26 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 533
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST-TIAENIRY-----GREDATMEDIVQAAKEanaynfIMDLPQQFDTLVgeggGQMSGGQKQRVAIARAL 607
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRA----RTLSGGMKRKLSLAIAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462578034 608 IRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAH 649
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1112-1290 |
5.95e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.79 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQFLRS 1188
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1189 NIGIVSQEP--VLFACSIMDNIKYGDNTKEIP---MERVIA-AAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIA 1262
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPrpeMIKIVRdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180
....*....|....*....|....*...
gi 2462578034 1263 IARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
455-683 |
6.34e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 90.43 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 455 EFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL-RDQIG 533
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST-TIAENIRYGREDATMEDIVQAAKEanaynFIMDL-P-----------------QQFdtlvgegggqms 594
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLE-----RVYELfPrlkerrrqragtlsggeQQM------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 595 ggqkqrVAIARALIRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLSTVRA-ADTIIGFEHGTAV 669
Cdd:COG0410 145 ------LAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIIRRlnreGVTILLVEQNARFALEiADRAYVLERGRIV 215
|
250
....*....|....
gi 2462578034 670 ERGTHEELLERKGV 683
Cdd:COG0410 216 LEGTAAELLADPEV 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
453-675 |
6.86e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 6.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 453 EIEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------DIRSLNIQ 526
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 527 WLRDQIGIVEQE----PVLfstTIAENI--------RYGREDATMEDI-----VQAAKEANAYNFIMDLPQQfdtlvgeg 589
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMkllarLRLTDKADRFPLHLSGGQQ-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 590 ggqmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVR-AADTIIGFEHGT 667
Cdd:COG4161 148 ---------QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARkVASQVVYMEKGR 218
|
....*...
gi 2462578034 668 AVERGTHE 675
Cdd:COG4161 219 IIEQGDAS 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1128-1289 |
8.05e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.70 E-value: 8.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQF------LRSNIGIVSQEPVLFA 1201
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP-----VRFrsprdaQAAGIAIIHQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 C-SIMDNIKYGDNTKE---IPMERVIAAAKQAqLHDFVMSLPEkyETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLD 1277
Cdd:COG1129 93 NlSVAENIFLGREPRRgglIDWRAMRRRAREL-LARLGLDIDP--DTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170
....*....|...
gi 2462578034 1278 EATSAL-DTESEK 1289
Cdd:COG1129 166 EPTASLtEREVER 178
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
786-1290 |
8.60e-20 |
|
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: 96.52 E-value: 8.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 786 WPYMLVGSV--GAAVNGTVTPLyafLFSQILGTFSiPDKEEQRSQIN----GVCLLFVAMgcvslfTQFLQGYAFAKSGE 859
Cdd:TIGR01271 80 WRFVFYGILlyFGEATKAVQPL---LLGRIIASYD-PFNAPEREIAYylalGLCLLFIVR------TLLLHPAIFGLHHL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 860 LLTKRLRKFG--FRAMLGQDIAWFDDLrnSPGALTTRLATDASQVQGaagsqiGMIVNSFTNVT-VAMIIAFSFSWKL-- 934
Cdd:TIGR01271 150 GMQMRIALFSliYKKTLKLSSRVLDKI--STGQLVSLLSNNLNKFDE------GLALAHFVWIApLQVILLMGLIWELle 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 935 --SLVILCFFPFLALSGATQTRMLTGFasRDKQAlEMVGQ---ITNEALSNIRTVAGIGKErrfiEALETELEKPFKTAI 1009
Cdd:TIGR01271 222 vnGFCGLGFLILLALFQACLGQKMMPY--RDKRA-GKISErlaITSEIIENIQSVKAYCWE----EAMEKIIKNIRQDEL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1010 QKANIYGFCFAFaqcimfiaNSASYRYGGYLIS---------NEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKI 1080
Cdd:TIGR01271 295 KLTRKIAYLRYF--------YSSAFFFSGFFVVflsvvpyalIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1081 SAARFFQ-LLDRQPPISV-YN-TAGE--------KWDNFQGKIdFVDCK----------------FTYPSRPDSQVLNGL 1133
Cdd:TIGR01271 367 GAITKIQdFLCKEEYKTLeYNlTTTEvemvnvtaSWDEGIGEL-FEKIKqnnkarkqpngddglfFSNFSLYVTPVLKNI 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1134 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqflrsnIGIVSQEPVLFACSIMDNIKYGDN 1213
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGLS 512
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 1214 TKEIPMERVIAAAkqaQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:TIGR01271 513 YDEYRYTSVIKAC---QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
472-678 |
1.04e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.17 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD----QIGIVEQEPVLFS-TTI 546
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 547 AENIRYGREDATM------EDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIARALIRNPKILLLDMAT 620
Cdd:PRK10070 124 LDNTAFGMELAGInaeerrEKALDALRQVGLENYAHSYPDELS-----------GGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 621 SALDNESEAMVQEVLSKIQ--HGHTIISVAHRL-STVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1112-1284 |
1.20e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.57 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1191
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEP--VLFACSIMDNIKYGD-----NTKEIpMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIA 1264
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPvnmglDKDEV-ERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180
....*....|....*....|
gi 2462578034 1265 RAIVRDPKILLLDEATSALD 1284
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLD 170
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1128-1284 |
1.27e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 88.96 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPVLFA-CSIMD 1206
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDrLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1207 NIKY--------GDNTKEipmeRVIAAAKQAQLHDFVmslpekyETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:cd03266 98 NLEYfaglyglkGDELTA----RLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIARALVHDPPVLLLDE 162
|
....*.
gi 2462578034 1279 ATSALD 1284
Cdd:cd03266 163 PTTGLD 168
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
454-677 |
1.51e-19 |
|
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: 88.97 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIG 533
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPvlfsttIAENIRYGREDATMEDIVQAAKEANAYNFI------MDLPQQFDTLVgeggGQMSGGQKQRVAIARAL 607
Cdd:cd03265 77 IVFQDL------SVDDELTGWENLYIHARLYGVPGAERRERIdelldfVGLLEAADRLV----KTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 608 IRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 677
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
789-1084 |
1.79e-19 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 90.19 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 789 MLVGSVGAAVnGTVTPLYAflfSQILGTFSipDKEEQRSQINGVCLLFVamgcVSLFTQFLQGYAFAKSGELLTKRLRKF 868
Cdd:cd18551 5 LLLSLLGTAA-SLAQPLLV---KNLIDALS--AGGSSGGLLALLVALFL----LQAVLSALSSYLLGRTGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 869 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 948
Cdd:cd18551 75 LWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 949 GATQTRMLTGfASRDKQalEMVGQIT---NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCI 1025
Cdd:cd18551 153 ILPLGRRIRK-ASKRAQ--DALGELSaalERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 1026 MFIANSASYRYGGYLISNEGLHFS-------YVFRVISAVvlsaTALGRAFSytpSYAKAKISAAR 1084
Cdd:cd18551 230 VQLALLVVLGVGGARVASGALTVGtlvafllYLFQLITPL----SQLSSFFT---QLQKALGALER 288
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1127-1290 |
1.89e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.68 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1127 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIM 1205
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1206 DNIKYGdnTKEIPM-ERVIAAA---KQAQLHDFVM--SLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:PRK10851 93 DNIAFG--LTVLPRrERPNAAAikaKVTQLLEMVQlaHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170
....*....|.
gi 2462578034 1280 TSALDTESEKQ 1290
Cdd:PRK10851 164 FGALDAQVRKE 174
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
457-649 |
2.45e-19 |
|
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: 87.70 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 457 HNVTFHYpsRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniQWLRDQIGIVE 536
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 537 QEP--VLFSTTIAENIRYGREDA--TMEDIVQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsggqkqRVAIAR 605
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELdaGNEQAETVLKDLDLYALKERHPlslsggqKQ------------------RLAIAA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462578034 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAH 649
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITH 184
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1128-1286 |
3.28e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDS---KKVNVQFLRSNIGIVSQEP-VLFACS 1203
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1204 IMDNIKY-----GDNTKEIpMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:PRK10908 96 VYDNVAIpliiaGASGDDI-RRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
....*...
gi 2462578034 1279 ATSALDTE 1286
Cdd:PRK10908 164 PTGNLDDA 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1119-1286 |
3.47e-19 |
|
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: 87.63 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRpdsQVLNGLSVSISPGQTlAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPV 1198
Cdd:cd03264 8 KRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFA-CSIMDNIKYGDNTKEIP----MERVIAAAKQAQLHDFvmslpekYETNVGSqgsqLSRGEKQRIAIARAIVRDPKI 1273
Cdd:cd03264 83 VYPnFTVREFLDYIAWLKGIPskevKARVDEVLELVNLGDR-------AKKKIGS----LSGGMRRRVGIAQALVGDPSI 151
|
170
....*....|...
gi 2462578034 1274 LLLDEATSALDTE 1286
Cdd:cd03264 152 LIVDEPTAGLDPE 164
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
454-680 |
5.33e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.78 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIG 533
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFS-TTIAENIRYG-REDAT-MEDIVQAAKEANAY----NFIMDLPQQFdtlvgegggqmSGGQKQRVAIARA 606
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlRMQKTpAAEITPRVMEALRMvqleEFAQRKPHQL-----------SGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 607 LIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAH----RLSTvraADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
454-710 |
6.01e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.01 E-value: 6.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIG 533
Cdd:COG4152 2 LELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLF-STTIAENIRY-GR-EDATMEDIVQAAKE--------ANAYNFIMDLP---QQfdtlvgegggqmsggqkq 599
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlARlKGLSKAEAKRRADEwlerlglgDRANKKVEELSkgnQQ------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 600 RVAIARALIRNPKILLLDMATSALD--NeSEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 676
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDpvN-VELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDE 215
|
250 260 270
....*....|....*....|....*....|....
gi 2462578034 677 LLERKGVYFTLVTLQSQGNQALNEEDIKDATEDD 710
Cdd:COG4152 216 IRRQFGRNTLRLEADGDAGWLRALPGVTVVEEDG 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
454-660 |
6.47e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.63 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--DIRSLNiQWLRDQ 531
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPR-DAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFST-TIAENIRYGREDATME--DIVQAAKE----ANAYNF-------IMDLP---QQfdtlvgegggqms 594
Cdd:COG3845 82 IGMVHQHFMLVPNlTVAENIVLGLEPTKGGrlDRKAARARirelSERYGLdvdpdakVEDLSvgeQQ------------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 595 ggqkqRVAIARALIRNPKILLLDMATSAL-DNESE-------AMVQEvlskiqhGHTIISVAHRLSTVRA-ADTI 660
Cdd:COG3845 149 -----RVEILKALYRGARILILDEPTAVLtPQEADelfeilrRLAAE-------GKSIIFITHKLREVMAiADRV 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1126-1307 |
9.82e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.41 E-value: 9.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF---YDPD---QGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL 1199
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 FA-CSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDfvMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462578034 1279 ATSALDTESEK--QPCCDHLDK-------SHTPQMAEQ 1307
Cdd:PRK14246 180 PTSMIDIVNSQaiEKLITELKNeiaivivSHNPQQVAR 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1127-1284 |
1.21e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.98 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1127 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH--DSKKVNVQFLRSNIGIVSQEP--VLFAC 1202
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDPdnQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 SIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKyetnvgsQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1282
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
..
gi 2462578034 1283 LD 1284
Cdd:PRK13636 172 LD 173
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1128-1286 |
1.56e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.73 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKV-----MIDGHDS---KKVNVQFLRSNIGIVSQE 1196
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ---PEAGTIrvgdiTIDTARSlsqQKGLIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 PVLFAC-SIMDNIKYGDN-TKEIPMERVIAAAKQaqlhdfvmsLPEKyetnVGSQGSQ------LSRGEKQRIAIARAIV 1268
Cdd:PRK11264 94 FNLFPHrTVLENIIEGPViVKGEPKEEATARARE---------LLAK----VGLAGKEtsyprrLSGGQQQRVAIARALA 160
|
170
....*....|....*...
gi 2462578034 1269 RDPKILLLDEATSALDTE 1286
Cdd:PRK11264 161 MRPEVILFDEPTSALDPE 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1125-1289 |
1.71e-18 |
|
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: 84.02 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1125 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvnvqflrsnigivsqEPVLFAcSI 1204
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFA-SP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYGdntkeipmervIAaakqaqlhdFVMslpekyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSAL- 1283
Cdd:cd03216 70 RDARRAG-----------IA---------MVY---------------QLSVGERQMVEIARALARNARLLILDEPTAALt 114
|
....*.
gi 2462578034 1284 DTESEK 1289
Cdd:cd03216 115 PAEVER 120
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1120-1284 |
1.87e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.84 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSRPDSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFLRSNIGIVSQEPV 1198
Cdd:COG4525 12 RYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRGVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFA-CSIMDNIKYGdntkeIPMERVIAAAKQAQLHDFVmslpekyeTNVGSQG------SQLSRGEKQRIAIARAIVRDP 1271
Cdd:COG4525 87 LLPwLNVLDNVAFG-----LRLRGVPKAERRARAEELL--------ALVGLADfarrriWQLSGGMRQRVGIARALAADP 153
|
170
....*....|...
gi 2462578034 1272 KILLLDEATSALD 1284
Cdd:COG4525 154 RFLLMDEPFGALD 166
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
468-680 |
1.89e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 468 EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLF 542
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 ST-TIAENIRYGREdatMEDIVQAAKEANA-YNFIMDLPQQFDTL---VGEGGGQMSGGQKQRVAIARALIRNPKILLLD 617
Cdd:PRK14247 95 PNlSIFENVALGLK---LNRLVKSKKELQErVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 618 MATSALDNESEAMVQEVLSKIQHGHTIISVAH-RLSTVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1126-1284 |
2.22e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.74 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNvQFLRSnIGIVSQEPVLFA-CS 1203
Cdd:PRK11607 30 DGQhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP-INMMFQSYALFPhMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1204 IMDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:PRK11607 108 VEQNIAFGLKQDKLPkaeiASRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
....*
gi 2462578034 1280 TSALD 1284
Cdd:PRK11607 177 MGALD 181
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
822-1084 |
2.31e-18 |
|
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: 87.10 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 822 KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQ 901
Cdd:cd18542 31 GGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 902 VQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGatqTRMLTGFASRDKQALEMVGQITN---EAL 978
Cdd:cd18542 109 IRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFS---YVFFKKVRPAFEEIREQEGELNTvlqENL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 979 SNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHF-------SYV 1051
Cdd:cd18542 186 TGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLgelvafiSYL 265
|
250 260 270
....*....|....*....|....*....|...
gi 2462578034 1052 FRVISAVvlsaTALGRAFSytpSYAKAKISAAR 1084
Cdd:cd18542 266 WMLIWPV----RQLGRLIN---DMSRASASAER 291
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1126-1283 |
2.42e-18 |
|
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: 85.18 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFA-CS 1203
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHERARAGIGYVPEGRRIFPeLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1204 IMDNIKYGdntkeipMERVIAAAKQAQLhDFVMSL-PEKYEtNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1282
Cdd:cd03224 92 VEENLLLG-------AYARRRAKRKARL-ERVYELfPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
.
gi 2462578034 1283 L 1283
Cdd:cd03224 163 L 163
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
463-661 |
3.80e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 463 YPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlrdQIGIVEQEPVlf 542
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ----RSEVPDSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 stTIAENI------------RYGREDatmEDIVQAAKEANAynfIMDL-PQQFDTLvgegggqmSGGQKQRVAIARALIR 609
Cdd:NF040873 73 --TVRDLVamgrwarrglwrRLTRDD---RAAVDDALERVG---LADLaGRQLGEL--------SGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 610 NPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRAADTII 661
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCV 189
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1128-1287 |
4.36e-18 |
|
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: 84.79 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDgHDSKKVNV------QFL---RSNIGIVSQ--- 1195
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLaqasprEILalrRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1196 ------------EPVLfacsimdnikygdntkEIPMERVIAAAKQAQLHDFvMSLPEK----YETNvgsqgsqLSRGEKQ 1259
Cdd:COG4778 104 viprvsaldvvaEPLL----------------ERGVDREEARARARELLAR-LNLPERlwdlPPAT-------FSGGEQQ 159
|
170 180
....*....|....*....|....*...
gi 2462578034 1260 RIAIARAIVRDPKILLLDEATSALDTES 1287
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAAN 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
474-680 |
4.55e-18 |
|
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: 87.46 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 474 DLNMAIKPGEMTALVGPSGAGKSTALQLI---QRfydPCEGMVTVDGH---DIRSLniQWL---RDQIGIVEQEPVLFST 544
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEvlqDSARG--IFLpphRRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 545 -TIAENIRYGREdatmedivQAAKEANAYNF--IMDL----------P-------QQfdtlvgegggqmsggqkqRVAIA 604
Cdd:COG4148 92 lSVRGNLLYGRK--------RAPRAERRISFdeVVELlgighlldrrPatlsggeRQ------------------RVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 605 RALIRNPKILLLDMATSALDNESEamvQEVLSKIQ--HGHT---IISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 678
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARK---AEILPYLErlRDELdipILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
..
gi 2462578034 679 ER 680
Cdd:COG4148 223 SR 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1121-1290 |
4.92e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1121 YPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkVNVQFLRSNIGIVSQ-EPVL 1199
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVVFQnEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 FACSIMDNIKYGDNTKEIPMERVIAAAKQAQlhdfvmslpekyeTNVGSQGS------QLSRGEKQRIAIARAIVRDPKI 1273
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQML-------------KKVGLEGAekryiwQLSGGQRQRVGIARALAANPQL 149
|
170
....*....|....*..
gi 2462578034 1274 LLLDEATSALDTESEKQ 1290
Cdd:PRK11248 150 LLLDEPFGALDAFTREQ 166
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1112-1284 |
5.56e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 85.14 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGK-VMIDGHDSKKVNVQFLRSNI 1190
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1191 GIVSQEpvlfacsIMDNIKYGDNTKEI--------------PMERVIAAAKQAqLHDFVMSlpEKYETNVGSqgsqLSRG 1256
Cdd:COG1119 81 GLVSPA-------LQLRFPRDETVLDVvlsgffdsiglyrePTDEQRERAREL-LELLGLA--HLADRPFGT----LSQG 146
|
170 180
....*....|....*....|....*...
gi 2462578034 1257 EKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLD 174
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1134-1284 |
6.04e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.63 E-value: 6.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1134 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIMDNIKYG- 1211
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 1212 ------DNTKEIPMERViaaAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK10771 97 npglklNAAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
454-680 |
7.77e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 86.32 E-value: 7.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYP--------SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN- 524
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 525 --IQWLRDQIGIVEQEPvlFS---------TTIAENIRY-------GREDATME--DIVQAAKE-ANAYnfimdlPQQFd 583
Cdd:COG4608 88 reLRPLRRRMQMVFQDP--YAslnprmtvgDIIAEPLRIhglaskaERRERVAEllELVGLRPEhADRY------PHEFs 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 584 tlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVR-AADTI 660
Cdd:COG4608 160 gg-----------qrqRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQdeLGLTYLFISHDLSVVRhISDRV 228
|
250 260
....*....|....*....|
gi 2462578034 661 IGFEHGTAVERGTHEELLER 680
Cdd:COG4608 229 AVMYLGKIVEIAPRDELYAR 248
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1126-1284 |
8.46e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.51 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQ-----GKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1198
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNiySPDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFA-CSIMDNIKYG-------DNTKEIPmERVIAAAKQAQLHDFVMSLPEKYETNvgsqgsqLSRGEKQRIAIARAIVRD 1270
Cdd:PRK14267 96 PFPhLTIYDNVAIGvklnglvKSKKELD-ERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALAMK 167
|
170
....*....|....
gi 2462578034 1271 PKILLLDEATSALD 1284
Cdd:PRK14267 168 PKILLMDEPTANID 181
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1124-1284 |
1.05e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1124 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN----------VQFL------- 1186
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1187 ---RSNIGIVSQEPVLFACSImdnikygdnTKEIPMERVIAAAKQAQLHDFVMS-LPEkyetnvgsqgsQLSRGEKQRIA 1262
Cdd:PRK10419 102 vnpRKTVREIIREPLRHLLSL---------DKAERLARASEMLRAVDLDDSVLDkRPP-----------QLSGGQLQRVC 161
|
170 180
....*....|....*....|..
gi 2462578034 1263 IARAIVRDPKILLLDEATSALD 1284
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLD 183
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1134-1284 |
1.59e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.63 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1134 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS----NIGIVSQEPVLFA-CSIMDNI 1208
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1209 KYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK10070 128 AFGMELAGINaeerREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1112-1289 |
1.61e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.03 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1191
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPV-LFACSIMD-NIKYGDNTKEIPMERVIAAAKQAqLHDFVMSLPEKYETNvgsqgsQLSRGEKQRIAIARAIVR 1269
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRRVSEA-LKQVDMLERADYEPN------ALSGGQKQRVAIAGVLAL 159
|
170 180
....*....|....*....|
gi 2462578034 1270 DPKILLLDEATSALDTESEK 1289
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQ 179
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
454-651 |
1.94e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.09 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTF---HYPSRpevkilndLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRD 530
Cdd:PRK10771 2 LKLTDITWlyhHLPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFS-TTIAENIRYG---------REDATMEDIvqaAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQR 600
Cdd:PRK10771 72 PVSMLFQENNLFShLTVAQNIGLGlnpglklnaAQREKLHAI---ARQMGIEDLLARLPGQL-----------SGGQRQR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 601 VAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSKIQhgHTIISVAHRL 651
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQ--LTLLMVSHSL 190
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
452-650 |
2.07e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.56 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYPS-RPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDiRSLniqwlrd 530
Cdd:COG4178 361 GALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-RVL------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 qigIVEQEPVLFSTTIAENIRY--GREDATMEDIVQAAKEANaynfimdLP--------------------QQfdtlvge 588
Cdd:COG4178 430 ---FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGhlaerldeeadwdqvlslgeQQ------- 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 589 gggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR 650
Cdd:COG4178 493 -----------RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1126-1284 |
2.47e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 81.94 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvNVQFL-RSNIGIVSQEPVLF-ACS 1203
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-----PLDIAaRNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1204 IMDNIKYGDNTKEIPMErviAAAKQAQ--LHDFvmSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1281
Cdd:cd03269 87 VIDQLVYLAQLKGLKKE---EARRRIDewLERL--ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
...
gi 2462578034 1282 ALD 1284
Cdd:cd03269 158 GLD 160
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1119-1290 |
2.65e-17 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 88.08 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYpSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvnvqflrsNIGIVSQEPV 1198
Cdd:TIGR00957 644 FTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFACSIMDNIKYGDNTKEIPMERVIAAAkqAQLHDFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:TIGR00957 710 IQNDSLRENILFGKALNEKYYQQVLEAC--ALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170
....*....|..
