|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-578 |
8.01e-135 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 404.93 E-value: 8.01e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 24 MLSEMYMEAKWIYSYVKSYKLAIIFYVFLGILGVVMGLGGSVASKYLIDAV-TGYDSGGIGFIAFVMVVMAIGNLVINAV 102
Cdd:COG1132 1 MSKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALlAGGDLSALLLLLLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 103 TNRISTRISIKIGNEIRADIYDRIINtdwESMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVIL 179
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLR---LPLSFFdrrRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 180 YYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETT 259
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 260 LEYNKFTIYTSSFMSLVGMIVTYSCFGWGVYRLWTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRIMEV 339
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 340 IKLPREkVLDEEIANEIaatcEENGVSIKLDNIKFKYEKsGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLN 419
Cdd:COG1132 318 LDEPPE-IPDPPGAVPL----PPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 420 ITEG----DGViynskDVKcKISAST-RKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEG 494
Cdd:COG1132 392 PTSGriliDGV-----DIR-DLTLESlRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 495 INSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNImsENL--NKTCIVTTHRLSVLSMCHK 572
Cdd:COG1132 466 YDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL--ERLmkGRTTIVIAHRLSTIRNADR 543
|
570
....*....|.
gi 429188963 573 IY-----RISE 578
Cdd:COG1132 544 ILvlddgRIVE 554
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
33-581 |
2.60e-128 |
|
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: 392.66 E-value: 2.60e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 33 KWIYSYVKSYKLAIIFYVFLGILGVVMGLGGSVASKYLIDAVTGY-DSGGIGFIAFVMVVMAIGNLVINAVTNRISTRIS 111
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNqDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 112 IKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLtSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALL 191
Cdd:COG2274 225 QRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 192 SAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSS 271
Cdd:COG2274 304 LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLST 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 272 FMSLVGMIVTYSCFGWGVYRLWTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRIMEVIKLPrekvlDEE 351
Cdd:COG2274 384 LSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLP-----PER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 352 IANEIAATCEENGVSIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSK 431
Cdd:COG2274 459 EEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR-ILIDGI 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 432 DVKcKIS-ASTRKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQ 510
Cdd:COG2274 538 DLR-QIDpASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQ 616
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 511 NQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
33-576 |
1.85e-79 |
|
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: 260.85 E-value: 1.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 33 KWIYSYVKSYKLAIIFYVFLGILGVVMGLGGSVASKYLIDAV----TGYDSGGIGFIAFVMVVmaIGNLVINAVTNRIST 108
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLiiggAPLSALLPLLGLLLAVL--LLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 109 RISIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVL 188
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 189 ALLSAP-----IALcvskvLMKKMRNRNKEvreissemmsfNEETFTNLQS-----------IKAFSLNDVFSDRLRKIQ 252
Cdd:COG4988 164 LLVTAPliplfMIL-----VGKGAAKASRR-----------QWRALARLSGhfldrlrglttLKLFGRAKAEAERIAEAS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 253 EKFKETTLEYNK--FTiytSS-----FMSL-VGMIVTYSCFgwgvyRLWTGHITYGTMtlflqlssslsssfSALIGLVP 324
Cdd:COG4988 228 EDFRKRTMKVLRvaFL---SSavlefFASLsIALVAVYIGF-----RLLGGSLTLFAA--------------LFVLLLAP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 325 -----------------SAISAttsAGRIMEVIKLPREKVLDEEIANEIAAtceenGVSIKLDNIKFKYEkSGKNVLENA 387
Cdd:COG4988 286 efflplrdlgsfyharaNGIAA---AEKIFALLDAPEPAAPAGTAPLPAAG-----PPSIELEDVSFSYP-GGRPALDGL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 388 NIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVK 467
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS-ILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 468 ADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKN 547
Cdd:COG4988 436 PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA 515
|
570 580
....*....|....*....|....*....
gi 429188963 548 IMSENLNKTCIVTTHRLSVLSMCHKIYRI 576
Cdd:COG4988 516 LRRLAKGRTVILITHRLALLAQADRILVL 544
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
33-581 |
2.09e-76 |
|
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: 253.15 E-value: 2.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 33 KWIYSYVKSYKLAIIFYVFLGILGVVMGLGGSVASKYLIDAvtgydSGGIGFIAFVMV--VM----AIGnlvinavtnRI 106
Cdd:COG4987 4 LRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAA-----AALAPPILNLFVpiVGvrafAIG---------RT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 107 STR---------ISIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSIL-GWVPSLitktVQFCSILV 176
Cdd:COG4987 70 VFRylerlvshdATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLrVLLPLL----VALLVILA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 177 VIL---YYDPTMAVLALLSAPIALCVSKVL-MKKMRNRNKEVREISSEMmsfNEETFTNLQS---IKAFSLNDVFSDRLR 249
Cdd:COG4987 146 AVAflaFFSPALALVLALGLLLAGLLLPLLaARLGRRAGRRLAAARAAL---RARLTDLLQGaaeLAAYGALDRALARLD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 250 KIQEKFKETTLEYNKFTIYTSSFMSLVGMIVTYSCFGWGVYRLWTGHITyGTMtlflqlssslsssfsalIGLV------ 323
Cdd:COG4987 223 AAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPL-----------------LALLvlaala 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 324 --------PSAISAT----TSAGRIMEVIKLPrekvldEEIANEIAATCEENGVSIKLDNIKFKYEKSGKNVLENANIIA 391
Cdd:COG4987 285 lfealaplPAAAQHLgrvrAAARRLNELLDAP------PAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 392 NPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVKADAT 471
Cdd:COG4987 359 PPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS-ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDAT 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 472 DEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSE 551
Cdd:COG4987 438 DEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA 517
|
570 580 590
....*....|....*....|....*....|
gi 429188963 552 NLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:COG4987 518 LAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
34-573 |
3.88e-67 |
|
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: 228.43 E-value: 3.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 34 WIYSYVKSYK----LAIIFYVFLGILGVVMGLggsvASKYLIDavTGYDSGGIGFI--AFVM-----VVMAIGNLVINAV 102
Cdd:TIGR02204 8 ALWPFVRPYRgrvlAALVALLITAAATLSLPY----AVRLMID--HGFSKDSSGLLnrYFAFllvvaLVLALGTAARFYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 103 TNRISTRISikigNEIRADIYDRIINTdweSMSYY---RSGDLLNRLTSDATTVsNSILGWVPSLITK-TVQFCSILVVI 178
Cdd:TIGR02204 82 VTWLGERVV----ADIRRAVFAHLISL---SPSFFdknRSGEVVSRLTTDTTLL-QSVIGSSLSMALRnALMCIGGLIMM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 179 LYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDvfSDRLRKIQEKfkET 258
Cdd:TIGR02204 154 FITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHED--AERSRFGGAV--EK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 259 TLEYNKFTIYTSSFMSlvgMIVTYSCFGWGVYRLWTG--HITYGTMTLFLQLSsslsssfsaligLVPSAISATTSAGRI 336
Cdd:TIGR02204 230 AYEAARQRIRTRALLT---AIVIVLVFGAIVGVLWVGahDVIAGKMSAGTLGQ------------FVFYAVMVAGSIGTL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 337 MEVI-KLPREKVLDEEIA------NEIAATCEENGVS------IKLDNIKFKY-EKSGKNVLENANIIANPGEIIALIGP 402
Cdd:TIGR02204 295 SEVWgELQRAAGAAERLIellqaePDIKAPAHPKTLPvplrgeIEFEQVNFAYpARPDQPALDGLNLTVRPGETVALVGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 403 SGEGKTTTMRILLGLLNITEG----DGViynskDVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRA 478
Cdd:TIGR02204 375 SGAGKSTLFQLLLRFYDPQSGrillDGV-----DLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 479 LKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRV---LKNIMSEnlnK 555
Cdd:TIGR02204 450 ARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVqqaLETLMKG---R 526
|
570
....*....|....*...
gi 429188963 556 TCIVTTHRLSVLSMCHKI 573
Cdd:TIGR02204 527 TTLIIAHRLATVLKADRI 544
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
35-565 |
1.55e-61 |
|
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: 213.42 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 35 IYSYVKSYKlaIIFYVFLGILGVVMGLGGSVAS--KYLID-AVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRIS 111
Cdd:TIGR02203 5 LWSYVRPYK--AGLVLAGVAMILVAATESTLAAllKPLLDdGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 112 IKIGNEIRADIYDRIINTdweSMSYYR---SGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVL 188
Cdd:TIGR02203 83 NKVVRDIRVRMFEKLLGL---PVSFFDrqpTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 189 ALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIY 268
Cdd:TIGR02203 160 VVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 269 TSSFMSLVGMIVTYSCFGWGVYRLWTGHITYGTMTLFLQLssslsssfsalIGLVPSAISATTSAGRIMEVIKLPREKV- 347
Cdd:TIGR02203 240 SSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITA-----------MIALIRPLKSLTNVNAPMQRGLAAAESLf 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 348 --LDEEI-ANEIAATCEENGVSIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGD 424
Cdd:TIGR02203 309 tlLDSPPeKDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 425 gVIYNSKDVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVK-ADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKG 503
Cdd:TIGR02203 389 -ILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENG 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 504 RSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRV---LKNIMSenlNKTCIVTTHRLS 565
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVqaaLERLMQ---GRTTLVIAHRLS 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
367-581 |
7.88e-60 |
|
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: 198.99 E-value: 7.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGViynskDVKCKISASTR 442
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGriliDGH-----DVRDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLR 522
Cdd:cd03251 76 RQIGLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 523 NAPVLLLDEATSALDMDTEKRVLKNImsENL--NKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAAL--ERLmkNRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
367-581 |
1.26e-59 |
|
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: 198.53 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKY-EKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLM 445
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGE-ILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAP 525
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 526 VLLLDEATSALDMDTEKRV---LKNIMsenLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:cd03249 160 ILLLDEATSALDAESEKLVqeaLDRAM---KGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
367-565 |
1.54e-57 |
|
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: 192.44 E-value: 1.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKsGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMA 446
Cdd:cd03254 3 IEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ-ILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPV 526
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 429188963 527 LLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLS 565
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLS 199
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
42-576 |
2.89e-57 |
|
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: 200.98 E-value: 2.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 42 YKLAIIFYVFLGILGVVMGLGGSVASKYLIDAVT--GYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIR 119
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLIsaGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 120 ADIYDRI--INTDWESMSyyRSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPI-- 195
Cdd:TIGR02857 81 ERLLEAVaaLGPRWLQGR--PSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLip 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 196 ---ALCVSKVlMKKMRNRNKEVREISSEMMsfneETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSS- 271
Cdd:TIGR02857 159 ifmILIGWAA-QAAARKQWAALSRLSGHFL----DRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 272 ---FMSL-VGMIVTYSCFgwgvyRLWTGHITYGTmtlflqlssslsssFSALIGLVP-----------------SAISAT 330
Cdd:TIGR02857 234 lelFATLsVALVAVYIGF-----RLLAGDLDLAT--------------GLFVLLLAPefylplrqlgaqyharaDGVAAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 331 TSAGRIMEVIKLPREKVLDEEIANEIaatceengvSIKLDNIKFKYEKSGkNVLENANIIANPGEIIALIGPSGEGKTTT 410
Cdd:TIGR02857 295 EALFAVLDAAPRPLAGKAPVTAAPAS---------SLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 411 MRILLGLLNITEGDGVIyNSKDVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEK 490
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAV-NGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 491 LPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMC 570
Cdd:TIGR02857 444 LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
....*.
gi 429188963 571 HKIYRI 576
Cdd:TIGR02857 524 DRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
367-581 |
7.95e-56 |
|
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: 188.21 E-value: 7.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEkSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIyNSKDVKCKISASTRKLMA 446
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI-DGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPV 526
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 527 LLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
367-580 |
1.65e-54 |
|
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: 182.58 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKIS-ASTRKLM 445
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE-ILIDGVDLR-DLDlESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTGTIAENMrmvkadatdeeiiralkyacayefveklpeginssvlekgrsFSEGQNQRLSIARALLRNAP 525
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 526 VLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENK 580
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
366-573 |
5.73e-54 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 182.79 E-value: 5.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISAST-RKL 444
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGS-VLLDGTDIR-QLDPADlRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNA 524
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 429188963 525 PVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKI 573
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRI 208
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
39-573 |
2.66e-53 |
|
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: 193.62 E-value: 2.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 39 VKSYKLAIIFYVFLGILGVVMGLGGSVASKYLIDA--VTGYDSGGIGFIAfVMVVMAIGNLVINAVTNRISTRISIKIGN 116
Cdd:TIGR03796 149 LRGSRGALLYLLLAGLLLVLPGLVIPAFSQIFVDEilVQGRQDWLRPLLL-GMGLTALLQGVLTWLQLYYLRRLEIKLAV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 117 EIRADIYDRIINTdweSMSYY---RSGDLLNRLTSDATtVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSA 193
Cdd:TIGR03796 228 GMSARFLWHILRL---PVRFFaqrHAGDIASRVQLNDQ-VAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 194 PIALCVSKVLMKKMRNRNKEVREISSEMMSFneeTFTNLQSI---KAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTS 270
Cdd:TIGR03796 304 AINVLALQLVSRRRVDANRRLQQDAGKLTGV---AISGLQSIetlKASGLESDFFSRWAGYQAKLLNAQQELGVLTQILG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 271 SFMSLVGMIVTYSCFGWGVYRLWTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRIMEVIKLPREKVLDE 350
Cdd:TIGR03796 381 VLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVDPLLEE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 351 EIAneIAATCEENGV---SIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG---- 423
Cdd:TIGR03796 461 PEG--SAATSEPPRRlsgYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGeilf 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 424 DGViyNSKDVKCKISASTrklMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKG 503
Cdd:TIGR03796 539 DGI--PREEIPREVLANS---VAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGG 613
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 504 RSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLnkTCIVTTHRLSVLSMCHKI 573
Cdd:TIGR03796 614 ANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRRGC--TCIIVAHRLSTIRDCDEI 681
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-582 |
7.41e-53 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 192.24 E-value: 7.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 28 MYMEAKWiysyvksyKLAIIFYVFLgilgVVMGLGGSVASKY---LIDAVTGyDSGGIGFIA--FVMVVMAIGNLVINAV 102
Cdd:TIGR00958 154 GLSGRDW--------PWLISAFVFL----TLSSLGEMFIPFYtgrVIDTLGG-DKGPPALASaiFFMCLLSIASSVSAGL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 103 TNRISTRISIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYD 182
Cdd:TIGR00958 221 RGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 183 PTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDV----FSDRLRKIQEKFKET 258
Cdd:TIGR00958 301 PRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETLQLNKRK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 259 TLEYNKFTIYTSSFMSLVGMIVTYscfgWGVYRLWTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRIME 338
Cdd:TIGR00958 381 ALAYAGYLWTTSVLGMLIQVLVLY----YGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 339 VIKLPREKVLDEEIANEiaatcEENGVsIKLDNIKFKY-EKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGL 417
Cdd:TIGR00958 457 YLDRKPNIPLTGTLAPL-----NLEGL-IEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 418 LNITEG----DGViyNSKDVKCKisaSTRKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPE 493
Cdd:TIGR00958 531 YQPTGGqvllDGV--PLVQYDHH---YLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 494 GINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEkRVLKNIMSENlNKTCIVTTHRLSVLSMCHKI 573
Cdd:TIGR00958 606 GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE-QLLQESRSRA-SRTVLLIAHRLSTVERADQI 683
|
....*....
gi 429188963 574 YRISENKVQ 582
Cdd:TIGR00958 684 LVLKKGSVV 692
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
43-581 |
7.55e-51 |
|
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: 186.48 E-value: 7.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 43 KLAIIFYVFLGILGVVMGLGGSVASKYLIDA-VTGYDSGGIGFIAFVMvvmaIGNLVINAVTNRISTRISIKIGNEIRAD 121
Cdd:TIGR01193 155 KKLIVNIVIAAIIVTLISIAGSYYLQKIIDTyIPHKMMGTLGIISIGL----IIAYIIQQILSYIQIFLLNVLGQRLSID 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 122 IYDRIINTDWE-SMSYY---RSGDLLNRLTsDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIAL 197
Cdd:TIGR01193 231 IILSYIKHLFElPMSFFstrRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 198 CVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDvfsDRLRKIQEKFK---ETTLEYNKFTIYTSSFMS 274
Cdd:TIGR01193 310 VIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEA---ERYSKIDSEFGdylNKSFKYQKADQGQQAIKA 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 275 LVGMIVTYSCFGWGVYRLWTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRIMEVIKLPREkvldEEIAN 354
Cdd:TIGR01193 387 VTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSE----FINKK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 355 EIAATCEENGvSIKLDNIKFKYeKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVK 434
Cdd:TIGR01193 463 KRTELNNLNG-DIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE-ILLNGFSLK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 435 CKISASTRKLMAYVPQEKTMFTGTIAENMRM-VKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQR 513
Cdd:TIGR01193 540 DIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQR 619
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 514 LSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENlNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
33-564 |
2.29e-50 |
|
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: 182.18 E-value: 2.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 33 KWIYSYVKSYKLAIIFYVFLGILGVVMGLGGSVASKYLIDAvtgydSGGIGFIAFVMV------VMAIGNLVINAVTNRI 106
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISR-----AAEMPPVLYLSVaavavrAFGIGRAVFRYLERLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 107 STRISIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWV-PSLITKTVQFCSILVVILYYDPTM 185
Cdd:TIGR02868 77 GHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIvPAGVALVVGAAAVAAIAVLSVPAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 186 AVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSfneETFTNLQSIKAFSLNDVFSDRLRKIQEKFKE-TTLEYN- 263
Cdd:TIGR02868 157 LILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAA---QLTDALDGAAELVASGALPAALAQVEEADRElTRAERRa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 264 -KFTIYTSSFMSLVGMIVTyscfgWGVyrLWTGHITY--GTMT-LFLQLSSSLSSSFSALIGLVPSAI----SATTSAGR 335
Cdd:TIGR02868 234 aAATALGAALTLLAAGLAV-----LGA--LWAGGPAVadGRLApVTLAVLVLLPLAAFEAFAALPAAAqqltRVRAAAER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 336 IMEViklPREKVLDEEIANEIAATCEENGVSIKLDNIKFKYEkSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILL 415
Cdd:TIGR02868 307 IVEV---LDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 416 GLLNITEGDgVIYNSKDVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGI 495
Cdd:TIGR02868 383 GLLDPLQGE-VTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGL 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 496 NSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRL 564
Cdd:TIGR02868 462 DTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
46-588 |
5.24e-49 |
|
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: 180.92 E-value: 5.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLID-AVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYD 124
Cdd:TIGR03797 138 LLAILAMGLLGTLLGMLVPIATGILIGtAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 125 RIINtdwESMSYYR---SGDLLNRLTSDAT---TVSNSILGwvpSLITKTVQFCSiLVVILYYDPTMAVLALLSAPIALC 198
Cdd:TIGR03797 218 RLLR---LPVSFFRqysTGDLASRAMGISQirrILSGSTLT---TLLSGIFALLN-LGLMFYYSWKLALVAVALALVAIA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 199 VSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIK-AFSLNDVF---SDRLRKIQEKFKETTLEYNKFTIYTSSFMS 274
Cdd:TIGR03797 291 VTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvAGAENRAFarwAKLFSRQRKLELSAQRIENLLTVFNAVLPV 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 275 LVGMIVTYSCfgwgVYRLWTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRImevikLPrekVLDEEiaN 354
Cdd:TIGR03797 371 LTSAALFAAA----ISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERA-----KP---ILEAL--P 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 355 EIAATCEENGV---SIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLniTEGDGVI-YNS 430
Cdd:TIGR03797 437 EVDEAKTDPGKlsgAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFE--TPESGSVfYDG 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 431 KDVKCKISASTRKLMAYVPQEKTMFTGTIAENMrMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQ 510
Cdd:TIGR03797 515 QDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQ 593
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 511 NQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNImsENLNKTCIVTTHRLSVLSMCHKIYRISENK-VQLVNYED 588
Cdd:TIGR03797 594 RQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL--ERLKVTRIVIAHRLSTIRNADRIYVLDAGRvVQQGTYDE 670
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
367-565 |
2.28e-46 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 172.07 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVlENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGViynskDVKCKISASTR 442
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGriliDGT-----DIRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLR 522
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 429188963 523 NAPVLLLDEATSALDMDTEKRV---LKNIMSenlNKTCIVTTHRLS 565
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVkaaLDELMK---GRTTFIIAHRLS 531
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
367-581 |
2.60e-46 |
|
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: 163.04 E-value: 2.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMA 446
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGR-VLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPV 526
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 527 LLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
366-581 |
6.43e-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: 161.12 E-value: 6.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISAST-RKL 444
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGS-ILIDGVDIS-KIGLHDlRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMFTGTIAENMrmvkaD----ATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARAL 520
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNL-----DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 521 LRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
89-568 |
1.59e-44 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 166.43 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 89 MVVMAIGNLVINAVTN---RISTRI-----SIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGW 160
Cdd:PRK10789 34 QILMWIGTMVLIAVVVyllRYVWRVllfgaSYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 161 VPSLITKTVQFCSILVVI---LYYDPTMavLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKA 237
Cdd:PRK10789 114 VLTLVDSLVMGCAVLIVMstqISWQLTL--LALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 238 FSLNDVFSDRLRKIQEKFKETTLEYNKF------TIYTSSFMSLVGMIvtyscfGWGVYRLWTGHITYGTMTLFLQLsss 311
Cdd:PRK10789 192 FGLEDRQSALFAADAEDTGKKNMRVARIdarfdpTIYIAIGMANLLAI------GGGSWMVVNGSLTLGQLTSFVMY--- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 312 lsssfsalIGLVPSAISATTSAGRIME--VIKLPREKVLDEE---IANEIAATCEENGVsikLD-NIK-FKYEKSGKNVL 384
Cdd:PRK10789 263 --------LGLMIWPMLALAWMFNIVErgSAAYSRIRAMLAEapvVKDGSEPVPEGRGE---LDvNIRqFTYPQTDHPAL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 385 ENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMAYVPQEKTMFTGTIAENMR 464
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD-IRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 465 MVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRV 544
Cdd:PRK10789 411 LGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
490 500
....*....|....*....|....
gi 429188963 545 LKNIMSENLNKTCIVTTHRLSVLS 568
Cdd:PRK10789 491 LHNLRQWGEGRTVIISAHRLSALT 514
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
363-565 |
2.74e-43 |
|
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: 163.45 E-value: 2.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 363 NGVSIKLDNIKFKYEkSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGViyNSKDVKckiS 438
Cdd:COG5265 354 GGGEVRFENVSFGYD-PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGriliDGQ--DIRDVT---Q 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 439 ASTRKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIAR 518
Cdd:COG5265 428 ASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIAR 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 429188963 519 ALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLS 565
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLS 554
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
367-581 |
5.15e-41 |
|
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: 148.39 E-value: 5.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKY-EKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLM 445
Cdd:cd03248 12 VKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQ-VLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAP 525
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 526 VLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
364-573 |
6.60e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 156.54 E-value: 6.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 364 GVSIKLDNIK-FKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNItEG----DGVIYNSKDVkckis 438
Cdd:PRK11174 347 PVTIEAEDLEiLSPD--GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGslkiNGIELRELDP----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 439 ASTRKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIAR 518
Cdd:PRK11174 419 ESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALAR 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 519 ALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKI 573
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI 553
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
331-581 |
8.10e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 156.14 E-value: 8.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 331 TSAGRIMEVIKLPREKVLDEEianeiaATCEENGVSIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTt 410
Cdd:PRK11160 309 ASARRINEITEQKPEVTFPTT------STAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKST- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 411 mriLLGLL----NITEGDgVIYNSKDVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYacaye 486
Cdd:PRK11160 382 ---LLQLLtrawDPQQGE-ILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQ----- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 487 fV--EKL---PEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTT 561
Cdd:PRK11160 453 -VglEKLledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT 531
|
250 260
....*....|....*....|
gi 429188963 562 HRLSVLSMCHKIYRISENKV 581
Cdd:PRK11160 532 HRLTGLEQFDRICVMDNGQI 551
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
89-565 |
2.03e-40 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 155.18 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 89 MVVMAIGNLVINAVTNRISTR----ISIKIGNEIRADIYDRIINTdweSMSYY---RSGDLLNRLTSDATTVSNSILGWV 161
Cdd:PRK11176 67 MPLVVIGLMILRGITSFISSYciswVSGKVVMTMRRRLFGHMMGM---PVSFFdkqSTGTLLSRITYDSEQVASSSSGAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 162 PSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLN 241
Cdd:PRK11176 144 ITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 242 DVFSDRLRKIQEKFKETTLeynKFTIYTSSFMSLVGMIVTYSCfgwgVYRLWTGHI-------TYGTMTLFLQLSsslss 314
Cdd:PRK11176 224 EVETKRFDKVSNRMRQQGM---KMVSASSISDPIIQLIASLAL----AFVLYAASFpsvmdtlTAGTITVVFSSM----- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 315 sfsalIGL---VPSAISATTSAGRIM-------EVIKLPREKvlDEeianeiaATCEENGVS--IKLDNIKFKYEKSGKN 382
Cdd:PRK11176 292 -----IALmrpLKSLTNVNAQFQRGMaacqtlfAILDLEQEK--DE-------GKRVIERAKgdIEFRNVTFTYPGKEVP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGViyNSKDVKCkisASTRKLMAYVPQEKTMFTGT 458
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGeillDGH--DLRDYTL---ASLRNQVALVSQNVHLFNDT 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 459 IAENMRMVKADA-TDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALD 537
Cdd:PRK11176 433 IANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
490 500
....*....|....*....|....*...
gi 429188963 538 MDTEKRVLKNIMSENLNKTCIVTTHRLS 565
Cdd:PRK11176 513 TESERAIQAALDELQKNRTSLVIAHRLS 540
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
367-581 |
4.01e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 145.34 E-value: 4.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCkISAST-RKLM 445
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGE-IYLDGKPLSA-MPPPEwRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTGTIAENMRMV---KADATDEEIIRALkyacayefVEKLpeGINSSVLEKG-RSFSEGQNQRLSIARALL 521
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFPfqlRERKFDRERALEL--------LERL--GLPPDILDKPvERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 522 RNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTH-RLSVLSMCHKIYRISENKV 581
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLreYLAEEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
46-303 |
1.22e-39 |
|
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: 146.54 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLIDAVTG-YDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYD 124
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPaGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 125 RIINtdwESMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSK 201
Cdd:cd07346 81 HLQR---LSLSFFdrnRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 202 VLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIVT 281
Cdd:cd07346 158 YFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260
....*....|....*....|..