gi 2462578034 1279 ATSALDTESEKQ 1290
Cdd:TIGR00957 787 PLSAVDAHVGKH 798
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
453-673 |
3.36e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.29 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 453 EIEFHNVTFHYPSRPEVKilnDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQ- 526
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 527 -WLRDQIGIVEQEPVLFSTTIAENIRYGRE----DATMEDIVQAA-KEANAYNFIMD-LPQQFDTLvgegggqmSGGQKQ 599
Cdd:PRK14243 87 vEVRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSlRQAALWDEVKDkLKQSGLSL--------SGGQQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 673
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1128-1284 |
3.45e-17 |
|
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: 82.21 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVqFLRSNIGI--VSQEPVLF-ACSI 1204
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIK-----YGDNTKEIpMERViaaakQAQLHDFvmslpeKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:cd03218 93 EENILavleiRGLSKKER-EEKL-----EELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
....*
gi 2462578034 1280 TSALD 1284
Cdd:cd03218 161 FAGVD 165
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
824-1029 |
3.51e-17 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 83.69 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 824 EQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQ 903
Cdd:cd18575 30 GNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 904 GAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPF----LALSGATQTRMltgfaSRDKQ-ALEMVGQITNEAL 978
Cdd:cd18575 108 TVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLvvlpIILFGRRVRRL-----SRASQdRLADLSAFAEETL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 979 SNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIA 1029
Cdd:cd18575 183 SAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGA 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
474-681 |
3.60e-17 |
|
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: 84.78 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 474 DLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRS------LNIQwlRDQIGIVEQEPVLFS-TTI 546
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPE--KRRIGYVFQEARLFPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 547 AENIRYGREDATMEDiVQAAKEAnaynfIMDLpQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE 626
Cdd:TIGR02142 93 RGNLRYGMKRARPSE-RRISFER-----VIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 627 SEAMVQEVLSKIqHGHT---IISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:TIGR02142 166 RKYEILPYLERL-HAEFgipILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
454-677 |
3.81e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.20 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVkiLNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL--RDQ 531
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEP--VLFSTTIAENIRYG------REDATMEDIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 603
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 677
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
454-624 |
4.44e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.37 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTfhyPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlRD-QI 532
Cdd:PRK10851 3 IEIANIK---KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDrKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLFS-TTIAENIRYG------REDATME----------DIVQAAKEANAYnfimdlPQQFdtlvgegggqmSG 595
Cdd:PRK10851 77 GFVFQHYALFRhMTVFDNIAFGltvlprRERPNAAaikakvtqllEMVQLAHLADRY------PAQL-----------SG 139
|
170 180
....*....|....*....|....*....
gi 2462578034 596 GQKQRVAIARALIRNPKILLLDMATSALD 624
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1128-1284 |
5.54e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 82.55 E-value: 5.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN----------VQFL----------R 1187
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqrrafrrdVQLVfqdspsavnpR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1188 SNIGIVSQEPvlfacsiMDNIKYGDNTKEipMERVIAAAKQAQLHDFVMS-LPEkyetnvgsqgsQLSRGEKQRIAIARA 1266
Cdd:TIGR02769 105 MTVRQIIGEP-------LRHLTSLDESEQ--KARIAELLDMVGLRSEDADkLPR-----------QLSGGQLQRINIARA 164
|
170
....*....|....*...
gi 2462578034 1267 IVRDPKILLLDEATSALD 1284
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLD 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
454-678 |
6.16e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpEVKILNDLNMAIKPGEMTALVGPSGAGKST-ALQLiQRFYDPCEGMVTVDGHDIRSLN-IQWLRDQ 531
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTlALHL-NGLLRPQKGKVLVSGIDTGDFSkLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEP--VLFSTTIAENIRYGREDATMEDIV------QAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAI 603
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEirkrvdRALAEIGLEKYRHRSPKTLS-----------GGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1126-1290 |
6.61e-17 |
|
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: 81.26 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD----SKKVnvqflRSNIGIVSQEPVLfa 1201
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvrePREV-----RRRIGIVFQDLSV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 csimDNIKYGDNTKEI-----PMERVIAAAKQAQLHDFvMSLPEKYETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:cd03265 85 ----DDELTGWENLYIharlyGVPGAERRERIDELLDF-VGLLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFL 155
|
170
....*....|....
gi 2462578034 1277 DEATSALDTESEKQ 1290
Cdd:cd03265 156 DEPTIGLDPQTRAH 169
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1129-1288 |
6.73e-17 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 81.33 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQfLRSNIGIVS--QEPVLFA-CSIM 1205
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPeLTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1206 DNI--------KYGDNTKEIPMERVIAAAKQAQLHDFVmSLPEKYETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLD 1277
Cdd:cd03219 94 ENVmvaaqartGSGLLLARARREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170
....*....|..
gi 2462578034 1278 EATSAL-DTESE 1288
Cdd:cd03219 169 EPAAGLnPEETE 180
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
468-667 |
7.14e-17 |
|
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: 81.33 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 468 EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDgHDIRSLNI------QWL---RDQIGIVEQe 538
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLaqasprEILalrRRTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 539 pvlFSTTI---------AENIRygrEDATMEDIVQA-AKEANAYnfiMDLP---------------QQfdtlvgegggqm 593
Cdd:COG4778 101 ---FLRVIprvsaldvvAEPLL---ERGVDREEARArARELLAR---LNLPerlwdlppatfsggeQQ------------ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 594 sggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGT 667
Cdd:COG4778 160 ------RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIeEAKARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
449-678 |
9.80e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 449 RIKGEiefhNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL 528
Cdd:PRK10253 7 RLRGE----QLTLGYGKY---TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 529 RDQIGIVEQEPVL-FSTTIAENIRYGR------------EDatmEDIVQAAKEANAynfIMDLP-QQFDTLvgegggqmS 594
Cdd:PRK10253 80 ARRIGLLAQNATTpGDITVQELVARGRyphqplftrwrkED---EEAVTKAMQATG---ITHLAdQSVDTL--------S 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 595 GGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVER 671
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQ 225
|
....*..
gi 2462578034 672 GTHEELL 678
Cdd:PRK10253 226 GAPKEIV 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
454-679 |
9.93e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 9.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHY-PSRP-EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQW 527
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 528 LRDQIGIVEQEP--VLFSTTIAENIRYGREDATMEDiVQAAKEANAYNFIMDLPQQFdtlVGEGGGQMSGGQKQRVAIAR 605
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPK-EKAEKIAAEKLEMVGLADEF---WEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1128-1286 |
1.15e-16 |
|
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: 79.95 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdSKKVNVQFLRSNIGIVSQEPVLF-ACSIMD 1206
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG--KSYQKNIEALRRIGALIEAPGFYpNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1207 NIKYGDNTKEIPMERViaaakqAQLHDFV-MSLPEKYETnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDT 1285
Cdd:cd03268 92 NLRLLARLLGIRKKRI------DEVLDVVgLKDSAKKKV------KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
.
gi 2462578034 1286 E 1286
Cdd:cd03268 160 D 160
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1111-1290 |
1.19e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.13 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1111 KIDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG----HDSKKVNVQ 1184
Cdd:PRK13646 2 TIRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1185 FLRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERVIAAAkqaqlHDFVMSLpeKYETNVGSQGS-QLSRGEKQRI 1261
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDL--GFSRDVMSQSPfQMSGGQMRKI 154
|
170 180
....*....|....*....|....*....
gi 2462578034 1262 AIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQ 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1112-1290 |
1.20e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.71 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPS-RP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG----HDSKKVNVQF 1185
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQaQLHDFVMSlPEKYETNvgsqGSQLSRGEKQRIAI 1263
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALARE-KLALVGIS-ESLFEKN----PFELSGGQMRRVAI 156
|
170 180
....*....|....*....|....*..
gi 2462578034 1264 ARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKE 183
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1119-1284 |
1.30e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 81.42 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPS----RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL-------- 1186
Cdd:COG4167 14 FKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRckhirmif 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1187 ---------RSNIGIVSQEPVLFacsimdnikygdNTKEIPMER---VIAAAKQAQLhdfvmsLPEkyETNVGSQgsQLS 1254
Cdd:COG4167 94 qdpntslnpRLNIGQILEEPLRL------------NTDLTAEEReerIFATLRLVGL------LPE--HANFYPH--MLS 151
|
170 180 190
....*....|....*....|....*....|
gi 2462578034 1255 RGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALD 181
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1112-1284 |
1.51e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIG 1191
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVL-FACSIMDNI-----KYGDNTKEIpmERVIAAakqaqLHDFVmSLPEKYETNVgsqgSQLSRGEKQRIAIAR 1265
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLlvfgrYFGMSTREI--EAVIPS-----LLEFA-RLESKADARV----SDLSGGMKRRLTLAR 185
|
170
....*....|....*....
gi 2462578034 1266 AIVRDPKILLLDEATSALD 1284
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLD 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
470-678 |
1.78e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 470 KILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVL-FSTTIAE 548
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 549 NIRYGR------------EDatmEDIVQAAKEANaynfimdlpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLL 616
Cdd:PRK11231 96 LVAYGRspwlslwgrlsaED---NARVNQAMEQT----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 617 DMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
455-661 |
1.82e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.45 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 455 EFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGHDIRSLNIQwlRDQ 531
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFS-TTIAENIRYG---------REDAtmedIVQAAKEANAYNFIMDLPqqfDTLvgegggqmSGGQKQRV 601
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLAFAlpptigraqRRAR----VEQALEEAGLAGFADRDP---ATL--------SGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 602 AIARALIRNPKILLLDMATSALDNESEAMVQE-VLSKI-QHGHTIISVAHRLSTVRAADTII 661
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIrQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1128-1284 |
2.16e-16 |
|
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: 79.62 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQFlrsNIGIVSQEPVLFAC-S 1203
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQK---CVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1204 IMDNIKYgdnTKEIPMeRVIAAAKQAQLHDFVMSLPEKYETNVGSQG-SQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1282
Cdd:cd03234 98 VRETLTY---TAILRL-PRKSSDAIRKKRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
..
gi 2462578034 1283 LD 1284
Cdd:cd03234 174 LD 175
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-678 |
2.19e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------DIRSLNIQWLRDQIGIVEQEPVLFS- 543
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 544 TTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSAL 623
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 624 DNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
812-1043 |
2.34e-16 |
|
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: 81.30 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 812 QILGTF--SIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPG 889
Cdd:cd18541 20 RIIGRAidALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQ--KNRTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 890 ALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTgfaSRDKQALEM 969
Cdd:cd18541 98 DLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIH---KRFRKVQEA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 970 VGQITN---EALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISN 1043
Cdd:cd18541 175 FSDLSDrvqESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIR 251
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1111-1284 |
2.43e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.20 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1111 KIDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERFYDpdqGKVMIDGhdsKKVN-VQFL 1186
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrMVAGLERITS---GEIWIGG---RVVNeLEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1187 RSNIGIVSQEPVLFA-CSIMDNIKYG-DNTK----EIpMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQR 1260
Cdd:PRK11650 75 DRDIAMVFQNYALYPhMSVRENMAYGlKIRGmpkaEI-EERVAEAARILELEPLLDRKP-----------RELSGGQRQR 142
|
170 180
....*....|....*....|....
gi 2462578034 1261 IAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
172-394 |
3.13e-16 |
|
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: 80.89 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 172 MIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQM 251
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 252 ALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIgaatiglSVSKFTDYELKAYAKA-GVVAD------EVISSMRT 324
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL-------ATYLFRKKSRKAYREVrEKLSRlnaflqESISGMSV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 325 VAAFGGEKREVERYEK---NLVFAQRWGIRkgiVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18544 193 IQLFNREKREFEEFDEinqEYRKANLKSIK---LFALFRPLVELLSSLALALVLWYGGGQVLS-GAVTLGVLY 261
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
202-398 |
3.40e-16 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 80.85 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 202 ARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTI--CGFLLGFfrGWKLTLVI 279
Cdd:cd18590 65 SRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLgmLGFMLSL--SWQLTLLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 280 ISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFF 359
Cdd:cd18590 143 LIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVY 222
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462578034 360 TGFVWCLIFLCYALAFWYGSTLvLDEGEYTPGTLVQIFL 398
Cdd:cd18590 223 LLVRRVLQLGVQVLMLYCGRQL-IQSGHLTTGSLVSFIL 260
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
471-679 |
3.77e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKSTA----LQLIqrfydPCEGMVTVDGHDIRSLNIQWL---RDQIGIVEQEP---- 539
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 540 -----VLfsTTIAENIRY--------GRED---ATMEDIVQAAKEANAYnfimdlPQQFdtlvgegggqmSGGQKQRVAI 603
Cdd:PRK15134 376 nprlnVL--QIIEEGLRVhqptlsaaQREQqviAVMEEVGLDPETRHRY------PAEF-----------SGGQRQRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTI--ISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
454-677 |
4.04e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.13 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVK---ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW-LR 529
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 530 DQIGIVEQEP--VLFSTTIAENIRYGRE------DATMEDIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRV 601
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPEnlgippEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 602 AIARALIRNPKILLLDMATSALDNESEamvQEVLSKIQ-----HGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEE 676
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGR---REVVNTIKelnkkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
.
gi 2462578034 677 L 677
Cdd:PRK13633 231 I 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
454-675 |
4.09e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------DIRSLNIQW 527
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 528 LRDQIGIVEQEPVLFS-TTIAENIRygreDATME----DIVQAAKEAN-----------AYNFIMDLP--QQfdtlvgeg 589
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLI----EAPCRvlglSKDQALARAEkllerlrlkpyADRFPLHLSggQQ-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 590 ggqmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVR-AADTIIGFEHGT 667
Cdd:PRK11124 148 ---------QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARkTASRVVYMENGH 218
|
....*...
gi 2462578034 668 AVERGTHE 675
Cdd:PRK11124 219 IVEQGDAS 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1129-1284 |
4.23e-16 |
|
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: 80.28 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDqGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 1208
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 1209 K-YGDNTKEipmeRVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:cd03289 98 DpYGKWSDE----EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
469-660 |
4.44e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 469 VKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIGI--VEQEPVLF-STT 545
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 546 IAENIRYG--REDATMEDIVQAAKEANAYnfiMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPKILLLDMATSAL 623
Cdd:PRK15439 103 VKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSL--------EVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462578034 624 D-NESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTI 660
Cdd:PRK15439 172 TpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRI 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1119-1287 |
5.06e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqfLRsnIGIVSQEPV 1198
Cdd:COG0488 6 KSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFA-CSIMDNIKYGDN---TKEIPMERVIAA--------AKQAQLHDFVMSL-------------------PEKYETNVG 1247
Cdd:COG0488 72 LDDdLTVLDTVLDGDAelrALEAELEELEAKlaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDLDRPVS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462578034 1248 SqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1287
Cdd:COG0488 152 E----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1127-1284 |
5.18e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1127 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF---LRSN-IGIVSQ-EPVLFA 1201
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNIKygdntkeipMERVIAAAKQAQLHD--FVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:PRK11629 102 FTALENVA---------MPLLIGKKKPAEINSraLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
....*
gi 2462578034 1280 TSALD 1284
Cdd:PRK11629 173 TGNLD 177
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
180-399 |
5.18e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 80.25 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQM-ALFIQRM 258
Cdd:cd18563 50 AGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLpDFLTNIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 259 TSTICGFLLgFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAK-AGVVADeVISSMRTVAAFGGEKREVER 337
Cdd:cd18563 130 MIIGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRlNSVLND-TLPGIRVVKAFGQEKREIKR 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 338 YEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQiFLS 399
Cdd:cd18563 208 FDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLS-GTMTLGTLVA-FLS 267
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1105-1284 |
5.65e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 83.81 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1105 WDNfQGKIDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDqGKVMIDGHDSKKVNVQ 1184
Cdd:TIGR01271 1212 WPS-GGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1185 FLRSNIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIA 1264
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLA 1365
|
170 180
....*....|....*....|
gi 2462578034 1265 RAIVRDPKILLLDEATSALD 1284
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLD 1385
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
454-678 |
6.25e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.97 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST-TIAENIRYGR----------EDatmEDIVQaakEANAYNFIMDLPQQF-DTLvgegggqmsggqkqRV 601
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFGRfpyskgrltaED---REIID---EAIAYLDLEDLADRYlDELsgg--------qrqRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 602 AIARALIRNPKILLLDMATSALD-NESEAMVQeVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 677
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMK-LLRRLadELGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEI 223
|
.
gi 2462578034 678 L 678
Cdd:COG4604 224 I 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
458-678 |
7.08e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.24 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL-------------N 524
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 525 IQWLRDQIGIVEQEPVLFS-TTIAENIrygredatMEDIVQA-------AKEANAynFIMDLPQQFDTLVGEGGGQMSGG 596
Cdd:PRK10619 87 LRLLRTRLTMVFQHFNLWShMTVLENV--------MEAPIQVlglskqeARERAV--KYLAKVGIDERAQGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 597 QKQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQH----GHTIISVAHRLSTVRAADTIIGFEH-GTAVER 671
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQlaeeGKTMVVVTHEMGFARHVSSHVIFLHqGKIEEE 233
|
....*..
gi 2462578034 672 GTHEELL 678
Cdd:PRK10619 234 GAPEQLF 240
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-399 |
7.11e-16 |
|
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: 79.86 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 179 YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQ-MALFIQr 257
Cdd:cd18564 60 LVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGvLPLLTN- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 258 mTSTICGFL-LGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVE 336
Cdd:cd18564 139 -LLTLVGMLgVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEER 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 337 RYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVqIFLS 399
Cdd:cd18564 218 RFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLA-GRLTPGDLL-VFLA 278
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-681 |
7.89e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.65 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 533
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVL-FSTTIAENI----RYGREDA-TMEDIVQAAKEanaynfIMDLPQQFDTLVGEGGGQMSGgqkqRVAIARAL 607
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLlvfgRYFGMSTrEIEAVIPSLLE------FARLESKADARVSDLSGGMKR----RLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 608 IRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
454-679 |
7.94e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVkilNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLRdQIG 533
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQR-PIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFS-TTIAENIRYG-REDATMEDIVQAAKE-----ANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIARA 606
Cdd:PRK11607 95 MMFQSYALFPhMTVEQNIAFGlKQDKLPKAEIASRVNemlglVHMQEFAKRKPHQLS-----------GGQRQRVALARS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 607 LIRNPKILLLDMATSALDNE-SEAMVQEVLSKIQH-GHTIISVAH-RLSTVRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
454-667 |
7.95e-16 |
|
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: 75.56 E-value: 7.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVdGHDIRslniqwlrdqIG 533
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQepvlFSttiaeniryGREDAtmedivqaakeanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03221 67 YFEQ----LS---------GGEKM------------------------------------------RLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 614 LLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAH-R--LSTVraADTIIGFEHGT 667
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1129-1284 |
8.83e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.90 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQ---FLRS-NIGIVSQE----PVLF 1200
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAkHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1201 AcsiMDNIKY-----GDNTKEiPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILL 1275
Cdd:PRK10584 105 A---LENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169
|
....*....
gi 2462578034 1276 LDEATSALD 1284
Cdd:PRK10584 170 ADEPTGNLD 178
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
454-654 |
8.94e-16 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 76.90 E-value: 8.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVK-ILNDLNMAIKPGEMTALVGPSGAGKSTALQ-LIQRFYD-PCEGMVTVDGhdiRSLNIQWLRd 530
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAgVITGEILING---RPLDKNFQR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFST-TIAENIRYgreDATMEDIVQAAKEanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIR 609
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALRF---SALLRGLSVEQRK-------------------------------RLTIGVELAA 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462578034 610 NPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV 654
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSAS 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
468-672 |
9.54e-16 |
|
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: 77.26 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 468 EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLRdQIGIVEQEPVLFST-TI 546
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALR-RIGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 547 AENIR-----YGREDATME---DIV----QAAKEANAYNFIMdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKIL 614
Cdd:cd03268 90 RENLRllarlLGIRKKRIDevlDVVglkdSAKKKVKGFSLGM---KQ------------------RLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 615 LLDMATSALDNESEAMVQE-VLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERG 672
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRElILSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
465-678 |
1.05e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 465 SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVL-FS 543
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 544 TTIAENIRYGR---------EDATMEDIVQAAKEANAYNFIMDLPqqFDTLvgegggqmSGGQKQRVAIARALIRNPKIL 614
Cdd:PRK09536 92 FDVRQVVEMGRtphrsrfdtWTETDRAAVERAMERTGVAQFADRP--VTSL--------SGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 615 LLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK09536 162 LLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
458-681 |
1.10e-15 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 77.95 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL-RDQIGIVE 536
Cdd:TIGR03410 5 NLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 537 QEPVLFST-TIAENIRYGREdatmediVQAAKEANAYNFIMDL-P-----------------QQfdtlvgegggqmsggq 597
Cdd:TIGR03410 82 QGREIFPRlTVEENLLTGLA-------ALPRRSRKIPDEIYELfPvlkemlgrrggdlsggqQQ---------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 598 kqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTH 674
Cdd:TIGR03410 139 --QLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAG 216
|
....*..
gi 2462578034 675 EELLERK 681
Cdd:TIGR03410 217 DELDEDK 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1128-1286 |
1.33e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.09 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-------------SKKVNVQFLRSNIGIVS 1194
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1195 QEPVLFacSIMDNIkygDNTKEIPMErVIAAAKQAQLHDFVmslpeKYETNVG----SQG---SQLSRGEKQRIAIARAI 1267
Cdd:PRK10619 99 QHFNLW--SHMTVL---ENVMEAPIQ-VLGLSKQEARERAV-----KYLAKVGiderAQGkypVHLSGGQQQRVSIARAL 167
|
170
....*....|....*....
gi 2462578034 1268 VRDPKILLLDEATSALDTE 1286
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPE 186
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
819-1046 |
1.52e-15 |
|
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: 78.97 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 819 IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATD 898
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTND 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 899 ASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGAT-QTRMLTGF-ASRDKQAlEMVGQItNE 976
Cdd:cd18544 108 TEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLfRKKSRKAYrEVREKLS-RLNAFL-QE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 977 ALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 1046
Cdd:cd18544 186 SISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAV 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1128-1290 |
1.52e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPDQGKVMIDGHDSKKVNVQFL---RSNIGIVSQEPV------ 1198
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNsslnpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFACSIMDN---IKYGDNTKEIPMERVIAAAKQAQLHdfvmslPE---KYEtnvgsqgSQLSRGEKQRIAIARAIVRDPK 1272
Cdd:PRK15134 379 LNVLQIIEEglrVHQPTLSAAQREQQVIAVMEEVGLD------PEtrhRYP-------AEFSGGQRQRIAIARALILKPS 445
|
170
....*....|....*...
gi 2462578034 1273 ILLLDEATSALDTESEKQ 1290
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQ 463
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1126-1290 |
2.09e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH--DSKKVNVQFLRSNIGIVSQEP--VLFA 1201
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNIKYGDNTKEIPMERViaaakqAQLHDFVMSLpekyetnVGSQGSQ------LSRGEKQRIAIARAIVRDPKILL 1275
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEI------TRRVDEALTL-------VDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLL 159
|
170
....*....|....*
gi 2462578034 1276 LDEATSALDTESEKQ 1290
Cdd:PRK13638 160 LDEPTAGLDPAGRTQ 174
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1112-1290 |
2.42e-15 |
|
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: 75.67 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPDS---QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ERFYDPDQGKVMIDGHDSKKVNvqfL 1186
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS---F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1187 RSNIGIVSQEPVLFAC-SIMDNIKYgdntkeipmerviaaakQAQLhdfvmslpekyetnvgsqgSQLSRGEKQRIAIAR 1265
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF-----------------AAKL-------------------RGLSGGERKRVSIAL 124
|
170 180
....*....|....*....|....*
gi 2462578034 1266 AIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQ 149
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
165-565 |
2.93e-15 |
|
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: 80.61 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 165 LLNIESEMIKFASYYAGIAVAVLITGYIQicfwVIAAARQIQ----KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDI 240
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLLSRLAS----QLLLTRLGQhavaRLRLRLSRRILAAPLERLERIGAARLLAALTEDV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 241 NKINDAIAdQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVsplIGIGAATIGLSVSKFtdyeLKAYAKAGVVADEVIS 320
Cdd:COG4615 116 RTISQAFV-RLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL---LGLGVAGYRLLVRRA----RRHLRRAREAEDRLFK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 321 SMRTVaaFGG--------EKRE----------VERYEKNLVFAQRWgirkgivmgFFTGFVW--CLIFLCYALAFWYGST 380
Cdd:COG4615 188 HFRAL--LEGfkelklnrRRRRaffdedlqptAERYRDLRIRADTI---------FALANNWgnLLFFALIGLILFLLPA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 381 LVLDEGEYTPG-TLVQIF----LSVIVGALnlgnasPcleAFATGRAAATSIfETIDRKpiIDCMSEDGYKLDRIK---- 451
Cdd:COG4615 257 LGWADPAVLSGfVLVLLFlrgpLSQLVGAL------P---TLSRANVALRKI-EELELA--LAAAEPAAADAAAPPapad 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 -GEIEFHNVTFHYPSRPEVK--ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL 528
Cdd:COG4615 325 fQTLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 2462578034 529 RDQIGIVEQEPVLFSTTiaenirYGREDATMEDIVQA 565
Cdd:COG4615 405 RQLFSAVFSDFHLFDRL------LGLDGEADPARARE 435
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
467-660 |
3.46e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.97 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 467 PEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYdPC---EGMVTVDGHDIRSLNIqwlRDQ----IGIVEQEP 539
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNI---RDTeragIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 540 VLFST-TIAENIRYGRE--------DATM----EDIVQAAK-EANAYNFIMDLP---QQFdtlvgegggqmsggqkqrVA 602
Cdd:PRK13549 92 ALVKElSVLENIFLGNEitpggimdYDAMylraQKLLAQLKlDINPATPVGNLGlgqQQL------------------VE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 603 IARALIRNPKILLLDMATSALdNESEAmvqEVLSKI-----QHGHTIISVAHRLSTVRA-ADTI 660
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASL-TESET---AVLLDIirdlkAHGIACIYISHKLNEVKAiSDTI 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
452-700 |
4.73e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.36 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYPSRP--EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI-----RSLN 524
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 525 IQWLRDQIGIVEQEP--VLFSTTIAENIRYGREDATmEDIVQAAKEANAYNFIMDLPQQFdtlVGEGGGQMSGGQKQRVA 602
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERG------T 673
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfeifS 240
|
250 260 270
....*....|....*....|....*....|..
gi 2462578034 674 HEELL-----ERKGVYFTLVTLQSQGNQALNE 700
Cdd:PRK13645 241 NQELLtkieiDPPKLYQLMYKLKNKGIDLLNK 272
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
808-1084 |
4.86e-15 |
|
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: 77.05 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 808 FLFSQILGTFSIPD----------KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQD 877
Cdd:cd18548 7 FKLLEVLLELLLPTlmadiidegiANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 878 IAWFDDLrnSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLT 957
Cdd:cd18548 87 FAEIDKF--GTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 958 GFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYG 1037
Cdd:cd18548 165 PLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFG 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 1038 GYLISNEGLHF-------SYVFRVISAVVLSATALGrafsytpSYAKAKISAAR 1084
Cdd:cd18548 245 GHLINAGSLQVgdlvafiNYLMQILMSLMMLSMVFV-------MLPRASASAKR 291
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1123-1290 |
5.17e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.11 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVL-NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqflrSNIGIVSQEPVLFA 1201
Cdd:cd03223 9 ATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFLPQRPYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNIKYgdntkeiPMERViaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATS 1281
Cdd:cd03223 78 GTLREQLIY-------PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
....*....
gi 2462578034 1282 ALDTESEKQ 1290
Cdd:cd03223 121 ALDEESEDR 129
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
823-1278 |
5.28e-15 |
|
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: 79.84 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 823 EEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNSpgALTTRLATDASQV 902
Cdd:COG4615 41 NATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAA--RLLAALTEDVRTI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 903 QGAAgSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFfpfLALSGATQTRMLtgfaSRDKQALEMVGQITNEALSNIR 982
Cdd:COG4615 119 SQAF-VRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL---LGLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 983 TVAGIGKE------RRfiEALeteLEKPFKTAIQKA--------NIYGFCFAFAQCIMFIansasyryggyLIsneGL-- 1046
Cdd:COG4615 191 ALLEGFKElklnrrRR--RAF---FDEDLQPTAERYrdlriradTIFALANNWGNLLFFA-----------LI---GLil 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1047 ----HFSYVF-RVISAVVL----SATALGRAFSYTPSYAKAKISAARFFQL---LDRQPPISVYNTAGEKWDNFQgKIDF 1114
Cdd:COG4615 252 fllpALGWADpAVLSGFVLvllfLRGPLSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLEL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1115 VDCKFTYPSRPDSQ--VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGI 1192
Cdd:COG4615 331 RGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1193 VSQEPVLFacsimDNIkYGDNTKEIPmERVIAAAKQAQLHDFVmslpeKYETNVGSQgSQLSRGEKQRIAIARAIVRDPK 1272
Cdd:COG4615 411 VFSDFHLF-----DRL-LGLDGEADP-ARARELLERLELDHKV-----SVEDGRFST-TDLSQGQRKRLALLVALLEDRP 477
|
....*.
gi 2462578034 1273 ILLLDE 1278
Cdd:COG4615 478 ILVFDE 483
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1120-1290 |
5.59e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.77 E-value: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP-- 1197
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1198 VLFACSIMDNIKYGDNT----KEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKI 1273
Cdd:PRK13652 90 QIFSPTVEQDIAFGPINlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQV 158
|
170
....*....|....*..
gi 2462578034 1274 LLLDEATSALDTESEKQ 1290
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKE 175
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1107-1289 |
6.43e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.97 E-value: 6.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1107 NFQGKIDFVDCKFTYPSRP--DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH----DSKK 1180
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1181 VN-VQFLRSNIGIVSQEP--VLFACSIMDNIKYG-----DNTKEipmerviAAAKQAQLHDFVmSLPEKYetnVGSQGSQ 1252
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvnlgENKQE-------AYKKVPELLKLV-QLPEDY---VKRSPFE 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462578034 1253 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK 1289
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEE 187
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1119-1290 |
7.20e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 76.43 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqflrsnIGIVSQEPV 1198
Cdd:cd03291 42 FSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFACSIMDNIKYGDNTKEIPMERVIaaaKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:cd03291 109 IMPGTIKENIIFGVSYDEYRYKSVV---KACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170
....*....|..
gi 2462578034 1279 ATSALDTESEKQ 1290
Cdd:cd03291 186 PFGYLDVFTEKE 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
454-661 |
7.35e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPE-VKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL---- 528
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 529 RDQIGIVEQEPVLFS-TTIAENIRYgreDATMEDIVQAAKEANAYNFIMDL---------PQQFdtlvgegggqmSGGQK 598
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRLgledrveyqPSQL-----------SGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 599 QRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTII 661
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
456-627 |
7.64e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 7.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 456 FHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhDIRslniqwlrdqIGIV 535
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 536 EQEPVLFST-TIAENIR----------------YGREDATMEDIVQAAK------EANAYNF------IM--------DL 578
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLdgdaelraleaeleelEAKLAEPDEDLERLAElqeefeALGGWEAearaeeILsglgfpeeDL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 579 PQQFDTL-----VgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNES 627
Cdd:COG0488 147 DRPVSELsggwrR-------------RVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1123-1284 |
8.92e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.96 E-value: 8.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL-FA 1201
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNIKYGdntkEIPMERVIAAAKQaqlhdfvmsLPEKYETNVGSQG------SQLSRGEKQRIAIARAIVR------ 1269
Cdd:PRK13548 91 FTVEEVVAMG----RAPHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdg 157
|
170
....*....|....*
gi 2462578034 1270 DPKILLLDEATSALD 1284
Cdd:PRK13548 158 PPRWLLLDEPTSALD 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-679 |
9.55e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.65 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQWL 528
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 529 --RDQIGIVEQEPVLFS-TTIAENIRYG-------REDATMEDIVQ-AAKEANAY----NFIMDLPQQFDtlvgegggqm 593
Cdd:PRK14267 82 evRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDERVEwALKKAALWdevkDRLNDYPSNLS---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 594 sGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR-LSTVRAADTIIGFEHGTAVERG 672
Cdd:PRK14267 152 -GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
....*..
gi 2462578034 673 THEELLE 679
Cdd:PRK14267 231 PTRKVFE 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
470-677 |
9.79e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.05 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 470 KILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN-IQWL--RDQIGIVEQEPvLFSTT- 545
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDP-LASLNp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 546 -------IAENIRYGREDATMEDIVQAAKEANAY-----NFIMDLPQQFdtlvgegggqmSGGQKQRVAIARALIRNPKI 613
Cdd:PRK15079 114 rmtigeiIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPHEF-----------SGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 614 LLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFEHGTAVERGTHEEL 677
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
458-680 |
1.03e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.93 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYPSR-----PE--VKILNDLNMAIKPGEMTALVGPSGAGKST---ALQLIQRfydPCEGMVTVDGHDIRSLN--- 524
Cdd:PRK11308 10 DLKKHYPVKrglfkPErlVKALDGVSFTLERGKTLAVVGESGCGKSTlarLLTMIET---PTGGELYYQGQDLLKADpea 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 525 IQWLRDQIGIVEQ-----------------EPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYnfimdlPQQFdtlvg 587
Cdd:PRK11308 87 QKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY------PHMF----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 588 egggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFE 664
Cdd:PRK11308 156 ------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEhIADEVMVMY 229
|
250
....*....|....*.
gi 2462578034 665 HGTAVERGTHEELLER 680
Cdd:PRK11308 230 LGRCVEKGTKEQIFNN 245
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
454-701 |
1.44e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 75.26 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHY------PSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--------- 518
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdyky 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 519 ---DIR--------SLNIqwlRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQfdtlvg 587
Cdd:COG4167 85 rckHIRmifqdpntSLNP---RLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQK------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 588 egggqmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVR-AADTIIGFE 664
Cdd:COG4167 156 -----------QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQekLGISYIYVSQHLGIVKhISDKVLVMH 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462578034 665 HGTAVERGTHEELLERKGVYFTLVTLQSQGNQALNEE 701
Cdd:COG4167 225 QGEVVEYGKTAEVFANPQHEVTKRLIESHFGEALTAD 261
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
466-645 |
1.76e-14 |
|
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: 74.23 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 466 RPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLI---QRFYDPCEGMVTVDGhdiRSLNIQWLRDQIGIVEQEPVLF 542
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 ST-TIAENIRYGREDATMEDIVQAAKEANAYnfIMDLPQQFDTLVGEGGGQMSGG-QKQRVAIARALIRNPKILLLDMAT 620
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVE--DVLLRDLALTRIGGNLVKGISGgERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180
....*....|....*....|....*
gi 2462578034 621 SALDNESEAMVQEVLSKIQHGHTII 645
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIV 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
889-1290 |
1.82e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.86 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 889 GALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIAFS----FSWKLSLVILCFFPFLALSGATQTRMLT-GFASRD 963
Cdd:PLN03232 398 GKVTNMITTDANALQQIAEQLHGLWSAPFR-IIVSMVLLYQqlgvASLFGSLILFLLIPLQTLIVRKMRKLTKeGLQWTD 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 964 KQalemVGqITNEALSNIRTVAGIGKERRF---IEALETELEKPFKTAiqkaniyGFCFAFAQcimFIANSASY-----R 1035
Cdd:PLN03232 477 KR----VG-IINEILASMDTVKCYAWEKSFesrIQGIRNEELSWFRKA-------QLLSAFNS---FILNSIPVvvtlvS 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1036 YGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQL-------LDRQPPISVYNTAgekwdnf 1108
Cdd:PLN03232 542 FGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELllseeriLAQNPPLQPGAPA------- 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1109 qgkIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQ-LLERFYDPDQGKVMIdghdskkvnvqflR 1187
Cdd:PLN03232 615 ---ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------R 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1188 SNIGIVSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAkqAQLHDFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARAI 1267
Cdd:PLN03232 679 GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVT--ALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAV 755
|
410 420
....*....|....*....|...
gi 2462578034 1268 VRDPKILLLDEATSALDTESEKQ 1290
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQ 778
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
454-672 |
2.04e-14 |
|
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: 73.47 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIG 533
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLF-STTIAENIRYGREDATMEdIVQAAKEANAYNFIMDLP----QQFDTLvgegggqmSGGQKQRVAIARALI 608
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYLAQLKGLK-KEEARRRIDEWLERLELSeyanKRVEEL--------SKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 609 RNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTV-RAADTIIGFEHGTAVERG 672
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
472-654 |
2.21e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.76 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI---RSLNIQWLRDQIGIVEQE-PVLFSTTIA 547
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDhHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 548 ENIRYGR--EDATMEDI---VQAAKEA-----NAYNFIMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKIL 614
Cdd:PRK10908 98 DNVAIPLiiAGASGDDIrrrVSAALDKvglldKAKNFPIQLSggeQQ------------------RVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462578034 615 LLDMATSALDNE-SEAMVQ--EVLSKIqhGHTIISVAHRLSTV 654
Cdd:PRK10908 160 LADEPTGNLDDAlSEGILRlfEEFNRV--GVTVLMATHDIGLI 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1133-1290 |
2.41e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.97 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1133 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH------DSKkvnVQFLRSNIGIVSQEPVlfaCSIMD 1206
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlsPGK---LQALRRDIQFIFQDPY---ASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1207 NIKYGDNTKEiPMeRV-------IAAAKQAQLHDFVMSLPE---KYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:PRK10261 417 RQTVGDSIME-PL-RVhgllpgkAAAARVAWLLERVGLLPEhawRYP-------HEFSGGQRQRICIARALALNPKVIIA 487
|
170
....*....|....
gi 2462578034 1277 DEATSALDTESEKQ 1290
Cdd:PRK10261 488 DEAVSALDVSIRGQ 501
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
454-680 |
2.50e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.84 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYpsRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEP--VLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFImdlpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 611
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 612 KILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1124-1284 |
2.71e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1124 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLErFYDPD----QGKVMIDGHdskKVNVQFLRSNIGIVSQEPVL 1199
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 F-------ACSIMDNIKYGDN-TKEIPMERViaaakQAQLHDfvMSLPEKYETNVGSQGSQ--LSRGEKQRIAIARAIVR 1269
Cdd:TIGR00955 111 IptltvreHLMFQAHLRMPRRvTKKEKRERV-----DEVLQA--LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLT 183
|
170
....*....|....*
gi 2462578034 1270 DPKILLLDEATSALD 1284
Cdd:TIGR00955 184 DPPLLFCDEPTSGLD 198
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1128-1284 |
2.82e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.15 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNvqflRSNIGIVSQEPVLFA-CSIMD 1206
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYPkMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1207 NIKYgdntkeipmerviaaakQAQLHDfvMS----------------LPEKYETNVGSqgsqLSRGEKQRIAIARAIVRD 1270
Cdd:COG4152 91 QLVY-----------------LARLKG--LSkaeakrradewlerlgLGDRANKKVEE----LSKGNQQKVQLIAALLHD 147
|
170
....*....|....
gi 2462578034 1271 PKILLLDEATSALD 1284
Cdd:COG4152 148 PELLILDEPFSGLD 161
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1129-1284 |
3.01e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.35 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFL----RSN-IGIVSQEPVLFAC- 1202
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-----VTKLpeykRAKyIGRVFQDPMMGTAp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 --SIMDN------------IKYGDNTKEIPM--ERViaaakqAQLHdfvMSLPEKYETNVGSqgsqLSRGEKQRIAIARA 1266
Cdd:COG1101 96 smTIEENlalayrrgkrrgLRRGLTKKRRELfrELL------ATLG---LGLENRLDTKVGL----LSGGQRQALSLLMA 162
|
170
....*....|....*...
gi 2462578034 1267 IVRDPKILLLDEATSALD 1284
Cdd:COG1101 163 TLTKPKLLLLDEHTAALD 180
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1126-1290 |
3.07e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMidghdSKKVNVQFLRSNIGIVSQEPVLFAC-SI 1204
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPWkKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYGDNTKEIPmerviaAAKQA----QLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:PRK11247 99 IDNVGLGLKGQWRD------AALQAlaavGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170
....*....|..
gi 2462578034 1281 SALD--TESEKQ 1290
Cdd:PRK11247 162 GALDalTRIEMQ 173
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
454-650 |
3.12e-14 |
|
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: 71.80 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPS-RPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYdpcegmvtvdghdirslniQWLRDQI 532
Cdd:cd03223 1 IELENLSLATPDgRV---LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-------------------PWGSGRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLF--------STTIAENIRYGREDATMEDivqaakEanaynfimdlpQQfdtlvgegggqmsggqkqRVAIA 604
Cdd:cd03223 59 GMPEGEDLLFlpqrpylpLGTLREQLIYPWDDVLSGG------E-----------QQ------------------RLAFA 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462578034 605 RALIRNPKILLLDMATSALDNESEAMVQEVLSkiQHGHTIISVAHR 650
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR 147
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
829-1009 |
3.17e-14 |
|
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: 75.24 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 829 INGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGS 908
Cdd:cd18564 53 LLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 909 QIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGfASRDKQALEmvGQIT---NEALSNIRTVA 985
Cdd:cd18564 131 GVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKE-ASREQRRRE--GALAsvaQESLSAIRVVQ 207
|
170 180
....*....|....*....|....
gi 2462578034 986 GIGKERRFIEALETELEKPFKTAI 1009
Cdd:cd18564 208 AFGREEHEERRFARENRKSLRAGL 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1129-1283 |
3.38e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN-VQFLRSNIGIVSQEPVLFA-CSIMD 1206
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPnLSVKE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 1207 NIKYGDNTKEIPMERVIAAAKQAQLHdfvmslpekyeTNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1283
Cdd:PRK15439 106 NILFGLPKRQASMQKMKQLLAALGCQ-----------LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1144-1284 |
3.50e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1144 AFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH---DS-KKVNVQFLRSNIGIVSQEPVLFA-CSIMDNIKYGdntkeip 1218
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPhYKVRGNLRYG------- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 1219 mervIAAAKQAQLHDFVM-----SLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK11144 101 ----MAKSMVAQFDKIVAllgiePLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1126-1280 |
3.62e-14 |
|
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: 73.48 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFLRSN------IGIVSQEPVL 1199
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-----ITGLPPHriarlgIGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 FA-CSIMDNIkygdntkEIPMERVIAAAKQAQLHDFVMSL-PEKYEtNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLD 1277
Cdd:COG0410 90 FPsLTVEENL-------LLGAYARRDRAEVRADLERVYELfPRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
...
gi 2462578034 1278 EAT 1280
Cdd:COG0410 162 EPS 164
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1128-1284 |
4.59e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.74 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMI---DGHDSKKV---------------------NV 1183
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTkekekvleklviqktrfkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1184 QFLRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERviaAAKQAQLHDFVMSLPEKYetnvgSQGS--QLSRGEKQ 1259
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEE---AKKRAAKYIELVGLDESY-----LQRSpfELSGGQKR 172
|
170 180
....*....|....*....|....*
gi 2462578034 1260 RIAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
470-617 |
4.75e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 72.96 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 470 KILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI-QWLRDQIGIVEQEPVLF-STTIA 547
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFrKLTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 548 ENIRYGREDATmEDIVQAAKEANAynFIMDLpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLD 617
Cdd:cd03218 94 ENILAVLEIRG-LSKKEREEKLEE--LLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1120-1278 |
4.86e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.14 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSiqllerFY------DPDQGKVMIDGHDSKKVNVqFLRSNIGI- 1192
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1193 -VSQEPVLFA-CSIMDNIK----YGDNTKEIPMERViaaakQAQLHDFvmSLpekyeTNV-GSQGSQLSRGEKQRIAIAR 1265
Cdd:COG1137 82 yLPQEASIFRkLTVEDNILavleLRKLSKKEREERL-----EELLEEF--GI-----THLrKSKAYSLSGGERRRVEIAR 149
|
170
....*....|...
gi 2462578034 1266 AIVRDPKILLLDE 1278
Cdd:COG1137 150 ALATNPKFILLDE 162
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1137-1284 |
4.87e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.45 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1137 ISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVN-VQFLRSNIGIVSQEPVLFA-CSIMDNIKYG--- 1211
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNdVPPAERGVGMVFQSYALYPhLSVAENMSFGlkl 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 1212 --DNTKEIPmERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK11000 103 agAKKEEIN-QRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
789-1046 |
6.99e-14 |
|
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: 73.67 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 789 MLVGSVGAAVNGTVTPlyaFLFSQILGTfSIPDKEEQRsqINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 868
Cdd:cd18550 4 VLLLILLSALLGLLPP---LLLREIIDD-ALPQGDLGL--LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 869 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 948
Cdd:cd18550 78 LYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 949 GATQTRMLTGFASRDKQALEMVGQITNEALSnirtVAGI------GKERRFIEALETELEKPFKTAIqKANIYG--FcFA 1020
Cdd:cd18550 156 TRRVGRRRRKLTREQQEKLAELNSIMQETLS----VSGAllvklfGREDDEAARFARRSRELRDLGV-RQALAGrwF-FA 229
|
250 260
....*....|....*....|....*.
gi 2462578034 1021 FAQCIMFIANSASYRYGGYLISNEGL 1046
Cdd:cd18550 230 ALGLFTAIGPALVYWVGGLLVIGGGL 255
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
458-680 |
7.04e-14 |
|
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: 75.88 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYPSRpEVKILNDLNMAIKPGEMTALVGPSGAGKS-TAL---QLIQRFYDPCEGMVTVDGHDIRSLNIQWLR---- 529
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALsilRLLPDPAAHPSGSILFDGQDLLGLSERELRrirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 530 DQIGIVEQEPV-----LFS--TTIAENIR----YGREDATME--------DIVQAAKEANAYnfimdlP-------QQfd 583
Cdd:COG4172 92 NRIAMIFQEPMtslnpLHTigKQIAEVLRlhrgLSGAAARARalellervGIPDPERRLDAY------PhqlsggqRQ-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 584 tlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTI 660
Cdd:COG4172 164 ----------------RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQreLGMALLLITHDLGVVRRfADRV 227
|
250 260
....*....|....*....|
gi 2462578034 661 IGFEHGTAVERGTHEELLER 680
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
212-394 |
8.16e-14 |
|
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: 73.63 E-value: 8.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 212 YFRRIMRMEIGWFDCNSVGELNTRFSdDINKINDAIADQM-ALFIQRMTSTICGFLLgFFRGWKLTLVIISVSPLIGIga 290
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTiSLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYIL-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 291 aTIGLSVSKFTDY---ELKAYAK--AGVVadEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKG---IVMGFFTGF 362
Cdd:cd18570 157 -IILLFNKPFKKKnreVMESNAElnSYLI--ESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGklsNLQSSIKGL 233
|
170 180 190
....*....|....*....|....*....|..
gi 2462578034 363 VwCLIFLcyALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18570 234 I-SLIGS--LLILWIGSYLVIK-GQLSLGQLI 261
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
457-670 |
8.73e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.18 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 457 HNVTFHYPS------RPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN------ 524
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrka 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 525 ----IQWL-RDQIGIVE---------QEPVLFSTTIAENIRYGREDAtMEDIVQAAKEanaynfIMD-LPQQFdtlvgeg 589
Cdd:PRK10419 87 frrdIQMVfQDSISAVNprktvreiiREPLRHLLSLDKAERLARASE-MLRAVDLDDS------VLDkRPPQL------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 590 ggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTV-RAADTIIGFEHG 666
Cdd:PRK10419 153 ----SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNG 228
|
....
gi 2462578034 667 TAVE 670
Cdd:PRK10419 229 QIVE 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1112-1290 |
9.23e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.32 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH----DSKKVNVQF 1185
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIVSQ--EPVLFACSIMDNIKYGDN----TKEIPMERVIAAAKQAQLHDFVMSlpekyetnvgSQGSQLSRGEKQ 1259
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfgfSEDEAKEKALKWLKKVGLSEDLIS----------KSPFELSGGQMR 152
|
170 180 190
....*....|....*....|....*....|.
gi 2462578034 1260 RIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1128-1284 |
1.24e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 75.11 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTS----IQLLERFYDPDQGKVMIDGHDSKKVNVQFLR----SNIGIVSQEP-- 1197
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPmt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1198 --------------VLFacsimdnIKYGDNTKEIpMERVIAAAKQAQLHDfvmslPEKyetNVGSQGSQLSRGEKQRIAI 1263
Cdd:COG4172 104 slnplhtigkqiaeVLR-------LHRGLSGAAA-RARALELLERVGIPD-----PER---RLDAYPHQLSGGQRQRVMI 167
|
170 180
....*....|....*....|.