gi 429188963 282 YSCFGWGVYRLWTGHITYGTMT 303
Cdd:cd07346 238 ALVLLYGGYLVLQGSLTIGELV 259
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
85-573 |
7.61e-37 |
|
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: 144.51 E-value: 7.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 85 IAFVMVVMAignlVINAVTNRISTRISIKIGNEIRADIYDRIIntdweSMSYYRSGDLLNRLTSDATTV-----SNSILG 159
Cdd:COG4618 66 ALGLYAVMG----LLDAVRSRILVRVGARLDRRLGPRVFDAAF-----RAALRGGGGAAAQALRDLDTLrqfltGPGLFA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 160 -----WVPslitktvqfcsILVVILYY-DPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQ 233
Cdd:COG4618 137 lfdlpWAP-----------IFLAVLFLfHPLLGLLALVGALVLVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 234 SIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIVTYSCFGWGVYRLWTGHITYGTMtlflqlsssls 313
Cdd:COG4618 206 VIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAM----------- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 314 ssfsalI--------GLVP---------SAISATTSAGRIMEVIK----------LPREKvldeeianeiaatceenGvS 366
Cdd:COG4618 275 ------IaasilmgrALAPieqaiggwkQFVSARQAYRRLNELLAavpaepermpLPRPK-----------------G-R 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIynskdvkckISASTR 442
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvrlDGAD---------LSQWDR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 ----KLMAYVPQEKTMFTGTIAENM-RMvkADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIA 517
Cdd:COG4618 402 eelgRHIGYLPQDVELFDGTIAENIaRF--GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 518 RALLRNAPVLLLDEATSALDMDTEKRVLKNImsENL---NKTCIVTTHRLSVLSMCHKI 573
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAI--RALkarGATVVVITHRPSLLAAVDKL 536
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
354-567 |
1.65e-36 |
|
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: 143.88 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 354 NEIAATCEENGVS--IKLDNIKFKYEKSGKNVlENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSK 431
Cdd:TIGR01192 320 EEPADAPELPNVKgaVEFRHITFEFANSSQGV-FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQ-ILIDGI 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 432 DVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQN 511
Cdd:TIGR01192 398 DINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 512 QRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVL 567
Cdd:TIGR01192 478 QRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTV 533
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
367-573 |
1.03e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 134.04 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLMA 446
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE-VRVLGEDVA-RDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-TIAENMRM------VKADATDEEIIRALkyacayEFVEkLPEGINSSVlekgRSFSEGQNQRLSIARA 519
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfarlygLPRKEARERIDELL------ELFG-LTDAADRKV----GTLSGGMKQRLGLALA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 520 LLRNAPVLLLDEATSALDMDTeKRVLKNIMSE--NLNKTCIVTTHRLSVL-SMCHKI 573
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEA-RRELWELLRElaAEGKTVLLSTHYLEEAeRLCDRV 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
367-573 |
4.50e-35 |
|
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: 130.03 E-value: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDvkckiSASTR 442
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGrvrlDGADISQWD-----PNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTGTIAENMrmvkadatdeeiiralkyacayefveklpeginssvlekgrsFSEGQNQRLSIARALLR 522
Cdd:cd03246 76 DHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 429188963 523 NAPVLLLDEATSALDMDTEKRVLKNIMSENL-NKTCIVTTHRLSVLSMCHKI 573
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRI 165
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
367-580 |
2.70e-33 |
|
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: 126.04 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKN---VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvkcKISASTRk 443
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG------------SVSVPGS- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 444 lMAYVPQEKTMFTGTIAEN----MRMvkadatDEEiiralKY-----ACAYEF-VEKLPEGINSSVLEKGRSFSEGQNQR 513
Cdd:cd03250 68 -IAYVSQEPWIQNGTIRENilfgKPF------DEE-----RYekvikACALEPdLEILPDGDLTEIGEKGINLSGGQKQR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 514 LSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENL--NKTCIVTTHRLSVLSMCHKIYRISENK 580
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLlnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
367-583 |
1.09e-32 |
|
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: 123.58 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLMA 446
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE-ITLDGVPVS-DLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTGTIAENMrmvkadatdeeiiralkyacayefveklpeginssvlekGRSFSEGQNQRLSIARALLRNAPV 526
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 527 LLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKVQL 583
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
367-581 |
1.67e-32 |
|
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: 122.89 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLMA 446
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE-IKVLGKDIK-KEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFtgtiaENMRmvkadatdeeiiralkyacAYEFVEklpeginssvlekgrsFSEGQNQRLSIARALLRNAPV 526
Cdd:cd03230 77 YLPEEPSLY-----ENLT-------------------VRENLK----------------LSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 527 LLLDEATSALDMDTEKRVLKNIMSENL-NKTCIVTTHRLS-VLSMCHKIYRISENKV 581
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEeAERLCDRVAILNNGRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
367-574 |
3.78e-32 |
|
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: 124.53 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKN--VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKL 444
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGE-VTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQE--------KTMFTgTIAENMRMVKADATDEEIIRALKYAcayefveklpeGINSSVLEK-GRSFSEGQNQRLS 515
Cdd:COG1124 81 VQMVFQDpyaslhprHTVDR-ILAEPLRIHGLPDREERIAELLEQV-----------GLPPSFLDRyPHQLSGGQRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 516 IARALLRNAPVLLLDEATSALDMDTEK---RVLKNIMSEnLNKTCIVTTHRLSVLS-MCHKIY 574
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAeilNLLKDLREE-RGLTYLFVSHDLAVVAhLCDRVA 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
384-534 |
3.85e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.22 E-value: 3.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 384 LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMAYVPQEKTMFTG-TIAEN 462
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGT-ILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 463 MRMV------KADATDEEIIRALKYAcayefveKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATS 534
Cdd:pfam00005 80 LRLGlllkglSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
371-576 |
9.49e-32 |
|
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: 122.61 E-value: 9.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 371 NIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDV---KCKISASTRKLMAY 447
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGS-IIFDGKDLlklSRRLRKIRRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 448 VPQE--------KTMFTgTIAENMRMVKADATDEEIIRAlkyacAYEFVEKLPegINSSVLEK-GRSFSEGQNQRLSIAR 518
Cdd:cd03257 87 VFQDpmsslnprMTIGE-QIAEPLRIHGKLSKKEARKEA-----VLLLLVGVG--LPEEVLNRyPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 519 ALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLSVLS-MCHKIYRI 576
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAkIADRVAVM 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
368-581 |
1.20e-31 |
|
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: 120.62 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 368 KLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTR-KLMA 446
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE-ILLDGKDLA-SLSPKELaRKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQektmftgtiaenmrmvkadatdeeiirALKYACAYEFVEklpeginssvlekgRSFSE---GQNQRLSIARALLRN 523
Cdd:cd03214 77 YVPQ---------------------------ALELLGLAHLAD--------------RPFNElsgGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 524 APVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLS-VLSMCHKIYRISENKV 581
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
46-303 |
1.92e-31 |
|
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: 123.77 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLIDAV-----TGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRA 120
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVliqlgPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 121 DIYDRIINTdweSMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIAL 197
Cdd:cd18563 81 DLYEHLQRL---SLSFFdkrQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 198 CVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVG 277
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLT 237
|
250 260
....*....|....*....|....*.
gi 429188963 278 MIVTYSCFGWGVYRLWTGHITYGTMT 303
Cdd:cd18563 238 SLGTLIVWYFGGRQVLSGTMTLGTLV 263
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
367-573 |
2.43e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 127.71 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKN---VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRK 443
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS-ILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 444 L---MAYVPQ--------EKTMFTgTIAE---NMRMVKADATDEEIIRALkyacayEFVeklpeGINSSVLEK-GRSFSE 508
Cdd:COG1123 340 LrrrVQMVFQdpysslnpRMTVGD-IIAEplrLHGLLSRAERRERVAELL------ERV-----GLPPDLADRyPHELSG 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 509 GQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMS--ENLNKTCIVTTHRLS-VLSMCHKI 573
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqRELGLTYLFISHDLAvVRYIADRV 475
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
367-581 |
6.57e-31 |
|
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: 119.90 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNV--LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKC----KISAS 440
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-VRVDGTDISKlsekELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 441 TRKLMAYVPQE----KTMftgTIAENMRM------VKADATDEEIIRALKYAcayefveKLPEGINSSVLEkgrsFSEGQ 510
Cdd:cd03255 80 RRRHIGFVFQSfnllPDL---TALENVELplllagVPKKERRERAEELLERV-------GLGDRLNHYPSE----LSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 511 NQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLreLNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
368-580 |
6.97e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 119.49 E-value: 6.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 368 KLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMAY 447
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGE-VLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 448 VPQE-KTMFTGT-----IA---ENMRMvkadaTDEEIIRALKYACA----YEFVEKLPEginssvlekgrSFSEGQNQRL 514
Cdd:cd03225 80 VFQNpDDQFFGPtveeeVAfglENLGL-----PEEEIEERVEEALElvglEGLRDRSPF-----------TLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 515 SIARALLRNAPVLLLDEATSALDMDTEKRVLKnIMSE--NLNKTCIVTTHRLS-VLSMCHKIYRISENK 580
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLE-LLKKlkAEGKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
83-581 |
9.17e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 128.56 E-value: 9.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 83 GFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVP 162
Cdd:PLN03232 950 GFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMN 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 163 SLITKTVQFCSILVVIlyydPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMS-----FNEeTFTNLQSIKA 237
Cdd:PLN03232 1030 MFMNQLWQLLSTFALI----GTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSpiyaqFGE-ALNGLSSIRA 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 238 FSLndvfSDRLRKIQEKFKETTLEYNKFTIYTSSFM-----SLVGMIV----TYSCFGWGVYRLWTGHITygTMTLFLQL 308
Cdd:PLN03232 1105 YKA----YDRMAKINGKSMDNNIRFTLANTSSNRWLtirleTLGGVMIwltaTFAVLRNGNAENQAGFAS--TMGLLLSY 1178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 309 SSSLSSSFSALIGLVPSAISATTSAGRIMEVIKLPREKVldEEIANEIAATCEENGVSIKLDNIKFKYEKSGKNVLENAN 388
Cdd:PLN03232 1179 TLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEAT--AIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLS 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 389 IIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKDVKCKISaSTRKLMAYVPQEKTMFTGTIAENMRMVkA 468
Cdd:PLN03232 1257 FFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLT-DLRRVLSIIPQSPVLFSGTVRFNIDPF-S 1334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 469 DATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNI 548
Cdd:PLN03232 1335 EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI 1414
|
490 500 510
....*....|....*....|....*....|...
gi 429188963 549 MSENLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:PLN03232 1415 REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
46-303 |
1.51e-30 |
|
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: 121.36 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLIDAVTGY-------DSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEI 118
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGlgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 119 RADIYDRIINTdweSMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPI 195
Cdd:cd18547 81 RKDLFEKLQRL---PLSYFdthSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 196 ALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLeynKFTIYTSSFMSL 275
Cdd:cd18547 158 SLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASF---KAQFYSGLLMPI 234
|
250 260 270
....*....|....*....|....*....|.
gi 429188963 276 VGMI--VTYSCFG-WGVYRLWTGHITYGTMT 303
Cdd:cd18547 235 MNFInnLGYVLVAvVGGLLVINGALTVGVIQ 265
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
367-562 |
2.85e-30 |
|
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: 119.38 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTR-KLM 445
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGE-VLLDGRDLA-SLSRRELaRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTM-FTGTIAENMRM---------VKADATDEEII-RALKYACAYEFveklpeginssvleKGRSFSE---GQN 511
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALgryphlglfGRPSAEDREAVeEALERTGLEHL--------------ADRPVDElsgGER 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 429188963 512 QRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTH 562
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLH 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
63-582 |
6.12e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 125.86 E-value: 6.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 63 GSVASKYLIDAVTGYDSGGIGFI-AFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTDWESMSYYRSGD 141
Cdd:PLN03232 320 GPVILSHLLQSMQEGDPAWVGYVyAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGK 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 142 LLNRLTSDATT---VSNSILG-WvpslitkTVQFCSILVVILYYDpTMAVLALLSAPIALCV---SKVLMKKMRNRNKEV 214
Cdd:PLN03232 400 VTNMITTDANAlqqIAEQLHGlW-------SAPFRIIVSMVLLYQ-QLGVASLFGSLILFLLiplQTLIVRKMRKLTKEG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 215 REISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEK----FKETTLeynkFTIYTSSFMSLVGMIVTYSCFGwgVY 290
Cdd:PLN03232 472 LQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEelswFRKAQL----LSAFNSFILNSIPVVVTLVSFG--VF 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 291 RLWTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRIMEVIkLPREKVLDEEianeiaATCEENGVSIKLD 370
Cdd:PLN03232 546 VLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELL-LSEERILAQN------PPLQPGAPAISIK 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 371 NIKFKYE-KSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIynskdvkckisasTRKLMAYVP 449
Cdd:PLN03232 619 NGYFSWDsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-------------IRGSVAYVP 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 450 QEKTMFTGTIAENMrMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLL 529
Cdd:PLN03232 686 QVSWIFNATVRENI-LFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIF 764
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 429188963 530 DEATSALDMDTEKRVLKNIMSENLN-KTCIVTTHRLSVLSMCHKIYRISENKVQ 582
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDSCMKDELKgKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
368-573 |
8.66e-30 |
|
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: 116.48 E-value: 8.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 368 KLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynSKDVKCKISASTRKLMAY 447
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSG------SIRVFGKPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 448 VPQEKTM---FTGTIAENMRM---------VKADATD-EEIIRALKYACAYEFVEklpeginssvlekgRSFSE---GQN 511
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMglyghkglfRRLSKADkAKVDEALERVGLSELAD--------------RQIGElsgGQQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429188963 512 QRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSEN-LNKTCIVTTHRL-SVLSMCHKI 573
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLgLVLEYFDRV 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
368-580 |
3.67e-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: 113.11 E-value: 3.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 368 KLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMAY 447
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE-ILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 448 VPQektmftgtiaenmrmvkadatdeeiiralkyacayefveklpeginssvlekgrsFSEGQNQRLSIARALLRNAPVL 527
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 528 LLDEATSALDMDTEKRVLKNIMSENL-NKTCIVTTHRLSVLSM-CHKIYRISENK 580
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
369-581 |
1.05e-28 |
|
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: 113.51 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 369 LDNIKFKYEKsGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKisaSTRKLMAYV 448
Cdd:cd03226 2 IENISFSYKK-GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGS-ILLNGKPIKAK---ERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 449 PQEKT--MFTGTIAENMRmVKADATDEEIIRA---LKYACAYEFVEKLPeginssvlekgRSFSEGQNQRLSIARALLRN 523
Cdd:cd03226 77 MQDVDyqLFTDSVREELL-LGLKELDAGNEQAetvLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 524 APVLLLDEATSALDMDTEKRVLKNIMSE-NLNKTCIVTTHRLSVLSM-CHKIYRISENKV 581
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
367-576 |
1.47e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.03 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKisastRKLMA 446
Cdd:COG1121 7 IELENLTVSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGT-VRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTM---FTGTIAENMRM---------VKADATDEEIIRAlkyacAYEFVEklpeginssvLE--KGRSFSE---G 509
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLMgrygrrglfRRPSRADREAVDE-----ALERVG----------LEdlADRPIGElsgG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 510 QNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSEN-LNKTCIVTTHRLS-VLSMCHKIYRI 576
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGaVREYFDRVLLL 212
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
46-302 |
2.61e-28 |
|
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: 114.28 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLIDAVTGY---DSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADI 122
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDgdpETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 123 YDRIINTDwesMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCV 199
Cdd:pfam00664 81 FKKILRQP---MSFFdtnSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 200 SKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMI 279
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260
....*....|....*....|...
gi 429188963 280 VTYSCFGWGVYRLWTGHITYGTM 302
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDL 260
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
46-280 |
4.56e-28 |
|
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: 114.06 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLIDAVTGY-DSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYD 124
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEkDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 125 RIINTDwesMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSK 201
Cdd:cd18552 81 KLLRLP---LSFFdrnSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 202 VLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIV 280
Cdd:cd18552 158 RIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIA 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
370-573 |
4.63e-28 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 120.13 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 370 DNIKFKYEKSGKN---VLENANIIANPGEiialiGPSGEGKT---TTMRILLGLLNITEgdgviYNSKDVkckisastRK 443
Cdd:PTZ00265 1235 DMTNEQDYQGDEEqnvGMKNVNEFSLTKE-----GGSGEDSTvfkNSGKILLDGVDICD-----YNLKDL--------RN 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 444 LMAYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRN 523
Cdd:PTZ00265 1297 LFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLRE 1376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 429188963 524 APVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLSVLSMCHKI 573
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKI 1428
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
367-580 |
9.44e-28 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 109.58 E-value: 9.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDV--KCKISASTRKL 444
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS-ILIDGEDLtdLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMFTG-TIAENmrmvkadatdeeIIRALkyacayefveklpeginssvlekgrsfSEGQNQRLSIARALLRN 523
Cdd:cd03229 78 IGMVFQDFALFPHlTVLEN------------IALGL---------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 524 APVLLLDEATSALDMDTEKRVLKNIMS--ENLNKTCIVTTHRLS-VLSMCHKIYRISENK 580
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
366-581 |
1.06e-27 |
|
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: 110.58 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIyNSKDVKCKISASTRKLM 445
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTGTIAENMRmVKADATDEEIIRALKyacayefveklpeginssVLEKGRSFSEGQNQRLSIARALLRNAP 525
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLD-PFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 526 VLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
367-577 |
1.45e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.90 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYeKSGKN---VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKckiSASTRK 443
Cdd:COG1136 5 LELRNLTKSY-GTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-VLIDGQDIS---SLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 444 L-------MAYVPQE----KTMftgTIAENMRM------VKADATDEEIIRALKY----ACAYEFVEKLpeginssvlek 502
Cdd:COG1136 80 LarlrrrhIGFVFQFfnllPEL---TALENVALplllagVSRKERRERARELLERvglgDRLDHRPSQL----------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 503 grsfSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLSVLSMCHKIYRIS 577
Cdd:COG1136 146 ----SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLreLNRELGTTIVMVTHDPELAARADRVIRLR 218
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
46-303 |
2.33e-27 |
|
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: 111.76 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLIDAVTGydSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDR 125
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSA--GGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 126 IINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMK 205
Cdd:cd18551 79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 206 KMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIVTYSCF 285
Cdd:cd18551 159 RIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVL 238
|
250
....*....|....*...
gi 429188963 286 GWGVYRLWTGHITYGTMT 303
Cdd:cd18551 239 GVGGARVASGALTVGTLV 256
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
367-584 |
2.44e-27 |
|
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: 109.53 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCkISASTRKLmA 446
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE-ILIDGRDVTG-VPPERRNI-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-TIAEN------MRMVKADATDEEIIRALKYACAYEFVEKLPEGInssvlekgrsfSEGQNQRLSIARA 519
Cdd:cd03259 76 MVFQDYALFPHlTVAENiafglkLRGVPKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 520 LLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLS-VLSMCHKIYRISENKVQLV 584
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELkeLQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQV 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
364-581 |
3.68e-27 |
|
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: 108.79 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 364 GVSIKLDNIKF----KYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLN--ITEGDgVIYNSKDVKcki 437
Cdd:cd03213 1 GVTLSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGE-VLINGRPLD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 438 SASTRKLMAYVPQEKTMF-TGTIAENMRmvkadatdeeiiralkyacayeFVEKLpeginssvlekgRSFSEGQNQRLSI 516
Cdd:cd03213 77 KRSFRKIIGYVPQDDILHpTLTVRETLM----------------------FAAKL------------RGLSGGERKRVSI 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 517 ARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSE-NLNKTCIVTTHRLS--VLSMCHKIYRISENKV 581
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSseIFELFDKLLLLSQGRV 190
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
364-565 |
1.11e-26 |
|
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: 109.23 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 364 GVSIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIyNSKDVkCKISAST-R 442
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGIDI-SKLPLHTlR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTGTIAENMRmVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLR 522
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 429188963 523 NAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLS 565
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVS 216
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
43-302 |
1.30e-26 |
|
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: 109.84 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 43 KLAIIFYVFLGILGVVMGLGGSVASKYLIDAVTGY-DSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRAD 121
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSgDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 122 IYDRIINTdweSMSYY---RSGDLLNRLtSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALC 198
Cdd:cd18570 81 YFKHLLKL---PLSFFetrKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 199 VSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGM 278
Cdd:cd18570 157 IILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISL 236
|
250 260
....*....|....*....|....
gi 429188963 279 IVTYSCFGWGVYRLWTGHITYGTM 302
Cdd:cd18570 237 IGSLLILWIGSYLVIKGQLSLGQL 260
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
383-573 |
1.52e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 107.18 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLMAYVPQEKTMFTG-TIAE 461
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE-VLWNGEPIR-DAREDYRRRLAYLGHADGLKPElTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 462 NMRMV----KADATDEEIIRALKYAcayefveklpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALD 537
Cdd:COG4133 95 NLRFWaalyGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 429188963 538 MDTEKRVLkNIMSENLNK--TCIVTTHRLSVLSMCHKI 573
Cdd:COG4133 164 AAGVALLA-ELIAAHLARggAVLLTTHQPLELAAARVL 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
367-574 |
1.77e-26 |
|
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: 107.56 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSG--KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkckisASTRKL 444
Cdd:cd03293 1 LEVRNVSKTYGGGGgaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE-VLVDGEPV-----TGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMFT-GTIAEN------MRMVKADATDEEIIRALKYACAYEFVEKLPeginssvlekgRSFSEGQNQRLSIA 517
Cdd:cd03293 75 RGYVFQQDALLPwLTVLDNvalgleLQGVPKAEARERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 518 RALLRNAPVLLLDEATSALDMDTEK---RVLKNIMSENlNKTCIVTTHRLS-VLSMCHKIY 574
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREqlqEELLDIWRET-GKTVLLVTHDIDeAVFLADRVV 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
367-579 |
3.10e-26 |
|
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: 106.88 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG---DG-VIYNSKDVKCKISA--S 440
Cdd:cd03260 1 IELRDLNVYYG--DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdEGeVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 441 TRKLMAYVPQEKTMFTGTIAENMR-------MVKADATDEEIIRALKYAcayefveKLPEGINSSVleKGRSFSEGQNQR 513
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgIKLKEELDERVEEALRKA-------ALWDEVKDRL--HALGLSGGQQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 514 LSIARALLRNAPVLLLDEATSALDmDTEKRVLKNIMSEnLNK--TCIVTTHRLsvlsmcHKIYRISEN 579
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALD-PISTAKIEELIAE-LKKeyTIVIVTHNM------QQAARVADR 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
332-582 |
1.10e-25 |
|
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: 112.70 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 332 SAGRIMEVIKLPRE--------------KVLdeEIANEIAATCEENGVSIKLDNIKFKYEKSGKNVLENANIIANPGEII 397
Cdd:TIGR01271 1171 SVSRVFKFIDLPQEeprpsggggkyqlsTVL--VIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRV 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 398 ALIGPSGEGKTTTMRILLGLLNiTEG----DGVIYNSKDVKckisaSTRKLMAYVPQEKTMFTGTIAENMRmVKADATDE 473
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLS-TEGeiqiDGVSWNSVTLQ-----TWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 474 EIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENL 553
Cdd:TIGR01271 1322 EIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS 1401
|
250 260
....*....|....*....|....*....