gi 2462578034 1264 ARAIVRDPKILLLDEATSALD 1284
Cdd:COG4172 168 AMALANEPDLLIADEPTTALD 188
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
472-649 |
1.32e-13 |
|
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: 71.73 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIGIVEQEPVLFSTTIAENIr 551
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRMVVFQNYSLLPWLTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 552 YGREDATMEDIVQAAKEAnaynfIMDLPQQFDTLVGEGGGQMSGGQ---KQRVAIARALIRNPKILLLDMATSALDNESE 628
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRA-----IVEEHIALVGLTEAADKRPGQLSggmKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|...
gi 2462578034 629 AMVQEVLSKI--QHGHTIISVAH 649
Cdd:TIGR01184 151 GNLQEELMQIweEHRVTVLMVTH 173
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
452-684 |
1.70e-13 |
|
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: 72.19 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYPSRPEVkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDpCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFSTTIAENIR-YGREDAtmEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRN 610
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 611 PKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVY 684
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1125-1296 |
2.33e-13 |
|
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: 70.82 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1125 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV----MIDGHDSKKVNVQFLRSNIGIVSQEPVLF 1200
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1201 ACSIMDNIKYGDNTKEipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:cd03290 92 NATVEENITFGSPFNK---QRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170
....*....|....*.
gi 2462578034 1281 SALDTEsekqpCCDHL 1296
Cdd:cd03290 169 SALDIH-----LSDHL 179
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1112-1287 |
2.43e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.07 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV----MIDGHDSKKVNVQF 1185
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIPMERVIA-AAKQAQLHDFVMSLPEKyetnvgsQGSQLSRGEKQRIA 1262
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEFWEK-------SPFELSGGQMRRVA 154
|
170 180
....*....|....*....|....*
gi 2462578034 1263 IARAIVRDPKILLLDEATSALDTES 1287
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKA 179
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1128-1290 |
2.62e-13 |
|
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: 71.22 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD--SKKVnvqFLRSNIGIVS--QEPVLFA-C 1202
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitGLPP---HRIARLGIARtfQNPRLFPeL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 SIMDNI------KYGDNTKEIPMERVIAAAKQAQLHDFVMS------LPEKYETNVGSqgsqLSRGEKQRIAIARAIVRD 1270
Cdd:COG0411 95 TVLENVlvaahaRLGRGLLAALLRLPRARREEREARERAEEllervgLADRADEPAGN----LSYGQQRRLEIARALATE 170
|
170 180
....*....|....*....|
gi 2462578034 1271 PKILLLDEATSALdTESEKQ 1290
Cdd:COG0411 171 PKLLLLDEPAAGL-NPEETE 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
453-677 |
2.63e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 453 EIEFHNVTFHYPSRP--EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL------- 523
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 524 -----------------NIQWLRDQIGIVEQ--EPVLFSTTIAENIRYGREDATMEDiVQAAKEANAYNFIMDLPQQFdt 584
Cdd:PRK13651 82 kvleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 585 lVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIG 662
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIF 237
|
250
....*....|....*.
gi 2462578034 663 FEHGTAVERG-THEEL 677
Cdd:PRK13651 238 FKDGKIIKDGdTYDIL 253
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1133-1290 |
3.09e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.36 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1133 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPvlfACSIMDNIKYGD 1212
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1213 --------NTKEIPMER---VIAAAKQAQLhdfvmsLPEkyetNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1281
Cdd:PRK15112 109 ildfplrlNTDLEPEQRekqIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
....*....
gi 2462578034 1282 ALDTESEKQ 1290
Cdd:PRK15112 179 SLDMSMRSQ 187
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
467-670 |
3.36e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 467 PEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYdPC---EGMVTVDG-----HDIRSlniqwlRDQIGIV--E 536
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRD------SEALGIViiH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 537 QE----PVLfstTIAENIRYGREDATM------EDIVQAAK-------EANAYNFIMDL---PQQFdtlvgegggqmsgg 596
Cdd:NF040905 85 QElaliPYL---SIAENIFLGNERAKRgvidwnETNRRAREllakvglDESPDTLVTDIgvgKQQL-------------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 597 qkqrVAIARALIRNPKILLLDMATSAL-DNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 670
Cdd:NF040905 148 ----VEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-681 |
3.39e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 533
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQ----EPvlfSTTIAENIR-----YGREDATMEDIVQAAKEanaynfIMDLPQQFDTLVGEGGGQMSGgqkqRVAIA 604
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLvfgryFGLSAAAARALVPPLLE------FAKLENKADAKVGELSGGMKR----RLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 605 RALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1127-1280 |
3.56e-13 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 70.63 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1127 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFA-CSI 1204
Cdd:TIGR03410 13 SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDiTKLPPHERARAGIAYVPQGREIFPrLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYG-----DNTKEIPmerviaaakqaqlhDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:TIGR03410 93 EENLLTGlaalpRRSRKIP--------------DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
.
gi 2462578034 1280 T 1280
Cdd:TIGR03410 159 T 159
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1112-1287 |
4.30e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.76 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPsrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhDSKKVNVQFLRSNIG 1191
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQepvlfacsiMDNIKYGDNTKEipMERVIA---AAKQAQLHDFVMSLPE--KYETNVGSQGSQLSRGEKQRIAIARA 1266
Cdd:PRK13537 84 VVPQ---------FDNLDPDFTVRE--NLLVFGryfGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180
....*....|....*....|.
gi 2462578034 1267 IVRDPKILLLDEATSALDTES 1287
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQA 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1130-1290 |
4.42e-13 |
|
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: 70.19 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVnvqflrsnigivsQEP-----VLFacsi 1204
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQI-------------TEPgpdrmVVF---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 mdnikygDNTKEIPMERV---IAAAKQAQLHDfvMSLPEKYETN------VGSQGS------QLSRGEKQRIAIARAIVR 1269
Cdd:TIGR01184 61 -------QNYSLLPWLTVrenIALAVDRVLPD--LSKSERRAIVeehialVGLTEAadkrpgQLSGGMKQRVAIARALSI 131
|
170 180
....*....|....*....|...
gi 2462578034 1270 DPKILLLDEATSALD--TESEKQ 1290
Cdd:TIGR01184 132 RPKVLLLDEPFGALDalTRGNLQ 154
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
465-672 |
4.49e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 465 SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQ--IGIVEQE-PVL 541
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQElSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 542 FSTTIAENIRYGRE------DATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGqkqrVAIARALIRNPKILL 615
Cdd:PRK09700 93 DELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM----LEIAKTLMLDAKVII 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 616 LDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 672
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1113-1284 |
4.80e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1113 DFVDCK---FTYPSRPDSQ---VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKV-NVQF 1185
Cdd:PRK13633 3 EMIKCKnvsYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIPME----RVIAAAKQAQLHDFvmslpEKYETNVgsqgsqLSRGEKQ 1259
Cdd:PRK13633 83 IRNKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPPEeireRVDESLKKVGMYEY-----RRHAPHL------LSGGQKQ 151
|
170 180
....*....|....*....|....*
gi 2462578034 1260 RIAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
794-1044 |
5.48e-13 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 71.19 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 794 VGAAVNGTVTPLYAflfSQILGTFSIPDKEEQRSQ-INGVCLLF----VAMGCVS-LFTqflqgYAFAKsgelLTKRLRK 867
Cdd:cd18784 6 LAAAVGEIFIPYYT---GQVIDGIVIEKSQDKFSRaIIIMGLLAiassVAAGIRGgLFT-----LAMAR----LNIRIRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 868 FGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLAL 947
Cdd:cd18784 74 LLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 948 SGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYG---FCFAFAQC 1024
Cdd:cd18784 152 VSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGgyvWSNELTEL 231
|
250 260
....*....|....*....|
gi 2462578034 1025 IMFIansASYRYGGYLISNE 1044
Cdd:cd18784 232 ALTV---STLYYGGHLVITG 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
458-679 |
5.51e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQ 537
Cdd:PRK10575 16 NVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 538 E-PVLFSTTIAENI------------RYGREDAtmedivQAAKEANAYNFIMDLPQQF-DTLvgegggqmSGGQKQRVAI 603
Cdd:PRK10575 93 QlPAAEGMTVRELVaigrypwhgalgRFGAADR------EKVEEAISLVGLKPLAHRLvDSL--------SGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 604 ARALIRNPKILLLDMATSALD----NESEAMVQEvLSKiQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDiahqVDVLALVHR-LSQ-ERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
.
gi 2462578034 679 E 679
Cdd:PRK10575 237 R 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1117-1290 |
6.08e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1117 CKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMI---------------DGHDSKKV 1181
Cdd:PRK13631 29 CVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheliTNPYSKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1182 -NVQFLRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIPMERviaAAKQAQLHDFVMSLPEKYetnVGSQGSQLSRGEK 1258
Cdd:PRK13631 109 kNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSY---LERSPFGLSGGQK 182
|
170 180 190
....*....|....*....|....*....|..
gi 2462578034 1259 QRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHE 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
454-638 |
6.18e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 70.28 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYP-SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI------Rslniq 526
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 527 wlrdqiGIVEQEPVLFS-TTIAENIRYG----------REDATMEDIVQAAKEANAYNFIMDLP---QQfdtlvgegggq 592
Cdd:COG4525 79 ------GVVFQKDALLPwLNVLDNVAFGlrlrgvpkaeRRARAEELLALVGLADFARRRIWQLSggmRQ----------- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462578034 593 msggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI 638
Cdd:COG4525 142 -------RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
182-342 |
6.77e-13 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 70.96 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 182 IAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTST 261
Cdd:cd18589 45 LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 262 ICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKN 341
Cdd:cd18589 125 LFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQR 204
|
.
gi 2462578034 342 L 342
Cdd:cd18589 205 L 205
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
173-394 |
7.14e-13 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 70.65 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 173 IKFASYYAgiAVAVLITGYIQicFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA 252
Cdd:cd18574 46 LKLLGLYL--LQSLLTFAYIS--LLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 253 LFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEK 332
Cdd:cd18574 122 QGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMED 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 333 REVERYEKNLVFAQRWGIRKGIVMGFFTG----FVWCLIFLCYalafWYGSTLVlDEGEYTPGTLV 394
Cdd:cd18574 202 RELELYEEEVEKAAKLNEKLGLGIGIFQGlsnlALNGIVLGVL----YYGGSLV-SRGELTAGDLM 262
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1130-1283 |
8.18e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNV----QFLRSNIGIVSQEPVLF-ACSI 1204
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIrsprDAIALGIGMVHQHFMLVpNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYGDNTKEIPMERVIAAAKQaqlhdfVMSLPEKY------ETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVE----DLSVGEQQRVEILKALYRGARILILDE 167
|
....*
gi 2462578034 1279 ATSAL 1283
Cdd:COG3845 168 PTAVL 172
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1120-1309 |
9.70e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN----VQFLRSNIGIVS 1194
Cdd:PRK10535 13 SYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1195 QEPVLFA-CSIMDNIkygdntkEIP-----MERviaAAKQAQLHDFVMSLpeKYETNVGSQGSQLSRGEKQRIAIARAIV 1268
Cdd:PRK10535 93 QRYHLLShLTAAQNV-------EVPavyagLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 1269 RDPKILLLDEATSALDTESE-------KQPCcdhlDKSHT-------PQMAEQED 1309
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGeevmailHQLR----DRGHTviivthdPQVAAQAE 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
468-682 |
1.08e-12 |
|
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: 68.32 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 468 EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRF--YDPCEGMVTVDGHDIRSLNIQwLRDQIGI--VEQEPVLFS 543
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 544 -TTIAENIRY------GREdatmedivqaakeanaynfimdlpqqfdtlvgegggqmsggqKQRVAIARALIRNPKILLL 616
Cdd:cd03217 91 gVKNADFLRYvnegfsGGE------------------------------------------KKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 617 DMATSALDNESEAMVQEVLSKIQH-GHTIISVAH--RLSTVRAADTIIGFEHGTAVERGTHE--ELLERKG 682
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1112-1284 |
1.18e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH----DSKKVNVQF 1185
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERviAAAKQAQLHDFVmSLPEKYETNvgsqgS--QLSRGEKQRI 1261
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEED--AKQKAREMIELV-GLPEELLAR-----SpfELSGGQMRRV 154
|
170 180
....*....|....*....|...
gi 2462578034 1262 AIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1123-1284 |
1.22e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.41 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL-FA 1201
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNIKYG-----------DNTKEIPMERVIAAAKQAQLHDFVMSlpekyetnvgsqgsQLSRGEKQRIAIARAIVRD 1270
Cdd:PRK09536 92 FDVRQVVEMGrtphrsrfdtwTETDRAAVERAMERTGVAQFADRPVT--------------SLSGGERQRVLLARALAQA 157
|
170
....*....|....
gi 2462578034 1271 PKILLLDEATSALD 1284
Cdd:PRK09536 158 TPVLLLDEPTASLD 171
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
452-651 |
1.32e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 73.02 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEIEFHNVTFHYPSRPEvKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDpCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFSTTIAENIRyGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 611
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462578034 612 KILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRL 651
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
181-404 |
1.36e-12 |
|
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: 69.73 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 181 GIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRM---EIGWFdcnSVGELNTRFSDDINKIndaiadQMALF-IQ 256
Cdd:cd18548 47 LLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFsfaEIDKF---GTSSLITRLTNDVTQV------QNFVMmLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 257 RMTST-----ICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGE 331
Cdd:cd18548 118 RMLVRapimlIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNRE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 332 KREVERYEK-NLVFAQRwGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVlDEGEYTPGTLV-------QIFLSVIVG 403
Cdd:cd18548 198 DYEEERFDKaNDDLTDT-SLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLI-NAGSLQVGDLVafinylmQILMSLMML 275
|
.
gi 2462578034 404 A 404
Cdd:cd18548 276 S 276
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
454-678 |
1.63e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.43 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNV--TFHYPS----RPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI------- 520
Cdd:PRK15112 5 LEVRNLskTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 521 RSLNIQWL----------RDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFiMDLPQQfdtlvgegg 590
Cdd:PRK15112 85 RSQRIRMIfqdpstslnpRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPH-MLAPGQ--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 591 gqmsggqKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTI--ISVAHRLSTVR-AADTIIGFEHGT 667
Cdd:PRK15112 155 -------KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKhISDQVLVMHQGE 227
|
250
....*....|.
gi 2462578034 668 AVERGTHEELL 678
Cdd:PRK15112 228 VVERGSTADVL 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1129-1284 |
1.65e-12 |
|
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: 68.51 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRsNIGIV--SQEPVLFACSIMD 1206
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 1207 NIKYGDNTKEIPMERviAAAKQAQLHDfVMSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:cd03267 115 SFYLLAAIYDLPPAR--FKKRLDELSE-LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
827-1030 |
1.74e-12 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 69.74 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 827 SQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAA 906
Cdd:cd18547 42 SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 907 GSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSgatqTRMLTGFASR--DKQAlEMVGQIT---NEALSNI 981
Cdd:cd18547 120 SQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV----TKFIAKRSQKyfRKQQ-KALGELNgyiEEMISGQ 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462578034 982 RTVAGIGKERRFIEALETELEKPFKTAIqKANIYGfcFAFAQCIMFIAN 1030
Cdd:cd18547 195 KVVKAFNREEEAIEEFDEINEELYKASF-KAQFYS--GLLMPIMNFINN 240
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-678 |
1.75e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGM-----VTVDGHDIRSL-NIQWLRDQIGIVEQEPVLFST 544
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 545 TIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALD 624
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 625 NESEAMVQEVLSKIQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
454-672 |
1.79e-12 |
|
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: 68.33 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPS-------------------RPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT 514
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 515 VDGhdirslNIQWLRD-QIGIveqEPVLfstTIAENIR-----YGREDATMEDIvqaakeanaYNFIMD---LPQQFDTL 585
Cdd:cd03220 81 VRG------RVSSLLGlGGGF---NPEL---TGRENIYlngrlLGLSRKEIDEK---------IDEIIEfseLGDFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 586 VgeggGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRA-ADTIIGF 663
Cdd:cd03220 140 V----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVL 215
|
....*....
gi 2462578034 664 EHGTAVERG 672
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
468-684 |
2.10e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.88 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 468 EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVD----GHDIRSL------------NIQWLRDQ 531
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEP--VLFSTTIAENIRYGREDATMEDIvQAAKEANAYNFIMDLPQQFdtlVGEGGGQMSGGQKQRVAIARALIR 609
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKS-EAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578034 610 NPKILLLDMATSALDNESEA-MVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERKGVY 684
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
466-679 |
2.22e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 466 RPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQrFYDP----CEGMVTVDGHDIrslNIQWLRDQIGIVEQEPVL 541
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 542 FST-TIAENI------RYGREDAT------MEDIVQAAKEANAYNFIMDLPQQFDTLvgegggqmSGGQKQRVAIARALI 608
Cdd:TIGR00955 111 IPTlTVREHLmfqahlRMPRRVTKkekrerVDEVLQALGLRKCANTRIGVPGRVKGL--------SGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 609 RNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLST--VRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1128-1290 |
2.26e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.27 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKS-TSIQLLERFYDPD----QGKVMIDGHDSKKVNVQFLR----SNIGIVSQEP- 1197
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1198 ---------------VLfacSIMDNIKYGDNTKEI--PMERV-IAAAKQaQLHDFvmslPEkyetnvgsqgsQLSRGEKQ 1259
Cdd:PRK15134 103 vslnplhtlekqlyeVL---SLHRGMRREAARGEIlnCLDRVgIRQAAK-RLTDY----PH-----------QLSGGERQ 163
|
170 180 190
....*....|....*....|....*....|.
gi 2462578034 1260 RIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQ 194
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
462-640 |
2.30e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.57 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 462 HYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWlrdqiGIVEQ-EPV 540
Cdd:PRK11248 10 DYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQnEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 541 LFSTTIAENIRYG----------REDATMEDIVQAAKEANAYNFIMDLpqqfdtlvgegggqmSGGQKQRVAIARALIRN 610
Cdd:PRK11248 82 LPWRNVQDNVAFGlqlagvekmqRLEIAHQMLKKVGLEGAEKRYIWQL---------------SGGQRQRVGIARALAAN 146
|
170 180 190
....*....|....*....|....*....|
gi 2462578034 611 PKILLLDMATSALDNESEAMVQEVLSKIQH 640
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQ 176
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
454-680 |
2.53e-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: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVdGHDIRslniqwlrdqIG 533
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLF--STTIAENIRYGREDATMEDIVQAAKeanAYNFImdlPQQFDTLVgegggqmsggqKQ-------RVAIA 604
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLG---RFLFS---GDDAFKPV-----------GVlsggekaRLALA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 605 RALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhGhTIISVAH-R--LSTVraADTIIGFEHGTAVER-GTHEELLER 680
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
458-651 |
2.72e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.57 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiQWLRDQ-IGIVE 536
Cdd:COG1101 8 SKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAKyIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 537 QEPVL---FSTTIAEN------------IRYGREDATMEDIVQAAKEANaynfiMDLPQQFDTlvgegggqmsggqkqRV 601
Cdd:COG1101 87 QDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDT---------------KV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 602 ---------AIA--RALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRL 651
Cdd:COG1101 147 gllsggqrqALSllMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
458-666 |
2.93e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQrfydpceGMVTVDGHDIRSLN--IQWLRDQIGIV 535
Cdd:PRK11247 17 AVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA-------GLETPSAGELLAGTapLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 536 EQEPVLFS-TTIAENIRYG-----REDATME-DIVQAAKEANAYNFIMDLPQQfdtlvgegggqmsggqkQRVAIARALI 608
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGlkgqwRDAALQAlAAVGLADRANEWPAALSGGQK-----------------QRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 609 RNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHG 666
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1126-1284 |
2.94e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.12 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---------SKKVNV--QFLRSNIGIVS 1194
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlARRLALlpQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1195 QEPVLFACSIMDNI--KYGDNTKeipmERVIAAAKQAQLHDFVmslpEKYETNvgsqgsqLSRGEKQRIAIARAIVRDPK 1272
Cdd:PRK11231 94 RELVAYGRSPWLSLwgRLSAEDN----ARVNQAMEQTRINHLA----DRRLTD-------LSGGQRQRAFLAMVLAQDTP 158
|
170
....*....|..
gi 2462578034 1273 ILLLDEATSALD 1284
Cdd:PRK11231 159 VVLLDEPTTYLD 170
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
461-694 |
5.60e-12 |
|
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: 70.81 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 461 FHYPSRPEVkilNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIGIVEQEPV 540
Cdd:TIGR01257 938 FEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 541 LFS-TTIAENIRY-----GR--EDATMEdiVQAAKEANAYNFIMDLPQQfdtlvgegggQMSGGQKQRVAIARALIRNPK 612
Cdd:TIGR01257 1014 LFHhLTVAEHILFyaqlkGRswEEAQLE--MEAMLEDTGLHHKRNEEAQ----------DLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 613 ILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE--RKGVYFTLV- 688
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLVr 1161
|
....*....
gi 2462578034 689 ---TLQSQG 694
Cdd:TIGR01257 1162 kmkNIQSQR 1170
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1129-1289 |
6.39e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDP-----DQGKVMIDGHDSKKV-NVQFLRSNIGIVSQEPVLFAC 1202
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 SIMDNIKYGDNTKEIPMERVIAAAKQAQLHDfvMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1282
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
....*...
gi 2462578034 1283 LD-TESEK 1289
Cdd:PRK14271 194 LDpTTTEK 201
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
179-394 |
7.39e-12 |
|
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: 67.88 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 179 YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRM 258
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 259 TSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIG-LSVSKFTDYELKayaKAGVVAD--EVISSMRTVAAFGGEKREV 335
Cdd:cd18545 126 LTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRrRARKAWQRVRKK---ISNLNAYlhESISGIRVIQSFAREDENE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 336 ERYE---KNLVFAQRWGIRkgivmgfFTGFVWCLIFLCYALA----FWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18545 203 EIFDelnRENRKANMRAVR-------LNALFWPLVELISALGtalvYWYGGKLVLG-GAITVGVLV 260
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
461-667 |
8.59e-12 |
|
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: 66.59 E-value: 8.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 461 FHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRdQIGIV--EQE 538
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 539 PVLFSTTIAENIRYGREDATMEDiVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGgqkqRVAIARALIRNPKILLLDM 618
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPP-ARFKKRLDELSELLDLEELLDTPVRQLSLGQRM----RAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 619 ATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGT 667
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNreRGTTVLLTSHYMKDIEAlARRVLVIDKGR 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
440-654 |
1.00e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 440 MSEDGYKLDRIKGEIEFH--NVTFHYPSRPEVK-ILNDLNMAIKPGEMTALVGPSGAGKSTALQ-LIQRFydpCEGMVT- 514
Cdd:TIGR00956 744 DVNDEKDMEKESGEDIFHwrNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERV---TTGVITg 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 515 ----VDGHDIRSLniqwLRDQIGIVEQEPV-LFSTTIAENIRYG---REDATMEDivqaaKEANAY-NFIMDL---PQQF 582
Cdd:TIGR00956 821 gdrlVNGRPLDSS----FQRSIGYVQQQDLhLPTSTVRESLRFSaylRQPKSVSK-----SEKMEYvEEVIKLlemESYA 891
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 583 DTLVGEGGGQMSGGQKQRVAIARALIRNPKILL-LDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV 654
Cdd:TIGR00956 892 DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQPSAI 965
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
466-636 |
1.09e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 466 RPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQWL--RDQIgiveqEP 539
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeaCHYLghRNAM-----KP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 540 VLfstTIAENIR-----YGREDATmediVQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsggqkQRVAIARAL 607
Cdd:PRK13539 87 AL---TVAENLEfwaafLGGEELD----IAAALEAVGLAPLAHLPfgylsagQK-----------------RRVALARLL 142
|
170 180
....*....|....*....|....*....
gi 2462578034 608 IRNPKILLLDMATSALDNESEAMVQEVLS 636
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELIR 171
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1128-1288 |
1.40e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN-IGIVSQE-PVLFACSIM 1205
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1206 DNIKYGDN-TKEIPMERVIAAAK---QAQLHDFVMSLPEKYETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATS 1281
Cdd:PRK09700 99 ENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
....*..
gi 2462578034 1282 ALdTESE 1288
Cdd:PRK09700 175 SL-TNKE 180
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1124-1289 |
1.83e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1124 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGivSQEPVLFACS 1203
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1204 IMDNIKYGDNTKEIPMERVIAAAKQAQLHDfVMSLPEKYetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1283
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
....*.
gi 2462578034 1284 DTESEK 1289
Cdd:PRK13539 159 DAAAVA 164
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
467-667 |
1.91e-11 |
|
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: 65.04 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 467 PEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMV--------TVDGHDIRSLNiqwlRDQIGIVEQE 538
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesEPSFEATRSRN----RYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 539 PVLFSTTIAENIRYGreDATMEDIVQAAKEANAYNFIMD-LPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLD 617
Cdd:cd03290 88 PWLLNATVEENITFG--SPFNKQRYKAVTDACSLQPDIDlLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 618 MATSALD-NESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:cd03290 166 DPFSALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
471-678 |
2.01e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKS-TALQLIQRFYDP----CEGMVTVDGHDIRSLNIQWLR----DQIGIVEQEPVL 541
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 542 fSTTIAENI-----------RYGREDATMEDIV---------QAAKEANaynfimDLPQQFdtlvgegggqmSGGQKQRV 601
Cdd:PRK15134 104 -SLNPLHTLekqlyevlslhRGMRREAARGEILncldrvgirQAAKRLT------DYPHQL-----------SGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 602 AIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF 245
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
170-340 |
2.04e-11 |
|
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: 66.27 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 170 SEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAD 249
Cdd:cd18547 42 SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 250 QMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFG 329
Cdd:cd18547 122 SLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFN 201
|
170
....*....|.
gi 2462578034 330 GEKREVERYEK 340
Cdd:cd18547 202 REEEAIEEFDE 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
458-666 |
2.31e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.98 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDghDIRSLNIQWLRDQIGIVEQ 537
Cdd:PRK11000 8 NVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 538 EPVLFS-TTIAENIRYGREDATMEDIvQAAKEANAYNFIMdlpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLL 616
Cdd:PRK11000 83 SYALYPhLSVAENMSFGLKLAGAKKE-EINQRVNQVAEVL----QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 617 DMATSALDNESEAMVQEVLSKIQH--GHTIISVAHrlSTVRA---ADTIIGFEHG 666
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTH--DQVEAmtlADKIVVLDAG 210
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
790-1067 |
2.31e-11 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 66.35 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 790 LVGSVGAAVNGTVTPLYAFLFSQILgtfsI--PDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRK 867
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRA----IdgPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 868 FGFRAMLGQDIAWFDDLRnsPGALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIAFSFSWKLSLVILCFFPFLAL 947
Cdd:cd18543 77 DLFAHLQRLDGAFHDRWQ--SGQLLSRATSDLSLVQRFLAFGPFLLGNLLT-LVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 948 SGATQTRMLTGfASRDKQalEMVGQIT---NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQC 1024
Cdd:cd18543 154 VARRFRRRYFP-ASRRAQ--DQAGDLAtvvEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1025 IMFIANSASYRYGGYLISNEGL-------HFSYV------FRVISAVVLSA----TALGR 1067
Cdd:cd18543 231 LPELGLAAVLALGGWLVANGSLtlgtlvaFSAYLtmlvwpVRMLGWLLAMAqrarAAAER 290
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
454-680 |
2.41e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYP-------------------SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT 514
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 515 VDGhdirslNIQWLrdqIGiveqepvlFST------TIAENIR-----YG---RE-DATMEDIVQAAkeanaynfimDLP 579
Cdd:COG1134 85 VNG------RVSAL---LE--------LGAgfhpelTGRENIYlngrlLGlsrKEiDEKFDEIVEFA----------ELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 580 QQFDT---------LVgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNE----SEAMVQEvlsKIQHGHTIIS 646
Cdd:COG1134 138 DFIDQpvktyssgmRA-------------RLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE---LRESGRTVIF 201
|
250 260 270
....*....|....*....|....*....|....*
gi 2462578034 647 VAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLER 680
Cdd:COG1134 202 VSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
455-677 |
2.67e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.63 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 455 EFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlRDQ--- 531
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST---TAAlaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 -IGIVEQE----PVLfstTIAENIRYGR--EDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGqkqrVAIA 604
Cdd:PRK11288 80 gVAIIYQElhlvPEM---TVAENLYLGQlpHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQM----VEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 605 RALIRNPKILLLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVErgTHEEL 677
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSaREIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1112-1287 |
2.83e-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: 62.47 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDghdsKKVNVQFLrsnig 1191
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 ivsqepvlfacsimdnikygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgSQLSRGEKQRIAIARAIVRDP 1271
Cdd:cd03221 69 -----------------------------------------------------------EQLSGGEKMRLALAKLLLENP 89
|
170
....*....|....*.
gi 2462578034 1272 KILLLDEATSALDTES 1287
Cdd:cd03221 90 NLLLLDEPTNHLDLES 105
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1125-1283 |
3.40e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1125 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkVNVQF------LRSNIGIVSQE-- 1196
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-----QEMRFasttaaLAAGVAIIYQElh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 --PVLfacSIMDNIKYGD--NTKEIPMERVIAAAKQAQLH----DFVMSLPEKYetnvgsqgsqLSRGEKQRIAIARAIV 1268
Cdd:PRK11288 90 lvPEM---TVAENLYLGQlpHKGGIVNRRLLNYEAREQLEhlgvDIDPDTPLKY----------LSIGQRQMVEIAKALA 156
|
170
....*....|....*
gi 2462578034 1269 RDPKILLLDEATSAL 1283
Cdd:PRK11288 157 RNARVIAFDEPTSSL 171
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1112-1287 |
3.73e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIdGHdskkvNVQflrsnIG 1191
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1192 IVSQEPVLFAC--SIMDNIK-YGDNTKEIpmerviaaakqaqlhdFVMSL-------PEKYETNVGSqgsqLSRGEKQRI 1261
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRdGAPGGTEQ----------------EVRGYlgrflfsGDDAFKPVGV----LSGGEKARL 441
|
170 180
....*....|....*....|....*.
gi 2462578034 1262 AIARAIVRDPKILLLDEATSALDTES 1287
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIET 467
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
839-998 |
3.74e-11 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 65.44 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 839 MGCVSLFTQF---LQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVN 915
Cdd:cd18590 42 MCLFSLGSSLsagLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTTLMSRSVALNANVLLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 916 SFTNVTVAMIIAFSFSWKLSLVILCFFPFLALsgaTQTRMLTGFASRDKQALEMV---GQITNEALSNIRTVAGIGKE-- 990
Cdd:cd18590 120 SLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAI---AQKVYNTYHQKLSQAVQDSIakaGELAREAVSSIRTVRSFKAEee 196
|
170
....*....|
gi 2462578034 991 --RRFIEALE 998
Cdd:cd18590 197 eaCRYSEALE 206
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1131-1290 |
3.76e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1131 NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN-VQFL--RSNIGIVSQEPVlfaCSIMDN 1207
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPL---ASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1208 IKYGDNTKEiPMERVIAAAKQAQLHDFVMSLPEKyetnVGSQGSQLSR-------GEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:PRK15079 115 MTIGEIIAE-PLRTYHPKLSRQEVKDRVKAMMLK----VGLLPNLINRyphefsgGQCQRIGIARALILEPKLIICDEPV 189
|
170
....*....|
gi 2462578034 1281 SALDTESEKQ 1290
Cdd:PRK15079 190 SALDVSIQAQ 199
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
471-677 |
3.85e-11 |
|
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: 65.26 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLrdqigiveqepvlFSTTIAENI 550
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWI-------------MPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 551 RYG--REDATMEDIVQAAKEANAynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESE 628
Cdd:cd03291 119 IFGvsYDEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462578034 629 AMVQE-VLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEEL 677
Cdd:cd03291 196 KEIFEsCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
457-617 |
3.95e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.67 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 457 HNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTAlqliqrFY------DPCEGMVTVDGHDIRSLNIqWLRD 530
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGI--VEQEPVLF-STTIAENIRygredATMEDIVQAAKEANAYnfIMDLPQQF----------DTLvgegggqmsggq 597
Cdd:COG1137 77 RLGIgyLPQEASIFrKLTVEDNIL-----AVLELRKLSKKEREER--LEELLEEFgithlrkskaYSLsgg--------e 141
|
170 180
....*....|....*....|
gi 2462578034 598 kqRVAIARALIRNPKILLLD 617
Cdd:COG1137 142 rrRVEIARALATNPKFILLD 161
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
473-677 |
4.01e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.01 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 473 NDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlrdQI---GIVE--QEPVLF-STTI 546
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH----QIarmGVVRtfQHVRLFrEMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 547 AENI--------------------RYGRedATMEDIVQAA---------KEAN------AYNfimdlpQQfdtlvgeggg 591
Cdd:PRK11300 98 IENLlvaqhqqlktglfsgllktpAFRR--AESEALDRAAtwlervgllEHANrqagnlAYG------QQ---------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 592 qmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTA 668
Cdd:PRK11300 160 -------RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrnEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTP 232
|
....*....
gi 2462578034 669 VERGTHEEL 677
Cdd:PRK11300 233 LANGTPEEI 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
460-666 |
4.48e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 460 TFHypsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQ----LIQRFYDPcEGMVTVDGHDIR-----SLNIQWLRD 530
Cdd:PRK09984 13 TFN-----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSA-GSHIELLGRTVQregrlARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIG-IVEQEPVLFSTTIAENIRYGREDAT--------------MEDIVQAAKEANAYNFIMdlpQQFDTLvgegggqmSG 595
Cdd:PRK09984 87 NTGyIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHFAH---QRVSTL--------SG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 596 GQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHG 666
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQG 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1123-1288 |
4.55e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNVQFLRSN----IGIVSQE-- 1196
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQEln 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 --PVLfacSIMDNIKYGDNTKE----IPMERVIAAAKQ--AQLhdfvmSLPEKYETNVGsqgsQLSRGEKQRIAIARAIV 1268
Cdd:PRK10762 90 liPQL---TIAENIFLGREFVNrfgrIDWKKMYAEADKllARL-----NLRFSSDKLVG----ELSIGEQQMVEIAKVLS 157
|
170 180
....*....|....*....|.
gi 2462578034 1269 RDPKILLLDEATSAL-DTESE 1288
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETE 178
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
454-683 |
4.72e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.52 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrslnIQW-----L 528
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDWqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 529 RDQIGIVEQEPVLFS-TTIAENIRYGREDATMEDIVQAAKEanaynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARAL 607
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 608 IRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
.
gi 2462578034 683 V 683
Cdd:PRK11614 230 V 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
458-680 |
5.06e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYpSRPEVKILNDLNMAIKPGEMTALVGPSGAGKS-TALQLIqRFYDPCEGMVTVDGHDIRSLNIQW--LRDQ--- 531
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLLRRRSRQVieLSEQsaa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 ---------IGIVEQEPV-----LFST--TIAENIR----YGREDATME--DIVQAAKEANAYNFIMDLPQQFDtlvgeg 589
Cdd:PRK10261 97 qmrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREEAMVEakRMLDQVRIPEAQTILSRYPHQLS------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 590 ggqmsGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHT--IISVAHRLSTV-RAADTIIGFEHG 666
Cdd:PRK10261 171 -----GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQG 245
|
250
....*....|....
gi 2462578034 667 TAVERGTHEELLER 680
Cdd:PRK10261 246 EAVETGSVEQIFHA 259
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
469-660 |
5.42e-11 |
|
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: 66.77 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 469 VKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYdPC---EGMVTVDGHDIRSLNIQWL-RDQIGIVEQEPVLF-S 543
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 544 TTIAENIRYGRE---------DATM----EDIVQAAK--EANAYNFIMDLPQQFDTLVGegggqmsggqkqrvaIARALI 608
Cdd:TIGR02633 93 LSVAENIFLGNEitlpggrmaYNAMylraKNLLRELQldADNVTRPVGDYGGGQQQLVE---------------IAKALN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 609 RNPKILLLDMATSAL-DNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTI 660
Cdd:TIGR02633 158 KQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTI 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
454-649 |
5.61e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHY-PSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW---LR 529
Cdd:PRK10584 7 VEVHHLKKSVgQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 530 DQ-IGIVEQEPVLFSTTIA-ENI------RYGREDATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRV 601
Cdd:PRK10584 87 AKhVGFVFQSFMLIPTLNAlENVelpallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLS-----------GGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462578034 602 AIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAH 649
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
471-652 |
6.14e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW---LRDQ-IGIVEQ-EPVLFSTT 545
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 546 IAENIrygredaTMEDIVQAAK--EANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSAL 623
Cdd:PRK11629 104 ALENV-------AMPLLIGKKKpaEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 2462578034 624 DNESEAMVQEVLSKI--QHGHTIISVAHRLS 652
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1130-1284 |
9.03e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.98 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV-------MIDGHDSKKVNVQFLRSNIGIVSQEPVLFA- 1201
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNIkygdnTKEIPMERVIAAAKQAQLHDFVMS-LPEKYETNVGSQ-GSQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:TIGR03269 380 RTVLDNL-----TEAIGLELPDELARMKAVITLKMVgFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
....*
gi 2462578034 1280 TSALD 1284
Cdd:TIGR03269 455 TGTMD 459
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
454-679 |
9.27e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.98 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPS--RPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT-------VDGHDIRSLN 524
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 525 IQWLRDQIGIVEQEPVLFS-TTIAENI----------RYGREDATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqm 593
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLteaiglelpdELARMKAVITLKMVGFDEEKAEEILDKYPDELS---------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 594 sGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL--SKIQHGHTIISVAHRLSTVR-AADTIIGFEHGTAVE 670
Cdd:TIGR03269 430 -EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLdVCDRAALMRDGKIVK 508
|
....*....
gi 2462578034 671 RGTHEELLE 679
Cdd:TIGR03269 509 IGDPEEIVE 517
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
454-656 |
1.04e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHdirslniqwLRdqIG 533
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFST---TIAENIRYgREDATMEDIVQAAKEANAYNFImDLPQQfdtlvgegggQMSGGQKQRVAIARALIRN 610
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462578034 611 PKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA 656
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMA 186
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
180-394 |
1.07e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 64.14 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQIC---FWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDdINKINDAIADQMALFIQ 256
Cdd:cd18566 46 IGVVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIREFLTGQALLALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 257 RMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGlsvskftdYELKAYAKAGVVAD--------EVISSMRTVAAF 328
Cdd:cd18566 125 DLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLG--------PILRRALKERSRADerrqnfliETLTGIHTIKAM 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 329 GGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18566 197 AMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVIN-GDLTVGALI 261
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
832-1046 |
1.08e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 64.07 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 832 VCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQG--AAGSQ 909
Cdd:cd18563 45 LVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDflSDGLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 910 iGMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGK 989
Cdd:cd18563 123 -DFLTNILMIIGIG-VVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQ 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 990 ERRFIEALETELEKPFKTAIQKANIYGFCFAFaqcIMFIANSASY---RYGGYLISNEGL 1046
Cdd:cd18563 201 EKREIKRFDEANQELLDANIRAEKLWATFFPL---LTFLTSLGTLivwYFGGRQVLSGTM 257
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
829-1046 |
1.09e-10 |
|
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: 64.03 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 829 INGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGS 908
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 909 QIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGAT-QTRMLTGF-ASRDKQAlEMVGQItNEALSNIRTVAG 986
Cdd:cd18545 117 GLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLlRRRARKAWqRVRKKIS-NLNAYL-HESISGIRVIQS 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 987 IGKE----RRFIEaLETELEKPFKTAIQKANIYG----FCFAFAQCIMFIansasyrYGGYLISNEGL 1046
Cdd:cd18545 195 FAREdeneEIFDE-LNRENRKANMRAVRLNALFWplveLISALGTALVYW-------YGGKLVLGGAI 254
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1128-1284 |
1.32e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV-QFLRSNIGIVSQEPVLFA-CSIM 1205
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1206 DNIkygdntkeIPMERVIAAAKQAQLHDFVMSLPEKYETN--VGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1283
Cdd:PRK10895 97 DNL--------MAVLQIRDDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
.
gi 2462578034 1284 D 1284
Cdd:PRK10895 169 D 169
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
465-649 |
1.52e-10 |
|
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: 62.13 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 465 SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFST 544
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 545 TIAENIRYGREDATMEDIVQAAKEANAYNFiMDLPqqFDTLvgegggqmSGGQKQRVAIARALIRNPKILLLDMATSALD 624
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-EDRP--VAQL--------SAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 2462578034 625 NESEAMVQEVL-SKIQHGHTIISVAH 649
Cdd:cd03231 158 KAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
826-1033 |
2.11e-10 |
|
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: 63.28 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 826 RSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQG- 904
Cdd:cd18546 35 LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSEl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 905 AAGSQIGMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALsgAT-QTRMLTGFASRdkQALEMVGQIT---NEALSN 980
Cdd:cd18546 113 LQTGLVQLVVSLLTLVGIA-VVLLVLDPRLALVALAALPPLAL--ATrWFRRRSSRAYR--RARERIAAVNadlQETLAG 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 981 IRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFaqcIMFIANSAS 1033
Cdd:cd18546 188 IRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPG---VELLGNLAT 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1119-1289 |
2.13e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.08 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN-VQFLRSNIGIVSQEP 1197
Cdd:PRK13644 9 YSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1198 --VLFACSIMDNIKYG-DNTKEIPME---RVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDP 1271
Cdd:PRK13644 87 etQFVGRTVEEDLAFGpENLCLPPIEirkRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAGILTMEP 155
|
170
....*....|....*...
gi 2462578034 1272 KILLLDEATSALDTESEK 1289
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGI 173
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1126-1287 |
2.23e-10 |
|
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: 61.39 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGKVMIDGHDSKKVNVQfLRSNIGI--VSQEPVlfa 1201
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 csimdnikygdntkEIPMERVIaaakqaqlhDFVMSLpekyetNVGsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATS 1281
Cdd:cd03217 88 --------------EIPGVKNA---------DFLRYV------NEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
....*.
gi 2462578034 1282 ALDTES 1287
Cdd:cd03217 134 GLDIDA 139
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1119-1290 |
2.36e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPdqgkvMIDGHdskkvnvQFLRSNIGIVSQEPV 1198
Cdd:PLN03130 622 FSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP-----RSDAS-------VVIRGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFACSIMDNIKYGDNTKEIPMERVIAAAkqAQLHDFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:PLN03130 690 IFNATVRDNILFGSPFDPERYERAIDVT--ALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170
....*....|..
gi 2462578034 1279 ATSALDTESEKQ 1290
Cdd:PLN03130 767 PLSALDAHVGRQ 778
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
461-693 |
3.46e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 461 FHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--DIRSLNIQWLRDQIGIVEQE 538
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 539 P--VLFSTTIAENIRYGREDATM--EDIVQAAKEA----NAYNFiMDLPQQfdtlvgegggQMSGGQKQRVAIARALIRN 610
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVpeAEITRRVDEAltlvDAQHF-RHQPIQ----------CLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 611 PKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISvAHRLSTV-RAADTIIGFEHGTAVERG------THEELLERK 681
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIIS-SHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQA 233
|
250
....*....|...
gi 2462578034 682 GVYFT-LVTLQSQ 693
Cdd:PRK13638 234 GLTQPwLVKLHTQ 246
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
470-640 |
3.58e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.83 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 470 KILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI-QWLRDQIGIVEQEPVLFST-TIA 547
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 548 ENIRYG---REDATMEdivQAAKEANaynfimDLPQQFDT--LVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSA 622
Cdd:PRK10895 97 DNLMAVlqiRDDLSAE---QREDRAN------ELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170
....*....|....*...
gi 2462578034 623 LDNESeamVQEVLSKIQH 640
Cdd:PRK10895 168 VDPIS---VIDIKRIIEH 182
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
208-400 |
4.05e-10 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 62.47 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 208 MRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDaiadqMA------LFIQrmTSTICG-FLLGFFRGWKLTLVII 280
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISE-----LAhhgpedLFIS--IITIIGsFIILLTINVPLTLIVF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 281 SVSPLIGIGAATIGLsvsKFTDYELKAYAKAGVVADEV---ISSMRTVAAFGGEKREVERYEK-NLVF--AQRWGIRkgi 354
Cdd:cd18549 150 ALLPLMIIFTIYFNK---KMKKAFRRVREKIGEINAQLedsLSGIRVVKAFANEEYEIEKFDEgNDRFleSKKKAYK--- 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462578034 355 VMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQIFLSV 400
Cdd:cd18549 224 AMAYFFSGMNFFTNLLNLVVLVAGGYFII-KGEITLGDLVAFLLYV 268
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1126-1284 |
4.40e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMidgHDSKkvnvqfLRsnIGIVSQ----EPVL-F 1200
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGK------LR--IGYVPQklylDTTLpL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1201 ACSIMDNIKYGDNTKEI--PMERVIAAakqaQLHDFVMSlpekyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:PRK09544 85 TVNRFLRLRPGTKKEDIlpALKRVQAG----HLIDAPMQ--------------KLSGGETQRVLLARALLNRPQLLVLDE 146
|
....*.
gi 2462578034 1279 ATSALD 1284
Cdd:PRK09544 147 PTQGVD 152
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1130-1288 |
4.67e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGKVMIDGHDSKKVNVQFL-RSNIGIVSQEPVLFA-CSI 1204
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKeLSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1205 MDNIKYGDNTKE---IPMERVIAAAKQ--AQLhdfvmslpeKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1279
Cdd:PRK13549 100 LENIFLGNEITPggiMDYDAMYLRAQKllAQL---------KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
....*....
gi 2462578034 1280 TSALdTESE 1288
Cdd:PRK13549 171 TASL-TESE 178
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1133-1289 |
5.40e-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: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1133 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSkKVNVQFLRSNIGIVSQEPVLF-ACSIMDNIKYG 1211
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFhHLTVAEHILFY 1027
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 1212 DNTKEIPMErviaaakQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK 1289
Cdd:TIGR01257 1028 AQLKGRSWE-------EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1109-1278 |
5.51e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1109 QGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL-- 1186
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1187 -RSNIGIVSQEPVLFA-CSIMDNIKYgdntkeiPMeRVIAAAKQAQLHDFVMSlpeKYETnVGSQG------SQLSRGEK 1258
Cdd:PRK11831 82 vRKRMSMLFQSGALFTdMNVFDNVAY-------PL-REHTQLPAPLLHSTVMM---KLEA-VGLRGaaklmpSELSGGMA 149
|
170 180
....*....|....*....|
gi 2462578034 1259 QRIAIARAIVRDPKILLLDE 1278
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDE 169
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1129-1284 |
7.41e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQepvlfacsimDNI 1208
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ----------NAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1209 KYGDntkeIPMERVIAAAKQAQLHDFVMSLPEKYE-----------TNVGSQG-SQLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:PRK10253 92 TPGD----ITVQELVARGRYPHQPLFTRWRKEDEEavtkamqatgiTHLADQSvDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
....*...