gi 429188963 554 NKTCIVTTHRLSVLSMCHKIYRISENKVQ 582
Cdd:TIGR01271 1402 NCTVILSEHRVEALLECQQFLVIEGSSVK 1430
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
366-562 |
1.89e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.85 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKlM 445
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGE-ILIGGRDVT-DLPPKDRN-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQE----KTMftgTIAENM----RMVKADAtdEEIIRALKYAcayefVEKLpeGInSSVLE-KGRSFSEGQNQRLSI 516
Cdd:COG3839 78 AMVFQSyalyPHM---TVYENIafplKLRKVPK--AEIDRRVREA-----AELL--GL-EDLLDrKPKQLSGGQRQRVAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 429188963 517 ARALLRNAPVLLLDEATSALD------MDTE-KRVLKnimseNLNKTCIVTTH 562
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHR-----RLGTTTIYVTH 192
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
367-536 |
7.45e-25 |
|
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: 102.90 E-value: 7.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSgkNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkckISASTRKL-- 444
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGS-IRFDGRDI---TGLPPHERar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 --MAYVPQEKTMFTG-TIAENMRMVKADATDEEIIRALKYacAYEFVEKLPEGINSsvleKGRSFSEGQNQRLSIARALL 521
Cdd:cd03224 75 agIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLER--VYELFPRLKERRKQ----LAGTLSGGEQQMLAIARALM 148
|
170
....*....|....*
gi 429188963 522 RNAPVLLLDEATSAL 536
Cdd:cd03224 149 SRPKLLLLDEPSEGL 163
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
367-566 |
2.89e-24 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 101.88 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYeKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIY---NSKDVKCKISAStRK 443
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdINKLKGKALRQL-RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 444 LMAYVPQE----KTMftgTIAENMRMVKADA-----------TDEEIIRALkyacayEFVEKLpeGINSSVLEKGRSFSE 508
Cdd:cd03256 79 QIGMIFQQfnliERL---SVLENVLSGRLGRrstwrslfglfPKEEKQRAL------AALERV--GLLDKAYQRADQLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 509 GQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRV---LKNImSENLNKTCIVTTHRLSV 566
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVmdlLKRI-NREEGITVIVSLHQVDL 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
367-562 |
4.01e-24 |
|
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: 100.66 E-value: 4.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISAsTRKLMA 446
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT-AYINGYSIRTDRKA-ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-TIAENMR---MVKADATDEEIIRALKYACAYEFVEKLpegiNSSVlekgRSFSEGQNQRLSIARALLR 522
Cdd:cd03263 79 YCPQFDALFDElTVREHLRfyaRLKGLPKSEIKEEVELLLRVLGLTDKA----NKRA----RTLSGGMKRKLSLAIALIG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 429188963 523 NAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTH 562
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
367-562 |
4.08e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 101.70 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNI--KFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKckiSASTRkl 444
Cdd:COG1116 8 LELRGVskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGE-VLVDGKPVT---GPGPD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMF---TgtIAEN----MRMVKAD-ATDEEIIRA------LKyacayEFVEKLPeginsSVLekgrsfSEGQ 510
Cdd:COG1116 82 RGVVFQEPALLpwlT--VLDNvalgLELRGVPkAERRERAREllelvgLA-----GFEDAYP-----HQL------SGGM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 511 NQRLSIARALLRNAPVLLLDEATSALDMDTekrvlKNIMSENL-------NKTCIVTTH 562
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALT-----RERLQDELlrlwqetGKTVLFVTH 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
367-573 |
4.39e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.14 E-value: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLL--NITEGDGVIYNSKDVKCKISASTRKL 444
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQE-KTMFTGT-----IAE---NMRMVKADAtDEEIIRALKYACAYEFVEKLPEginssvlekgrSFSEGQNQRLS 515
Cdd:COG1123 85 IGMVFQDpMTQLNPVtvgdqIAEaleNLGLSRAEA-RARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 516 IARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLSVLS-MCHKI 573
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAeIADRV 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
140-573 |
7.87e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.79 E-value: 7.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 140 GDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPtMAVLALlsAPIALCVSKvLMKKMRNRNKEVREISS 219
Cdd:PTZ00243 1055 GRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQP-FVLVAL--VPCGYLYYR-LMQFYNSANREIRRIKS 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 220 EM----MSFNEETFTNLQSIKAFS-LNDVFSDRLRKIQEKFKETTLEyNKFTIYTSSFMSLVGMIVTYSCFGWGVYR--L 292
Cdd:PTZ00243 1131 VAkspvFTLLEEALQGSATITAYGkAHLVMQEALRRLDVVYSCSYLE-NVANRWLGVRVEFLSNIVVTVIALIGVIGtmL 1209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 293 WTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRIMEVI-KLPREKV--LDEEI---------ANEIAATC 360
Cdd:PTZ00243 1210 RATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDMpeLDEEVdalerrtgmAADVTGTV 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 361 EENGVS-------------IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTtmrILLGLLNITE--GDG 425
Cdd:PTZ00243 1290 VIEPASptsaaphpvqagsLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKST---LLLTFMRMVEvcGGE 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 426 VIYNSKDVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVkADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRS 505
Cdd:PTZ00243 1367 IRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPF-LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSN 1445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 506 FSEGQNQRLSIARALL-RNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKI 573
Cdd:PTZ00243 1446 YSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKI 1514
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
329-565 |
8.52e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 105.57 E-value: 8.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 329 ATTSAGRIMEVIKLPREKVLDEEIAneiaatceENGVSIKLDNIKFKYeKSGKNVLENANIIANPGEIIALIGPSGEGKT 408
Cdd:PRK10790 311 AVVAGERVFELMDGPRQQYGNDDRP--------LQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKS 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 409 TTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMAYVPQEKTMFTGTIAENMRMVKaDATDEEIIRALKYACAYEFV 488
Cdd:PRK10790 382 TLASLLMGYYPLTEGE-IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELA 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 489 EKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLS 565
Cdd:PRK10790 460 RSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLS 536
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
367-589 |
1.25e-23 |
|
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: 100.70 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNiTEG----DGVIYNSKDVKckisaSTR 442
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGdiqiDGVSWNSVPLQ-----KWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTGTIAENMRmVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLR 522
Cdd:cd03289 77 KAFGVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 523 NAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKVQlvNYEDI 589
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVR--QYDSI 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
367-562 |
2.46e-23 |
|
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: 98.60 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYeksGKNV-LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIyNSKDVKCKiSASTRKLM 445
Cdd:cd03265 1 IEVENLVKKY---GDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV-AGHDVVRE-PREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTM---FTGTiaENMRM------VKADATDEEIIRALKYACAYEFVEKLPeginssvlekgRSFSEGQNQRLSI 516
Cdd:cd03265 76 GIVFQDLSVddeLTGW--ENLYIharlygVPGAERRERIDELLDFVGLLEAADRLV-----------KTYSGGMRRRLEI 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 429188963 517 ARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTH 562
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIekLKEEFGMTILLTTH 190
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
367-562 |
3.48e-23 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 98.53 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYeKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMA 446
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGE-IFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-TIAENMRMV-KADATDEEIIRALkyacAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNA 524
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALVpKLLKWPKEKIRER----ADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 429188963 525 PVLLLDEATSALDMDTEKRV---LKNIMSEnLNKTCIVTTH 562
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLqeeFKRLQQE-LGKTIVFVTH 194
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
367-581 |
5.52e-23 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 98.04 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNV--LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKL 444
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS-VLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 ---MAYVPQEKTMFTG-TIAENMrmvkadATDEEIIRALKyACAYEFVEKLPEGINSSvlEKGRSF----SEGQNQRLSI 516
Cdd:cd03258 81 rrrIGMIFQHFNLLSSrTVFENV------ALPLEIAGVPK-AEIEERVLELLELVGLE--DKADAYpaqlSGGQKQRVGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 517 ARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSEN--LNKTCIVTTHRLSVL-SMCHKIYRISENKV 581
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINreLGLTIVLITHEMEVVkRICDRVAVMEKGEV 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
363-573 |
8.72e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 100.17 E-value: 8.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 363 NGVSIKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkckisastr 442
Cdd:COG3842 2 AMPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGR-ILLDGRDV--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 klmAYVPQEK----TMFTG-------TIAEN------MRMVKADATDEEIIRALK------YAcayefvEKLPeginssv 499
Cdd:COG3842 70 ---TGLPPEKrnvgMVFQDyalfphlTVAENvafglrMRGVPKAEIRARVAELLElvglegLA------DRYP------- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 500 lekgRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRV---LKNIMSEnLNKTCIVTTHRLS-VLSMCHKI 573
Cdd:COG3842 134 ----HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMreeLRRLQRE-LGITFIYVTHDQEeALALADRI 206
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
366-582 |
1.08e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 103.28 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNskdvkCKIS----AST 441
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG-----CDISkfglMDL 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 442 RKLMAYVPQEKTMFTGTIAENMRMVKaDATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALL 521
Cdd:PLN03130 1312 RKVLGIIPQAPVLFSGTVRFNLDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 522 RNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKVQ 582
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVV 1451
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
393-582 |
1.16e-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: 96.21 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 393 PGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVKCKISASTRKLmAYVPQEKTMFTG-TIAENMRMV- 466
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlNGTVLFDSRKKINLPPQQRKI-GLVFQQYALFPHlNVRENLAFGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 467 KADATDEEIIRalkyacayefVEKLPEGINSSVLEKGRS--FSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRV 544
Cdd:cd03297 101 KRKRNREDRIS----------VDELLDLLGLDHLLNRYPaqLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 429188963 545 LK--NIMSENLNKTCIVTTHRLS-VLSMCHKIYRISENKVQ 582
Cdd:cd03297 171 LPelKQIKKNLNIPVIFVTHDLSeAEYLADRIVVMEDGRLQ 211
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
46-301 |
1.38e-22 |
|
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: 98.38 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLIDAVTGY--DSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIY 123
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGskSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 124 DRIINTdweSMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVS 200
Cdd:cd18778 81 DKLQRL---SLRYFddrQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 201 KVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIV 280
Cdd:cd18778 158 WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLG 237
|
250 260
....*....|....*....|.
gi 429188963 281 TYSCFGWGVYRLWTGHITYGT 301
Cdd:cd18778 238 TVLVLGFGGRLVLAGELTIGD 258
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
42-303 |
1.65e-22 |
|
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: 97.89 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 42 YKLAIIFYVFLGILGVVMGLggsvASKYLIDAV-TGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRA 120
Cdd:cd18542 1 YLLAILALLLATALNLLIPL----LIRRIIDSViGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 121 DIYDRIINtdwESMSYY---RSGDLLNRLTSDATTVSNsILGWV-PSLITKTVQFCSILVVILYYDPTMAVLALLSAPIA 196
Cdd:cd18542 77 DLYDHLQR---LSFSFHdkaRTGDLMSRCTSDVDTIRR-FLAFGlVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 197 LCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNK-FTIY--TSSFM 273
Cdd:cd18542 153 ALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKlLAKYwpLMDFL 232
|
250 260 270
....*....|....*....|....*....|
gi 429188963 274 SLVGMIVTYSCFGWGVYRlwtGHITYGTMT 303
Cdd:cd18542 233 SGLQIVLVLWVGGYLVIN---GEITLGELV 259
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
367-582 |
3.73e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.12 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKsGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISAST----R 442
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQ-VLVNGQDLS-RLKRREipylR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQE-KTMFTGTIAENMRMV-KADATDEEIIRalkyacayefvEKLPEginssVLE------KGRSF----SEGQ 510
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALPlRVTGKSRKEIR-----------RRVRE-----VLDlvglsdKAKALphelSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 511 NQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKniMSENLNK---TCIVTTHRLSVL-SMCHKIYRISENKVQ 582
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIME--LLEEINRrgtTVLIATHDLELVdRMPKRVLELEDGRLV 216
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
54-250 |
4.74e-22 |
|
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: 96.81 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 54 ILGVVMGLGGSVAS-------KYLIDAVTGYDSGG----------------IGFIAFVMVVMAIGNLVINAVTNRISTRI 110
Cdd:cd18564 2 ALALLALLLETALRllepwplKVVIDDVLGDKPLPgllglapllgpdplalLLLAAAALVGIALLRGLASYAGTYLTALV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 111 SIKIGNEIRADIYDRIINTdweSMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAV 187
Cdd:cd18564 82 GQRVVLDLRRDLFAHLQRL---SLSFHdrrRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 188 LALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRK 250
Cdd:cd18564 159 IALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
367-562 |
5.38e-22 |
|
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: 94.52 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVKckiSASTR 442
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiiDGLKLTDDKKN---INELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTG-TIAENM--------RMVKADATDEeiiralkyacAYEFVEK--LPEGINSSVlekgRSFSEGQN 511
Cdd:cd03262 76 QKVGMVFQQFNLFPHlTVLENItlapikvkGMSKAEAEER----------ALELLEKvgLADKADAYP----AQLSGGQQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 429188963 512 QRLSIARALLRNAPVLLLDEATSALDMDTEKRVL---KNIMSENLnkTCIVTTH 562
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLdvmKDLAEEGM--TMVVVTH 193
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
367-581 |
6.84e-22 |
|
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: 94.88 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkCKISAS----TR 442
Cdd:cd03261 1 IELRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGE-VLIDGEDI-SGLSEAelyrLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTG-TIAEN----MRMVKADatDEEIIRalkyacayEFV-EKLPE-GINSSVLEKGRSFSEGQNQRLS 515
Cdd:cd03261 77 RRMGMLFQSGALFDSlTVFENvafpLREHTRL--SEEEIR--------EIVlEKLEAvGLRGAEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 516 IARALLRNAPVLLLDEATSALDMDTEKRVLKNIMS--ENLNKTCIVTTHRL-SVLSMCHKIYRISENKV 581
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLdTAFAIADRIAVLYDGKI 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
367-582 |
9.93e-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: 93.80 E-value: 9.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKsgKNVLENANIIANPGeIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLMA 446
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGT-IRIDGQDVL-KQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTGTIAENM--------RMVKADAtDEEIIRALkyacayefvEKLpeGINSSVLEKGRSFSEGQNQRLSIAR 518
Cdd:cd03264 76 YLPQEFGVYPNFTVREFldyiawlkGIPSKEV-KARVDEVL---------ELV--NLGDRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 519 ALLRNAPVLLLDEATSALdmDTEKRV-LKNIMSE-NLNKTCIVTTHRLS-VLSMCHKIYRISENKVQ 582
Cdd:cd03264 144 ALVGDPSILIVDEPTAGL--DPEERIrFRNLLSElGEDRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
367-567 |
1.01e-21 |
|
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: 100.41 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTtmrILLGLLNITEG-------DGViyNSKDVKCKisa 439
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFRINESaegeiiiDGL--NIAKIGLH--- 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 440 STRKLMAYVPQEKTMFTGTIAENMRMVkADATDEEIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARA 519
Cdd:TIGR00957 1357 DLRFKITIIPQDPVLFSGSLRMNLDPF-SQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARA 1435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 429188963 520 LLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVL 567
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1483
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
49-302 |
2.57e-21 |
|
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: 94.46 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 49 YVFLGILGVVMGLGGSVASKYLI-----DAVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIY 123
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIkiaidEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 124 DRIINTdweSMSYYRS---GDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVS 200
Cdd:cd18545 81 SHLQKL---SFSFFDSrpvGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 201 KVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSlndvfsdRLRKIQEKFKETTLEYNK----FTIYTSSFMSLV 276
Cdd:cd18545 158 FLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFA-------REDENEEIFDELNRENRKanmrAVRLNALFWPLV 230
|
250 260
....*....|....*....|....*....
gi 429188963 277 ---GMIVTYSCFGWGVYRLWTGHITYGTM 302
Cdd:cd18545 231 eliSALGTALVYWYGGKLVLGGAITVGVL 259
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
367-584 |
2.87e-21 |
|
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: 92.32 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIyNSKDVKcKISASTRKLmA 446
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI-GGRDVT-DLPPKDRDI-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-TIAENM------RMVKADATDEEIIRALKYACAYEFVEKLPeginssvlekgRSFSEGQNQRLSIARA 519
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIafglklRKVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429188963 520 LLRNAPVLLLDEATSALD------MDTEkrvLKNiMSENLNKTCIVTTH-RLSVLSMCHKIYRISENKVQLV 584
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDaklrvqMRAE---LKR-LQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQI 212
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
46-302 |
3.01e-21 |
|
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: 94.38 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLID---AVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADI 122
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyiVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 123 YDRIINTdweSMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCV 199
Cdd:cd18544 81 FSHIQRL---PLSFFdrtPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 200 SKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSlndvfsdRLRKIQEKFKETTLEY---NKFTIYTSS----F 272
Cdd:cd18544 158 TYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFN-------REKREFEEFDEINQEYrkaNLKSIKLFAlfrpL 230
|
250 260 270
....*....|....*....|....*....|
gi 429188963 273 MSLVGMIVTYSCFGWGVYRLWTGHITYGTM 302
Cdd:cd18544 231 VELLSSLALALVLWYGGGQVLSGAVTLGVL 260
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
174-582 |
4.06e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 98.27 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 174 ILVVILYYDptMAVLALLSAPIALC---VSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRK 250
Cdd:PLN03130 430 IAMVLLYQQ--LGVASLIGSLMLVLmfpIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQT 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 251 IQEK----FKETTLeynkFTIYTSSFMSLVGMIVTYSCFGwgVYRLWTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSA 326
Cdd:PLN03130 508 VRDDelswFRKAQL----LSAFNSFILNSIPVLVTVVSFG--VFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 327 ISATTSAGRIMEVIkLPREKVL--DEEIANEIAAtceengVSIKldNIKFKYE-KSGKNVLENANIIANPGEIIALIGPS 403
Cdd:PLN03130 582 VNANVSLKRLEELL-LAEERVLlpNPPLEPGLPA------ISIK--NGYFSWDsKAERPTLSNINLDVPVGSLVAIVGST 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 404 GEGKTTTMRILLGLLNITEGDGVIynskdvkckisasTRKLMAYVPQEKTMFTGTIAENMrMVKADATDEEIIRALKYAC 483
Cdd:PLN03130 653 GEGKTSLISAMLGELPPRSDASVV-------------IRGTVAYVPQVSWIFNATVRDNI-LFGSPFDPERYERAIDVTA 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 484 AYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENL-NKTCIVTTH 562
Cdd:PLN03130 719 LQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELrGKTRVLVTN 798
|
410 420
....*....|....*....|
gi 429188963 563 RLSVLSMCHKIYRISENKVQ 582
Cdd:PLN03130 799 QLHFLSQVDRIILVHEGMIK 818
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
367-577 |
4.06e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.18 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYE-KSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVI---YNSKDVKCKIsasTR 442
Cdd:PTZ00265 383 IQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndsHNLKDINLKW---WR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTGTIAENMR-------------------------------------------MVKADATDE------ 473
Cdd:PTZ00265 460 SKIGVVSQDPLLFSNSIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNEliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 474 --------EIIRALKYACAYEFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVL 545
Cdd:PTZ00265 540 nyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270
....*....|....*....|....*....|....
gi 429188963 546 KNI--MSENLNKTCIVTTHRLSVLSMCHKIYRIS 577
Cdd:PTZ00265 620 KTInnLKGNENRITIIIAHRLSTIRYANTIFVLS 653
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
379-579 |
4.14e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.19 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 379 SGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvkcKISASTRKLMAYVPQEKTMFTGT 458
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG------------RIARPAGARVLFLPQRPYLPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 459 IAENMR--MVKADATDEEIIRALKYACAYEFVEKLPEGIN-SSVLekgrsfSEGQNQRLSIARALLRNAPVLLLDEATSA 535
Cdd:COG4178 442 LREALLypATAEAFSDAELREALEAVGLGHLAERLDEEADwDQVL------SLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 429188963 536 LDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSMCHKIYRISEN 579
Cdd:COG4178 516 LDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
367-582 |
4.36e-21 |
|
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: 92.30 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKckisastrKLMA 446
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGE-ILLDGKDIT--------NLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-------TIAEN------MRMVKADATDEEIIRALKYACAYEFVEKLPEGInssvlekgrsfSEGQNQR 513
Cdd:cd03300 70 HKRPVNTVFQNyalfphlTVFENiafglrLKKLPKAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 514 LSIARALLRNAPVLLLDEATSALDMDTEKRV---LKNImSENLNKTCIVTTHRLS-VLSMCHKIYRISENKVQ 582
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKDMqleLKRL-QKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQ 210
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
56-303 |
7.66e-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: 350020 [Multi-domain] Cd Length: 289 Bit Score: 92.93 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 56 GVVMGLGGSVAS-------KYLIDAVTG-YDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRII 127
Cdd:cd18576 1 GLILLLLSSAIGlvfpllaGQLIDAALGgGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 128 NTdweSMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLM 204
Cdd:cd18576 81 RL---PLSFFherRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 205 KKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLeynKFTIYTSSFMSLVGMIVTYSC 284
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLAL---KRARIRALFSSFIIFLLFGAI 234
|
250 260
....*....|....*....|..
gi 429188963 285 FG--W-GVYRLWTGHITYGTMT 303
Cdd:cd18576 235 VAvlWyGGRLVLAGELTAGDLV 256
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
368-533 |
9.19e-21 |
|
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: 91.58 E-value: 9.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 368 KLDNIKFKYEKSgkNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkckISASTRKL--- 444
Cdd:COG0410 5 EVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGS-IRFDGEDI---TGLPPHRIarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 -MAYVPQEKTMFTG-TIAENMRM----VKADATDEEIIRAlkyacAYEFVEKLPEGINSsvleKGRSFSEGQNQRLSIAR 518
Cdd:COG0410 79 gIGYVPEGRRIFPSlTVEENLLLgayaRRDRAEVRADLER-----VYELFPRLKERRRQ----RAGTLSGGEQQMLAIGR 149
|
170
....*....|....*
gi 429188963 519 ALLRNAPVLLLDEAT 533
Cdd:COG0410 150 ALMSRPKLLLLDEPS 164
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
367-588 |
1.02e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvKCKISASTRklMA 446
Cdd:COG0488 316 LELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG----------TVKLGETVK--IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG--TIAENMRMVKADATDEEIIRAL-----KYACAYEFVEKLpeginssvlekgrsfSEGQNQRLSIARA 519
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLgrflfSGDDAFKPVGVL---------------SGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 520 LLRNAPVLLLDEATSALDMDTekrvlKNIMSENLNK---TCIVTTH-R--LSvlSMCHKIYRISENKVQLV--NYED 588
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIET-----LEALEEALDDfpgTVLLVSHdRyfLD--RVATRILEFEDGGVREYpgGYDD 516
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
392-573 |
1.26e-20 |
|
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: 92.81 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 392 NPGEIIALIGPSGEGKTTTMRILLGLL---NITEGDgVIYNSKDVkckISASTRKL-------MAYVPQEK------TMF 455
Cdd:COG0444 29 RRGETLGLVGESGSGKSTLARAILGLLpppGITSGE-ILFDGEDL---LKLSEKELrkirgreIQMIFQDPmtslnpVMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 456 TGT-IAENMR---MVKADATDEEIIRALKY---ACAYEFVEKLP-EginssvlekgrsFSEGQNQRLSIARALLRNAPVL 527
Cdd:COG0444 105 VGDqIAEPLRihgGLSKAEARERAIELLERvglPDPERRLDRYPhE------------LSGGMRQRVMIARALALEPKLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 429188963 528 LLDEATSALDMDTEKRVLkNIMSE---NLNKTCIVTTHRLSVLS-MCHKI 573
Cdd:COG0444 173 IADEPTTALDVTIQAQIL-NLLKDlqrELGLAILFITHDLGVVAeIADRV 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
367-537 |
1.55e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.58 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksgkNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKlMA 446
Cdd:COG3840 2 LRLDDLTYRYG----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGR-ILWNGQDLT-ALPPAERP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-TIAEN--------MRMVKADAtdEEIIRALKYACAYEFVEKLPEginssvlekgrSFSEGQNQRLSIA 517
Cdd:COG3840 75 MLFQENNLFPHlTVAQNiglglrpgLKLTAEQR--AQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALA 141
|
170 180
....*....|....*....|
gi 429188963 518 RALLRNAPVLLLDEATSALD 537
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALD 161
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
320-581 |
1.67e-20 |
|
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: 96.55 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 320 IGLVPSAISATTSAGRIMEVIK--LPREKVLDEEIANEIAATCEENGVSIKldNIKFKYEKSGKNVLENANIIANPGEII 397
Cdd:TIGR00957 590 LNILPMVISSIVQASVSLKRLRifLSHEELEPDSIERRTIKPGEGNSITVH--NATFTWARDLPPTLNGITFSIPEGALV 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 398 ALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSkdvkckisastrklMAYVPQEKTMFTGTIAENMRMVKAdaTDEEIIR 477
Cdd:TIGR00957 668 AVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWIQNDSLRENILFGKA--LNEKYYQ 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 478 ALKYACAY-EFVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSEN---L 553
Cdd:TIGR00957 732 QVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvlK 811
|
250 260
....*....|....*....|....*...
gi 429188963 554 NKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:TIGR00957 812 NKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
380-562 |
1.85e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkckISASTRKLMAYV-PQE--KTMFT 456
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGT-IKLDGGDI---DDPDVAEACHYLgHRNamKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 457 gtIAENMRMVKA--DATDEEIIRALkyaCAYEF--VEKLPeginssvlekGRSFSEGQNQRLSIARALLRNAPVLLLDEA 532
Cdd:PRK13539 90 --VAENLEFWAAflGGEELDIAAAL---EAVGLapLAHLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 429188963 533 TSALDMDTEKRVLkNIMSENLNK--TCIVTTH 562
Cdd:PRK13539 155 TAALDAAAVALFA-ELIRAHLAQggIVIAATH 185
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
49-303 |
1.94e-20 |
|
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: 91.85 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 49 YVFLgILGVVMGLGGSVASKYLIDAVTGYDSGG-IGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRII 127
Cdd:cd18557 2 LLFL-LISSAAQLLLPYLIGRLIDTIIKGGDLDvLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 128 NTDwesMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLM 204
Cdd:cd18557 81 RQE---IAFFdkhKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 205 KKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSlndvfsdRLRKIQEKFKETTLEY----NKFTIYTSSFM---SLVG 277
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFS-------AEEKEIRRYSEALDRSyrlaRKKALANALFQgitSLLI 230
|
250 260
....*....|....*....|....*.
gi 429188963 278 MIVTYSCFGWGVYRLWTGHITYGTMT 303
Cdd:cd18557 231 YLSLLLVLWYGGYLVLSGQLTVGELT 256
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
366-562 |
4.77e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.75 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKlM 445
Cdd:COG1118 2 SIEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGR-IVLNGRDLFTNLPPRERR-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQE----KTMftgTIAEN----MRMVKadaTDEEIIRALkyacayefVEKLPEGINSSVLEK-------GrsfseGQ 510
Cdd:COG1118 78 GFVFQHyalfPHM---TVAENiafgLRVRP---PSKAEIRAR--------VEELLELVQLEGLADrypsqlsG-----GQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 511 NQRLSIARALLRNAPVLLLDEATSALDMDTEK---RVLKNIMSEnLNKTCIVTTH 562
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAKVRKelrRWLRRLHDE-LGGTTVFVTH 192
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
380-565 |
4.82e-20 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 88.81 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISAsTRKLMAYVpqEKTMFTG-- 457
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE-ITFDGKSYQKNIEA-LRRIGALI--EAPGFYPnl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 458 TIAENMRmvkadatdeeiIRALKYACAYEFVEKLPE--GINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSA 535
Cdd:cd03268 88 TARENLR-----------LLARLLGIRKKRIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190
....*....|....*....|....*....|.
gi 429188963 536 LDMDTEKRVLKNIMSEN-LNKTCIVTTHRLS 565
Cdd:cd03268 157 LDPDGIKELRELILSLRdQGITVLISSHLLS 187
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
54-303 |
5.42e-20 |
|
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: 90.55 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 54 ILGVVMGLGGSVAS-------KYLIDAVT--GYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYD 124
Cdd:cd18541 2 LLGILFLILVDLLQllipriiGRAIDALTagTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 125 RIINtdwESMSYY---RSGDLLNRLTSDATTVSNSiLGW-VPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVS 200
Cdd:cd18541 82 HLLT---LSPSFYqknRTGDLMARATNDLNAVRMA-LGPgILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 201 KVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKftiYTSSFMSLVGMIV 280
Cdd:cd18541 158 YRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLAR---VDALFFPLIGLLI 234
|
250 260
....*....|....*....|....*.