gi 2462578034 1277 DEATSALD 1284
Cdd:PRK10253 168 DEPTTWLD 175
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1128-1285 |
7.61e-10 |
|
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: 60.62 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSkkvnvQFLRSNIGIvsqEPVLfacSIMDN 1207
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGGGF---NPEL---TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1208 IK-----YGDNTKEIP--MERVIAAakqAQLHDFvMSLPEKyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:cd03220 105 IYlngrlLGLSRKEIDekIDEIIEF---SELGDF-IDLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVL 170
|
....*
gi 2462578034 1281 SALDT 1285
Cdd:cd03220 171 AVGDA 175
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
794-1000 |
8.17e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 61.81 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 794 VGAAVNGTV--TPLYAFLFSQILGTfsipdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFR 871
Cdd:cd18565 22 IGVAIDAVFngEASFLPLVPASLGP------ADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 872 AMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLAL-SGA 950
Cdd:cd18565 96 HVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAgTYW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462578034 951 TQTRMLTGFASRDKQALEMVGQITNeALSNIRTVAGIGKERRFIEALETE 1000
Cdd:cd18565 174 FQRRIEPRYRAVREAVGDLNARLEN-NLSGIAVIKAFTAEDFERERVADA 222
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
791-1044 |
1.08e-09 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 61.02 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 791 VGSVGAAVNGTVTPLyafLFSQILGTFSIPDKEEQRSQINGV-------CLLFVAMgcvSLFTqFLQGYAFAKSGELLTK 863
Cdd:cd18574 3 LSALAAALVNIQIPL---LLGDLVNVISRSLKETNGDFIEDLkkpalklLGLYLLQ---SLLT-FAYISLLSVVGERVAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 864 RLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFP 943
Cdd:cd18574 76 RLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 944 FLALSGATQTRMLTGFAsrdKQALEMVGQITN---EALSNIRTVAGIGKERRFIEALETELEKPFKTAIQkaniYGFCFA 1020
Cdd:cd18574 154 VVVLVGTLYGSFLRKLS---RRAQAQVAKATGvadEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK----LGLGIG 226
|
250 260
....*....|....*....|....*...
gi 2462578034 1021 FAQCIMFIA-NS---ASYRYGGYLISNE 1044
Cdd:cd18574 227 IFQGLSNLAlNGivlGVLYYGGSLVSRG 254
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1123-1290 |
1.10e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.43 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFAC 1202
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 SIMDNIKY--GDNTKeipmERVIAAAKQAQLHDFvmslpEKYETNvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEAT 1280
Cdd:cd03231 89 SVLENLRFwhADHSD----EQVEEALARVGLNGF-----EDRPVA------QLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170
....*....|
gi 2462578034 1281 SALDTESEKQ 1290
Cdd:cd03231 154 TALDKAGVAR 163
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
200-424 |
1.14e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 61.01 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 200 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIqrmTST-----ICGFLlgFFRGWK 274
Cdd:cd18778 67 AEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI---TNVltlvgVAIIL--FSINPK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 275 LTLVIISVSPLIGIGAAtiglsvsKFTDYELKAYAKA--------GVVADEvISSMRTVAAFGGEKREVERYEK------ 340
Cdd:cd18778 142 LALLTLIPIPFLALGAW-------LYSKKVRPRYRKVrealgelnALLQDN-LSGIREIQAFGREEEEAKRFEAlsrryr 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 341 --NLVFAQRWGIrKGIVMGFFTGfvwclifLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVI-----VGALNLGNaspc 413
Cdd:cd18778 214 kaQLRAMKLWAI-FHPLMEFLTS-------LGTVLVLGFGGRLVLA-GELTIGDLVAFLLYLGlfyepITSLHGLN---- 280
|
250
....*....|.
gi 2462578034 414 lEAFATGRAAA 424
Cdd:cd18778 281 -EMLQRALAGA 290
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
457-649 |
1.63e-09 |
|
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: 62.26 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 457 HNVTFHYPsrPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLiqrfydpcegMVTVD----GHDIRSLNIQwlrdqI 532
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI----------MAGVDkdfnGEARPQPGIK-----V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLFST-TIAENI-------------------RYGREDATM----------EDIVQAAkeaNAYNFIMDLPQQF 582
Cdd:TIGR03719 71 GYLPQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFdklaaeqaelQEIIDAA---DAWDLDSQLEIAM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 583 DTLVGEGGGQMSGGQK----QRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLskIQHGHTIISVAH 649
Cdd:TIGR03719 148 DALRCPPWDADVTKLSggerRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGTVVAVTH 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1134-1284 |
1.91e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1134 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQ---------FLRSNIGIVSQEP---VLFA 1201
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYalseaerrrLLRTEWGFVHQHPrdgLRMQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNI----------KYGD--NTKEIPMERV-IAAAKqaqLHDfvmsLPekyetnvgsqgSQLSRGEKQRIAIARAIV 1268
Cdd:PRK11701 106 VSAGGNIgerlmavgarHYGDirATAGDWLERVeIDAAR---IDD----LP-----------TTFSGGMQQRLQIARNLV 167
|
170
....*....|....*.
gi 2462578034 1269 RDPKILLLDEATSALD 1284
Cdd:PRK11701 168 THPRLVFMDEPTGGLD 183
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
454-670 |
2.19e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRP--------------------EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFY--DPCEG 511
Cdd:COG2401 8 FVLMRVTKVYSSVLdlservaivleafgvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 512 MVTVDghdirslNIQWLRDqigiveqepvlfsTTIAENI-RYGREDATMEdIVQAAKEANAYNFI-----MDLPQQFdtl 585
Cdd:COG2401 88 CVDVP-------DNQFGRE-------------ASLIDAIgRKGDFKDAVE-LLNAVGLSDAVLWLrrfkeLSTGQKF--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 586 vgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA--ADTII 661
Cdd:COG2401 144 --------------RFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarRAGITLVVATHHYDVIDDlqPDLLI 209
|
....*....
gi 2462578034 662 GFEHGTAVE 670
Cdd:COG2401 210 FVGYGGVPE 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1139-1290 |
2.64e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1139 PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV-MIDGHDSKKVNVQFLRsnigivsqepvlfacsimdnikygdntkei 1217
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 1218 pmerviaaakqaqlhdfvmslpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:smart00382 51 -------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1126-1284 |
2.77e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.31 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL---ERfYDPDQGKVMIDGHD---------SKK------------- 1180
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDilelspderARAgiflafqypveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1181 -VNV-QFLRSNIGIVSQEPVlfacSIMDNIKygdntkeipmeRVIAAAKQaqlhdfvMSLPEKY---ETNVGsqgsqLSR 1255
Cdd:COG0396 91 gVSVsNFLRTALNARRGEEL----SAREFLK-----------LLKEKMKE-------LGLDEDFldrYVNEG-----FSG 143
|
170 180
....*....|....*....|....*....
gi 2462578034 1256 GEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
465-651 |
2.89e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 465 SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdiRSLNIQWLRDQ----IGIVEQEPV 540
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 541 LFST-TIAENIRYGREDATMEDIVQAAK---EANAYNFIMDLPQQFDTLVGEGGGQMSGGqkqrVAIARALIRNPKILLL 616
Cdd:PRK10762 90 LIPQlTIAENIFLGREFVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQM----VEIAKVLSFESKVIIM 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462578034 617 DMATSAL-DNESEAMVQeVLSKIQ-HGHTIISVAHRL 651
Cdd:PRK10762 166 DEPTDALtDTETESLFR-VIRELKsQGRGIVYISHRL 201
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1128-1287 |
2.97e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.02 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL-ERFYDPD-QGKVMIDGhdsKKVNVQFLRSnIGIVSQEPVLFACSim 1205
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILING---RPLDKNFQRS-TGYVEQQDVHSPNL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1206 dnikygdnTKEIPMErvIAAAKQAqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSALDT 1285
Cdd:cd03232 95 --------TVREALR--FSALLRG-----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
..
gi 2462578034 1286 ES 1287
Cdd:cd03232 142 QA 143
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1128-1283 |
3.22e-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: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFA-CSIM 1205
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAIVPEGRRVFSrMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1206 DNIKYGD--NTKEIPMERViaaakqAQLHDFvmsLPEKYETNVGSQGSqLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1283
Cdd:PRK11614 99 ENLAMGGffAERDQFQERI------KWVYEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1126-1290 |
3.43e-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: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGKVMIDGHDSKKVNVQFL-RSNIGIVSQEPVLFA 1201
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 -CSIMDNIKYGdNTKEIPMERVIAAAKQAQLHDFV--MSLPEkyeTNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:TIGR02633 92 eLSVAENIFLG-NEITLPGGRMAYNAMYLRAKNLLreLQLDA---DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170
....*....|..
gi 2462578034 1279 ATSALdTESEKQ 1290
Cdd:TIGR02633 168 PSSSL-TEKETE 178
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1133-1290 |
3.59e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1133 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD-PdqGKVM-----IDGHD----SKKVNVQFLRSNIGIVSQEPV--LF 1200
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaekleFNGQDlqriSEKERRNLVGAEVAMIFQDPMtsLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1201 AC-----SIMDNIKY--GDNTKEiPMERVIAAAKQAQLHDfvmslPEkyeTNVGSQGSQLSRGEKQRIAIARAIVRDPKI 1273
Cdd:PRK11022 104 PCytvgfQIMEAIKVhqGGNKKT-RRQRAIDLLNQVGIPD-----PA---SRLDVYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170
....*....|....*..
gi 2462578034 1274 LLLDEATSALDTESEKQ 1290
Cdd:PRK11022 175 LIADEPTTALDVTIQAQ 191
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
178-382 |
3.86e-09 |
|
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: 59.44 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 178 YYAGIAVAVLITGYIQICFWVIA---AARQI-QKMrkfyFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMAL 253
Cdd:cd18580 44 YAALLVLASVLLVLLRWLLFVLAglrASRRLhDKL----LRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 254 FIQRMTSTICGFllgffrgwkltLVIISVSPLIGIGAATIGLSVSKFTDY------ELK---AYAKAGVVA--DEVISSM 322
Cdd:cd18580 120 FLQSLFSVLGSL-----------IVIAIVSPYFLIVLPPLLVVYYLLQRYylrtsrQLRrleSESRSPLYShfSETLSGL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 323 RTVAAFGGEKREVERYEKNL----------VFAQRWgirKGIVMGFF-TGFVWCLIFLCYALAFWYGSTLV 382
Cdd:cd18580 189 STIRAFGWQERFIEENLRLLdasqrafyllLAVQRW---LGLRLDLLgALLALVVALLAVLLRSSISAGLV 256
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1119-1286 |
4.06e-09 |
|
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: 58.57 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRpdSQVLNGLSVSISPG-----QTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnvqflrsnigiV 1193
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1194 SQEPVLFacsimdNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSlPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKI 1273
Cdd:cd03237 64 SYKPQYI------KADYEGTVRDLLSSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170
....*....|...
gi 2462578034 1274 LLLDEATSALDTE 1286
Cdd:cd03237 137 YLLDEPSAYLDVE 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
481-673 |
7.03e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 481 PGEMTALVGPSGAGKSTALQLIQRFYDP-CEGMVTVDGHDIRSLNIQWLRdqigiveqepvlfsttiaeNIRYGREDATM 559
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPpGGGVIYIDGEDILEEVLDQLL-------------------LIIVGGKKASG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 560 EDIVQAakeanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLS--- 636
Cdd:smart00382 62 SGELRL----------------------------------RLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462578034 637 ----KIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 673
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1123-1288 |
8.69e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNV----QFLRSNIGIVSQE-P 1197
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFksskEALENGISMVHQElN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1198 VLFACSIMDNIKYGdntkEIPMERVIaaAKQAQLHDFVMSLPEKYETNVG--SQGSQLSRGEKQRIAIARAIVRDPKILL 1275
Cdd:PRK10982 84 LVLQRSVMDNMWLG----RYPTKGMF--VDQDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170
....*....|...
gi 2462578034 1276 LDEATSALdTESE 1288
Cdd:PRK10982 158 MDEPTSSL-TEKE 169
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
468-688 |
1.13e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 468 EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQ----LIQrfydPCEGMVTVDGHDIRSLNIQWLRdQIGIV----EQ-- 537
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgILV----PTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 538 --EPVLFSTTIAENIrYGREDA----TMEDIVQaakeanaynfIMDLPQQFDTLVgegggqmsggqkqR---------VA 602
Cdd:COG4586 109 wdLPAIDSFRLLKAI-YRIPDAeykkRLDELVE----------LLDLGELLDTPV-------------RqlslgqrmrCE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 679
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
....*....
gi 2462578034 680 RKGVYFTLV 688
Cdd:COG4586 245 RFGPYKTIV 253
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
471-678 |
1.13e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRfyDPCE----------GMVTVDGHDIRSLNIQWLRDQIGIVEQ--E 538
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 539 PVlFSTTIAENIRYGR----------EDATMEDIVQAAKEANAynfimdlpqqfDTLVGEGGGQMSGGQKQRVAIARAL- 607
Cdd:PRK13547 94 PA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 608 --------IRNPKILLLDMATSALDNESE----AMVQEVLSKIQHGhtIISVAHRLS-TVRAADTIIGFEHGTAVERGTH 674
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLG--VLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239
|
....
gi 2462578034 675 EELL 678
Cdd:PRK13547 240 ADVL 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1124-1290 |
1.15e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1124 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV-------------MIDGHDSKKVNVQFLR-SN 1189
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1190 IGIVSQEPV-----LFAC--SIMDNIKYGDNTKEipmERVIAAAKQaqLHDFVmSLPEKyETNVGSQGSQLSRGEKQRIA 1262
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQGASR---EEAMVEAKR--MLDQV-RIPEA-QTILSRYPHQLSGGMRQRVM 178
|
170 180
....*....|....*....|....*...
gi 2462578034 1263 IARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQ 206
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
179-362 |
1.30e-08 |
|
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: 57.87 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 179 YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRM 258
Cdd:cd18606 41 YAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 259 TSTICGFLLgffrgwkltlvIISVSPLIGIGAATIGLSVSKFTDY------ELK---AYAKAGVVA--DEVISSMRTVAA 327
Cdd:cd18606 121 SSIIGTFIL-----------IIIYLPWFAIALPPLLVLYYFIANYyrassrELKrleSILRSFVYAnfSESLSGLSTIRA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462578034 328 FGGEKREVERYEKN---------LVFA-QRW-GIR---KGIVMGFFTGF 362
Cdd:cd18606 190 YGAQDRFIKKNEKLidnmnrayfLTIAnQRWlAIRldlLGSLLVLIVAL 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
465-649 |
1.34e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.21 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 465 SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG------HDIRSLNIQWLRDQIGIveqE 538
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqRDEPHENILYLGHLPGL---K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 539 PVLfstTIAENIRYGREDATMEDI-VQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsggqkQRVAIARALIRN 610
Cdd:TIGR01189 86 PEL---SALENLHFWAAIHGGAQRtIEDALAAVGLTGFEDLPaaqlsagQQ-----------------RRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462578034 611 PKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAH 649
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLrAHLARGGIVLLTTH 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1128-1289 |
1.34e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQ---GKVMIDGHDSKKV-----NVQFLRSNIGIVSQEPVL 1199
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 F-ACSIMDNIKYGdNTKEIPMERV-IAAAKQAQLHDFVMSLpekyeTNVG------SQGSQLSRGEKQRIAIARAIVRDP 1271
Cdd:PRK09984 98 VnRLSVLENVLIG-ALGSTPFWRTcFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQA 171
|
170
....*....|....*...
gi 2462578034 1272 KILLLDEATSALDTESEK 1289
Cdd:PRK09984 172 KVILADEPIASLDPESAR 189
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
180-394 |
1.34e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 57.88 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18550 46 VAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEV--ISSMRTVAAFGGEKREVER 337
Cdd:cd18550 126 TLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAAR 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 338 YEKNLVFAQRWGIRK-------GIVMGFFTGFVwcliflcYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18550 206 FARRSRELRDLGVRQalagrwfFAALGLFTAIG-------PALVYWVGGLLVIG-GGLTIGTLV 261
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
213-398 |
1.39e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 57.96 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 213 FRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGaat 292
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAG--- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 293 iglsVSKFTDYELKAYA----KAGVVA---DEVISSMRTVAAFGGEKREVERYEK--NLVFAQRWG-IRKGIVmgfFTGF 362
Cdd:cd18565 171 ----TYWFQRRIEPRYRavreAVGDLNarlENNLSGIAVIKAFTAEDFERERVADasEEYRDANWRaIRLRAA---FFPV 243
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462578034 363 VWCLIFLCYALAFWYGSTLVLD-----EGEYTPGTLVqIFL 398
Cdd:cd18565 244 IRLVAGAGFVATFVVGGYWVLDgpplfTGTLTVGTLV-TFL 283
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
465-649 |
1.40e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 465 SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL------NIQWLRDQIGIveqE 538
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 539 PVLfstTIAENIRY---GREDATMEDIVQAAKEANAYNFiMDLP-------QQfdtlvgegggqmsggqkQRVAIARALI 608
Cdd:PRK13538 87 TEL---TALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVPvrqlsagQQ-----------------RRVALARLWL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462578034 609 RNPKILLLDMATSALDNESEAMVQEVLSK-IQHGHTIISVAH 649
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
182-394 |
1.57e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 57.57 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 182 IAVAVLITGYIQIcfwVIAAARQI---QKMRKF-------YFRRIMRMEIGWFDCNSVGELNTRFSDDiNKINDAIADQ- 250
Cdd:cd18568 44 ILIGLLIVGIFQI---LLSAVRQYlldYFANRIdlsllsdFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSa 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 251 MALFIQRMTSTICGFLLgFFRGWKLTLVIISVSPLIgigaATIGLSVSKFTDYELKAYAKAGVVAD----EVISSMRTVA 326
Cdd:cd18568 120 LTTILDLLMVFIYLGLM-FYYNLQLTLIVLAFIPLY----VLLTLLSSPKLKRNSREIFQANAEQQsflvEALTGIATIK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 327 AFGGEKREVERYEK---NLVFAQRWGIRKGIVMGFFTGFvwcLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18568 195 ALAAERPIRWRWENkfaKALNTRFRGQKLSIVLQLISSL---INHLGTIAVLWYGAYLVIS-GQLTIGQLV 261
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1126-1289 |
1.62e-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: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGKVM-----------ID------------GHDSKK 1180
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVErpskvgepcpvcGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1181 VNVQF----------LRSNIGIVSQEPvlFAC----SIMDNIKYGDNTKEIPMERVIAAA----KQAQLHDFVMSLpeky 1242
Cdd:TIGR03269 92 EEVDFwnlsdklrrrIRKRIAIMLQRT--FALygddTVLDNVLEALEEIGYEGKEAVGRAvdliEMVQLSHRITHI---- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462578034 1243 etnvgsqGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK 1289
Cdd:TIGR03269 166 -------ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1110-1286 |
2.02e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1110 GKIDFVDCKFTYpSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidgHDSKKVNVQFLRSN 1189
Cdd:PRK11147 316 GKIVFEMENVNY-QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1190 IGIVSQEPvlfacSIMDNIkyGDNTKEIPM---ERVIAaakqAQLHDFVMSlPEKYETNVgsqgSQLSRGEKQRIAIARA 1266
Cdd:PRK11147 391 RAELDPEK-----TVMDNL--AEGKQEVMVngrPRHVL----GYLQDFLFH-PKRAMTPV----KALSGGERNRLLLARL 454
|
170 180
....*....|....*....|
gi 2462578034 1267 IVRDPKILLLDEATSALDTE 1286
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVE 474
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1123-1287 |
2.23e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 55.83 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFAC 1202
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 SIMDNIKYgdntkeipmerviaaakQAQLHDFVMSLPEKYETNVGSQG------SQLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:TIGR01189 89 SALENLHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170
....*....|.
gi 2462578034 1277 DEATSALDTES 1287
Cdd:TIGR01189 152 DEPTTALDKAG 162
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1125-1284 |
2.78e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1125 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH-----DSKKvnvqFLRSNIGIVSQEPVL 1199
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswSSKA----FARKVAYLPQQLPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 FACSIMDNI------------KYGDNTKEipmeRVIAAAKQAQLHDFVMSLpekyetnVGSqgsqLSRGEKQRIAIARAI 1267
Cdd:PRK10575 98 EGMTVRELVaigrypwhgalgRFGAADRE----KVEEAISLVGLKPLAHRL-------VDS----LSGGERQRAWIAMLV 162
|
170
....*....|....*..
gi 2462578034 1268 VRDPKILLLDEATSALD 1284
Cdd:PRK10575 163 AQDSRCLLLDEPTSALD 179
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1129-1289 |
3.35e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFY--DPDQGKVMIDghdskkvNVQFlrsnigivSQEpvlfaCSIMD 1206
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP-------DNQF--------GRE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1207 NIKYGDNTKEipmerVIAAAKQAQLHDFVMSLpEKYetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1286
Cdd:COG2401 105 AIGRKGDFKD-----AVELLNAVGLSDAVLWL-RRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
...
gi 2462578034 1287 SEK 1289
Cdd:COG2401 171 TAK 173
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
454-677 |
4.04e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFhypSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL---RD 530
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEPVLFS-TTIAENIRYG-RE-----DATMEDIVQAAKEANAYNFIMDL-PQQFdtlvgegggqmSGGQKQRVA 602
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPlREhtqlpAPLLHSTVMMKLEAVGLRGAAKLmPSEL-----------SGGMARRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADT--IIGFEHgtAVERGTHEEL 677
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHayIVADKK--IVAHGSAQAL 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
458-677 |
4.76e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 458 NVTFHYPSrPEVKILNDLNMAIKPGEMTALVGPSGAGKS-TALQLIQRFYDP--CEGMVTVDGHDIRSLN---IQWLR-D 530
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPekeLNKLRaE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 531 QIGIVEQEP----------------VLF-------STTIAENIRygredatMEDIV---QAAKEANAYnfimdlPQQFdt 584
Cdd:PRK09473 98 QISMIFQDPmtslnpymrvgeqlmeVLMlhkgmskAEAFEESVR-------MLDAVkmpEARKRMKMY------PHEF-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 585 lvgegggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTII 661
Cdd:PRK09473 163 ---------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVL 233
|
250
....*....|....*.
gi 2462578034 662 GFEHGTAVERGTHEEL 677
Cdd:PRK09473 234 VMYAGRTMEYGNARDV 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1129-1287 |
6.08e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLE-RFYDPD-QGKVMIDGhdsKKVNVQFLRsNIGIVSQEPVLFA----- 1201
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 -----CSIMDNIK-YGDNTKEIPMERVIAAakqaqlhdfvMSLPEKYETNVGSQGSQ-LSRGEKQRIAIARAIVRDPKIL 1274
Cdd:PLN03211 159 etlvfCSLLRLPKsLTKQEKILVAESVISE----------LGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLL 228
|
170
....*....|...
gi 2462578034 1275 LLDEATSALDTES 1287
Cdd:PLN03211 229 ILDEPTSGLDATA 241
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1123-1286 |
6.17e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1123 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNvqflRSN-IGIVSQEPVLFA 1201
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 -CSIMDNIKY-----GDNTKEIPMERVIaaakqaqlhdfVMSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILL 1275
Cdd:PRK13543 96 dLSTLENLHFlcglhGRRAKQMPGSALA-----------IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWL 160
|
170
....*....|.
gi 2462578034 1276 LDEATSALDTE 1286
Cdd:PRK13543 161 LDEPYANLDLE 171
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
180-394 |
6.66e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 55.57 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQIcFWVIAAARQIQ-KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAdqMALFIQRM 258
Cdd:cd18543 46 LALGVAEAVLSFLRR-YLAGRLSLGVEhDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA--FGPFLLGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 259 TSTIC-GFLLGFFRGWKLTLVIISVSPLIGIGAAtigLSVSKFTDYELKAYAKAGVVA---DEVISSMRTVAAFGGEKRE 334
Cdd:cd18543 123 LLTLVvGLVVMLVLSPPLALVALASLPPLVLVAR---RFRRRYFPASRRAQDQAGDLAtvvEESVTGIRVVKAFGRERRE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 335 VERYEK--NLVFAQRwgIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18543 200 LDRFEAaaRRLRATR--LRAARLRARFWPLLEALPELGLAAVLALGGWLVAN-GSLTLGTLV 258
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
464-647 |
6.69e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 464 PSRPEVKILNDLNMAIKPGEMTALVGPSGAGKST---ALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIgIVEQEPV 540
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 541 LFSTTiaenirygredaTMEDIVQAAKEANAYNFIMDLP--QQfdtlvgegggqmsggqkQRVAIARALIRNPKILLLDM 618
Cdd:cd03233 94 HFPTL------------TVRETLDFALRCKGNEFVRGISggER-----------------KRVSIAEALVSRASVLCWDN 144
|
170 180 190
....*....|....*....|....*....|..