gi 429188963 281 TYS---CFGWGVYRLWTGHITYGTMT 303
Cdd:cd18541 235 GLSfliVLWYGGRLVIRGTITLGDLV 260
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
367-582 |
7.57e-20 |
|
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: 88.88 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkCKISAST----R 442
Cdd:COG1127 6 IEVRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE-ILVDGQDI-TGLSEKElyelR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTG-TIAEN----MRMvKADATDEEIIRA---------LKyacayEFVEKLPEGInssvlekgrsfSE 508
Cdd:COG1127 82 RRIGMLFQGGALFDSlTVFENvafpLRE-HTDLSEAEIRELvleklelvgLP-----GAADKMPSEL-----------SG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 509 GQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRL-SVLSMCHKIYRISENKVQ 582
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIreLRDELGLTSVVVTHDLdSAFAIADRVAVLADGKII 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
367-573 |
1.55e-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: 87.42 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNI--KFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKDVKCKISASTRkl 444
Cdd:cd03266 2 ITADALtkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMFTG-TIAENMRMVKAdatdeeiIRALKYACAYEFVEKLPE--GINSSVLEKGRSFSEGQNQRLSIARALL 521
Cdd:cd03266 80 LGFVSDSTGLYDRlTARENLEYFAG-------LYGLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 522 RNAPVLLLDEATSALDMdTEKRVLKNIMSE--NLNKTCIVTTHRLS-VLSMCHKI 573
Cdd:cd03266 153 HDPPVLLLDEPTTGLDV-MATRALREFIRQlrALGKCILFSTHIMQeVERLCDRV 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
367-589 |
2.99e-19 |
|
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: 86.83 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDV-KCKISASTRKLM 445
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGK-ILLDGQDItKLPMHKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTG-TIAENMRMVKADATDEEIIRALKyacAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNA 524
Cdd:cd03218 78 GYLPQEASIFRKlTVEENILAVLEIRGLSKKEREEK---LEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 525 PVLLLDEATSALDmdteKRVLKNI--MSENLNKTCI---VTTHRLS-VLSMCHKIYRISENKV-------QLVNYEDI 589
Cdd:cd03218 153 KFLLLDEPFAGVD----PIAVQDIqkIIKILKDRGIgvlITDHNVReTLSITDRAYIIYEGKVlaegtpeEIAANELV 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
367-573 |
3.66e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkckisastrklmA 446
Cdd:PRK09452 15 VELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR-IMLDGQDI------------T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEK----TMFTG-------TIAEN------MRMVKADATDEEIIRALKYACAYEFVEKLPeginssvlekgRSFSEG 509
Cdd:PRK09452 80 HVPAENrhvnTVFQSyalfphmTVFENvafglrMQKTPAAEITPRVMEALRMVQLEEFAQRKP-----------HQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 510 QNQRLSIARALLRNAPVLLLDEATSALD------MDTEKRVLKnimsENLNKTCIVTTH-RLSVLSMCHKI 573
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDyklrkqMQNELKALQ----RKLGITFVFVTHdQEEALTMSDRI 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
157-578 |
3.91e-19 |
|
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: 91.90 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 157 ILGWVPSLITKTVqFCSILVVILyydptmavLALLSApialCVSKVLMKkmrNRNKEVREISsEMMSFNEETFTNLQSIK 236
Cdd:TIGR01271 212 LMGLIWELLEVNG-FCGLGFLIL--------LALFQA----CLGQKMMP---YRDKRAGKIS-ERLAITSEIIENIQSVK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 237 AFSLNDVFS---DRLRKIQEKF--KETTLEY-NKFTIYTSSFMSLVGMIVTYSCF-GWGVYRLWTGhITYGTMTLFLQLS 309
Cdd:TIGR01271 275 AYCWEEAMEkiiKNIRQDELKLtrKIAYLRYfYSSAFFFSGFFVVFLSVVPYALIkGIILRRIFTT-ISYCIVLRMTVTR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 310 SslsssfsaliglVPSAIS----ATTSAGRIMEVIKLPREKVL------------------DE---EIANEIAATCEENG 364
Cdd:TIGR01271 354 Q------------FPGAIQtwydSLGAITKIQDFLCKEEYKTLeynltttevemvnvtaswDEgigELFEKIKQNNKARK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 365 VSIKLDNIKF-KYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvkcKISASTRk 443
Cdd:TIGR01271 422 QPNGDDGLFFsNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG------------KIKHSGR- 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 444 lMAYVPQEKTMFTGTIAENMrmVKADATDEEIIRALKYACAYEF-VEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLR 522
Cdd:TIGR01271 489 -ISFSPQTSWIMPGTIKDNI--IFGLSYDEYRYTSVIKACQLEEdIALFPEKDKTVLGEGGITLSGGQRARISLARAVYK 565
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 523 NAPVLLLDEATSALDMDTEKRVLKNIMSENL-NKTCIVTTHRLSVLSMCHKIYRISE 578
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIFESCLCKLMsNKTRILVTSKLEHLKKADKILLLHE 622
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
54-302 |
2.31e-18 |
|
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: 85.61 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 54 ILGVVMGLGGSVAS-------KYLID-AVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDR 125
Cdd:cd18543 2 ILALLAALLATLAGlaiplltRRAIDgPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 126 IINTDwesMSYY---RSGDLLNRLTSDATTVsNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKV 202
Cdd:cd18543 82 LQRLD---GAFHdrwQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 203 LMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIVTY 282
Cdd:cd18543 158 FRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLA 237
|
250 260
....*....|....*....|
gi 429188963 283 SCFGWGVYRLWTGHITYGTM 302
Cdd:cd18543 238 AVLALGGWLVANGSLTLGTL 257
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
369-562 |
4.01e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 369 LDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgvIYNSKDVKckisastrklMAYV 448
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE--VSIPKGLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 449 PQEKTMFTG-TIAENMRMV----------------KADATDEEIIRA------LKYACAYEF---VEKLPE--GINSSVL 500
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGdaelraleaeleeleaKLAEPDEDLERLaelqeeFEALGGWEAearAEEILSglGFPEEDL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 501 EKG-RSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDT----EkRVLKnimseNLNKTCIVTTH 562
Cdd:COG0488 147 DRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlE-EFLK-----NYPGTVLVVSH 207
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
367-577 |
5.33e-18 |
|
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: 81.43 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEkSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvkcKISASTRKLMA 446
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG------------RIGMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTGTIAEnmrmvkadatdeeiirALKYACayefveklpeginssvlekGRSFSEGQNQRLSIARALLRNAPV 526
Cdd:cd03223 68 FLPQRPYLPLGTLRE----------------QLIYPW-------------------DDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 429188963 527 LLLDEATSALDMDTEKRVLKniMSENLNKTCIVTTHRLSVLSMCHKIYRIS 577
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQ--LLKELGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
365-537 |
6.33e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 83.55 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 365 VSIKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG---DG-VIYNSKDvkckISAS 440
Cdd:COG1117 10 PKIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGarvEGeILLDGED----IYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 441 T------RKLMAYVPQEKTMFTGTIAEN------MRMVKADATDEEII-RALKYACAYEFV-EKLpegiNSSvlekGRSF 506
Cdd:COG1117 84 DvdvvelRRRVGMVFQKPNPFPKSIYDNvayglrLHGIKSKSELDEIVeESLRKAALWDEVkDRL----KKS----ALGL 155
|
170 180 190
....*....|....*....|....*....|.
gi 429188963 507 SEGQNQRLSIARALLRNAPVLLLDEATSALD 537
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
377-545 |
6.40e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 377 EKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMAYVPQEKTM-- 454
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT-VLVAGDDVEALSARAASRRVASVPQDTSLsf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 455 -FTGTIAENM-------RMVKADATDEEII-RALKYACAYEFVEKlpeginsSVlekgRSFSEGQNQRLSIARALLRNAP 525
Cdd:PRK09536 91 eFDVRQVVEMgrtphrsRFDTWTETDRAAVeRAMERTGVAQFADR-------PV----TSLSGGERQRVLLARALAQATP 159
|
170 180
....*....|....*....|
gi 429188963 526 VLLLDEATSALDMDTEKRVL 545
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTL 179
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
367-578 |
7.19e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRIL--LGLLN--ITEGDGVIYNSKDVKCKISAST- 441
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpeVTITGSIVYNGHNIYSPRTDTVd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 442 -RKLMAYVPQEKTMFTGTIAEN----MRM--VKADAT-DEEIIRALKYACAYEFVEklpEGINSSVLekgrSFSEGQNQR 513
Cdd:PRK14239 84 lRKEIGMVFQQPNPFPMSIYENvvygLRLkgIKDKQVlDEAVEKSLKGASIWDEVK---DRLHDSAL----GLSGGQQQR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 514 LSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSmchkiyRISE 578
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAS------RISD 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
363-562 |
7.41e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.89 E-value: 7.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 363 NGVSIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVKckis 438
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGeikiDGITISKENLK---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 439 aSTRKLMAYVPQE-KTMFTGT-----IA---ENmRMVKADATDEEIIRALKYACAYEFVEKLPEginssvlekgrSFSEG 509
Cdd:PRK13632 80 -EIRKKIGIIFQNpDNQFIGAtveddIAfglEN-KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 510 QNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKnIMSE---NLNKTCIVTTH 562
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK-IMVDlrkTRKKTLISITH 201
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
367-573 |
9.27e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 84.74 E-value: 9.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNV--LENANIIANPGEIIALIGPSGEGKTTtmriLLGLLNI----TEGDgVIYNSKDVKckiSAS 440
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINLlerpTSGS-VLVDGVDLT---ALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 441 TRKL------MAYVPQ------EKTMFtGTIA---ENMRMVKADATD--EEIIralkyacayEFVeklpeGINssvlEKG 503
Cdd:COG1135 74 ERELraarrkIGMIFQhfnllsSRTVA-ENVAlplEIAGVPKAEIRKrvAELL---------ELV-----GLS----DKA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 504 RSF----SEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEK---RVLKNIMSEnLNKTCIVTTHRLSVL-SMCHKI 573
Cdd:COG1135 135 DAYpsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRsilDLLKDINRE-LGLTIVLITHEMDVVrRICDRV 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
367-580 |
9.54e-18 |
|
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: 80.19 E-value: 9.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvkcKISASTRKLMA 446
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------IVTWGSTVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQektmftgtiaenmrmvkadatdeeiiralkyacayefveklpeginssvlekgrsFSEGQNQRLSIARALLRNAPV 526
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 527 LLLDEATSALDMDTeKRVLKNIMSeNLNKTCIVTTHRLSVLSM-CHKIYRISENK 580
Cdd:cd03221 92 LLLDEPTNHLDLES-IEALEEALK-EYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
381-586 |
1.34e-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: 81.56 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 381 KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKdvkcKISASTRKLMAYVPQEKTMFTG-TI 459
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE-VLFDGK----PLDIAARNRIGYLPEERGLYPKmKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 460 AENMR-------MVKADATDEeiiralkyacAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEA 532
Cdd:cd03269 88 IDQLVylaqlkgLKKEEARRR----------IDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 533 TSALD-MDTEkrVLKNIMSENL--NKTCIVTTHRL-SVLSMCHKIYRIseNKVQLVNY 586
Cdd:cd03269 156 FSGLDpVNVE--LLKDVIRELAraGKTVILSTHQMeLVEELCDRVLLL--NKGRAVLY 209
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
380-573 |
1.43e-17 |
|
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: 83.37 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvkcKISASTRklMAYVPQEKTMFTGTI 459
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG------------KIKHSGR--ISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 460 AENMrmVKADATDEEIIRALKYACAYEF-VEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDM 538
Cdd:cd03291 115 KENI--IFGVSYDEYRYKSVVKACQLEEdITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190
....*....|....*....|....*....|....*.
gi 429188963 539 DTEKRVLKNIMSENL-NKTCIVTTHRLSVLSMCHKI 573
Cdd:cd03291 193 FTEKEIFESCVCKLMaNKTRILVTSKMEHLKKADKI 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
380-581 |
2.00e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.86 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKDVKCKISASTRKLMAYVPQEKTMFTG-T 458
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 459 IAENMRMV---KADATDEEiiralkyacAYEFVEKLPEGINSSVLEK--GRSFSEGQNQRLSIARALLRNAPVLLLDEAT 533
Cdd:PRK10895 95 VYDNLMAVlqiRDDLSAEQ---------REDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 429188963 534 SALD----MDTeKRVLKNIMSENLNktCIVTTHRL-SVLSMCHKIYRISENKV 581
Cdd:PRK10895 166 AGVDpisvIDI-KRIIEHLRDSGLG--VLITDHNVrETLAVCERAYIVSQGHL 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
373-565 |
2.11e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.11 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 373 KFKyeksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILlGLLN------ITEGDGVIYNSKDVKCKISA--STRKL 444
Cdd:PRK11264 12 KFH----GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEqpeagtIRVGDITIDTARSLSQQKGLirQLRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMFTG-TIAENM----RMVKADATDEEIIRAlkyacaYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARA 519
Cdd:PRK11264 87 VGFVFQNFNLFPHrTVLENIiegpVIVKGEPKEEATARA------RELLAKV--GLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 429188963 520 LLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENlNKTCIVTTHRLS 565
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIrqLAQE-KRTMVIVTHEMS 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
381-563 |
2.44e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.16 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 381 KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIyNSKDVKCkisastrklmayvPQEKTmftgtIA 460
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-DVPDNQF-------------GREAS-----LI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 461 ENMRMVKADATDEEIIRALKYACAYEFVEKLPEginssvlekgrsFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDT 540
Cdd:COG2401 104 DAIGRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*
gi 429188963 541 EKRVLKNI--MSENLNKTCIVTTHR 563
Cdd:COG2401 172 AKRVARNLqkLARRAGITLVVATHH 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
383-573 |
5.99e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCK-ISASTRKLMAYVPQEKTMFTG-TIA 460
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGE-ILLDGEPVRFRsPRDAQAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 461 ENMRM----VKADATDEEIIRALkyacAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSAL 536
Cdd:COG1129 98 ENIFLgrepRRGGLIDWRAMRRR----ARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 429188963 537 DmDTEKRVLKNIMSE--NLNKTCIVTTHRLS-VLSMCHKI 573
Cdd:COG1129 172 T-EREVERLFRIIRRlkAQGVAIIYISHRLDeVFEIADRV 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
368-533 |
6.01e-17 |
|
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: 80.26 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 368 KLDNIKFKYEKSgkNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdGVIYNSKDV-KCKISASTRKLMA 446
Cdd:TIGR03410 2 EVSNLNVYYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSG-SIRLDGEDItKLPPHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-TIAENMRMVkADATDeeiiRALKyacayefveKLPEGINS--SVLE-----KGRSFSEGQNQRLSIAR 518
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTG-LAALP----RRSR---------KIPDEIYElfPVLKemlgrRGGDLSGGQQQQLAIAR 144
|
170
....*....|....*
gi 429188963 519 ALLRNAPVLLLDEAT 533
Cdd:TIGR03410 145 ALVTRPKLLLLDEPT 159
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
379-567 |
8.50e-17 |
|
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: 79.68 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 379 SGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdGVIYNSKDVKCKISASTRKL----MAYVPQEKTM 454
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG-KVHWSNKNESEPSFEATRSRnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 455 FTGTIAENMRMvkADATDEEIIRALKYACAYE-FVEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEAT 533
Cdd:cd03290 91 LNATVEENITF--GSPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 429188963 534 SALDMDTEKRVLKNIMSENLN---KTCIVTTHRLSVL 567
Cdd:cd03290 169 SALDIHLSDHLMQEGILKFLQddkRTLVLVTHKLQYL 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-573 |
9.70e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.92 E-value: 9.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKdvkcKISASTRKLM 445
Cdd:COG4152 1 MLELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE-VLWDGE----PLDPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQE----KTMftgTIAENMR-------MVKADATdeeiiRALKYacayeFVEKLpeGINSSVLEKGRSFSEGQNQRL 514
Cdd:COG4152 74 GYLPEErglyPKM---KVGEQLVylarlkgLSKAEAK-----RRADE-----WLERL--GLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 515 SIARALLRNAPVLLLDEATSALD---MDTEKRVLKNIMSEnlNKTCIVTTHRL-SVLSMCHKI 573
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDpvnVELLKDVIRELAAK--GTTVIFSSHQMeLVEELCDRI 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
366-562 |
1.03e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.05 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSgkNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLm 445
Cdd:PRK10851 2 SIEIANIKKSFGRT--QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH-IRFHGTDVS-RLHARDRKV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTG-TIAEN----MRMV-KADATDEEIIRAlKYACAYEFV--EKLPEGINSSVlekgrsfSEGQNQRLSIA 517
Cdd:PRK10851 77 GFVFQHYALFRHmTVFDNiafgLTVLpRRERPNAAAIKA-KVTQLLEMVqlAHLADRYPAQL-------SGGQKQRVALA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 429188963 518 RALLRNAPVLLLDEATSALDMDTEK---RVLKNIMSEnLNKTCIVTTH 562
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKelrRWLRQLHEE-LKFTSVFVTH 195
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
367-562 |
1.04e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 79.65 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKfkyeKS-GKN-VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDV---KCKISAsT 441
Cdd:COG1126 2 IEIENLH----KSfGDLeVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT-ITVDGEDLtdsKKDINK-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 442 RKLMAYVPQEKTMFTG-TIAENM--------RMVKADATDEeiiralkyacAYEFVEKLpeGInssvLEKGRSF----SE 508
Cdd:COG1126 76 RRKVGMVFQQFNLFPHlTVLENVtlapikvkKMSKAEAEER----------AMELLERV--GL----ADKADAYpaqlSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 509 GQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLkNIMSE--NLNKTCIVTTH 562
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVL-DVMRDlaKEGMTMVVVTH 194
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
52-303 |
1.06e-16 |
|
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: 81.00 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 52 LGILGVVMGLGGSVASKYLI-----DAVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYD-- 124
Cdd:cd18546 3 LALLLVVVDTAASLAGPLLVrygidSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAhl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 125 -RIintdweSMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVS 200
Cdd:cd18546 83 qRL------SLDFHereTSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 201 KVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNK-FTIYTsSFMSLVGMI 279
Cdd:cd18546 157 RWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRlVAIYF-PGVELLGNL 235
|
250 260
....*....|....*....|....
gi 429188963 280 VTYSCFGWGVYRLWTGHITYGTMT 303
Cdd:cd18546 236 ATAAVLLVGAWRVAAGTLTVGVLV 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
362-544 |
1.10e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 79.37 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 362 ENGVSIKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISAST 441
Cdd:PRK10247 3 ENSPLLQLQNVGYLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGT-LLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 442 RKLMAYVPQEKTMFTGTIAENMRM---VKADATDEEIIRA-LKYacayeFveKLPEGInssvLEKG-RSFSEGQNQRLSI 516
Cdd:PRK10247 80 RQQVSYCAQTPTLFGDTVYDNLIFpwqIRNQQPDPAIFLDdLER-----F--ALPDTI----LTKNiAELSGGEKQRISL 148
|
170 180
....*....|....*....|....*...
gi 429188963 517 ARALLRNAPVLLLDEATSALDMDTEKRV 544
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNV 176
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
367-565 |
2.24e-16 |
|
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: 78.53 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKfkyeKSGKN-VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLm 445
Cdd:cd03299 1 LKVENLS----KDWKEfKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGK-ILLNGKDIT-NLPPEKRDI- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTG-TIAEN----MRMVKADAtdEEIIRALKyacayEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARAL 520
Cdd:cd03299 74 SYVPQNYALFPHmTVYKNiaygLKKRKVDK--KEIERKVL-----EIAEML--GIDHLLNRKPETLSGGEQQRVAIARAL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 429188963 521 LRNAPVLLLDEATSALDMDTEKRV---LKNIMSENlNKTCIVTTHRLS 565
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTKEKLreeLKKIRKEF-GVTVLHVTHDFE 191
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
40-562 |
2.39e-16 |
|
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: 82.15 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 40 KSYKLAIIFYVFLGILGvvmGLGGsVASKYLIDAVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIR 119
Cdd:COG4615 9 RESRWLLLLALLLGLLS---GLAN-AGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 120 ADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSiLGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCV 199
Cdd:COG4615 85 LRLSRRILAAPLERLERIGAARLLAALTEDVRTISQA-FVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 200 SKVLMKKMRNRNKEVREISSEMmsfneetFTNLQSI----KAFSLN-----DVFSDRLRKIQEKFKETTLEYNKFTIYTS 270
Cdd:COG4615 164 YRLLVRRARRHLRRAREAEDRL-------FKHFRALlegfKELKLNrrrrrAFFDEDLQPTAERYRDLRIRADTIFALAN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 271 SFMS-----LVGMIVtyscFGWGVYrlwtGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRIMEviklpre 345
Cdd:COG4615 237 NWGNllffaLIGLIL----FLLPAL----GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEE------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 346 kvLDEEIANEIAATCEENGV-------SIKLDNIKFKY-EKSGKNVLE----NANIiaNPGEIIALIGPSGEGKTTTMRI 413
Cdd:COG4615 302 --LELALAAAEPAAADAAAPpapadfqTLELRGVTYRYpGEDGDEGFTlgpiDLTI--RRGELVFIVGGNGSGKSTLAKL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 414 LLGLLNITEG----DGVIYNSKDVkckisASTRKLMAYVPQEKTMFTGTIAEnmrmvkADATDEEIIRALkyacayefVE 489
Cdd:COG4615 378 LTGLYRPESGeillDGQPVTADNR-----EAYRQLFSAVFSDFHLFDRLLGL------DGEADPARAREL--------LE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 490 KLpeGINSSV-LEKGR----SFSEGQNQRLSIARALLRNAPVLLLDEAtsALDMDTE-KRV--------LKnimseNLNK 555
Cdd:COG4615 439 RL--ELDHKVsVEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEW--AADQDPEfRRVfytellpeLK-----ARGK 509
|
....*..
gi 429188963 556 TCIVTTH 562
Cdd:COG4615 510 TVIAISH 516
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
377-562 |
3.73e-16 |
|
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: 77.15 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 377 EKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKL--MAYVPQEKTM 454
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGR-VLLNGGPLDFQRDSIARGLlyLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 455 FtgTIAENMRMVKADATDEEIIRALKYACAYEFvEKLPEGinssvlekgrSFSEGQNQRLSIARALLRNAPVLLLDEATS 534
Cdd:cd03231 88 L--SVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|
gi 429188963 535 ALDMDTEKRvLKNIMSENLNK--TCIVTTH 562
Cdd:cd03231 155 ALDKAGVAR-FAEAMAGHCARggMVVLTTH 183
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
376-562 |
4.35e-16 |
|
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: 77.01 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 376 YEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKL--MAYVPQEKT 453
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGE-VRWNGTPLAEQRDEPHENIlyLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 454 MFtgTIAENMRMVKAD--ATDEEIIRALKYACAYEFvEKLPeginssvlekGRSFSEGQNQRLSIARALLRNAPVLLLDE 531
Cdd:TIGR01189 87 EL--SALENLHFWAAIhgGAQRTIEDALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 429188963 532 ATSALDMDTEkRVLKNIMSENLNKTCIV--TTH 562
Cdd:TIGR01189 154 PTTALDKAGV-ALLAGLLRAHLARGGIVllTTH 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
379-573 |
9.97e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.97 E-value: 9.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 379 SGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIY-NSKDVKCK-ISASTRKLMAYVPQEKTMFT 456
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfEGEELQASnIRDTERAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 457 G-TIAENMRMvkadatDEEIIRA--LKYACAYEFVEKLPE--GINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDE 531
Cdd:PRK13549 96 ElSVLENIFL------GNEITPGgiMDYDAMYLRAQKLLAqlKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 429188963 532 ATSALdMDTEKRVLKNIMSE--NLNKTCIVTTHRLS-VLSMCHKI 573
Cdd:PRK13549 170 PTASL-TESETAVLLDIIRDlkAHGIACIYISHKLNeVKAISDTI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
348-564 |
1.02e-15 |
|
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: 81.21 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 348 LDEEIANEIAATCEENGVSIkldnikfkYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVI 427
Cdd:TIGR01257 918 FERELPGLVPGVCVKNLVKI--------FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT-VL 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 428 YNSKDVKCKISAsTRKLMAYVPQEKTMFTG-TIAENM---RMVKADATDEEIIRalkyacayefVEKLPE--GINSSVLE 501
Cdd:TIGR01257 989 VGGKDIETNLDA-VRQSLGMCPQHNILFHHlTVAEHIlfyAQLKGRSWEEAQLE----------MEAMLEdtGLHHKRNE 1057
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 502 KGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRL 564
Cdd:TIGR01257 1058 EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
366-566 |
1.42e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSgkNVLENANIIANPGEIIALIGPSGEGKTTTMRILlGLLNI-TEGDGVIYNSK-DVKCKISAST-- 441
Cdd:PRK11124 2 SIQLNGINCFYGAH--QALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEMpRSGTLNIAGNHfDFSKTPSDKAir 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 442 --RKLMAYVPQEKTMFTG-TIAEN-----MR---MVKADATDE--EIIRALKYAcayEFVEKLPeginssvlekgRSFSE 508
Cdd:PRK11124 79 elRRNVGMVFQQYNLWPHlTVQQNlieapCRvlgLSKDQALARaeKLLERLRLK---PYADRFP-----------LHLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 509 GQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKnIMSEnLNKTCI---VTTHRLSV 566
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS-IIRE-LAETGItqvIVTHEVEV 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
392-573 |
1.87e-15 |
|
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: 79.34 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 392 NPGEIIALIGPSGEGKTTTMRILLGLLNiTEGDgVIYNSKDvkckISASTRKLMAyvPQEKTM---F------------- 455
Cdd:COG4172 310 RRGETLGLVGESGSGKSTLGLALLRLIP-SEGE-IRFDGQD----LDGLSRRALR--PLRRRMqvvFqdpfgslsprmtv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 456 TGTIAENMRM----VKADATDEEIIRALkyacayEFVEKLPEGINssvlekgR---SFSEGQNQRLSIARALLRNAPVLL 528
Cdd:COG4172 382 GQIIAEGLRVhgpgLSAAERRARVAEAL------EEVGLDPAARH-------RyphEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 429188963 529 LDEATSALDMDTEKRV---LKNIMSEnLNKTCIVTTHRLSVL-SMCHKI 573
Cdd:COG4172 449 LDEPTSALDVSVQAQIldlLRDLQRE-HGLAYLFISHDLAVVrALAHRV 496
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
367-531 |
2.06e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.84 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkckisasT----- 441
Cdd:COG1137 4 LEAENLVKSY--GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGR-IFLDGEDI-------Thlpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 442 ---RKLMAYVPQEKTMFTG-TIAENMRMV-----KADATDEEIIRALkyacayefvekLPE-GI----NSsvleKGRSFS 507
Cdd:COG1137 74 kraRLGIGYLPQEASIFRKlTVEDNILAVlelrkLSKKEREERLEEL-----------LEEfGIthlrKS----KAYSLS 138
|
170 180
....*....|....*....|....
gi 429188963 508 EGQNQRLSIARALLRNAPVLLLDE 531
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDE 162
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-301 |
2.97e-15 |
|
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: 76.75 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 40 KSYKLAIIFYVFLGILGVVMGLggsvASKYLID-AVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEI 118
Cdd:cd18540 2 KLLILLIILMLLVALLDAVFPL----LTKYAIDhFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 119 RADIYDRIINTdweSMSYY---RSGDLLNRLTSDATTVSNSI------LGWVPSLITktvqfcSILVVILYYDPTMAVLA 189
Cdd:cd18540 78 RKKAFEHLQTL---SFSYFdktPVGWIMARVTSDTQRLGEIIswglvdLVWGITYMI------GILIVMLILNWKLALIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 190 LLSAPIALCVSKVLMKKMRNRNKEVREISSEMM-SFNeETFTNLQSIKAFSLNDvfsdrlrKIQEKFKETTLEYNKFTI- 267
Cdd:cd18540 149 LAVVPVLAVVSIYFQKKILKAYRKVRKINSRITgAFN-EGITGAKTTKTLVREE-------KNLREFKELTEEMRRASVr 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 429188963 268 ---YTSSFMSLV---GMIVTYSCFGWGVYRLWTGHITYGT 301
Cdd:cd18540 221 aarLSALFLPIVlflGSIATALVLWYGGILVLAGAITIGT 260
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
376-568 |
5.24e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.67 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 376 YEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvkckiSASTRKLMAYVPQEKTMF 455
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG--------------RVWAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 456 TGTIAENMRMVkaDATDEEIIRALKYACAYEF-VEKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATS 534
Cdd:PTZ00243 734 NATVRGNILFF--DEEDAARLADAVRVSQLEAdLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190
....*....|....*....|....*....|....*
gi 429188963 535 ALDMDTEKRVLKNIMSENL-NKTCIVTTHRLSVLS 568
Cdd:PTZ00243 812 ALDAHVGERVVEECFLGALaGKTRVLATHQVHVVP 846
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
46-303 |
6.04e-15 |
|
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: 75.60 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLID-AVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYD 124
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDdALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 125 RIINtdwESMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSK 201
Cdd:cd18550 81 HLQR---MSLAFFtrtRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 202 VLMKKMRNRNKEVREISSEMMSFNEETFT--NLQSIKAFSLNDVFSDRLRKIQEKFKETTLeynKFTIYTSSFMSLVGM- 278
Cdd:cd18550 158 RVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGV---RQALAGRWFFAALGLf 234
|
250 260
....*....|....*....|....*..
gi 429188963 279 --IVTYSCFGWGVYRLWTGHITYGTMT 303
Cdd:cd18550 235 taIGPALVYWVGGLLVIGGGLTIGTLV 261
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
367-585 |
6.45e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 74.07 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVlenaNIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdGVIYNSKDVKckISASTRKLMA 446
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF----DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSG-RVLINGVDVT--AAPPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-TIAENMRM-----VKADATDEEiirALKYACAYEfveklpeGINSSVLEKGRSFSEGQNQRLSIARAL 520
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLglspgLKLTAEDRQ---AIEVALARV-------GLAGLEKRLPGELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 521 LRNAPVLLLDEATSALDmdtekRVLKNIMSENLNKTCIVTthRLSVLSMCHK---IYRISENKVQLVN 585
Cdd:cd03298 144 VRDKPVLLLDEPFAALD-----PALRAEMLDLVLDLHAET--KMTVLMVTHQpedAKRLAQRVVFLDN 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
392-566 |
8.83e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.54 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 392 NPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISAST----RKLMAYVPQE--------KTMFTgTI 459
Cdd:COG4608 42 RRGETLGLVGESGCGKSTLGRLLLRLEEPTSGE-ILFDGQDIT-GLSGRElrplRRRMQMVFQDpyaslnprMTVGD-II 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 460 AENMR---MVKADATDEEIIRALkyacayEFVeklpeGINSSVLEK-GRSFSEGQNQRLSIARALLRNAPVLLLDEATSA 535
Cdd:COG4608 119 AEPLRihgLASKAERRERVAELL------ELV-----GLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190
....*....|....*....|....*....|....
gi 429188963 536 LDMDTEKRVLkNIMSE---NLNKTCIVTTHRLSV 566
Cdd:COG4608 188 LDVSIQAQVL-NLLEDlqdELGLTYLFISHDLSV 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
384-562 |
9.04e-15 |
|
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: 73.91 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 384 LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLmAYVPQEKTMFTG-TIAEN 462
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGT-ILFGGEDAT-DVPVQERNV-GFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 463 ----MRMVK-ADATDEEIIRALkyacayefVEKLPEGINSSVLEKG--RSFSEGQNQRLSIARALLRNAPVLLLDEATSA 535
Cdd:cd03296 95 vafgLRVKPrSERPPEAEIRAK--------VHELLKLVQLDWLADRypAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190
....*....|....*....|....*....|
gi 429188963 536 LDMDTEK---RVLKNIMSEnLNKTCIVTTH 562
Cdd:cd03296 167 LDAKVRKelrRWLRRLHDE-LHVTTVFVTH 195
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
69-303 |
1.15e-14 |
|
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: 74.74 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 69 YLID-AVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLT 147
Cdd:cd18548 24 DIIDeGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 148 SDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEE 227
Cdd:cd18548 104 NDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 228 TFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLV---GMIVTYscfgW-GVYRLWTGHITYGTMT 303
Cdd:cd18548 184 NLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLImnlAIVAIL----WfGGHLINAGSLQVGDLV 259
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
384-562 |
1.28e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 73.21 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 384 LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDV---KCKISASTRKLMAYVPQE-KTMFTGTI 459
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGT-IRVNGQDVsdlRGRAIPYLRRKIGVVFQDfRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 460 AENMrmvkadatdeeiiralkyACAYEFVEKLPEGINSSVLE---------KGRSF----SEGQNQRLSIARALLRNAPV 526
Cdd:cd03292 96 YENV------------------AFALEVTGVPPREIRKRVPAalelvglshKHRALpaelSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 429188963 527 LLLDEATSALDMDTEKRVLkNIMsENLNK---TCIVTTH 562
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIM-NLL-KKINKagtTVVVATH 194
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
367-583 |
1.39e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.25 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYeKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkCKISA--STRKL 444
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGK-VLVSGIDT-GDFSKlqGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQE-KTMFTGTIAEnmrmvkadatdEEIIRALKYAC--AYEFVEKLPEGINSSVLEKGR-----SFSEGQNQRLSI 516
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVE-----------EDLAFGPENLClpPIEIRKRVDRALAEIGLEKYRhrspkTLSGGQGQCVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 517 ARALLRNAPVLLLDEATSALDMDTEKRVLKNIMS-ENLNKTCIVTTHRLSVLSMCHKIYRISENKVQL 583
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKIVL 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
367-573 |
1.45e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.46 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksgkNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIyNSKDvkCKISASTRKLMA 446
Cdd:PRK10771 2 LKLTDITWLYH----HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL-NGQD--HTTTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTG-TIAENMRM-----VKADATDEEIIRALKYACAYE-FVEKLPEGInssvlekgrsfSEGQNQRLSIARA 519
Cdd:PRK10771 75 MLFQENNLFSHlTVAQNIGLglnpgLKLNAAQREKLHAIARQMGIEdLLARLPGQL-----------SGGQRQRVALARC 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 429188963 520 LLRNAPVLLLDEATSALDmdtekRVLKNIMSENLNKTCivTTHRLSVLSMCHKI 573
Cdd:PRK10771 144 LVREQPILLLDEPFSALD-----PALRQEMLTLVSQVC--QERQLTLLMVSHSL 190
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
383-562 |
1.61e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.20 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVKCKIsasTRKLMAYVPQEKTMFTGT 458
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivDGLKVNDPKVDERL---IRQEAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 459 IA-ENM--------RMVKADATDEeiiralkyacAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLL 529
Cdd:PRK09493 93 TAlENVmfgplrvrGASKEEAEKQ----------ARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190
....*....|....*....|....*....|....*
gi 429188963 530 DEATSALDMDTEKRVLKnIMSENLNK--TCIVTTH 562
Cdd:PRK09493 161 DEPTSALDPELRHEVLK-VMQDLAEEgmTMVIVTH 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
374-582 |
1.79e-14 |
|
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: 73.14 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 374 FKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGD----GVI--YNSKDVKCKISAstrkLMAy 447
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEvrvaGLVpwKRRKKFLRRIGV----VFG- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 448 vpqEKTMFTGTI--AENMRMVKAdatdeeiIRALKYACAYEFVEKLPEGIN-SSVLEKG-RSFSEGQNQRLSIARALLRN 523
Cdd:cd03267 102 ---QKTQLWWDLpvIDSFYLLAA-------IYDLPPARFKKRLDELSELLDlEELLDTPvRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429188963 524 APVLLLDEATSALDMDTEKRVLKNIMSENLNK--TCIVTTHRL-SVLSMCHKIYRISENKVQ 582
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMkDIEALARRVLVIDKGRLL 233
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
50-298 |
2.21e-14 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 74.06 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 50 VFLGILGVVMGLGGSVASKYLIDAVTGYDSGGIG---FIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRI 126
Cdd:cd18579 3 GLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSegyLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 127 INTDWESMSYYRSGDLLNRLTSDATTVSNSILgWVPSLITKTVQFCsILVVILYYD---PTMAVLALLSapIALCVSKVL 203
Cdd:cd18579 83 LRLSSSARQETSTGEIVNLMSVDVQRIEDFFL-FLHYLWSAPLQII-VALYLLYRLlgwAALAGLGVLL--LLIPLQAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 204 MKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIVTYS 283
Cdd:cd18579 159 AKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLA 238
|
250
....*....|....*
gi 429188963 284 CFgwGVYRLWTGHIT 298
Cdd:cd18579 239 TF--ATYVLLGNPLT 251
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
373-581 |
2.21e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 373 KFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLL--NITEGDGVIYNSKDVKCKisaSTRKLMAYVpQ 450
Cdd:TIGR00955 30 CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkGVKGSGSVLLNGMPIDAK---EMRAISAYV-Q 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 451 EKTMFTGT--------IAENMRMVKADATDE------EIIRALKYA-CAyefveKLPEGINSSVlekgRSFSEGQNQRLS 515
Cdd:TIGR00955 106 QDDLFIPTltvrehlmFQAHLRMPRRVTKKEkrervdEVLQALGLRkCA-----NTRIGVPGRV----KGLSGGERKRLA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 516 IARALLRNAPVLLLDEATSALDMDTEK---RVLKNImsENLNKTCIVTTHRLS--VLSMCHKIYRISENKV 581
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYsvvQVLKGL--AQKGKTIICTIHQPSseLFELFDKIILMAEGRV 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
383-564 |
2.54e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.08 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNS-------KDVKCKIS-----ASTRKLMAYVPQ 450
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLKVAdknqlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 451 EKTMFTG-TIAEN--------MRMVKADATDeeiiRALKYacayefVEKLpeGINSSVLEKGRS-FSEGQNQRLSIARAL 520
Cdd:PRK10619 100 HFNLWSHmTVLENvmeapiqvLGLSKQEARE----RAVKY------LAKV--GIDERAQGKYPVhLSGGQQQRVSIARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 429188963 521 LRNAPVLLLDEATSALDMDTEKRVLKnIMSE--NLNKTCIVTTHRL 564
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLR-IMQQlaEEGKTMVVVTHEM 212
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
70-302 |
2.72e-14 |
|
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: 73.66 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 70 LIDAVTGYDSG---------GIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTDwesMSYYR-- 138
Cdd:cd18577 25 LFDAFTDFGSGesspdefldDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQD---IAWFDkn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 139 -SGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREI 217
Cdd:cd18577 102 gAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 218 SSEMMSFNEETFTNLQSIKAFSLNDVFSDRLrkiQEKFKETTLEYNKFTIYTSSFMSLVgMIVTYSCFG----WGVYRLW 293
Cdd:cd18577 182 YAKAGSIAEEALSSIRTVKAFGGEEKEIKRY---SKALEKARKAGIKKGLVSGLGLGLL-FFIIFAMYAlafwYGSRLVR 257
|
....*....
gi 429188963 294 TGHITYGTM 302
Cdd:cd18577 258 DGEISPGDV 266
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
391-569 |
3.09e-14 |
|
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: 75.59 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 391 ANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynSKDVKCKISastrklmaYVPQE-KTMFTGTIAENMRMVKAD 469
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG------EVDEDLKIS--------YKPQYiSPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 470 ATD-----EEIIRALKyacayefVEKLpegINSSVlekgRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRV 544
Cdd:COG1245 429 DFGssyykTEIIKPLG-------LEKL---LDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180
....*....|....*....|....*..
gi 429188963 545 LKNI--MSENLNKTCIVTTHRLSVLSM 569
Cdd:COG1245 495 AKAIrrFAENRGKTAMVVDHDIYLIDY 521
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
376-537 |
3.86e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.50 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 376 YEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKckiSASTRKL---MAYVPQEK 452
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGE-VRLNGRPLA---DWSPAELarrRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 453 TM-FTGTIAENMRM-----VKADATDEEIIRAlkyacayefveklpeginssVLEK-------GRSF---SEGQNQRLSI 516
Cdd:PRK13548 86 SLsFPFTVEEVVAMgraphGLSRAEDDALVAA--------------------ALAQvdlahlaGRDYpqlSGGEQQRVQL 145
|
170 180
....*....|....*....|....*..
gi 429188963 517 ARALLR------NAPVLLLDEATSALD 537
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALD 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-570 |
5.95e-14 |
|
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: 74.45 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 335 RIMEVIKLPrEKVLDEEIANEIaatceengvsIKLDNIKFKYEKSGKNVL---ENANIIANPGEIIALIGPSGEGKTTTM 411
Cdd:TIGR03269 259 VFMEGVSEV-EKECEVEVGEPI----------IKVRNVSKRYISVDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 412 RILLGLLNITEG--------DGVIYNSKDVKCKISAstRKLMAYVPQEKTMFT-GTIAENM-RMVKADATDE-EIIRALK 480
Cdd:TIGR03269 328 KIIAGVLEPTSGevnvrvgdEWVDMTKPGPDGRGRA--KRYIGILHQEYDLYPhRTVLDNLtEAIGLELPDElARMKAVI 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 481 YACAYEFVEKLPEginsSVLEKGRS-FSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMS--ENLNKTC 557
Cdd:TIGR03269 406 TLKMVGFDEEKAE----EILDKYPDeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKarEEMEQTF 481
|
250
....*....|....
gi 429188963 558 IVTTHRLS-VLSMC 570
Cdd:TIGR03269 482 IIVSHDMDfVLDVC 495
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
367-577 |
7.36e-14 |
|
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: 69.38 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVKckisASTR 442
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGeilvDGKEVSFASPR----DARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQektmftgtiaenmrmvkadatdeeiiralkyacayefveklpeginssvlekgrsFSEGQNQRLSIARALLR 522
Cdd:cd03216 75 AGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 523 NAPVLLLDEATSALDMDTEKRVLKNImsENL---NKTCIVTTHRLsvlsmcHKIYRIS 577
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVI--RRLraqGVAVIFISHRL------DEVFEIA 149
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
392-562 |
9.69e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 71.29 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 392 NPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKdvkckisastrklMAYVPQE-KTMFTGTIAENMRMVKADA 470
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQYiKADYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 471 TDE-----EIIRALKyacayefVEKLpegINSSVLEkgrsFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVL 545
Cdd:cd03237 90 YTHpyfktEIAKPLQ-------IEQI---LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170
....*....|....*....
gi 429188963 546 KNI--MSENLNKTCIVTTH 562
Cdd:cd03237 156 KVIrrFAENNEKTAFVVEH 174
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
70-303 |
1.02e-13 |
|
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: 72.16 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 70 LIDAVTG--YDSGGIGFIAFVMVVMAIGNLVINAVTN--RIS--TRISIKIGNEIRADIYDRIINTDwesMSYY---RSG 140
Cdd:cd18573 22 LIDVASKesGDIEIFGLSLKTFALALLGVFVVGAAANfgRVYllRIAGERIVARLRKRLFKSILRQD---AAFFdknKTG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 141 DLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSE 220
Cdd:cd18573 99 ELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALAD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 221 MMSFNEETFTNLQSIKAFSLNDVFSDRL-RKIQEKFKETTLEynkfTIYTSSFMSLVGM---IVTYSCFGWGVYRLWTGH 296
Cdd:cd18573 179 ATKVAEERLSNIRTVRAFAAERKEVERYaKKVDEVFDLAKKE----ALASGLFFGSTGFsgnLSLLSVLYYGGSLVASGE 254
|
....*..
gi 429188963 297 ITYGTMT 303
Cdd:cd18573 255 LTVGDLT 261
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
391-562 |
1.36e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 391 ANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynSKDVKCKISastrklmaYVPQE-KTMFTGTIAENMRMVKAD 469
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG------EVDPELKIS--------YKPQYiKPDYDGTVEDLLRSITDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 470 ATD----EEIIRALKyacayefVEKLPEginSSVLEkgrsFSEGQNQRLSIARALLRNAPVLLLDEATSALDMD---TEK 542
Cdd:PRK13409 428 LGSsyykSEIIKPLQ-------LERLLD---KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVA 493
|
170 180
....*....|....*....|
gi 429188963 543 RVLKNIMsENLNKTCIVTTH 562
Cdd:PRK13409 494 KAIRRIA-EEREATALVVDH 512
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
371-581 |
1.71e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.88 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 371 NIKFKYEKsGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISA--STRKLMAYV 448
Cdd:PRK13639 6 DLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGE-VLIKGEPIKYDKKSllEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 449 PQ--EKTMFTGTIAE-------NMRMVKaDATDEEIIRALKYACAYEFVEKLPEginssvlekgrSFSEGQNQRLSIARA 519
Cdd:PRK13639 84 FQnpDDQLFAPTVEEdvafgplNLGLSK-EEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 520 LLRNAPVLLLDEATSALDMDTEKRVLKniMSENLNK---TCIVTTHRLSVLSM-CHKIYRISENKV 581
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKegiTIIISTHDVDLVPVyADKVYVMSDGKI 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
367-539 |
1.94e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvkcKISASTRKLMA 446
Cdd:PRK09544 5 VSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG------------VIKRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQE---KTMFTGTIAENMRMvKADATDEEIIRALKYACAYEFVEklpeginsSVLEKgrsFSEGQNQRLSIARALLRN 523
Cdd:PRK09544 71 YVPQKlylDTTLPLTVNRFLRL-RPGTKKEDILPALKRVQAGHLID--------APMQK---LSGGETQRVLLARALLNR 138
|
170
....*....|....*.
gi 429188963 524 APVLLLDEATSALDMD 539
Cdd:PRK09544 139 PQLLVLDEPTQGVDVN 154
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
367-564 |
2.44e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.43 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVkckisASTR 442
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtitvGGMVLSEETV-----WDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQE-KTMFTGT-----IA---ENmRMVKADATDEEIIRALKYACAYEFVEKLPEginssvlekgrSFSEGQNQR 513
Cdd:PRK13635 81 RQVGMVFQNpDNQFVGAtvqddVAfglEN-IGVPREEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 429188963 514 LSIARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRL 564
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDL 201
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
376-564 |
2.48e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 70.37 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 376 YEKSGKNV-LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISAST-----RKLMAYVP 449
Cdd:cd03294 31 LKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK-VLIDGQDIA-AMSRKElrelrRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 450 QEKTMFTG-TIAEN------MRMVKADATDEEIIRALKYACAYEFVEKLPeginssvlekgRSFSEGQNQRLSIARALLR 522
Cdd:cd03294 109 QSFALLPHrTVLENvafgleVQGVPRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 429188963 523 NAPVLLLDEATSALD------MDTEkrVLKniMSENLNKTCIVTTHRL 564
Cdd:cd03294 178 DPDILLMDEAFSALDplirreMQDE--LLR--LQAELQKTIVFITHDL 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
367-581 |
3.19e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.99 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNV--LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVkckISASTRKL 444
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGR-VLVDGQDL---TALSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMFTG-------TIAENMRM-VKADATDEEIIRALkyacayefVEKLPE--GINssvlEKGRSF----SEGQ 510
Cdd:PRK11153 78 RKARRQIGMIFQHfnllssrTVFDNVALpLELAGTPKAEIKAR--------VTELLElvGLS----DKADRYpaqlSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 511 NQRLSIARALLRNAPVLLLDEATSALDMDTEKRVL---KNIMSEnLNKTCIVTTHRLSVL-SMCHKIYRISENKV 581
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILellKDINRE-LGLTIVLITHEMDVVkRICDRVAVIDAGRL 219
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-343 |
3.81e-13 |
|
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: 70.56 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 48 FYVFLGILG-VVMGLGGSVASKYLIDAVTGYDSGG-------IGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIR 119
Cdd:cd18578 9 PLLLLGLIGaIIAGAVFPVFAILFSKLISVFSLPDddelrseANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 120 ADIYDRIINTDwesMSYY-----RSGDLLNRLTSDATTVsNSILGWVPSLItktVQFCSILV---VI-LYYDPTMAVLAL 190
Cdd:cd18578 89 KLAFRAILRQD---IAWFddpenSTGALTSRLSTDASDV-RGLVGDRLGLI---LQAIVTLVaglIIaFVYGWKLALVGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 191 LSAPIALCVSKV---LMKKMRNRNKEVREISSEMMSfneETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLeynKFTI 267
Cdd:cd18578 162 ATVPLLLLAGYLrmrLLSGFEEKNKKAYEESSKIAS---EAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGL---RRAL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 268 YTSSFMSL---VGMIVTYSCFGWGVYRLWTGHITYGTMTLFLQLSSSLSSSFSALIGLVPSAISATTSAGRIMEVIKLP 343
Cdd:cd18578 236 ISGLGFGLsqsLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRK 314
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
367-564 |
4.12e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKfKYEKSG----KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTR 442
Cdd:COG1101 2 LELKNLS-KTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGS-ILIDGKDVT-KLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 -KLMAYVPQEKTMFTG---TIAENMRMVKADATDEEIIRALKYACAYEFVEKLpeginsSVLEKG---R------SFSEG 509
Cdd:COG1101 79 aKYIGRVFQDPMMGTApsmTIEENLALAYRRGKRRGLRRGLTKKRRELFRELL------ATLGLGlenRldtkvgLLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 510 QNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVL---KNIMSENlNKTCIVTTHRL 564
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLeltEKIVEEN-NLTTLMVTHNM 209
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
394-581 |
4.37e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.66 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 394 GEIIALIGPSGEGKTTTMRILLGLL--NITEGDGVIYNSKDVKC--KISASTRKLMAYvpqektmfTGTIAENMRMVKAD 469
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLSGLItgDKSAGSHIELLGRTVQRegRLARDIRKSRAN--------TGYIFQQFNLVNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 470 ATDEEI-IRALK-----YACAYEFVEKLPE---------GINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATS 534
Cdd:PRK09984 102 SVLENVlIGALGstpfwRTCFSWFTREQKQralqaltrvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 429188963 535 ALDMDTEKRVLKNIMSENLNK--TCIVTTHRLS-VLSMCHKIYRISENKV 581
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
367-580 |
5.18e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLlnITEGDGVIYNSKDVKCKISASTRKLMA 446
Cdd:PRK13537 8 IDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL--THPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTM---FTgtIAENMRM------VKADATDEEIIRALKYAcayefveKLPEGINSSVlekgRSFSEGQNQRLSIA 517
Cdd:PRK13537 84 VVPQFDNLdpdFT--VRENLLVfgryfgLSAAAARALVPPLLEFA-------KLENKADAKV----GELSGGMKRRLTLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 518 RALLRNAPVLLLDEATSALDMDTEKRV---LKNIMSEnlNKTCIVTTHRL-SVLSMCHKIYRISENK 580
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMwerLRSLLAR--GKTILLTTHFMeEAERLCDRLCVIEEGR 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
367-565 |
5.44e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.39 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKLMA 446
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE-IFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQE-KTMFTGTIA--------ENmRMVKADATDEEIIRALKYACAYEFVEKLPEginssvlekgrSFSEGQNQRLSIA 517
Cdd:PRK13648 87 IVFQNpDNQFVGSIVkydvafglEN-HAVPYDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 429188963 518 RALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLS 565
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVrkVKSEHNITIISITHDLS 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
383-574 |
6.04e-13 |
|
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: 68.62 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDV-KCKISASTRKLMAYVPQEKTMFTG-TIA 460
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS-VLFDGEDItGLPPHEIARLGIGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 461 ENMRMV----------------KADATDEEIIRALkyacayEFVEkLPEGINSSVlekgRSFSEGQNQRLSIARALLRNA 524
Cdd:cd03219 94 ENVMVAaqartgsglllararrEEREARERAEELL------ERVG-LADLADRPA----GELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 429188963 525 PVLLLDEATSALDmDTEKRVLKNIMsENLNK---TCIVTTHRLS-VLSMCHKIY 574
Cdd:cd03219 163 KLLLLDEPAAGLN-PEETEELAELI-RELRErgiTVLLVEHDMDvVMSLADRVT 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
366-564 |
6.78e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKckiSASTRKL- 444
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGT-VFLGDKPIS---MLSSRQLa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 --MAYVPQEKTMFTG-TIAEnmrMV------------KADATDEEII-RALKYACAYEFVEKLPEginssvlekgrSFSE 508
Cdd:PRK11231 76 rrLALLPQHHLTPEGiTVRE---LVaygrspwlslwgRLSAEDNARVnQAMEQTRINHLADRRLT-----------DLSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 509 GQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKnIMSEnLN---KTCIVTTHRL 564
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMR-LMRE-LNtqgKTVVTVLHDL 198
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
381-573 |
7.42e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 381 KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRK-------------LMAY 447
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGN-VSWRGEPLA-KLNRAQRKafrrdiqmvfqdsISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 448 VPQeKTMfTGTIAENMR----MVKAD--ATDEEIIRALKYACayEFVEKLPEginssvlekgrSFSEGQNQRLSIARALL 521
Cdd:PRK10419 103 NPR-KTV-REIIREPLRhllsLDKAErlARASEMLRAVDLDD--SVLDKRPP-----------QLSGGQLQRVCLARALA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 522 RNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLS-VLSMCHKI 573
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRlVERFCQRV 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
380-589 |
7.44e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.25 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDvkckisastrklMAYVPQEK----TMF 455
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQ-IMLDGVD------------LSHVPPYQrpinMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 456 tgtiaENMRMVKADATDEEIIRALKYacayefvEKLPEG-INSSVLE-------------KGRSFSEGQNQRLSIARALL 521
Cdd:PRK11607 98 -----QSYALFPHMTVEQNIAFGLKQ-------DKLPKAeIASRVNEmlglvhmqefakrKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429188963 522 RNAPVLLLDEATSALDMDTEKRVLKNIMS--ENLNKTCIVTTH-RLSVLSMCHKIYRISENK-VQLVNYEDI 589
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKfVQIGEPEEI 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
366-570 |
7.91e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYeKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKDVKckisASTRKLM 445
Cdd:PRK15056 6 GIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQ------------EKTMFTGTIAENMRMVKADATDEEIIRAlkyacAYEFVEKLpEGINSSVLEkgrsFSEGQNQR 513
Cdd:PRK15056 81 AYVPQseevdwsfpvlvEDVVMMGRYGHMGWLRRAKKRDRQIVTA-----ALARVDMV-EFRHRQIGE----LSGGQKKR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 514 LSIARALLRNAPVLLLDEATSALDMDTEKRV---LKNIMSEnlNKTCIVTTHRL-SVLSMC 570
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIislLRELRDE--GKTMLVSTHNLgSVTEFC 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
373-562 |
1.00e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 67.68 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 373 KFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLN---ITEGDgVIYNSKDVKckiSASTRKLMAYVP 449
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQ-ILFNGQPRK---PDQFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 450 QEKTMFTG-TIAE------NMRM--VKADATDEEI--IRALKyACAYEFV-EKLPEGInssvlekgrsfSEGQNQRLSIA 517
Cdd:cd03234 88 QDDILLPGlTVREtltytaILRLprKSSDAIRKKRveDVLLR-DLALTRIgGNLVKGI-----------SGGERRRVSIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 429188963 518 RALLRNAPVLLLDEATSALDMDTEK---RVLKNIMSEnlNKTCIVTTH 562
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTALnlvSTLSQLARR--NRIVILTIH 201
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
43-302 |
1.05e-12 |
|
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: 69.08 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 43 KLAIIFYVFLGILGVVMGLGGSVASKYLID-AVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRAD 121
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDnVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 122 IYDRIINTdweSMSYY--RS-GDLLNRLTSDAT---TVSNSILgwvpSLITKTVQFCSILVVILYYDPTMAVLALLSAPI 195
Cdd:cd18555 81 FFEHLLKL---PYSFFenRSsGDLLFRANSNVYirqILSNQVI----SLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 196 ALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSL 275
Cdd:cd18555 154 IVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSS 233
|
250 260
....*....|....*....|....*..