gi 2462578034 619 ATSALDNESE---AMVQEVLSKIQHGHTIISV 647
Cdd:cd03233 145 STRGLDSSTAleiLKCIRTMADVLKTTTFVSL 176
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1125-1288 |
7.07e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.07 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1125 PDSQVL-NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvnvqflRSNIGIVSQEPVLFACS 1203
Cdd:TIGR00954 462 PNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1204 IMDNIKYGDNTKEIPMERV-----IAAAKQAQLHDFVmslpekyETNVGSQGSQ-----LSRGEKQRIAIARAIVRDPKI 1273
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLsdkdlEQILDNVQLTHIL-------EREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQF 603
|
170
....*....|....*
gi 2462578034 1274 LLLDEATSALDTESE 1288
Cdd:TIGR00954 604 AILDECTSAVSVDVE 618
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
420-654 |
7.08e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 420 GRAAATSIFETIDRKPIIDCMSedGYKLD--------RIKGEI-EFHNVTFHYPSRPEVKILNDLNMAIKPGEMTALVGP 490
Cdd:TIGR02633 217 GQHVATKDMSTMSEDDIITMMV--GREITslyphephEIGDVIlEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 491 SGAGKSTALQLIQRFYD-PCEGMVTVDGH--DIRSLnIQWLRDQI----------GIVEQEPVLFSTTIAENIRY---GR 554
Cdd:TIGR02633 295 VGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRNP-AQAIRAGIamvpedrkrhGIVPILGVGKNITLSVLKSFcfkMR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 555 EDATMED--IVQAAKEANAYNFIMDLP--------QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALD 624
Cdd:TIGR02633 374 IDAAAELqiIGSAIQRLKVKTASPFLPigrlsggnQQ------------------KAVLAKMLLTNPRVLILDEPTRGVD 435
|
250 260 270
....*....|....*....|....*....|.
gi 2462578034 625 NESEAMVQEVLSKI-QHGHTIISVAHRLSTV 654
Cdd:TIGR02633 436 VGAKYEIYKLINQLaQEGVAIIVVSSELAEV 466
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
179-363 |
1.13e-07 |
|
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: 55.17 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 179 YAGIAVAVLITGYIQICFWVIA---AARQI-QKMrkfyFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALF 254
Cdd:cd18604 49 YALISLLSVLLGTLRYLLFFFGslrASRKLhERL----LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 255 IQRMTSTICGFllgffrgwkltLVIISVSP---LIGIGAATIGLSVSKFtdY-----ELK---AYAKAGVVA--DEVISS 321
Cdd:cd18604 125 LESTLSLLVIL-----------IAIVVVSPaflLPAVVLAALYVYIGRL--YlrasrELKrleSVARSPILShfGETLAG 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 322 MRTVAAFGGEKREVER-YEK---------NLVFAQRW-GIRKGIVMGFFTGFV 363
Cdd:cd18604 192 LVTIRAFGAEERFIEEmLRRidrysrafrYLWNLNRWlSVRIDLLGALFSFAT 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
468-653 |
1.24e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.04 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 468 EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQ-RFYDPC-EGMVTVDGhdiRSLNIQWLRdQIGIVEQEPVLFS-T 544
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 545 TIAENIRYGREDATMEDIVQAAKEANAYNFI--MDLPQQFDTLV-GEGGGQMSGGQKQRVAIARALIRNPKILLLDMATS 621
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIgNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190
....*....|....*....|....*....|...
gi 2462578034 622 ALDNESE-AMVQEVLSKIQHGHTIISVAHRLST 653
Cdd:PLN03211 236 GLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
468-679 |
1.38e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 468 EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRDQIGIVEQEPV---- 540
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 541 ---LFSTTIAENIRY-----GREDAT-----MEDIVQAAKEANAYnfimdlPQQFDtlvgegggqmsGGQKQRVAIARAL 607
Cdd:PRK10261 416 prqTVGDSIMEPLRVhgllpGKAAAArvawlLERVGLLPEHAWRY------PHEFS-----------GGQRQRICIARAL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 608 IRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
200-394 |
1.49e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 54.52 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 200 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSdDINKINDAIADQM-ALFIQRMTSTICGFLLgFFRGWKLTLV 278
Cdd:cd18782 69 TANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTAlTTLLDVLFSVIYIAVL-FSYSPLLTLV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 279 IISVSPLIGIgaatIGLSVSKFTDYELKAYAKAGVVAD----EVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGI 354
Cdd:cd18782 147 VLATVPLQLL----LTFLFGPILRRQIRRRAEASAKTQsylvESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTV 222
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462578034 355 VMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLV 394
Cdd:cd18782 223 LGTTSGSLSQFLNKLSSLLVLWVGAYLVL-RGELTLGQLI 261
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1120-1287 |
2.16e-07 |
|
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: 55.33 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTsiqLLerfydpdqgKVM--IDghdsKKVNVQFLRS---NIGIVS 1194
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST---LL---------RIMagVD----KDFNGEARPQpgiKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1195 QEP-----------VLFACS----IMD-----NIKYGDNTKEipMERViaAAKQAQLHDFV------------------M 1236
Cdd:TIGR03719 75 QEPqldptktvrenVEEGVAeikdALDrfneiSAKYAEPDAD--FDKL--AAEQAELQEIIdaadawdldsqleiamdaL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 1237 SLPEKyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1287
Cdd:TIGR03719 151 RCPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
472-678 |
2.22e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.69 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYdPCEGMVTVDGHDIRSLNIQ-------WLRDQigiveQEPVLF-- 542
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQ-----QSPPFAmp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 -----STTIAENIRYGREDATMEDIVQAAKeanaynfIMD-LPQQFDTLvgegggqmSGGQKQRVAIARALIR-----NP 611
Cdd:COG4138 86 vfqylALHQPAGASSEAVEQLLAQLAEALG-------LEDkLSRPLTQL--------SGGEWQRVRLAAVLLQvwptiNP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 612 --KILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:COG4138 151 egQLLLLDEPMNSLDVAQQAALDRLLRELcQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
864-998 |
2.83e-07 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 53.63 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 864 RLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFP 943
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLP 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 944 FLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKE----RRFIEALE 998
Cdd:cd18589 148 LLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEegeaQRYRQRLQ 206
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
180-394 |
3.12e-07 |
|
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: 53.65 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVLITGYIQICFWVIAAARQIQKM----RKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA-LF 254
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLlydlRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVqLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 255 IQRMTSTICGFLLGFFRgWKLTLVIISVSPLIGIgaATIglsvsKFTDYELKAYAK-----AGVVAD--EVISSMRTVAA 327
Cdd:cd18546 122 VSLLTLVGIAVVLLVLD-PRLALVALAALPPLAL--ATR-----WFRRRSSRAYRRareriAAVNADlqETLAGIRVVQA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 328 FGGEKREVERY-EKNLVF--AQRWGIRkgiVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18546 194 FRRERRNAERFaELSDDYrdARLRAQR---LVAIYFPGVELLGNLATAAVLLVGAWRVAA-GTLTVGVLV 259
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
454-502 |
5.88e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 5.88e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLI 502
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
454-624 |
6.26e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.31 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPEVkiLNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDqIG 533
Cdd:PRK11650 4 LKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRD-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFS-TTIAENIRYGREDATM------EDIVQAAKeanaynfIMDL-------PQQFdtlvgegggqmSGGQKQ 599
Cdd:PRK11650 80 MVFQNYALYPhMSVRENMAYGLKIRGMpkaeieERVAEAAR-------ILELeplldrkPREL-----------SGGQRQ 141
|
170 180
....*....|....*....|....*
gi 2462578034 600 RVAIARALIRNPKILLLDMATSALD 624
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1125-1284 |
7.77e-07 |
|
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: 51.98 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1125 PDSQVLNGLSVsISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV------------------------MIDGHDSKK 1180
Cdd:cd03236 12 PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildefrgselqnyftkLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1181 VNVQFlrsnigiVSQEPVLFACSIMDNIKYGD--NTKEIPMERviaaakqaqlhdfvMSLPEKYETNVgsqgSQLSRGEK 1258
Cdd:cd03236 91 VKPQY-------VDLIPKAVKGKVGELLKKKDerGKLDELVDQ--------------LELRHVLDRNI----DQLSGGEL 145
|
170 180
....*....|....*....|....*.
gi 2462578034 1259 QRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:cd03236 146 QRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1130-1288 |
7.81e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVnvqfLRSN-IGIVSQE-------PVLFA 1201
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNlVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNiKYGD-----NTKEIPMERVIAAAKQAQLHDFvmslpeKYEtnvgsQGSQLSRGEKQRIAIARAIVRDPKILLL 1276
Cdd:PRK15056 99 DVVMMG-RYGHmgwlrRAKKRDRQIVTAALARVDMVEF------RHR-----QIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170
....*....|..
gi 2462578034 1277 DEATSALDTESE 1288
Cdd:PRK15056 167 DEPFTGVDVKTE 178
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1126-1305 |
8.52e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 51.88 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ERFYDPDQGKVMIDGHDSKKVNVQfLRSNIGIV--SQEPV--- 1198
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEPD-ERARAGLFlaFQYPEeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 -----LFACSIMDNIKYGDNTKEIPMERVIAAAKQA-QLHDFVMSLPEKYeTNVGsqgsqLSRGEKQRIAIARAIVRDPK 1272
Cdd:TIGR01978 91 gvsnlEFLRSALNARRSARGEEPLDLLDFEKLLKEKlALLDMDEEFLNRS-VNEG-----FSGGEKKRNEILQMALLEPK 164
|
170 180 190
....*....|....*....|....*....|...
gi 2462578034 1273 ILLLDEATSALDTESEKQpCCDHLDKSHTPQMA 1305
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKI-VAEGINRLREPDRS 196
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
181-394 |
9.02e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 52.16 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 181 GIAVAVLITGYIQICF---WVIAAAR---QIQKMRKFyFRRIMRMEIGWFDCNSVGELNTRFSDdinkiNDAIADqmaLF 254
Cdd:cd18779 45 GLGLAALVLTQLLAGLlrsHLLLRLRtrlDTQLTLGF-LEHLLRLPYRFFQQRSTGDLLMRLSS-----NATIRE---LL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 255 IQRMTSTIC--GFLLGFFrgwkltLVIISVSPL-----IGIGAATIGL------SVSKFTDYELKAYAKAGVVADEVISS 321
Cdd:cd18779 116 TSQTLSALLdgTLVLGYL------ALLFAQSPLlglvvLGLAALQVALllatrrRVRELMARELAAQAEAQSYLVEALSG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 322 MRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18779 190 IETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLD-GQLSLGTML 261
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
467-624 |
1.07e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 467 PEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLI----QRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLF 542
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 STTIAENIRYG--------REDATMEDiVQAAKEANAYNFIMDLPQQFDTLV-GEGGGQMSGGQKQRVAIARALIRNPKI 613
Cdd:TIGR00956 152 HLTVGETLDFAarcktpqnRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVgNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170
....*....|.
gi 2462578034 614 LLLDMATSALD 624
Cdd:TIGR00956 231 QCWDNATRGLD 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
453-535 |
1.17e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 453 EIEFHNVTFHYPSRPEVkiLNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQI 532
Cdd:PRK10522 322 TLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
...
gi 2462578034 533 GIV 535
Cdd:PRK10522 400 SAV 402
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1112-1287 |
1.57e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1112 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKK------VNVQF 1185
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlctyqKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1186 LRSNIGIvsqEPVLfacSIMDNIKYGDNTKEIPME--RVIAAAKQAQLHDFVMSLpekyetnvgsqgsqLSRGEKQRIAI 1263
Cdd:PRK13540 79 VGHRSGI---NPYL---TLRENCLYDIHFSPGAVGitELCRLFSLEHLIDYPCGL--------------LSSGQKRQVAL 138
|
170 180
....*....|....*....|....
gi 2462578034 1264 ARAIVRDPKILLLDEATSALDTES 1287
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELS 162
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
454-703 |
1.92e-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: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPsrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRF--YDPCEGMVTVdgHDIRSLNIQWLRDQ 531
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIY--HVALCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 532 IGIVEQEPVLFST-------------TIAENIR-------------YGrEDATMEDIVQAAKEA-----NAYNFIMDLPQ 580
Cdd:TIGR03269 76 SKVGEPCPVCGGTlepeevdfwnlsdKLRRRIRkriaimlqrtfalYG-DDTVLDNVLEALEEIgyegkEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 581 --QFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSK--IQHGHTIISVAHRLSTV-R 655
Cdd:TIGR03269 155 mvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIeD 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462578034 656 AADTIIGFEHGTAVERGTHEELLErkgVYFTLVTLQSQGNQALNEEDI 703
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGEPI 279
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
457-649 |
2.97e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 457 HNVTFHYPsrPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLiqrfydpcegMVTVD----GHDIRSLNIQwlrdqI 532
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRI----------MAGVDkefeGEARPAPGIK-----V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 533 GIVEQEPVLFST-TIAENI-------------------RYGREDATM----------EDIVQAAkeaNAYNF------IM 576
Cdd:PRK11819 73 GYLPQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFdalaaeqgelQEIIDAA---DAWDLdsqleiAM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 577 D---LPQQfDTLVGEGGGQMSGgqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQevlskiQHGH----TIISVAH 649
Cdd:PRK11819 150 DalrCPPW-DAKVTKLSGGERR----RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE------QFLHdypgTVVAVTH 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
470-624 |
3.04e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.03 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 470 KILNDLNMAIK---PGE-MTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH---DIRS-LNIQWLRDQIGIVEQEPVL 541
Cdd:PRK11144 8 QQLGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 542 FS-TTIAENIRYGReDATMedivqaakeanaynfimdlPQQFDTLVGEGGGQMSGG---------QKQRVAIARALIRNP 611
Cdd:PRK11144 88 FPhYKVRGNLRYGM-AKSM-------------------VAQFDKIVALLGIEPLLDrypgslsggEKQRVAIGRALLTAP 147
|
170
....*....|...
gi 2462578034 612 KILLLDMATSALD 624
Cdd:PRK11144 148 ELLLMDEPLASLD 160
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
457-672 |
3.79e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 457 HNVTFHYPSRpevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL-------- 528
Cdd:PRK11701 10 RGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 529 -RDQIGIVEQEP-------VLFSTTIAENI------RYGREDATMEDIVQAAKEANAYnfIMDLPQQFdtlvgegggqmS 594
Cdd:PRK11701 87 lRTEWGFVHQHPrdglrmqVSAGGNIGERLmavgarHYGDIRATAGDWLERVEIDAAR--IDDLPTTF-----------S 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 595 GGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFEHGTAVER 671
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARlLAHRLLVMKQGRVVES 233
|
.
gi 2462578034 672 G 672
Cdd:PRK11701 234 G 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1130-1286 |
4.10e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQ-----TLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidghdSKKVNV----QFLRSNI-GIVSQepvl 1199
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELKIsykpQYIKPDYdGTVED---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1200 FACSIMDNikYGDN--TKEIpmerviaaAKQAQLHDFvmslpekYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLD 1277
Cdd:PRK13409 420 LLRSITDD--LGSSyyKSEI--------IKPLQLERL-------LDKNV----KDLSGGELQRVAIAACLSRDADLYLLD 478
|
....*....
gi 2462578034 1278 EATSALDTE 1286
Cdd:PRK13409 479 EPSAHLDVE 487
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
148-295 |
4.14e-06 |
|
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: 50.40 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 148 WTNSSLNQNMT----NGTRCGLLNIESEMIKFASY-YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIG 222
Cdd:cd18601 29 WANLEEKLNDTtdrvQGENSTNVDIEDLDRDFNLGiYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIR 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 223 WFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTsTICGFLlgffrgwkltLVIISVSPLIGIGAATIGL 295
Cdd:cd18601 109 FFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLL-QVVGVV----------LLAVVVNPWVLIPVIPLVI 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1120-1287 |
4.88e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1120 TYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTsiqLLerfydpdqgKVM--IDghdsKKVNVQFLRS---NIGIVS 1194
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKST---LL---------RIMagVD----KEFEGEARPApgiKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1195 QEPVLfacsimdnikygDNTK---EIPMERV------------IAA-------------AKQAQLHDFV----------- 1235
Cdd:PRK11819 77 QEPQL------------DPEKtvrENVEEGVaevkaaldrfneIYAayaepdadfdalaAEQGELQEIIdaadawdldsq 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 1236 -------MSLPEKyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1287
Cdd:PRK11819 145 leiamdaLRCPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
454-680 |
8.51e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFhYPSRPEVKilnDLNMAIKPGEMTALVGPSGAGKSTAlqliqrfydpCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK10418 5 IELRNIAL-QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSLT----------CAAALGILPAGVRQTAGRVLLDGKP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQE-PVLFSTTIAENIR-----------YGRE----------DATMEDIVQAAKEANA------YNFIMdlpqqfdtl 585
Cdd:PRK10418 71 VAPCAlRGRKIATIMQNPRsafnplhtmhtHAREtclalgkpadDATLTAALEAVGLENAarvlklYPFEM--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 586 vgegggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIG 662
Cdd:PRK10418 142 --------SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVaRLADDVAV 213
|
250
....*....|....*...
gi 2462578034 663 FEHGTAVERGTHEELLER 680
Cdd:PRK10418 214 MSHGRIVEQGDVETLFNA 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1119-1284 |
9.42e-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: 48.03 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1119 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL----ERFYDPDqGKVMIDGHDSKKVNVQFlRSNIGIVS 1194
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtEGNVSVE-GDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1195 QEPVLFAcsimdnikygdntkEIPMERVIAAAKQAQLHDFVmslpekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKIL 1274
Cdd:cd03233 90 EEDVHFP--------------TLTVRETLDFALRCKGNEFV---------------RGISGGERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 2462578034 1275 LLDEATSALD 1284
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1126-1293 |
9.78e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL-ERFYDP--DQGKVMIDGHdskKVNVQFLRSnIGIVSQEPV-LFA 1201
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTGviTGGDRLVNGR---PLDSSFQRS-IGYVQQQDLhLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1202 CSIMDNIKYG---DNTKEIP----MERViaaakqaqlhDFVMSLPE--KY-ETNVGSQGSQLSRGEKQRIAIARAIVRDP 1271
Cdd:TIGR00956 851 STVRESLRFSaylRQPKSVSksekMEYV----------EEVIKLLEmeSYaDAVVGVPGEGLNVEQRKRLTIGVELVAKP 920
|
170 180
....*....|....*....|...
gi 2462578034 1272 KILL-LDEATSALDTESEKQPCC 1293
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSQTAWSICK 943
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
472-666 |
1.03e-05 |
|
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: 47.43 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI-QWLRDQIGIV-E---QEPVLFSTTI 546
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVpEdrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 547 AENIRygredatmedivqaakeanaynfimdLP-------QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMA 619
Cdd:cd03215 96 AENIA--------------------------LSsllsggnQQ------------------KVVLARWLARDPRVLILDEP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462578034 620 TSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHG 666
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
182-394 |
1.10e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 48.66 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 182 IAVAVLITGYIQICFwVIAAARQIQKMRKF--------YFRRIMRMEIGWFDCNSVGELNTRFSdDINKINDAIADQMAL 253
Cdd:cd18555 44 LGIGILILFLLYGLF-SFLRGYIIIKLQTKldkslmsdFFEHLLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSNQVIS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 254 FIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIgaaTIGLS---VSKFTDYELKAYAKAGVVADEVISSMRTVAAFGG 330
Cdd:cd18555 122 LIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVL---LLLLTrkkIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGS 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 331 EKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18555 199 EKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVIN-GELTLGELI 261
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
832-1046 |
1.54e-05 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 48.22 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 832 VCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIG 911
Cdd:cd18549 44 IGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDISELAHHGPE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 912 MIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQT-RMLTGF-ASRDKQAlEMVGQITNeALSNIRTVAGIGK 989
Cdd:cd18549 122 DLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNkKMKKAFrRVREKIG-EINAQLED-SLSGIRVVKAFAN 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 990 ERRFIEALETELEKpFKTAIQKANIY-GFCFAFAQCIMFIANSASYRYGGYLISNEGL 1046
Cdd:cd18549 200 EEYEIEKFDEGNDR-FLESKKKAYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEI 256
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
465-651 |
2.02e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 465 SRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR-SLNIQWLRDQIGIVEQE-PVLF 542
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 STTIAENIRYGR---------EDATMEDIVQAAKEanaYNFIMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPKI 613
Cdd:PRK10982 87 QRSVMDNMWLGRyptkgmfvdQDKMYRDTKAIFDE---LDIDIDPRAKVATL--------SVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462578034 614 LLLDMATSALdneSEAMVQEVLSKI----QHGHTIISVAHRL 651
Cdd:PRK10982 156 VIMDEPTSSL---TEKEVNHLFTIIrklkERGCGIVYISHKM 194
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
786-1046 |
2.37e-05 |
|
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: 47.86 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 786 WPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQrsqINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRL 865
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDG---LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 866 RKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVqgaagSQI---GMI--VNSFTNVTVAMIIAFSFSWKLSLVILC 940
Cdd:cd18540 78 RKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRL-----GEIiswGLVdlVWGITYMIGILIVMLILNWKLALIVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 941 FFPFLAL-SGATQTRMLtgFASRdkQALEMVGQIT---NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYG 1016
Cdd:cd18540 151 VVPVLAVvSIYFQKKIL--KAYR--KVRKINSRITgafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSA 226
|
250 260 270
....*....|....*....|....*....|
gi 2462578034 1017 FCFAFAQCIMFIANSASYRYGGYLISNEGL 1046
Cdd:cd18540 227 LFLPIVLFLGSIATALVLWYGGILVLAGAI 256
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
468-534 |
2.91e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 2.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578034 468 EVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLI--QRFYDPCEGMVTVDGHDIRSLNIQwLRDQIGI 534
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGI 86
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1063-1278 |
3.06e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1063 TALGRAFSYTPSYAKAKISAARF--FQLLDRQPPISVYNtAGEKWDnfqgKIDFVDCKFTYPSRPDSqvLNGLSVSISPG 1140
Cdd:PRK10522 277 TPLLSAVGALPTLLSAQVAFNKLnkLALAPYKAEFPRPQ-AFPDWQ----TLELRNVTFAYQDNGFS--VGPINLTIKRG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1141 QTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSImdnikyGDNTKEIPME 1220
Cdd:PRK10522 350 ELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEGKPANPA 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 1221 RVIAAAKQAQLHDFVmSLPEKYETNVgsqgsQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:PRK10522 424 LVEKWLERLKMAHKL-ELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
463-649 |
4.22e-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: 46.63 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 463 YPSRpeVKILNDLNMAIKPG-----EMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLR-DQIGIVe 536
Cdd:cd03237 3 YPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKaDYEGTV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 537 qepvlfsttiaenirygreDATMEDIVQAAKEANAYNF-IMDlPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILL 615
Cdd:cd03237 79 -------------------RDLLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462578034 616 LDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 649
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFaeNNEKTAFVVEH 174
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1137-1287 |
4.50e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1137 ISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDghdsKKVNVQFLRsnigivsQEP---VlfACSIMDNIKYGdn 1213
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARLQ-------QDPprnV--EGTVYDFVAEG-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1214 TKEI-----------------PMERVIA--AAKQA--------QLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARA 1266
Cdd:PRK11147 91 IEEQaeylkryhdishlvetdPSEKNLNelAKLQEqldhhnlwQLENRINEVLAQLGLDPDAALSSLSGGWLRKAALGRA 170
|
170 180
....*....|....*....|.
gi 2462578034 1267 IVRDPKILLLDEATSALDTES 1287
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1126-1289 |
4.71e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIdgHDSKKVNVQ-----FLRSNIGIVSQEPVLf 1200
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAkpyctYIGHNLGLKLEMTVF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1201 acsimDNIKYgdnTKEI--PMERVIAAAKQAQLHDFvmsLPEKYETnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:PRK13541 89 -----ENLKF---WSEIynSAETLYAAIHYFKLHDL---LDEKCYS--------LSSGMQKIVAIARLIACQSDLWLLDE 149
|
170
....*....|.