gi 429188963 276 VGMIVTYSCFGWGVYRLWTGHITYGTM 302
Cdd:cd18555 234 IQFIAPLLILWIGAYLVINGELTLGEL 260
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
366-562 |
1.06e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.92 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSG---KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVKCKis 438
Cdd:PRK13637 2 SIKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiiDGVDITDKKVKLS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 439 aSTRKLMAYVPQ--EKTMFTGTIAENMRM--VKADATDEEIIRALKYacAYEFVeklpeGINSSVLeKGRS---FSEGQN 511
Cdd:PRK13637 80 -DIRKKVGLVFQypEYQLFEETIEKDIAFgpINLGLSEEEIENRVKR--AMNIV-----GLDYEDY-KDKSpfeLSGGQK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 429188963 512 QRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTH 562
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSH 203
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
367-564 |
1.39e-12 |
|
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: 67.80 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGV-IYNSK-------DVKCKI- 437
Cdd:COG1119 4 LELRNVTVRRG--GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERrggedvwELRKRIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 438 --SAStrkLMAYVPQEKTM-------FTGTIAenmrmVKADATDEEIIRALKYACAYEfVEKLpeginssvleKGRSF-- 506
Cdd:COG1119 82 lvSPA---LQLRFPRDETVldvvlsgFFDSIG-----LYREPTDEQRERARELLELLG-LAHL----------ADRPFgt 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 507 -SEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLK--NIMSENLNKTCIVTTHRL 564
Cdd:COG1119 143 lSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAllDKLAAEGAPTLVLVTHHV 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
380-562 |
1.51e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.98 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKN-VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIyNSKDVKcKISASTRKLmAYVPQEKTMFTG- 457
Cdd:PRK11432 17 GSNtVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEDVT-HRSIQQRDI-CMVFQSYALFPHm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 458 TIAEN----MRMVKADAtdEEIIRALKYacAYEFVEKlpEGINSSVLEKgrsFSEGQNQRLSIARALLRNAPVLLLDEAT 533
Cdd:PRK11432 94 SLGENvgygLKMLGVPK--EERKQRVKE--ALELVDL--AGFEDRYVDQ---ISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190
....*....|....*....|....*....|.
gi 429188963 534 SALDMDTEKRVLKNI--MSENLNKTCIVTTH 562
Cdd:PRK11432 165 SNLDANLRRSMREKIreLQQQFNITSLYVTH 195
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
386-573 |
1.81e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 386 NANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNskdvkckisastrKLMAYVPQEK----TMFTG---- 457
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-------------KRMNDVPPAErgvgMVFQSyaly 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 458 ---TIAENMR--MVKADATDEEIIRALKYACAYEFVEKLPEginssvlEKGRSFSEGQNQRLSIARALLRNAPVLLLDEA 532
Cdd:PRK11000 88 phlSVAENMSfgLKLAGAKKEEINQRVNQVAEVLQLAHLLD-------RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 429188963 533 TSALD--MDTEKRVLKNIMSENLNKTCIVTTH-RLSVLSMCHKI 573
Cdd:PRK11000 161 LSNLDaaLRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKI 204
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
395-564 |
2.47e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 395 EIIALIGPSGEGKTTTMRILLGLLNITEG---DG-VIYNSKDVKCK--ISASTRKLMAYVPQEKTMFTGTIAENMRM--- 465
Cdd:PRK14243 37 QITAFIGPSGCGKSTILRCFNRLNDLIPGfrvEGkVTFHGKNLYAPdvDPVEVRRRIGMVFQKPNPFPKSIYDNIAYgar 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 466 ---VKADaTDEEIIRALKYACAYEFV-EKLPEginssvleKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTE 541
Cdd:PRK14243 117 ingYKGD-MDELVERSLRQAALWDEVkDKLKQ--------SGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIST 187
|
170 180
....*....|....*....|...
gi 429188963 542 KRVLKNIMSENLNKTCIVTTHRL 564
Cdd:PRK14243 188 LRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
371-560 |
2.53e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.13 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 371 NIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNIT---EGDgVIYNSKDVKcKISASTRKLMAY 447
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGD-IHYNGIPYK-EFAEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 448 VPQEKTMF-TGTIAENMRMvkadatdeeiirALKyACAYEFVeklpeginssvlekgRSFSEGQNQRLSIARALLRNAPV 526
Cdd:cd03233 88 VSEEDVHFpTLTVRETLDF------------ALR-CKGNEFV---------------RGISGGERKRVSIAEALVSRASV 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 429188963 527 LLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVT 560
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIrtMADVLKTTTFVS 175
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
367-536 |
2.55e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.83 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSgkNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDV-KCKISASTRKLM 445
Cdd:PRK11614 6 LSFDKVSAHYGKI--QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGR-IVFDGKDItDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTG-TIAENMRM----VKADATDEEIIRalkyacAYEFVEKLPEginsSVLEKGRSFSEGQNQRLSIARAL 520
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMggffAERDQFQERIKW------VYELFPRLHE----RRIQRAGTMSGGEQQMLAIGRAL 152
|
170
....*....|....*.
gi 429188963 521 LRNAPVLLLDEATSAL 536
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL 168
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
43-300 |
3.09e-12 |
|
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: 67.62 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 43 KLAIIFYVFLGILGVVMGLGGSVASKYLIDAVTGYDS-GGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRAD 121
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDlATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 122 IYDRIINTdweSMSYYRS---GDLLNRLtSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALC 198
Cdd:cd18782 81 IIDHLLRL---PLGFFDKrpvGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 199 VSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRL-----RKIQEKFKET-TLEYNKFTIYTSSF 272
Cdd:cd18782 157 LTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWqnryaRSLGEGFKLTvLGTTSGSLSQFLNK 236
|
250 260
....*....|....*....|....*...
gi 429188963 273 MSLVGMIVTyscfgwGVYRLWTGHITYG 300
Cdd:cd18782 237 LSSLLVLWV------GAYLVLRGELTLG 258
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
380-573 |
3.76e-12 |
|
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: 68.70 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIY--NSKDVKCKISASTRKLMAYVPQEKTMFTG 457
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPLKASNIRDTERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 458 -TIAENMRMvkadatDEEII---RALKYACAYEFVEKLPEGINSSVLEKGRSFSE---GQNQRLSIARALLRNAPVLLLD 530
Cdd:TIGR02633 93 lSVAENIFL------GNEITlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDyggGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 429188963 531 EATSALdMDTEKRVLKNIMSE--NLNKTCIVTTHRLS-VLSMCHKI 573
Cdd:TIGR02633 167 EPSSSL-TEKETEILLDIIRDlkAHGVACVYISHKLNeVKAVCDTI 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
367-564 |
3.96e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGK---NVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG-------------------- 423
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 424 ---DGVIYNSKDVKCKISASTRKLMAYVPQ--EKTMFTGTIAEN-------MRMVKADATDeeiiRALKYacaYEFVekl 491
Cdd:PRK13651 83 vleKLVIQKTRFKKIKKIKEIRRRVGVVFQfaEYQLFEQTIEKDiifgpvsMGVSKEEAKK----RAAKY---IELV--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 492 peGINSSVLEKGR-SFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKniMSENLN---KTCIVTTHRL 564
Cdd:PRK13651 153 --GLDESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNkqgKTIILVTHDL 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-578 |
5.29e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNI-----TEGDGVIYNSKDVKCKISAS 440
Cdd:PRK14258 7 AIKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 441 T-RKLMAYVPQEKTMFTGTIAENMRM-VKADA------TDEEIIRALKYAcayEFVEKLPEGINSSVLEkgrsFSEGQNQ 512
Cdd:PRK14258 85 RlRRQVSMVHPKPNLFPMSVYDNVAYgVKIVGwrpkleIDDIVESALKDA---DLWDEIKHKIHKSALD----LSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 513 RLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNK--TCIVTTHRLsvlsmcHKIYRISE 578
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNL------HQVSRLSD 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
383-562 |
5.41e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.09 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNI-----TEGDgVIYNSKDV-KCKISASTRKLMAYVPQEKTMFT 456
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGE-VYLDGQDIfKMDVIELRRRVQMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 457 GTIAENM-------RMVKADATDEEIIR-ALKYACAYEFVEK---LPEGinssvlekgrSFSEGQNQRLSIARALLRNAP 525
Cdd:PRK14247 97 LSIFENValglklnRLVKSKKELQERVRwALEKAQLWDEVKDrldAPAG----------KLSGGQQQRLCIARALAFQPE 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 429188963 526 VLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTH 562
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
49-295 |
6.35e-12 |
|
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: 66.35 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 49 YVFLgILGVVMGLGGSVASKYLIDA-VTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRII 127
Cdd:cd18575 2 LIAL-LIAAAATLALGQGLRLLIDQgFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 128 NTdweSMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLM 204
Cdd:cd18575 81 RL---SPSFFettRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 205 KKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKfketTLEYNKFTIYTSSFMSLVGMIVTYSC 284
Cdd:cd18575 158 RRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEA----AFAAALRRIRARALLTALVIFLVFGA 233
|
250
....*....|.
gi 429188963 285 FGWGvyrLWTG 295
Cdd:cd18575 234 IVFV---LWLG 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
383-545 |
6.68e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.53 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKI-SASTRKLMA-------YVPQektm 454
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS-ILVRHDGGWVDLaQASPREILAlrrrtigYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 455 FTGTI---------AENMRmvkADATDEEIIRALkyacAYEFVEKL--PEginssvlekgR-------SFSEGQNQRLSI 516
Cdd:COG4778 101 FLRVIprvsaldvvAEPLL---ERGVDREEARAR----ARELLARLnlPE----------RlwdlppaTFSGGEQQRVNI 163
|
170 180
....*....|....*....|....*....
gi 429188963 517 ARALLRNAPVLLLDEATSALDMDTEKRVL 545
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVV 192
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
65-302 |
6.80e-12 |
|
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: 66.32 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 65 VASKYLID-AVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTdweSMSYY---RSG 140
Cdd:cd18549 23 LIVRYIIDdLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKL---SFSFFdnnKTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 141 DLLNRLTSDATTVSNsILGWVPS-LITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISS 219
Cdd:cd18549 100 QLMSRITNDLFDISE-LAHHGPEdLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 220 EMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKftiYTSSFMSLVGM---IVTYSCFGWGVYRLWTGH 296
Cdd:cd18549 179 EINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYK---AMAYFFSGMNFftnLLNLVVLVAGGYFIIKGE 255
|
....*.
gi 429188963 297 ITYGTM 302
Cdd:cd18549 256 ITLGDL 261
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
394-566 |
8.24e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.65 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 394 GEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISAS----TRKLMAYVPQEK------TMFTG-TIAEN 462
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGE-VAWLGKDLL-GMKDDewraVRSDIQMIFQDPlaslnpRMTIGeIIAEP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 463 MRMVKADATDEEIIRALKYACAYefVEKLPEGINSSVLEkgrsFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEK 542
Cdd:PRK15079 125 LRTYHPKLSRQEVKDRVKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180
....*....|....*....|....*..
gi 429188963 543 RV---LKNIMSEnLNKTCIVTTHRLSV 566
Cdd:PRK15079 199 QVvnlLQQLQRE-MGLSLIFIAHDLAV 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
381-580 |
1.25e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 381 KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDG-VIYNSKdvkcKISASTRKLMAYVPQEKTMFTG-T 458
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGtILANNR----KPTKQILKRTGFVTQDDILYPHlT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 459 IAENM------RMVKADATDEEIIRALKYACAYEFVEKLPEGINSSVLekgRSFSEGQNQRLSIARALLRNAPVLLLDEA 532
Cdd:PLN03211 157 VRETLvfcsllRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFI---RGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 429188963 533 TSALDMDTEKRVLKNIMS-ENLNKTCIVTTHRLS--VLSMCHKIYRISENK 580
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSlAQKGKTIVTSMHQPSsrVYQMFDSVLVLSEGR 284
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
365-573 |
1.30e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.01 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 365 VSIKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGD----GVIYNSKdvkckiSAS 440
Cdd:PRK13536 40 VAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlGVPVPAR------ARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 441 TRKLMAYVPQEKTM-FTGTIAENM----RMVKADATD-EEIIRALkyacaYEFVeKLPEGINSSVLEkgrsFSEGQNQRL 514
Cdd:PRK13536 112 ARARIGVVPQFDNLdLEFTVRENLlvfgRYFGMSTREiEAVIPSL-----LEFA-RLESKADARVSD----LSGGMKRRL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429188963 515 SIARALLRNAPVLLLDEATSALDMDTEKRV---LKNIMSenLNKTCIVTTH----------RLSVLSMCHKI 573
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIwerLRSLLA--RGKTILLTTHfmeeaerlcdRLCVLEAGRKI 251
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
87-280 |
1.60e-11 |
|
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: 65.26 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 87 FVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTDwesMSYY---RSGDLLNRLTSDATTVSNSILGWVPS 163
Cdd:cd18572 40 LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQD---IAFFdatKTGELTSRLTSDCQKVSDPLSTNLNV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 164 LITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDV 243
Cdd:cd18572 117 FLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEER 196
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 429188963 244 ----FSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIV 280
Cdd:cd18572 197 earrYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLV 237
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
385-562 |
1.83e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 385 ENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLMAYV---PQEKTMFTGtiAE 461
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE-VLWQGEPIR-RQRDEYHQDLLYLghqPGIKTELTA--LE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 462 NMRMVKA---DATDEEIIRALKyACAYEFVEKLPeginssvlekGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDM 538
Cdd:PRK13538 94 NLRFYQRlhgPGDDEALWEALA-QVGLAGFEDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170 180
....*....|....*....|....*.
gi 429188963 539 DTEKRvLKNIMSENLNK--TCIVTTH 562
Cdd:PRK13538 163 QGVAR-LEALLAQHAEQggMVILTTH 187
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
383-574 |
2.81e-11 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 63.90 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDV-KCKISASTRKLMAYVPQEKTMFTG-TIA 460
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR-ILFDGRDItGLPPHRIARLGIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 461 ENMRM----------------VKADATDEEIIRALkyacAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNA 524
Cdd:COG0411 98 ENVLVaaharlgrgllaallrLPRARREEREARER----AEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 429188963 525 PVLLLDEATSALDmDTEKRVLKNI---MSENLNKTCIVTTHRLS-VLSMCHKIY 574
Cdd:COG0411 172 KLLLLDEPAAGLN-PEETEELAELirrLRDERGITILLIEHDMDlVMGLADRIV 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
381-573 |
3.21e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 381 KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNiTEGDgVIYNSKDVKckiSASTRKLMAYVPQEKTMFTG--- 457
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGE-IWFDGQPLH---NLNRRQLLPVRHRIQVVFQDpns 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 458 ----------TIAENMRM----VKADATDEEIIRALkyacayEFVEKLPEGINSSVLEkgrsFSEGQNQRLSIARALLRN 523
Cdd:PRK15134 374 slnprlnvlqIIEEGLRVhqptLSAAQREQQVIAVM------EEVGLDPETRHRYPAE----FSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 524 APVLLLDEATSALDMDTEKRVLknimseNLNKTcIVTTHRLS----------VLSMCHKI 573
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQIL------ALLKS-LQQKHQLAylfishdlhvVRALCHQV 496
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
388-573 |
5.87e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 388 NIIAN--------PGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRKL---MayVPQEKTMF- 455
Cdd:COG3845 17 GVVANddvsltvrPGEIHALLGENGAGKSTLMKILYGLYQPDSGE-ILIDGKPVRIRSPRDAIALgigM--VHQHFMLVp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 456 TGTIAEN----MRMVKADATD----EEIIRALkyACAYEF-------VEKLpeginsSVlekgrsfseGQNQRLSIARAL 520
Cdd:COG3845 94 NLTVAENivlgLEPTKGGRLDrkaaRARIREL--SERYGLdvdpdakVEDL------SV---------GEQQRVEILKAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 521 LRNAPVLLLDEATSAL-DMDTEK--RVLKNIMSEnlNKTCIVTTHRLS-VLSMCHKI 573
Cdd:COG3845 157 YRGARILILDEPTAVLtPQEADElfEILRRLAAE--GKSIIFITHKLReVMAIADRV 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
367-568 |
6.48e-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: 64.82 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDG-VIYN-------------SKD 432
Cdd:TIGR03269 1 IEVKNLTKKFD--GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGrIIYHvalcekcgyverpSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 433 -VKCKISASTRKLMA---YVPQEK----------TMFTGTIA--ENMRMVkadatdEEIIRALKYA--CAYEFVEKLPEG 494
Cdd:TIGR03269 79 gEPCPVCGGTLEPEEvdfWNLSDKlrrrirkriaIMLQRTFAlyGDDTVL------DNVLEALEEIgyEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 495 INSSVLEK-----GRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMS--ENLNKTCIVTTHRLSVL 567
Cdd:TIGR03269 153 IEMVQLSHrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVI 232
|
.
gi 429188963 568 S 568
Cdd:TIGR03269 233 E 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
393-569 |
6.87e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 393 PGEIIALIGPSGEGKTTTMRILLGL----LNITEG----DGVI----------YNSKDVKCKISAStRKLMaYVPQEKTM 454
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGElipnLGDYEEepswDEVLkrfrgtelqnYFKKLYNGEIKVV-HKPQ-YVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 455 FTGTIAENMRmvkadATDEEIIRAlkyacayEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATS 534
Cdd:PRK13409 176 FKGKVRELLK-----KVDERGKLD-------EVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|....*
gi 429188963 535 ALDMDTEKRVLKNIMSENLNKTCIVTTHRLSVLSM 569
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDY 276
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
367-581 |
7.15e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.13 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEkSGK---NVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgvIYN--SKDVKC----KI 437
Cdd:PRK10535 5 LELKDIRRSYP-SGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG---TYRvaGQDVATldadAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 438 SASTRKLMAYVPQEKTMFTG-TIAENmrmVKADATDEEIIRALKYACAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSI 516
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHlTAAQN---VEVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 517 ARALLRNAPVLLLDEATSALDMDTEKRVLkNIMSENLNK--TCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVM-AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
366-573 |
7.66e-11 |
|
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: 62.16 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSGKN-VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynSKDVKCKISASTRKL 444
Cdd:cd03220 19 SLKKLGILGRKGEVGEFwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG------TVTVRGRVSSLLGLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPqektMFTGTiaENMRMVKA--DATDEEIirALKYACAYEFVEkLPEGINSSVlekgRSFSEGQNQRLSIARALLR 522
Cdd:cd03220 93 GGFNP----ELTGR--ENIYLNGRllGLSRKEI--DEKIDEIIEFSE-LGDFIDLPV----KTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 523 NAPVLLLDEATSALD---MDTEKRVLKNIMSEnlNKTCIVTTHRL-SVLSMCHKI 573
Cdd:cd03220 160 EPDILLIDEVLAVGDaafQEKCQRRLRELLKQ--GKTVILVSHDPsSIKRLCDRA 212
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
84-301 |
1.04e-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: 62.97 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 84 FIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTDwesMSYY---RSGDLLNRLTSDATTVSNSILGW 160
Cdd:cd18565 55 LLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLD---MAFFedrQTGDLMSVLNNDVNQLERFLDDG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 161 VPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSL 240
Cdd:cd18565 132 ANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTA 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 241 NDVFSDRLRKIQEKFKETTLEynkfTIYTSS-------FMSLVGMIVTYSCFGWGV---YRLWTGHITYGT 301
Cdd:cd18565 212 EDFERERVADASEEYRDANWR----AIRLRAaffpvirLVAGAGFVATFVVGGYWVldgPPLFTGTLTVGT 278
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
367-582 |
1.05e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.83 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKN-VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKDVKCKISASTRKLM 445
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTGTIAEN-------MRMVKADATDEEIIRALKYACAYEFVEKLPEginssvlekgrSFSEGQNQRLSIAR 518
Cdd:PRK13650 85 MVFQNPDNQFVGATVEDdvafgleNKGIPHEEMKERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 519 ALLRNAPVLLLDEATSALDMDTEKRVLKNIMS--ENLNKTCIVTTHRLSVLSMCHKIYRISENKVQ 582
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGirDDYQMTVISITHDLDEVALSDRVLVMKNGQVE 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
332-581 |
1.39e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.95 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 332 SAGRIMEVIKLprEKVLDEEIANEIAAtceengvsikLDNIKFKYEKSgknvlenaniianpgEIIALIGPSGEGKTTTM 411
Cdd:PRK13631 17 SDDIILRVKNL--YCVFDEKQENELVA----------LNNISYTFEKN---------------KIYFIIGNSGSGKSTLV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 412 RILLGLLNITEGD---GVIYNSKDV------------KCKISASTRKLMAYVPQ--EKTMFTGTIAENMrMVKADATDEE 474
Cdd:PRK13631 70 THFNGLIKSKYGTiqvGDIYIGDKKnnhelitnpyskKIKNFKELRRRVSMVFQfpEYQLFKDTIEKDI-MFGPVALGVK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 475 IIRALKYACAYefVEKLpeGINSSVLEKGR-SFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIM-SEN 552
Cdd:PRK13631 149 KSEAKKLAKFY--LNKM--GLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILdAKA 224
|
250 260 270
....*....|....*....|....*....|
gi 429188963 553 LNKTCIVTTHRL-SVLSMCHKIYRISENKV 581
Cdd:PRK13631 225 NNKTVFVITHTMeHVLEVADEVIVMDKGKI 254
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
367-583 |
1.42e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.56 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYeKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSK--DVKCKISASTRKL 444
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGR-ILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQ--EKTMFTGTIAENMRM--VKADATDEEIIRALKYACAYEFVEKLPEginssvlEKGRSFSEGQNQRLSIARAL 520
Cdd:PRK13636 84 VGMVFQdpDNQLFSASVYQDVSFgaVNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 521 LRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRLSVLSM-CHKIYRISENKVQL 583
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLveMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGRVIL 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
367-581 |
1.57e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.13 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYeKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKDVKCKISaSTRKLMA 446
Cdd:PRK13652 4 IETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR-EVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQ--EKTMFTGTIAENMRMVKAD-ATDEEIIR-----ALKYACAYEFVEKLPEginssvlekgrSFSEGQNQRLSIAR 518
Cdd:PRK13652 82 LVFQnpDDQIFSPTVEQDIAFGPINlGLDEETVAhrvssALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429188963 519 ALLRNAPVLLLDEATSALDMDTEKRVLK--NIMSENLNKTCIVTTHRLS-VLSMCHKIYRISENKV 581
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDflNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRI 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
384-538 |
2.00e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 384 LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVK----CKISASTRKLM-----AYVPQEKTM 454
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGE-IIFNGQRIDtlspGKLQALRRDIQfifqdPYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 455 FTG-TIAENMR---MVKADATDEEIIRALkyacayEFVEKLPEginsSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLD 530
Cdd:PRK10261 419 TVGdSIMEPLRvhgLLPGKAAAARVAWLL------ERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
....*...
gi 429188963 531 EATSALDM 538
Cdd:PRK10261 489 EAVSALDV 496
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
370-572 |
2.19e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.98 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 370 DNIKFKYEKsGK---NVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTR---- 442
Cdd:PRK11629 9 DNLCKRYQE-GSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD-VIFNGQPMS-KLSSAAKaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 -KLMAYVPQEKTMFTG-TIAENMRM---VKADATDEEIIRALKYACAYefveklpeGINSSVLEKGRSFSEGQNQRLSIA 517
Cdd:PRK11629 86 nQKLGFIYQFHHLLPDfTALENVAMpllIGKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 518 RALLRNAPVLLLDEATSALDMDTEKRVLkNIMSEnLNK----TCIVTTHRLSVLSMCHK 572
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIF-QLLGE-LNRlqgtAFLVVTHDLQLAKRMSR 214
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
44-300 |
2.92e-10 |
|
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: 61.42 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 44 LAIIFY--VFLGILGVVMGLggsvASKYLIDAVTGYDSGG-IGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRA 120
Cdd:cd18568 4 LAEILLasLLLQLLGLALPL----FTQIILDRVLVHKNISlLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 121 DIYDRIINTdweSMSYYRS---GDLLNRLTSDAT---TVSNSILGWVPSLITKTVQFCsilvVILYYDPTMAVLALLSAP 194
Cdd:cd18568 80 DFYKHLLSL---PLSFFASrkvGDIITRFQENQKirrFLTRSALTTILDLLMVFIYLG----LMFYYNLQLTLIVLAFIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 195 IALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMS 274
Cdd:cd18568 153 LYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISS 232
|
250 260
....*....|....*....|....*.
gi 429188963 275 LVGMIVTYSCFGWGVYRLWTGHITYG 300
Cdd:cd18568 233 LINHLGTIAVLWYGAYLVISGQLTIG 258
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
380-576 |
3.13e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.27 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDV---KCKISASTRKLMAYVPQEKTMFT 456
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGK-IWFSGHDItrlKNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 457 G-TIAEN--MRMVKADATDEEIIRALKYAcayefVEKLpeginsSVLEKGRSF----SEGQNQRLSIARALLRNAPVLLL 529
Cdd:PRK10908 93 DrTVYDNvaIPLIIAGASGDDIRRRVSAA-----LDKV------GLLDKAKNFpiqlSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 429188963 530 DEATSALDMDTEKRVLKniMSENLNK---TCIVTTHRLSVLSmcHKIYRI 576
Cdd:PRK10908 162 DEPTGNLDDALSEGILR--LFEEFNRvgvTVLMATHDIGLIS--RRSYRM 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
392-562 |
3.80e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 392 NPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvKCKIsastrklMAYVPQEKTM-FTGTIA---------- 460
Cdd:COG4586 46 EPGEIVGFIGPNGAGKSTTIKMLTGILVPTSG----------EVRV-------LGYVPFKRRKeFARRIGvvfgqrsqlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 461 ------ENMRMVKA--DATDEEIIRALKyacayEFVE--KLPEGINSSVlekgRSFSEGQNQRLSIARALLRNAPVLLLD 530
Cdd:COG4586 109 wdlpaiDSFRLLKAiyRIPDAEYKKRLD-----ELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190
....*....|....*....|....*....|....*
gi 429188963 531 EATSALDMDTEKRV---LKNIMSENlNKTCIVTTH 562
Cdd:COG4586 180 EPTIGLDVVSKEAIrefLKEYNRER-GTTILLTSH 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
367-573 |
4.30e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.88 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEK-SGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKDVKCKISASTRKLM 445
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTGTIAEN---MRMVKADATDEEIIR----ALKYACAYEFVEKLPEginssvlekgrSFSEGQNQRLSIAR 518
Cdd:PRK13642 85 MVFQNPDNQFVGATVEDdvaFGMENQGIPREEMIKrvdeALLAVNMLDFKTREPA-----------RLSGGQKQRVAVAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 519 ALLRNAPVLLLDEATSALDMDTEKRVLKNIMSenlnktcIVTTHRLSVLSMCHKI 573
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHE-------IKEKYQLTVLSITHDL 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
393-569 |
4.37e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 393 PGEIIALIGPSGEGKTTTMRILLGLL--------NITEGDGVI----------YNSKDVKCKISAStRKLMaYVPQEKTM 454
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgdydEEPSWDEVLkrfrgtelqdYFKKLANGEIKVA-HKPQ-YVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 455 FTGTIAENMRmvkadATDEEIIralkyacAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATS 534
Cdd:COG1245 176 FKGTVRELLE-----KVDERGK-------LDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|....*.
gi 429188963 535 ALDMDTEKRVLKNIMSE-NLNKTCIVTTHRLSVLSM 569
Cdd:COG1245 242 YLDIYQRLNVARLIRELaEEGKYVLVVEHDLAILDY 277
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
367-564 |
4.40e-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: 63.11 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIyNSKDVKCKISaSTRKLMA 446
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV-AGKSILTNIS-DVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKT---MFTGT----IAENMRMVKAdatdEEIIRALKYAcayefVEKLPEGINSSVLekGRSFSEGQNQRLSIARA 519
Cdd:TIGR01257 2016 YCPQFDAiddLLTGRehlyLYARLRGVPA----EEIEKVANWS-----IQSLGLSLYADRL--AGTYSGGNKRKLSTAIA 2084
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 429188963 520 LLRNAPVLLLDEATSALDMDTEKRVLKNIMS-ENLNKTCIVTTHRL 564
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSM 2130
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
392-562 |
4.40e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 392 NPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIynskDVKCKISASTRKLMAYVpqektmftgtiaENMRMVKADAT 471
Cdd:PRK13543 35 DAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI----DGKTATRGDRSRFMAYL------------GHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 472 DEEiirALKYACAYE--FVEKLPEGINSSVLEKG------RSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTeKR 543
Cdd:PRK13543 99 TLE---NLHFLCGLHgrRAKQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG-IT 174
|
170 180
....*....|....*....|.
gi 429188963 544 VLKNIMSENLNK--TCIVTTH 562
Cdd:PRK13543 175 LVNRMISAHLRGggAALVTTH 195
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
384-562 |
5.31e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 59.79 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 384 LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdGVIYNSKdvkcKISASTRKLMAyVPQEKTMFTG-TIAEN 462
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSG-GVILEGK----QITEPGPDRMV-VFQNYSLLPWlTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 463 MRM----VKADATDEEiiralKYACAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDM 538
Cdd:TIGR01184 75 IALavdrVLPDLSKSE-----RRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180
....*....|....*....|....*..
gi 429188963 539 DTEKRV---LKNIMSENlNKTCIVTTH 562
Cdd:TIGR01184 148 LTRGNLqeeLMQIWEEH-RVTVLMVTH 173
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
379-565 |
9.27e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 379 SGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLN----------ITEGDGVIYNSKDVkckisASTRKLMAYV 448
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrysgdVLLGGRSIFNYRDV-----LEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 449 PQEKTMFTGTIAEN-MRMVKADA-TDEEIIRALKYACAYEFveKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPV 526
Cdd:PRK14271 107 FQRPNPFPMSIMDNvLAGVRAHKlVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 429188963 527 LLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTHRLS 565
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLA 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
386-538 |
1.35e-09 |
|
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: 60.11 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 386 NANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVKCKISASTRKLmAYVPQEKTMF-TGTIA 460
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGrirlGGEVLQDSARGIFLPPHRRRI-GYVFQEARLFpHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 461 ENM-----RMVKADATD--EEIIRALkyacayefveklpeGInSSVLEKG-RSFSEGQNQRLSIARALLRNAPVLLLDEA 532
Cdd:COG4148 96 GNLlygrkRAPRAERRIsfDEVVELL--------------GI-GHLLDRRpATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
....*.
gi 429188963 533 TSALDM 538
Cdd:COG4148 161 LAALDL 166
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
367-581 |
1.54e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGK---NVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLnITEGDGVIYNSKDV-----KCKIS 438
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-ISETGQTIVGDYAIpanlkKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 439 ASTRKLMAYVPQ--EKTMFTGTIAENMRM--VKADATDEEIIRalKYACAYEFVEKLPEGINSSVLEkgrsFSEGQNQRL 514
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQETIEKDIAFgpVNLGENKQEAYK--KVPELLKLVQLPEDYVKRSPFE----LSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 515 SIARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTHRL-SVLSMCHKIYRISENKV 581
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKV 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
393-569 |
1.61e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 393 PGEIIALIGPSGEGKTTTMRILLGLL--------NITEGDGVI----------YNSKDVKCKISASTRKlmAYVPQEKTM 454
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLkpnlgkfdDPPDWDEILdefrgselqnYFTKLLEGDVKVIVKP--QYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 455 FTGTIAENMRmvKADATD--EEIIRALkyacayefveklpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEA 532
Cdd:cd03236 103 VKGKVGELLK--KKDERGklDELVDQL--------------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 429188963 533 TSALDMD---TEKRVLKNIMSEnlNKTCIVTTHRLSVLSM 569
Cdd:cd03236 167 SSYLDIKqrlNAARLIRELAED--DNYVLVVEHDLAVLDY 204
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
393-567 |
1.80e-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: 56.61 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 393 PGEIIALIGPSGEGKTTTMRILLGLLNITEGdGVIYnskdvkckISASTRKLMAYVpqektmftgtiaenmrmvkadatd 472
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-GVIY--------IDGEDILEEVLD------------------------ 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 473 eeiiralkyacayefveklpEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSEN 552
Cdd:smart00382 48 --------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180
....*....|....*....|..
gi 429188963 553 L-------NKTCIVTTHRLSVL 567
Cdd:smart00382 108 LlllksekNLTVILTTNDEKDL 129
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
394-571 |
2.29e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 394 GEIIALIGPSGEGKTTTMRILLGLL----NITEG----DGVIYNSKDVKCKISAStrkLM-----AYVPQeKTMFTGTIa 460
Cdd:PRK10418 29 GRVLALVGGSGSGKSLTCAAALGILpagvRQTAGrvllDGKPVAPCALRGRKIAT---IMqnprsAFNPL-HTMHTHAR- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 461 ENMRMVKADATDEEIIRALKyACAYEFVEKLPEginSSVLEkgrsFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDT 540
Cdd:PRK10418 104 ETCLALGKPADDATLTAALE-AVGLENAARVLK---LYPFE----MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190
....*....|....*....|....*....|.
gi 429188963 541 EKRVLKNIMSenlnktcIVTTHRLSVLSMCH 571
Cdd:PRK10418 176 QARILDLLES-------IVQKRALGMLLVTH 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
369-588 |
2.73e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 369 LDNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskDVKCKISAStrklMAYV 448
Cdd:PRK15064 322 VENLTKGFD--NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG--------TVKWSENAN----IGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 449 PQEKT-MFTG--TIAENMRMVKADATDEEIIRAlkyacayeFVEKL---PEGINSSVlekgRSFSEGQNQRLSIARALLR 522
Cdd:PRK15064 388 AQDHAyDFENdlTLFDWMSQWRQEGDDEQAVRG--------TLGRLlfsQDDIKKSV----KVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 523 NAPVLLLDEATSALDMDTEKRVlkNIMSENLNKTCIVTTH-RLSVLSMCHKIYRISENKVQ--LVNYED 588
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESL--NMALEKYEGTLIFVSHdREFVSSLATRIIEITPDGVVdfSGTYEE 522
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-562 |
2.74e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 381 KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DG-VIYNSKDVKCKISASTRKLMAYVPQEKTMF 455
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkikvDGkVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 456 TG-TIAENMR--MVKADATDEEIIRALKYACAYEFveKLPEGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEA 532
Cdd:PRK14246 103 PHlSIYDNIAypLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190
....*....|....*....|....*....|
gi 429188963 533 TSALDMDTEKRVLKNIMSENLNKTCIVTTH 562
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
370-566 |
3.07e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 370 DNIKFKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskdvkcKISASTRKLMAYVP 449
Cdd:PRK10253 11 EQLTLGYGK--YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHG------------HVWLDGEHIQHYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 450 QEKTMFTGTIAENMrMVKADATDEEIIRALKYACAYEFVEKLPE------------GINSSVLEKGRSFSEGQNQRLSIA 517
Cdd:PRK10253 77 KEVARRIGLLAQNA-TTPGDITVQELVARGRYPHQPLFTRWRKEdeeavtkamqatGITHLADQSVDTLSGGQRQRAWIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 518 RALLRNAPVLLLDEATSALDMDTEKRVLKnIMSE--------------NLNKTCIVTTHRLSV 566
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLE-LLSElnrekgytlaavlhDLNQACRYASHLIAL 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
367-536 |
3.42e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLlnITEGDGVIYNSKDVKCKIS-ASTRKLM 445
Cdd:PRK15439 12 LCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI--VPPDSGTLEIGGNPCARLTpAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AY-VPQEKTMFTG-TIAENMrmvkadatdeeIIRALKYACAYEFVEKLPEGINSSV-LEKGRSFSEGQNQRL-SIARALL 521
Cdd:PRK15439 88 IYlVPQEPLLFPNlSVKENI-----------LFGLPKRQASMQKMKQLLAALGCQLdLDSSAGSLEVADRQIvEILRGLM 156
|
170
....*....|....*
gi 429188963 522 RNAPVLLLDEATSAL 536
Cdd:PRK15439 157 RDSRILILDEPTASL 171
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
393-566 |
3.52e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 393 PGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSK-----DVKCKISASTRKLM----AYVPQEKtmftgtiAENM 463
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPDAGE-VHYRMRdgqlrDLYALSEAERRRLLrtewGFVHQHP-------RDGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 464 RM-VKADATDEEIIRAL---KY----ACAYEFVEKLPegINSSVL-EKGRSFSEGQNQRLSIARALLRNAPVLLLDEATS 534
Cdd:PRK11701 103 RMqVSAGGNIGERLMAVgarHYgdirATAGDWLERVE--IDAARIdDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTG 180
|
170 180 190
....*....|....*....|....*....|....*
gi 429188963 535 ALDMDTEKRVL---KNIMSEnLNKTCIVTTHRLSV 566
Cdd:PRK11701 181 GLDVSVQARLLdllRGLVRE-LGLAVVIVTHDLAV 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
369-577 |
5.78e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 369 LDNIKFKyeksgknvlenaniiANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVKCKISAStrkl 444
Cdd:PRK11288 20 LDDISFD---------------CRAGQVHALMGENGAGKSTLLKILSGNYQPDAGsiliDGQEMRFASTTAALAAG---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMFTG-TIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEGINSSvlEKGRSFSEGQNQRLSIARALLRN 523
Cdd:PRK11288 81 VAIIYQELHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPD--TPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 524 APVLLLDEATSALDM-DTEK--RVLKNIMSEnlNKTCIVTTHRLSvlsmchKIYRIS 577
Cdd:PRK11288 159 ARVIAFDEPTSSLSArEIEQlfRVIRELRAE--GRVILYVSHRME------EIFALC 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
367-562 |
7.23e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.05 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYeKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKdvkckISAST----R 442
Cdd:PRK13647 5 IEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-----VNAENekwvR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQE--KTMFTGTIAE-------NMRMvKADATDEEIIRALKYACAYEFVEKLPeginssvlekgRSFSEGQNQR 513
Cdd:PRK13647 79 SKVGLVFQDpdDQVFSSTVWDdvafgpvNMGL-DKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 429188963 514 LSIARALLRNAPVLLLDEATSALDmDTEKRVLKNIMSE--NLNKTCIVTTH 562
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLD-PRGQETLMEILDRlhNQGKTVIVATH 196
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
89-302 |
8.73e-09 |
|
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: 57.21 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 89 MVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTdweSMSYY---RSGDLLNRLTsDATTVSNSILGwvPSLI 165
Cdd:cd18566 48 VVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSL---PLSFFerePSGAHLERLN-SLEQIREFLTG--QALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 166 TKT-VQFCSI-LVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDV 243
Cdd:cd18566 122 ALLdLPFVLIfLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQ 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 244 FSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIVTYSCFGWGVYRLWTGHITYGTM 302
Cdd:cd18566 202 MLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGAL 260
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
367-565 |
1.03e-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: 58.22 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFkYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviYNSKDVKCKIsastrklmA 446
Cdd:TIGR00954 452 IKFENIPL-VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG----RLTKPAKGKL--------F 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 447 YVPQEKTMFTGTIAENM-------RMVKADATDEEIIRALKYACAYEFVEKlpEGINSSVLEKGRSFSEGQNQRLSIARA 519
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIiypdsseDMKRRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 429188963 520 LLRNAPVLLLDEATSALDMDTEKRVLKNimSENLNKTCIVTTHRLS 565
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYMYRL--CREFGITLFSVSHRKS 640
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
377-573 |
1.07e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 57.35 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 377 EKSGKNV-LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGV----IYNS--KDVKCKISASTRKLM 445
Cdd:PRK10070 36 EKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGqvliDGVdiakISDAelREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 446 AYVPQEKTMFTGTIAENMRMVKADATDEEIIRALKYACAYEFVEKLPEginssvlekgrSFSEGQNQRLSIARALLRNAP 525
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 429188963 526 VLLLDEATSALDmdtekRVLKNIMSENLNKtcIVTTHRLSVLSMCHKI 573
Cdd:PRK10070 185 ILLMDEAFSALD-----PLIRTEMQDELVK--LQAKHQRTIVFISHDL 225
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
46-303 |
1.09e-08 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 56.66 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLIDAVTGYDSGG-------IGFIAFVMV-VMAIGNLVINAVTNRISTRISIKIGNE 117
Cdd:cd18554 1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTldekvykLFTIIGIMFfIFLILRPPVEYYRQYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 118 IRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIAL 197
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 198 CVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVG 277
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTIT 240
|
250 260
....*....|....*....|....*.
gi 429188963 278 MIVTYSCFGWGVYRLWTGHITYGTMT 303
Cdd:cd18554 241 DLAPLLVIGFAAYLVIEGNLTVGTLV 266
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
367-562 |
1.56e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.28 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKS---GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGD---GVIYNSKDVKCKISAS 440
Cdd:PRK13643 2 IKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 441 TRKLMAYVPQ--EKTMFTGTI-------AENMRMVKADATDEEIIRALKYACAYEFVEKLPeginssvlekgRSFSEGQN 511
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVlkdvafgPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 429188963 512 QRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMS-ENLNKTCIVTTH 562
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTH 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
375-540 |
2.08e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 375 KYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLN---ITEGDgVIYNSKdvkcKISASTRKLMAYVPQ- 450
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGD-RLVNGR----PLDSSFQRSIGYVQQq 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 451 ----------EKTMFTG--------TIAENMRMVkadatdEEIIRALKyacayefVEKLPEGInssVLEKGRSFSEGQNQ 512
Cdd:TIGR00956 845 dlhlptstvrESLRFSAylrqpksvSKSEKMEYV------EEVIKLLE-------MESYADAV---VGVPGEGLNVEQRK 908
|
170 180
....*....|....*....|....*....
gi 429188963 513 RLSIARALLRNAPVLL-LDEATSALDMDT 540
Cdd:TIGR00956 909 RLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
382-582 |
2.54e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 382 NVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNS------KDVKCKISAstrKLMAYVPQEKTMF 455
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdEEARAKLRA---KHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 456 -TGTIAENMR---MVKADATDEEIIRALkyacayEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDE 531
Cdd:PRK10584 101 pTLNALENVElpaLLRGESSRQSRNGAK------ALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 429188963 532 ATSALDMDTEKRVLKNIMSEN--LNKTCIVTTHRLSVLSMCHKIYRISENKVQ 582
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNreHGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
393-566 |
3.28e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 393 PGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISASTRKLM-------------AYVPQEKTmftGTI 459
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGE-LYYQGQDLL-KADPEAQKLLrqkiqivfqnpygSLNPRKKV---GQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 460 AENMRMVKADATDEEiiRALKYACAYEFVEKLPEginssvlEKGR---SFSEGQNQRLSIARALLRNAPVLLLDEATSAL 536
Cdd:PRK11308 115 LEEPLLINTSLSAAE--RREKALAMMAKVGLRPE-------HYDRyphMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190
....*....|....*....|....*....|...
gi 429188963 537 DMDTEKRVLkNIM---SENLNKTCIVTTHRLSV 566
Cdd:PRK11308 186 DVSVQAQVL-NLMmdlQQELGLSYVFISHDLSV 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
376-540 |
3.34e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 376 YEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdgviynskDVKCkisaSTRKLMAYVPQ----- 450
Cdd:PRK11147 327 YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG--------RIHC----GTKLEVAYFDQhrael 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 451 --EKtmftgTIAENMRMVKADATDEEIIR-ALKYACAYEFVeklPEGINSSVlekgRSFSEGQNQRLSIARALLRNAPVL 527
Cdd:PRK11147 395 dpEK-----TVMDNLAEGKQEVMVNGRPRhVLGYLQDFLFH---PKRAMTPV----KALSGGERNRLLLARLFLKPSNLL 462
|
170
....*....|...
gi 429188963 528 LLDEATSALDMDT 540
Cdd:PRK11147 463 ILDEPTNDLDVET 475
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-562 |
3.48e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.85 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYeksGKN-VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNIT-----EGDGVIYNSKDVKCKISA 439
Cdd:PRK14267 4 AIETVNLRVYY---GSNhVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 440 -STRKLMAYVPQEKTMFTG-TIAENM-------RMVKA-DATDEEIIRALKYACAYEFVEklpeginSSVLEKGRSFSEG 509
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHlTIYDNVaigvklnGLVKSkKELDERVEWALKKAALWDEVK-------DRLNDYPSNLSGG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 429188963 510 QNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMSENLNKTCIVTTH 562
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
46-253 |
4.00e-08 |
|
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: 55.20 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSVASKYLIDAVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRIS-TRISIKIGNEIRADIYD 124
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLfVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 125 RIINTdweSMSYY---RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMavlaLLSAPIALCVSK 201
Cdd:cd18580 81 SVLRA---PMSFFdttPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYF----LIVLPPLLVVYY 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 202 VLMKKMRNRNKEVREISSEMMS-----FNeETFTNLQSIKAFSLNDVFSDRLRKIQE 253
Cdd:cd18580 154 LLQRYYLRTSRQLRRLESESRSplyshFS-ETLSGLSTIRAFGWQERFIEENLRLLD 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
367-537 |
4.79e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 54.48 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSG--KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCkiSASTRkl 444
Cdd:COG4525 4 LTVRHVSVRYPGGGqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGE-ITLDGVPVTG--PGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 mAYVPQEKTMFTG-TIAEN------MRMVKadatdeeiiRALKYACAYEFVEK--LPEGINSSVLEkgrsFSEGQNQRLS 515
Cdd:COG4525 79 -GVVFQKDALLPWlNVLDNvafglrLRGVP---------KAERRARAEELLALvgLADFARRRIWQ----LSGGMRQRVG 144
|
170 180
....*....|....*....|..
gi 429188963 516 IARALLRNAPVLLLDEATSALD 537
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALD 166
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
367-562 |
5.62e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.32 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKN----VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVK-----CKI 437
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGK-VYVDGLDTSdeenlWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 438 SAST--------RKLMAYVPQEKTMFTgtiAENMRmVKADATDEEIIRALKYACAYEFVEKLPEginssvlekgrSFSEG 509
Cdd:PRK13633 84 RNKAgmvfqnpdNQIVATIVEEDVAFG---PENLG-IPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 510 QNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMseNLNK----TCIVTTH 562
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIK--ELNKkygiTIILITH 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
367-562 |
5.79e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.64 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSG---KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG-----DGVIYNSKdvKCKIS 438
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigERVITAGK--KNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 439 ASTRKLMAYVPQ--EKTMFTGTIAE-------NMRMVKADATdeeiiralkyACAYEFVEKLpeGINSSVLEKGR-SFSE 508
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKdicfgpmNFGVSEEDAK----------QKAREMIELV--GLPEELLARSPfELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 509 GQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKniMSENLNK----TCIVTTH 562
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMME--MFYKLHKekglTTVLVTH 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
366-537 |
6.43e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSG---KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNS----KDVK 434
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvDDTLITStsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 435 ckisaSTRKLMAYVPQ--EKTMFTGTI-------AENMRMVKADAtdEEIIRalkyacayefvEKLP-EGINSSVLEKGR 504
Cdd:PRK13649 82 -----QIRKKVGLVFQfpESQLFEETVlkdvafgPQNFGVSQEEA--EALAR-----------EKLAlVGISESLFEKNP 143
|
170 180 190
....*....|....*....|....*....|....
gi 429188963 505 -SFSEGQNQRLSIARALLRNAPVLLLDEATSALD 537
Cdd:PRK13649 144 fELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
375-567 |
6.57e-08 |
|
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: 52.91 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 375 KYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLN--ITEGDgVIYNSKDVKcKISASTRKL----MAYv 448
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGE-ILFKGEDIT-DLPPEERARlgifLAF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 449 pQEKTMFTG-TIAENMRMVKadatdeeiiralkyacayefveklpEGinssvlekgrsFSEGQNQRLSIARALLRNAPVL 527
Cdd:cd03217 84 -QYPPEIPGvKNADFLRYVN-------------------------EG-----------FSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 429188963 528 LLDEATSALDMDTEKRVLKNIMS-ENLNKTCIVTTHRLSVL 567
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQRLL 167
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
388-573 |
6.85e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.73 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 388 NIIANPGEIIALIGPSGEGKTTTMRILLGLL--NITEGDGVIYNSKDVkckISASTRKLMAYVPQEKTMF----TGTIAE 461
Cdd:PRK09473 36 NFSLRAGETLGIVGESGSGKSQTAFALMGLLaaNGRIGGSATFNGREI---LNLPEKELNKLRAEQISMIfqdpMTSLNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 462 NMR--------------MVKADATdEEIIRALKYAcayefveKLPEGinssvleKGR------SFSEGQNQRLSIARALL 521
Cdd:PRK09473 113 YMRvgeqlmevlmlhkgMSKAEAF-EESVRMLDAV-------KMPEA-------RKRmkmyphEFSGGMRQRVMIAMALL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 522 RNAPVLLLDEATSALDMDTEKRV--LKNIMSENLNKTCIVTTHRLSVLS-MCHKI 573
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQImtLLNELKREFNTAIIMITHDLGVVAgICDKV 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
366-562 |
8.09e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.46 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEksGKN-VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgvIYNSKDVKCKISASTRKL 444
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE--IWIGGRVVNELEPADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 mAYVPQEKT----MftgTIAENM-------RMVKA--DATDEEIIRALKyacayefVEKLpeginssvLE-KGRSFSEGQ 510
Cdd:PRK11650 79 -AMVFQNYAlyphM---SVRENMayglkirGMPKAeiEERVAEAARILE-------LEPL--------LDrKPRELSGGQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 511 NQRLSIARALLRNAPVLLLDEATSALD------MDTEKRVLKnimsENLNKTCIVTTH 562
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDaklrvqMRLEIQRLH----RRLKTTSLYVTH 193
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
367-581 |
1.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.65 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLL--------NITEgDGVIYNSKDVkckis 438
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnpnsKITV-DGITLTAKTV----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 439 ASTRKLMAYVPQE-KTMFTG-TIAENM------RMVKADATDEEIIRALKYACAYEFVEKLPEGInssvlekgrsfSEGQ 510
Cdd:PRK13640 80 WDIREKVGIVFQNpDNQFVGaTVGDDVafglenRAVPRPEMIKIVRDVLADVGMLDYIDSEPANL-----------SGGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429188963 511 NQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLK---NIMSENlNKTCIVTTHRLSVLSMCHKIYRISENKV 581
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKlirKLKKKN-NLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
364-562 |
1.19e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 364 GVSIKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISASTRK 443
Cdd:PRK10575 9 DTTFALRNVSFRV--PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGE-ILLDAQPLESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 444 LMAYVPQEKTMftgtiAENMrmvkadaTDEEIIRALKYA-------CAYEFVEKLPEGINSSVLE--KGR---SFSEGQN 511
Cdd:PRK10575 86 KVAYLPQQLPA-----AEGM-------TVRELVAIGRYPwhgalgrFGAADREKVEEAISLVGLKplAHRlvdSLSGGER 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 429188963 512 QRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSENLNKTCIVTTH 562
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVhrLSQERGLTVIAVLH 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
371-568 |
1.31e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 371 NIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSK-----DVKCKISAST 441
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcDKMLLRRRsrqviELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 442 RKL----MAYVPQE-----KTMFT--GTIAENMRMVKADATDEEIIRALKyacAYEFVeKLPEGinSSVLEK-GRSFSEG 509
Cdd:PRK10261 99 RHVrgadMAMIFQEpmtslNPVFTvgEQIAESIRLHQGASREEAMVEAKR---MLDQV-RIPEA--QTILSRyPHQLSGG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 510 QNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLK--NIMSENLNKTCIVTTHRLSVLS 568
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQKEMSMGVIFITHDMGVVA 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
365-564 |
2.50e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.52 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 365 VSIKLDNIKFKY------EKSGknvLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVI--------YNS 430
Cdd:PRK13641 1 MSIKFENVDYIYspgtpmEKKG---LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpeTGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 431 KDVKckisaSTRKLMAYVPQ--EKTMFTGTIAENMRMVKAD--ATDEEI-IRALKYacayefVEKLpeGINSSVLEKGR- 504
Cdd:PRK13641 78 KNLK-----KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAkEKALKW------LKKV--GLSEDLISKSPf 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 505 SFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMS-ENLNKTCIVTTHRL 564
Cdd:PRK13641 145 ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNM 205
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
383-562 |
2.55e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLG--LLNITEGDgVIYNSKDVkCKISASTRK-----LMAYVPQEKTMF 455
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGD-ILFKGESI-LDLEPEERAhlgifLAFQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 456 TGT----IAENMRMVKADATDEEIIRALKYacayeFVEKLPE-GINSSVLEK--GRSFSEGQNQRLSIARALLRNAPVLL 528
Cdd:CHL00131 100 SNAdflrLAYNSKRKFQGLPELDPLEFLEI-----INEKLKLvGMDPSFLSRnvNEGFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190
....*....|....*....|....*....|....*
gi 429188963 529 LDEATSALDMDTEKRVLKNI-MSENLNKTCIVTTH 562
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGInKLMTSENSIILITH 209
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
365-562 |
3.03e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.47 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 365 VSIKLDNIKFKYEKSG---KNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKdVKCKI 437
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvDDITITHK-TKDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 438 SASTRKLMAYVPQ--EKTMFtgtiaenmrmvkADATDEEIIRA-------LKYACAYEFVEKLPEGINSSVLEKGR-SFS 507
Cdd:PRK13646 80 IRPVRKRIGMVFQfpESQLF------------EDTVEREIIFGpknfkmnLDEVKNYAHRLLMDLGFSRDVMSQSPfQMS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 508 EGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRV---LKNIMSENlNKTCIVTTH 562
Cdd:PRK13646 148 GGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVmrlLKSLQTDE-NKTIILVSH 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
383-581 |
3.42e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.07 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKcKISAS----TRKLMAYVPQEKTMFTG- 457
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGE-ILFDGENIP-AMSRSrlytVRKRMSMLFQSGALFTDm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 458 TIAENMrmvkadatdeeiiralkyacAYEFVE--KLPEGI-NSSVLEKGRS-------------FSEGQNQRLSIARALL 521
Cdd:PRK11831 100 NVFDNV--------------------AYPLREhtQLPAPLlHSTVMMKLEAvglrgaaklmpseLSGGMARRAALARAIA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 522 RNAPVLLLDEATSALDMDTEKRVLKNIMSEN--LNKTCIVTTHRL-SVLSMCHKIYRISENKV 581
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNsaLGVTCVVVSHDVpEVLSIADHAYIVADKKI 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
367-537 |
3.59e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 51.62 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGD---------------GVIYNS- 430
Cdd:PRK11248 2 LQISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgkpvegpgaerGVVFQNe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 431 -----KDVKCKISASTRklMAYVPQEKTMftgTIAENM-RMVKADATDEEIIRALkyacayefveklpeginssvlekgr 504
Cdd:PRK11248 80 gllpwRNVQDNVAFGLQ--LAGVEKMQRL---EIAHQMlKKVGLEGAEKRYIWQL------------------------- 129
|
170 180 190
....*....|....*....|....*....|...