gi 2462578034 1279 ATSALDTESEK 1289
Cdd:PRK13541 150 VETNLSKENRD 160
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
835-1046 |
4.84e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 46.81 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 835 LFVAMGCVSLFtQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLAtDASQVQGAAGSQIGMIV 914
Cdd:cd18566 48 VVIAILLESLL-RLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLTGQALLAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 915 NSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFI 994
Cdd:cd18566 124 LDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQML 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 995 EALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 1046
Cdd:cd18566 204 RRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDL 255
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
600-677 |
1.16e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 676
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHD 240
|
.
gi 2462578034 677 L 677
Cdd:PRK11022 241 I 241
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1131-1284 |
1.31e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.37 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1131 NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-----SKKV----------NVQFLRS-----NI 1190
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpGHQIarmgvvrtfqHVRLFREmtvieNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1191 gIVSQ----EPVLFAcSIMDNIKYGDNTKEiPMERVIAAAKQAQLHDFvmslpekyetnVGSQGSQLSRGEKQRIAIARA 1266
Cdd:PRK11300 102 -LVAQhqqlKTGLFS-GLLKTPAFRRAESE-ALDRAATWLERVGLLEH-----------ANRQAGNLAYGQQRRLEIARC 167
|
170
....*....|....*...
gi 2462578034 1267 IVRDPKILLLDEATSALD 1284
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLN 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
454-522 |
1.36e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 1.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 454 IEFHNVTFHYPSrpeVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLI------QrfydpcEGMVTVDGHDIRS 522
Cdd:NF033858 2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkiQ------QGRVEVLGGDMAD 67
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
150-283 |
1.41e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 45.63 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 150 NSSLNQNMTNGTRCGLLNIE--SEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCN 227
Cdd:cd18599 33 GSGNTTNNVDNSTVDSGNISdnPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTT 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 228 SVGELNTRFSDDINKINDAIADQMALFIQRMtsticgfLLGFFrgwklTLVIISVS 283
Cdd:cd18599 113 PTGRILNRFSKDLDEVDVRLPFTLENFLQNV-------LLVVF-----SLIIIAIV 156
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1122-1284 |
1.43e-04 |
|
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: 45.97 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1122 PSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPDQ--GKVMIDGHDSKKVN-VQFLRSNIGIVSQE-- 1196
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVDIRNpAQAIRAGIAMVPEDrk 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 -----PVLfacSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSqLSRGEKQRIAIARAIVRDP 1271
Cdd:TIGR02633 347 rhgivPIL---GVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNP 422
|
170
....*....|...
gi 2462578034 1272 KILLLDEATSALD 1284
Cdd:TIGR02633 423 RVLILDEPTRGVD 435
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
433-754 |
1.60e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.55 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 433 RKPIIDCMSEDGYKLDRI-----KGEI-EFHNVTFHYP--SRPEVkilNDLNMAIKPGEMTALVGPSGAGKSTALQLIQR 504
Cdd:TIGR01257 1911 KEPIFDEDDDVAEERQRIisggnKTDIlRLNELTKVYSgtSSPAV---DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 505 FYDPCEGMVTVDGHDIRSlNIQWLRDQIGIVEQEPVLfsttiaENIRYGREDATMEDIVQA--AKE----ANAYNFIMDL 578
Cdd:TIGR01257 1988 DTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGREHLYLYARLRGvpAEEiekvANWSIQSLGL 2060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 579 PQQFDTLVgeggGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMV-QEVLSKIQHGHTIISVAHRLSTVRAA 657
Cdd:TIGR01257 2061 SLYADRLA----GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEAL 2136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 658 DTIIGFE-HGTAVERGTHEELLERKGVYFtLVTLQsqgnqalneedIKdATEDDML-----ARTFSRGSYQDSLRasiRQ 731
Cdd:TIGR01257 2137 CTRLAIMvKGAFQCLGTIQHLKSKFGDGY-IVTMK-----------IK-SPKDDLLpdlnpVEQFFQGNFPGSVQ---RE 2200
|
330 340
....*....|....*....|....*...
gi 2462578034 732 RSKSQLSYLVHEPPLA-----VVDHKST 754
Cdd:TIGR01257 2201 RHYNMLQFQVSSSSLArifqlLISHKDS 2228
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
442-513 |
1.63e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 1.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 442 EDGYKLDRIKGEIEfhNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMV 513
Cdd:PRK15064 310 EQDKKLHRNALEVE--NLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
472-667 |
1.84e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQliqrfydpcEGMVTVDGHDIRSLNIQWLRDQIGIVEQepvlFSTTIAENIR 551
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFIDQ----LQFLIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 552 YgredatmedivqaakeanaynfiMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPK--ILLLDMATSALDNESEA 629
Cdd:cd03238 78 Y-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462578034 630 MVQEVLSK-IQHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
148-351 |
2.07e-04 |
|
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: 44.90 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 148 WTNSSLNQNMTNGTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQ---ICFWVIAAARQI-QKMrkfyFRRIMRMEIGW 223
Cdd:cd18602 25 WTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTnlaGELAGLRAARRLhDRM----LRNIVRAPMRF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 224 FDCNSVGELNTRFSDDINKIndaiaDQ-MALFIQRMTSTICgFLLGFFrgwkltLVIISVSPLIGIGAATIGLS---VSK 299
Cdd:cd18602 101 FDTTPIGRILNRFSSDTNVI-----DQkLPTTLERLLRFLL-LCLSAI------IVNAIVTPYFLIALIPIIIVyyfLQK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 300 F---TDYELK---AYAKAGVVA--DEVISSMRTVAAFGGEKREVERYEK-----NLVF-----AQRW-GIR 351
Cdd:cd18602 169 FyraSSRELQrldNITKSPVFShfSETLGGLTTIRAFRQQARFTQQMLElidrnNTAFlflntANRWlGIR 239
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
172-403 |
2.09e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 44.78 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 172 MIKFASYYAG-IAVAVLITgyiqicFWVIAAARQIQK-----MRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIND 245
Cdd:cd18540 41 LTGFILLYLGlILIQALSV------FLFIRLAGKIEMgvsydLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 246 AIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIgigaatIGLSVsKFTDYELKAYAKA-----GVVAD--EV 318
Cdd:cd18540 115 IISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVL------AVVSI-YFQKKILKAYRKVrkinsRITGAfnEG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 319 ISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVqIFL 398
Cdd:cd18540 188 ITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVL-AGAITIGTLV-AFI 265
|
....*
gi 2462578034 399 SVIVG 403
Cdd:cd18540 266 SYATQ 270
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1251-1284 |
2.18e-04 |
|
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: 45.55 E-value: 2.18e-04
10 20 30
....*....|....*....|....*....|....
gi 2462578034 1251 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
471-523 |
2.42e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 2.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 471 ILNDLNMAIKPGEMTALVGPSGAGKST--ALQLIQRFYDPCEGMVTVDGHDIRSL 523
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTlsATLAGREDYEVTGGTVEFKGKDLLEL 70
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1251-1284 |
2.54e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 2.54e-04
10 20 30
....*....|....*....|....*....|....
gi 2462578034 1251 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1284
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1130-1286 |
2.63e-04 |
|
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: 45.16 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQ-----TLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidghdSKKVNV----QFLRSNIGIVSQEpVLF 1200
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKIsykpQYISPDYDGTVEE-FLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1201 AC--SIMDNIKYgdNTkEIpmerviaaAKQAQLHDFvmslpekYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1278
Cdd:COG1245 424 SAntDDFGSSYY--KT-EI--------IKPLGLEKL-------LDKNV----KDLSGGELQRVAIAACLSRDADLYLLDE 481
|
....*...
gi 2462578034 1279 ATSALDTE 1286
Cdd:COG1245 482 PSAHLDVE 489
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
148-347 |
2.69e-04 |
|
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: 44.44 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 148 WTNSSLNQNmtngtrcgLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCN 227
Cdd:cd18605 25 WVSHSNNSF--------FNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 228 SVGELNTRFSDDINKINDAIADQMALFIqRMTSTICGFLLGFFRGwkLTLVIISVSPLIGIGAatiglSVSKF---TDYE 304
Cdd:cd18605 97 PVGRILNRFSSDVYTIDDSLPFILNILL-AQLFGLLGYLVVICYQ--LPWLLLLLLPLAFIYY-----RIQRYyraTSRE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462578034 305 LK---AYAKAGVVA--DEVISSMRTVAAFGGEKREVERYEKNLVFAQR 347
Cdd:cd18605 169 LKrlnSVNLSPLYThfSETLKGLVTIRAFRKQERFLKEYLEKLENNQR 216
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
180-394 |
4.53e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 43.66 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 180 AGIAVAVL---ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELnTRFSDDINKINDAIADQMaLFIQ 256
Cdd:cd18783 46 IGVVIALLfegILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVL-TKHMQQIERIRQFLTGQL-FGTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 257 RMTSTICGFL-LGFFRGWKLTLVIISVSPLIgigAATIGLSVSKFTDYELKAY---AKAGVVADEVISSMRTVAAFGGEK 332
Cdd:cd18783 124 LDATSLLVFLpVLFFYSPTLALVVLAFSALI---ALIILAFLPPFRRRLQALYraeGERQAFLVETVHGIRTVKSLALEP 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 333 REVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18783 201 RQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFA-GSLTVGALI 261
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
213-394 |
4.62e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 43.60 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 213 FRRIMRMEIGWFDCNSVGELNTRFsDDINKINDAIADQM-ALFIQRMTSTICGFLLgFFRGWKLTLVIISVSPL-IGIGA 290
Cdd:cd18567 82 FRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFvEALLDGLMAILTLVMM-FLYSPKLALIVLAAVALyALLRL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 291 ATIGlSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLC 370
Cdd:cd18567 160 ALYP-PLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLE 238
|
170 180
....*....|....*....|....
gi 2462578034 371 YALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18567 239 NILVIYLGALLVLD-GEFTVGMLF 261
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1130-1289 |
4.80e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1130 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGKVMIDG--------HDSKKVNvqflrsnIGIVSQE-- 1196
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfkdiRDSEALG-------IVIIHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1197 --PVLfacSIMDNIKYGDntkEIPMERVI----AAAKQAQLHDFVmSLPEKYETNVGSQGSqlsrGEKQRIAIARAIVRD 1270
Cdd:NF040905 89 liPYL---SIAENIFLGN---ERAKRGVIdwneTNRRARELLAKV-GLDESPDTLVTDIGV----GKQQLVEIAKALSKD 157
|
170 180
....*....|....*....|
gi 2462578034 1271 PKILLLDEATSAL-DTESEK 1289
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAA 177
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
452-624 |
4.99e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 452 GEI--EFHNVTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYdP--CEGMVTVDGH--DIRS--- 522
Cdd:PRK13549 256 GEVilEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIDGKpvKIRNpqq 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 523 ---LNIQWL---RDQIGIVEQEPVLFSTTIAENIRY--------GREDATMEDIVQ--AAKEANAYNFIMDLP---QQfd 583
Cdd:PRK13549 335 aiaQGIAMVpedRKRDGIVPVMGVGKNITLAALDRFtggsriddAAELKTILESIQrlKVKTASPELAIARLSggnQQ-- 412
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462578034 584 tlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALD 624
Cdd:PRK13549 413 ----------------KAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
454-513 |
5.06e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 5.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSRPevKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMV 513
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
457-522 |
5.94e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.91 E-value: 5.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 457 HNVTFhypSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRS 522
Cdd:PRK13543 15 HALAF---SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR 77
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
480-652 |
1.02e-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: 42.35 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 480 KPGEMTALVGPSGAGKSTALQLIQ--------RFYDPCEGMVTVD---GHDIRSLNIQWLRDQIGI------VEQEPVLF 542
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 543 STTIAENIRYGREDATMEDIVQAakeanaynfiMDLpqqfDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSA 622
Cdd:cd03236 104 KGKVGELLKKKDERGKLDELVDQ----------LEL----RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|.
gi 2462578034 623 LD-NESEAMVQEVLSKIQHGHTIISVAHRLS 652
Cdd:cd03236 170 LDiKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1122-1284 |
1.11e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1122 PSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD--QGKVMIDGhdsKKVNV----QFLRSNIGIVSQ 1195
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGrwEGEIFIDG---KPVKIrnpqQAIAQGIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1196 E-------PVLfacSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSqLSRGEKQRIAIARAIV 1268
Cdd:PRK13549 346 DrkrdgivPVM---GVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIAR-LSGGNQQKAVLAKCLL 421
|
170
....*....|....*.
gi 2462578034 1269 RDPKILLLDEATSALD 1284
Cdd:PRK13549 422 LNPKILILDEPTRGID 437
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
420-617 |
1.28e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 420 GRAAATSIFETIDRKPIIDCM-----SEDGYKLDRIKGEI--EFHNVtfhypSRPEVkiLNDLNMAIKPGEMTALVGPSG 492
Cdd:COG1129 216 GRLVGTGPVAELTEDELVRLMvgrelEDLFPKRAAAPGEVvlEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 493 AGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlRDQI--------------GIVEQEPVLFSTTIAeN--------- 549
Cdd:COG1129 289 AGRTELARALFGADPADSGEIRLDGKPVRIRSP---RDAIragiayvpedrkgeGLVLDLSIRENITLA-Sldrlsrggl 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 550 IRYGREDATMEDIVQA--AKEANAYNFIMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLD 617
Cdd:COG1129 365 LDRRRERALAEEYIKRlrIKTPSPEQPVGNLSggnQQ------------------KVVLAKWLATDPKVLILD 419
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
809-1046 |
1.61e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 42.11 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 809 LFSQILgTFSIP----------DKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDI 878
Cdd:cd18555 12 LLLQLL-TLLIPiltqyvidnvIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 879 AWFDdlRNSPGALTTRlATDASQVQGAAGSQ-IGMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALsgatqTRMLT 957
Cdd:cd18555 91 SFFE--NRSSGDLLFR-ANSNVYIRQILSNQvISLIIDLLLLVIYL-IYMLYYSPLLTLIVLLLGLLIVL-----LLLLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 958 GFASRDKQALEMVGQ-----ITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSA 1032
Cdd:cd18555 162 RKKIKKLNQEEIVAQtkvqsYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLL 241
|
250
....*....|....
gi 2462578034 1033 SYRYGGYLISNEGL 1046
Cdd:cd18555 242 ILWIGAYLVINGEL 255
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
454-502 |
1.74e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.61 E-value: 1.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462578034 454 IEFHNVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLI 502
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI 368
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
468-571 |
1.77e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.30 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 468 EVKILN-----DLNMAIKPGeMTALVGPSGAGKSTALQLIQRFYDPcEGMVTVDGHDI-RSLNIQWLRDQIGIVeqepvl 541
Cdd:COG3593 5 KIKIKNfrsikDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGP-SSSRKFDEEDFyLGDDPDLPEIEIELT------ 76
|
90 100 110
....*....|....*....|....*....|
gi 2462578034 542 FSTTIAENIRYGREDATMEDIVQAAKEANA 571
Cdd:COG3593 77 FGSLLSRLLRLLLKEEDKEELEEALEELNE 106
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
882-1084 |
1.80e-03 |
|
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: 42.10 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 882 DDLRNSPGALTTRLATDASQVQGAAgSQIGMIVNSFTNVTVAMIIAFSFSWKLSLV----ILCFFP---FLA-LSGATQT 953
Cdd:cd18596 108 EKSSASVGKINNLMSVDANRISEFA-AFLHLLVSAPLQIVIAIVFLYRLLGWSALVglavMVLLLPlngYLAkRYSRAQK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 954 RMLtgfASRDKQAlemvgQITNEALSNIRTVagigK----ERRFIEAL----ETELekpfkTAIQKANIYGFCFAFAQ-- 1023
Cdd:cd18596 187 ELM---KARDARV-----QLVTEVLQGIRMI----KffawERKWEERIlearEEEL-----KWLRKRFLLDLLLSLLWfl 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 1024 ---CIMFIAnsasyrYGGY-LISNEGLHFSYVFrviSAVVLSAT---ALGRAFSYTPSYAKAKISAAR 1084
Cdd:cd18596 250 ipiLVTVVT------FATYtLVMGQELTASVAF---TSLALFNMlrgPLNVLPELITQLLQAKVSLDR 308
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
907-1046 |
2.17e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 41.78 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 907 GSQIGMIVNSFTnVTVAMIIAFSFSWKLSLVILCFFP-FLALSGATQTRMLTG----FASRDKQALEMVgqitnEALSNI 981
Cdd:cd18568 117 RSALTTILDLLM-VFIYLGLMFYYNLQLTLIVLAFIPlYVLLTLLSSPKLKRNsreiFQANAEQQSFLV-----EALTGI 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 982 RTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 1046
Cdd:cd18568 191 ATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
207-419 |
2.25e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 41.64 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 207 KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLI 286
Cdd:cd18554 80 DIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 287 GIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEK-NLVFAQRWGIRKGIVMGFFTGfVWC 365
Cdd:cd18554 160 ILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKrNGHFLTRALKHTRWNAKTFSA-VNT 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462578034 366 LIFLCYALAFWYGSTLVLdEGEYTPGTLVQIF--LSVIVGAL-NLGNASPCL-EAFAT 419
Cdd:cd18554 239 ITDLAPLLVIGFAAYLVI-EGNLTVGTLVAFVgyMERMYSPLrRLVNSFTTLtQSFAS 295
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
454-652 |
2.52e-03 |
|
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: 42.04 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 454 IEFHNVTFHYPSrpEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdirslniqwlRDQIG 533
Cdd:TIGR00954 452 IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 534 IVEQEPVLFSTTIAENIRY--GREDATMEDIVQAAKEAnaynfIMDLPQQFDTL--------VGEGGGQMSGGQKQRVAI 603
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIIYpdSSEDMKRRGLSDKDLEQ-----ILDNVQLTHILereggwsaVQDWMDVLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462578034 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIqhGHTIISVAHRLS 652
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1129-1280 |
2.81e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.93 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1129 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLerF--YDPDQGKVMIDGhdsKKVNV----QFLRSNIGIVS----QEPV 1198
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDG---KPVRIrsprDAIRAGIAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1199 LFACSIMDNI------KYGDNtkeipmeRVIAAAKQAQL-HDFVMSLPEKY---ETNVGSqgsqLSRGEKQRIAIARAIV 1268
Cdd:COG1129 342 VLDLSIRENItlasldRLSRG-------GLLDRRRERALaEEYIKRLRIKTpspEQPVGN----LSGGNQQKVVLAKWLA 410
|
170
....*....|..
gi 2462578034 1269 RDPKILLLDEAT 1280
Cdd:COG1129 411 TDPKVLILDEPT 422
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1126-1155 |
2.82e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.46 E-value: 2.82e-03
10 20 30
....*....|....*....|....*....|
gi 2462578034 1126 DSQVLNGLSVSISPGQTLAFVGSSGCGKST 1155
Cdd:PRK01889 181 DGEGLDVLAAWLSGGKTVALLGSSGVGKST 210
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
487-577 |
2.96e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 40.42 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 487 LVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIGIVEQEPvlfsttiAENIRYGREDAT--MEDIVQ 564
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELH----PHYRELQAADP-------KTASEYTQPDASrwVEKLLQ 84
|
90
....*....|...
gi 2462578034 565 AAKEaNAYNFIMD 577
Cdd:pfam06414 85 HAIE-NGYNIILE 96
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1128-1285 |
3.29e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1128 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL----ERFYDPDQGKVMIDGHDSKKVnVQFLRSNIGIVSQEPVLFA-C 1202
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFPhL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 1203 SIMDNIKYGDNTKEiPMERVIAAAKQ---AQLHDFVMS---LPEKYETNVGS---QGsqLSRGEKQRIAIARAIVRDPKI 1273
Cdd:TIGR00956 154 TVGETLDFAARCKT-PQNRPDGVSREeyaKHIADVYMAtygLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKI 230
|
170
....*....|..
gi 2462578034 1274 LLLDEATSALDT 1285
Cdd:TIGR00956 231 QCWDNATRGLDS 242
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1249-1286 |
3.63e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.86 E-value: 3.63e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2462578034 1249 QGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1286
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
475-678 |
3.88e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.69 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 475 LNMAIKPGEMTALVGPSGAGKSTALQLIQRFYdPCEGMVTVDGHDIRSLNIQWLRDQIG-IVEQEPVLFSTTIAENIRYG 553
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 554 REDATMEDIVQAAKE--ANAYNFIMDLPQQFDTLvgegggqmSGGQKQRVAIARALIR-----NP--KILLLDMATSALD 624
Cdd:PRK03695 94 QPDKTRTEAVASALNevAEALGLDDKLGRSVNQL--------SGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578034 625 NESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK03695 166 VAQQAALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
458-521 |
4.30e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.93 E-value: 4.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578034 458 NVTFHYPSRPevkILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR 521
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK 66
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
601-667 |
4.60e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 4.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578034 601 VAIARALIRNPK---ILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:PRK00635 1708 IKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLrTLVSLGHSVIYIDHDPALLKQADYLIEMGPGS 1778
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
924-1056 |
5.43e-03 |
|
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: 40.31 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 924 MIIAFSFSW-KLSLVILCFFPFLALSGATQTRMLTGFAS-RDKQAL---EMVGqITNEALSNIRTVAGIGKERRF---IE 995
Cdd:cd18594 126 VIVLTGLLWrEIGPSSLAGLGVLLLLLPLQAYLGKLFAKyRRKTAGltdERVK-IMNEIISGMRVIKMYTWEESFaklIE 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578034 996 AL-ETELEKPFKTA-IQKAN--IYGFCFAFAQCIMFIansasyrygGYLISNEGLHFSYVFRVIS 1056
Cdd:cd18594 205 NIrKKELKLIRKAAyIRAFNmaFFFFSPTLVSFATFV---------PYVLTGNTLTARKVFTVIS 260
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
600-678 |
6.36e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.17 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 676
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLsQWADKINVLYCGQTVETAPSKE 245
|
..
gi 2462578034 677 LL 678
Cdd:PRK15093 246 LV 247
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1253-1290 |
6.65e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 6.65e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2462578034 1253 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKQ 1290
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKE 433
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
812-1009 |
7.16e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 39.88 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 812 QILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQF---LQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSP 888
Cdd:cd18782 21 NPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVltaLRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 889 GALTTRLAtDASQVQG-AAGSQIGMIVNS-FtnVTVAMIIAFSFSWKLSLVILCFFPFLAL-----SGATQTRMLTGFAS 961
Cdd:cd18782 99 GELSTRIS-ELDTIRGfLTGTALTTLLDVlF--SVIYIAVLFSYSPLLTLVVLATVPLQLLltflfGPILRRQIRRRAEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462578034 962 RDKQALEMVgqitnEALSNIRTVAGIGKERRFIEALETE----LEKPFKTAI 1009
Cdd:cd18782 176 SAKTQSYLV-----ESLTGIQTVKAQNAELKARWRWQNRyarsLGEGFKLTV 222
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
459-518 |
7.63e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 7.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578034 459 VTFHYPSRPEVKILNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGH 518
Cdd:PLN03140 168 LGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPslkVSGEITYNGY 230
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
790-992 |
8.69e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 39.83 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 790 LVGSVGAAVNGTVTPLYAFLFSQILgTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFG 869
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIREL-VDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 870 FRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQI-GMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALS 948
Cdd:cd18778 80 YDKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIADGIpQGITNVLTLVGVA-IILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462578034 949 GATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERR 992
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEE 200
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
472-654 |
9.46e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 39.48 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 472 LNDLNMAIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRslniQWLRDQ-IGIVEQE-------PVLFS 543
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578034 544 TTIAENiRYG------REDATMEDIVQAAKEAnaYNFIMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPKILLLD 617
Cdd:PRK15056 99 DVVMMG-RYGhmgwlrRAKKRDRQIVTAALAR--VDMVEFRHRQIGEL--------SGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462578034 618 MATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTV 654
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| |