gi 429188963 505 sfSEGQNQRLSIARALLRNAPVLLLDEATSALD 537
Cdd:PRK11248 130 --SGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
374-578 |
3.65e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 374 FKYEKsgKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGdGVIYNSKdvkcKISASTRKLMAYVPQEKT 453
Cdd:PRK13638 9 FRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKG-AVLWQGK----PLDYSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 454 MFT------------GTIAENMRMVkaDATDEEIIR----ALKYACAYEFVEklpeginssvlEKGRSFSEGQNQRLSIA 517
Cdd:PRK13638 82 VFQdpeqqifytdidSDIAFSLRNL--GVPEAEITRrvdeALTLVDAQHFRH-----------QPIQCLSHGQKKRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429188963 518 RALLRNAPVLLLDEATSALDMDTEKR---VLKNIMSEnlNKTCIVTTHRLSVlsmchkIYRISE 578
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQmiaIIRRIVAQ--GNHVIISSHDIDL------IYEISD 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
367-573 |
3.82e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.86 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEG----DGVIYNSKDVKckisASTR 442
Cdd:PRK09700 6 ISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitiNNINYNKLDHK----LAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 KLMAYVPQEKTMFTG-TIAENM--------RMVKADATDEEIIRALkyacAYEFVEKLpeGINSSVLEKGRSFSEGQNQR 513
Cdd:PRK09700 80 LGIGIIYQELSVIDElTVLENLyigrhltkKVCGVNIIDWREMRVR----AAMMLLRV--GLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 514 LSIARALLRNAPVLLLDEATSALdMDTEKRVLKNIMSE--NLNKTCIVTTHRLS-VLSMCHKI 573
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQlrKEGTAIVYISHKLAeIRRICDRY 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
379-533 |
4.30e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 379 SGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCK-ISASTRKLMAYVPQE-KT--- 453
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE-IRLDGKPVRIRsPRDAIRAGIAYVPEDrKGegl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 454 MFTGTIAENM------RMVKADATDEEIIRALkyacAYEFVEKLpeGIN-SSVLEKGRSFSEGQNQRLSIARALLRNAPV 526
Cdd:COG1129 342 VLDLSIRENItlasldRLSRGGLLDRRRERAL----AEEYIKRL--RIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKV 415
|
....*..
gi 429188963 527 LLLDEAT 533
Cdd:COG1129 416 LILDEPT 422
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
94-275 |
4.47e-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: 51.70 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 94 IGNLVINAVTNRISTRIsikigneiRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCS 173
Cdd:cd18589 55 VCDLIYNITMSRIHSRL--------QGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 174 ILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLR-KIQ 252
Cdd:cd18589 127 LFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRqRLQ 206
|
170 180
....*....|....*....|....*
gi 429188963 253 EKFKETTLEYNKFTI--YTSSFMSL 275
Cdd:cd18589 207 KTYRLNKKEAAAYAVsmWTSSFSGL 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
383-573 |
4.88e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 51.24 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIynskdVKCKISAstrkLMA----YVPQektmFTGt 458
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR-VE-----VNGRVSA----LLElgagFHPE----LTG- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 459 iAENMRMV-------KADATD--EEIIralkyacayEFVEkLPEGINSSVlekgRSFSEGQNQRLSIARALLRNAPVLLL 529
Cdd:COG1134 106 -RENIYLNgrllglsRKEIDEkfDEIV---------EFAE-LGDFIDQPV----KTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 429188963 530 DEATSALDMD-TEK--RVLKNIMSEnlNKTCIVTTHRLSVL-SMCHKI 573
Cdd:COG1134 171 DEVLAVGDAAfQKKclARIRELRES--GRTVIFVSHSMGAVrRLCDRA 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
366-566 |
5.21e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 366 SIKLDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLnitEGDGVIYNSKDV----KCKISAST 441
Cdd:PRK15134 7 AIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL---PSPPVVYPSGDIrfhgESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 442 RKL-------MAYVPQEKtMFT----GTIAENM-------RMVKADATDEEIIRALkyacayEFVeklpeGINSSvleKG 503
Cdd:PRK15134 84 QTLrgvrgnkIAMIFQEP-MVSlnplHTLEKQLyevlslhRGMRREAARGEILNCL------DRV-----GIRQA---AK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429188963 504 R------SFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLK--NIMSENLNKTCIVTTHRLSV 566
Cdd:PRK15134 149 RltdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQllRELQQELNMGLLFITHNLSI 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
377-564 |
5.30e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 377 EKS--GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCK-ISASTRKLMAYVPQEKT 453
Cdd:PRK10762 11 DKAfpGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS-ILYLGKEVTFNgPKSSQEAGIGIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 454 MFTG-TIAENMRMVKadatdeEIIRAL-------KYACAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAP 525
Cdd:PRK10762 90 LIPQlTIAENIFLGR------EFVNRFgridwkkMYAEADKLLARL--NLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 429188963 526 VLLLDEATSALdMDTEKRVLKNIMSENLNKTC-IV-TTHRL 564
Cdd:PRK10762 162 VIIMDEPTDAL-TDTETESLFRVIRELKSQGRgIVyISHRL 201
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
394-537 |
7.03e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 394 GEIIALIGPSGEGKTTTMRILLGLLNITEGD----GVIYNSKDVkckisaSTRKLMAYVPQEKTMFTG-TIAENM----- 463
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfGQPVDAGDI------ATRRRVGYMSQAFSLYGElTVRQNLelhar 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 464 --RMVKADATD--EEIIRALKYAcayEFVEKLPEginssvlekgrSFSEGQNQRLSIARALLRNAPVLLLDEATSALD 537
Cdd:NF033858 366 lfHLPAAEIAArvAEMLERFDLA---DVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
392-546 |
7.31e-07 |
|
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: 51.99 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 392 NPGEIIALIGPSGEGKTTTMRILLGLL--NITEGDG-VIYNSKDVkckISASTRKL-------MAYVPQEKtM------F 455
Cdd:COG4172 34 AAGETLALVGESGSGKSVTALSILRLLpdPAAHPSGsILFDGQDL---LGLSERELrrirgnrIAMIFQEP-MtslnplH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 456 T-GT-IAENMR----MVKADATdEEIIRALkyacayEFVeKLPEginssvlEKGR------SFSEGQNQRLSIARALLrN 523
Cdd:COG4172 110 TiGKqIAEVLRlhrgLSGAAAR-ARALELL------ERV-GIPD-------PERRldayphQLSGGQRQRVMIAMALA-N 173
|
170 180
....*....|....*....|....
gi 429188963 524 APVLLL-DEATSALDMDTEKRVLK 546
Cdd:COG4172 174 EPDLLIaDEPTTALDVTVQAQILD 197
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
364-583 |
1.58e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.68 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 364 GVSIKLDNIKFKYekSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgviynskdvkckISASTRK 443
Cdd:PRK11247 10 GTPLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE------------LLAGTAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 444 LMAYVPQEKTMFTG-------TIAENMRM-VKADATDeeiiRALKyacAYEFVeklpeGINSSVLEKGRSFSEGQNQRLS 515
Cdd:PRK11247 76 LAEAREDTRLMFQDarllpwkKVIDNVGLgLKGQWRD----AALQ---ALAAV-----GLADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 516 IARALLRNAPVLLLDEATSALDMDTekRVLKNIMSENL----NKTCIVTTHRLS-VLSMCHKIYRISENKVQL 583
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALT--RIEMQDLIESLwqqhGFTVLLVTHDVSeAVAMADRVLLIEEGKIGL 214
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
384-531 |
1.63e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 49.73 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 384 LENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISAST------RKLmayvpQEKTMFTG 457
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGS-VLFGGTDLTGLDEHEIarlgigRKF-----QKPTVFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 458 -TIAENMRMvkADATDEEIIRALKYACAYEFVEKLPEginssVLE----------KGRSFSEGQNQRLSIARALLRNAPV 526
Cdd:COG4674 100 lTVFENLEL--ALKGDRGVFASLFARLTAEERDRIEE-----VLEtigltdkadrLAGLLSHGQKQWLEIGMLLAQDPKL 172
|
....*
gi 429188963 527 LLLDE 531
Cdd:COG4674 173 LLLDE 177
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
380-537 |
1.81e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKckiSASTRKL----MAYVPQE---- 451
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGS-IRLDGEDIT---GLSPRERrrlgVAYIPEDrlgr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 452 ---KTMftgTIAENMrMVKaDATDEEIIRA--LKYACAYEFVEKL-------PEGINSSVlekgRSFSEGQNQRLSIARA 519
Cdd:COG3845 346 glvPDM---SVAENL-ILG-RYRRPPFSRGgfLDRKAIRAFAEELieefdvrTPGPDTPA----RSLSGGNQQKVILARE 416
|
170
....*....|....*...
gi 429188963 520 LLRNAPVLLLDEATSALD 537
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLD 434
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
394-567 |
2.02e-06 |
|
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: 48.34 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 394 GEIIALIGPSGEGKTTTMRILLGLLNITEGDgviynskdvkckiSASTRKLMAYVPQEKtmftgtiaenmrmvkadatde 473
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-------------DEWDGITPVYKPQYI--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 474 eiiralkyacayefveklpeginssvlekgrSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNI--MSE 551
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIrrLSE 119
|
170
....*....|....*.
gi 429188963 552 NLNKTCIVTTHRLSVL 567
Cdd:cd03222 120 EGKKTALVVEHDLAVL 135
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
393-562 |
3.06e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.02 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 393 PGEIIALIGPSGEGKTTTMRILLGLLNITEGDGVI-----------YNSKDVKCKISASTRKLMayvPQEKTmftGTIAE 461
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhfgdysYRSQRIRMIFQDPSTSLN---PRQRI---SQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 462 -NMRM---VKADATDEEIIRALKYacayefVEKLPEGINSSvlekGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALD 537
Cdd:PRK15112 112 fPLRLntdLEPEQREKQIIETLRQ------VGLLPDHASYY----PHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180
....*....|....*....|....*....
gi 429188963 538 MDTEKRVLkNIMSENLNKTCI----VTTH 562
Cdd:PRK15112 182 MSMRSQLI-NLMLELQEKQGIsyiyVTQH 209
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
85-302 |
3.53e-06 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 49.14 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 85 IAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNrltsDATTVSNSILGWVPSL 164
Cdd:cd18586 44 LTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLLR----DLDTLRNFLTGPSLFA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 165 ITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVF 244
Cdd:cd18586 120 FFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 245 SDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIVTYSCFGWGVYRLWTGHITYGTM 302
Cdd:cd18586 200 RRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGAL 257
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
50-195 |
3.81e-06 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 48.94 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 50 VFLGILGVVMGLGGSVASKYLIDAV--TGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRII 127
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVflEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 128 NTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPI 195
Cdd:cd18584 82 ALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPL 149
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
377-537 |
1.43e-05 |
|
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: 46.08 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 377 EKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLN--ITEGDgVIYNSKdvkcKISASTRKLMAYVPQEKTM 454
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGE-ILINGR----PLDKNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 455 FTG-TIAENMRMvkadatdeeiiralkyacayefveklpeginSSVLekgRSFSEGQNQRLSIARALLRNAPVLLLDEAT 533
Cdd:cd03232 91 SPNlTVREALRF-------------------------------SALL---RGLSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
....
gi 429188963 534 SALD 537
Cdd:cd03232 137 SGLD 140
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
475-583 |
2.11e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 475 IIRALKYACAYEFVEKLPEGINSSVLEKGRS----------FSEGQNQRLSIARAL----LRNAPVLLLDEATSALDMDT 540
Cdd:cd03227 37 ILDAIGLALGGAQSATRRRSGVKAGCIVAAVsaeliftrlqLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRD 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 429188963 541 EKRvLKNIMSENLNKTC--IVTTHRLSVLSMCHKIYRISENKVQL 583
Cdd:cd03227 117 GQA-LAEAILEHLVKGAqvIVITHLPELAELADKLIHIKKVITGV 160
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
86-302 |
2.59e-05 |
|
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: 46.15 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 86 AFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVPSLI 165
Cdd:cd18784 39 IIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 166 TKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFS 245
Cdd:cd18784 119 RSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 246 DRLRkiqEKFKETTLEYNKFTIYTSSFMS---LVGMIVTYSCFGWGVYRLWTGHITYGTM 302
Cdd:cd18784 199 NRYS---EKLKDTYKLKIKEALAYGGYVWsneLTELALTVSTLYYGGHLVITGQISGGNL 255
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
82-298 |
2.75e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 46.12 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 82 IGFIAFVMVVMAIGNlvinAVTNRISTRISIKIGNEIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWV 161
Cdd:cd18561 39 LAGIAGVIVLRAALL----WLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 162 PSLITKTVQFCSILVVILYYDPTMAVLALLSAPIALC----VSKVLMKKMRNRNKEvreisseMMSFNEETFTNLQSI-- 235
Cdd:cd18561 115 PQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLspalWDRLAKDTGRRHWAA-------YGRLSAQFLDSLQGMtt 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429188963 236 -KAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSSFMSLVGMIVTYSCFGWGVYRLWTGHIT 298
Cdd:cd18561 188 lKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLT 251
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
383-539 |
3.50e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 383 VLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNiTEGDGVIY---------NSKDVKCKISA---------STRKL 444
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEIS-ADGGSYTFpgnwqlawvNQETPALPQPAleyvidgdrEYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 445 MAYVPQEKTMFTGTIAENMRMvKADATDEEIIRALkyacAYEFVEKLpeGINSSVLEKG-RSFSEGQNQRLSIARALLRN 523
Cdd:PRK10636 95 EAQLHDANERNDGHAIATIHG-KLDAIDAWTIRSR----AASLLHGL--GFSNEQLERPvSDFSGGWRMRLNLAQALICR 167
|
170
....*....|....*.
gi 429188963 524 APVLLLDEATSALDMD 539
Cdd:PRK10636 168 SDLLLLDEPTNHLDLD 183
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
46-251 |
4.72e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 45.54 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILGVVMGLGGSV-----ASKYLIDAVTGYDSGGIGFIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRA 120
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWwlgiwASAYETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 121 DIYDRIINTdweSMSYYRS---GDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIAL 197
Cdd:cd18604 81 RLLHSVLRA---PLRWLDTtpvGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 198 CVSKVLMKKMRnrnkEVREISSEMMS-----FNeETFTNLQSIKAFSLNDVFSDRL-RKI 251
Cdd:cd18604 158 YIGRLYLRASR----ELKRLESVARSpilshFG-ETLAGLVTIRAFGAEERFIEEMlRRI 212
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
117-295 |
4.86e-05 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 45.55 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 117 EIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWV-PSLitktVQFCSILVVIL---YYDPTMAVLALLS 192
Cdd:cd18585 69 NLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLsPPV----VALLVILATILflaFFSPALALILLAG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 193 APIALCVSKVLMKKMRNRN-KEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYTSS 271
Cdd:cd18585 145 LLLAGVVIPLLFYRLGKKIgQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQA 224
|
170 180
....*....|....*....|....
gi 429188963 272 FMSLVGMIVTyscfgWGVyrLWTG 295
Cdd:cd18585 225 LMILLSGLTV-----WLV--LWLG 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
380-573 |
5.24e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 380 GKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKCKISA-STRKLMAYVPQEKTMFTG- 457
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS-ILFQGKEIDFKSSKeALENGISMVHQELNLVLQr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 458 TIAENMRM----VKADATDEEIIralkYACAYEFVEKLpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEAT 533
Cdd:PRK10982 89 SVMDNMWLgrypTKGMFVDQDKM----YRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 429188963 534 SALdmdTEKRV--LKNIMSENLNKTC--IVTTHRL-SVLSMCHKI 573
Cdd:PRK10982 163 SSL---TEKEVnhLFTIIRKLKERGCgiVYISHKMeEIFQLCDEI 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
396-538 |
5.46e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.64 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 396 IIALIGPSGEGKTTTMRILLGLLN-----ITEGDGVIYnskDVKCKISASTRKL-MAYVPQEKTMFTG-TIAENMR--MV 466
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRpqkgrIVLNGRVLF---DAEKGICLPPEKRrIGYVFQDARLFPHyKVRGNLRygMA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429188963 467 KADATD-EEIIRALkyacayefveklpeGINSSVLEKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDM 538
Cdd:PRK11144 103 KSMVAQfDKIVALL--------------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
365-567 |
6.00e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 365 VSIKldNIKFKYEksGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGL--LNITEGDgVIYNSKDVkCKISASTR 442
Cdd:PRK09580 2 LSIK--DLHVSVE--DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGT-VEFKGKDL-LELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 443 K----LMAY-VPQE-----KTMFTGTIAENMRMVKA-------DATD--EEIIRALkyacayefveKLPEGINSSVLEKG 503
Cdd:PRK09580 76 AgegiFMAFqYPVEipgvsNQFFLQTALNAVRSYRGqepldrfDFQDlmEEKIALL----------KMPEDLLTRSVNVG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 504 rsFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDTEKRVLKNIMS-ENLNKTCIVTTHRLSVL 567
Cdd:PRK09580 146 --FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSlRDGKRSFIIVTHYQRIL 208
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
118-303 |
1.57e-04 |
|
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: 43.78 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 118 IRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIAL 197
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 198 CVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLrkiQEKFKETTLEYNKFTIYTSSFMSLVG 277
Cdd:cd18780 157 IGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY---SEKINESYLLGKKLARASGGFNGFMG 233
|
170 180 190
....*....|....*....|....*....|...
gi 429188963 278 MIVTYSCfgwgVYRLWTG-------HITYGTMT 303
Cdd:cd18780 234 AAAQLAI----VLVLWYGgrlvidgELTTGLLT 262
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
369-551 |
1.76e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.01 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 369 LDNIKFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKckisastRKLMAYv 448
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE-ILFERQSIK-------KDLCTY- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 449 pQEKTMFTG---------TIAEN----MRMVKADATDEEIIRALKYACAYEFveklPEGInssvlekgrsFSEGQNQRLS 515
Cdd:PRK13540 73 -QKQLCFVGhrsginpylTLRENclydIHFSPGAVGITELCRLFSLEHLIDY----PCGL----------LSSGQKRQVA 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 429188963 516 IARALLRNAPVLLLDEATSALDmdteKRVLKNIMSE 551
Cdd:PRK13540 138 LLRLWMSKAKLWLLDEPLVALD----ELSLLTIITK 169
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
396-582 |
1.93e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 396 IIALIGPSGEGKTTtmrILLGLLNITEGDGvIYNSKDVKC--KISASTRKLmAYVpqeKTMFTGTIAENMrmvkadatde 473
Cdd:cd03240 24 LTLIVGQNGAGKTT---IIEALKYALTGEL-PPNSKGGAHdpKLIREGEVR-AQV---KLAFENANGKKY---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 474 EIIRALKYACAYEFVEKlpEGINSSVLEKGRSFSEGQNQ------RLSIARALLRNAPVLLLDEATSALDMDTEKRVLKN 547
Cdd:cd03240 86 TITRSLAILENVIFCHQ--GESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAE 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 429188963 548 IMSE---NLNKTCIVTTHRLSVLSMCHKIYRISENKVQ 582
Cdd:cd03240 164 IIEErksQKNFQLIVITHDEELVDAADHIYRVEKDGRQ 201
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
386-551 |
2.60e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 43.05 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 386 NANIIANPGEIIALIGPSGEGKTTTMRILLGLLNITEGDgVIYNSKDVKC----KISastRKLMAYVPQEKTMFTG-TIA 460
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT-ILLRGQHIEGlpghQIA---RMGVVRTFQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 461 ENMRMVKADATDEEIIRALKYACAYEFVEKlpEGINSSV--LEK-------GRS---FSEGQNQRLSIARALLRNAPVLL 528
Cdd:PRK11300 99 ENLLVAQHQQLKTGLFSGLLKTPAFRRAES--EALDRAAtwLERvgllehaNRQagnLAYGQQRRLEIARCMVTQPEILM 176
|
170 180
....*....|....*....|...
gi 429188963 529 LDEATSALDmDTEKRVLKNIMSE 551
Cdd:PRK11300 177 LDEPAAGLN-PKETKELDELIAE 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
367-562 |
3.77e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 367 IKLDNikFKYEKSGKNVLENANIIANPGEIIALIGPSGEGKTTTMR--ILLGLLNITEGDGVIYNSKDV--------KCK 436
Cdd:PLN03073 178 IHMEN--FSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymAMHAIDGIPKNCQILHVEQEVvgddttalQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 437 ISAST-RKLM-----AYVPQEKTMFTGTIAENMRMVKADATD--------EEIIRALKYACAYEfveklPEGINSSVL-- 500
Cdd:PLN03073 256 LNTDIeRTQLleeeaQLVAQQRELEFETETGKGKGANKDGVDkdavsqrlEEIYKRLELIDAYT-----AEARAASILag 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429188963 501 ---------EKGRSFSEGQNQRLSIARALLRNAPVLLLDEATSALDMDT----EKRVLKnimsenLNKTCIVTTH 562
Cdd:PLN03073 331 lsftpemqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAvlwlETYLLK------WPKTFIVVSH 399
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
139-250 |
5.55e-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: 42.13 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 139 SGDLLNRLTSDATTVSNSIlgwvPS----LITKTVQFCSILVVILYYDPTMAVLALLSAPIALCVSKVLmkkmRNRNKEV 214
Cdd:cd18605 98 VGRILNRFSSDVYTIDDSL----PFilniLLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYY----RATSREL 169
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 429188963 215 REISSEMMS-----FNeETFTNLQSIKAFSLNDVFSDRLRK 250
Cdd:cd18605 170 KRLNSVNLSplythFS-ETLKGLVTIRAFRKQERFLKEYLE 209
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
138-302 |
6.47e-04 |
|
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: 41.94 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 138 RSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSAPIAlcvskVLMKKMRN-RNKEV-R 215
Cdd:cd18590 91 KTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLT-----AIAQKVYNtYHQKLsQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 216 EISSEMMSFNE---ETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETT----LEYNKFTIYTSSFMSLVGMIVTYscfgWG 288
Cdd:cd18590 166 AVQDSIAKAGElarEAVSSIRTVRSFKAEEEEACRYSEALERTYNLKdrrdTVRAVYLLVRRVLQLGVQVLMLY----CG 241
|
170
....*....|....
gi 429188963 289 VYRLWTGHITYGTM 302
Cdd:cd18590 242 RQLIQSGHLTTGSL 255
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
114-242 |
7.62e-04 |
|
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: 41.76 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 114 IGNEIRADIYDRIINTDWESMSYYRSGDLLNRLTSDATTVSNSILGWVPSLITKTVQFCSILVVILYYDPTMAVLALLSA 193
Cdd:cd18574 73 VAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIV 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 429188963 194 PIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLND 242
Cdd:cd18574 153 PVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMED 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
394-587 |
9.37e-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: 42.12 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 394 GEIIALIGPSGEGKTTTMRILLGLLNITEGDGVIYNSKDVKCKISA-STRKLMAYVPQEK-------TMFTG---TIAE- 461
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRNPAqAIRAGIAMVPEDRkrhgivpILGVGkniTLSVl 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 462 ---NMRMVKADATDEEIIRA----LKYACAYEFvekLPEGinssvlekgrSFSEGQNQRLSIARALLRNAPVLLLDEATS 534
Cdd:TIGR02633 366 ksfCFKMRIDAAAELQIIGSaiqrLKVKTASPF---LPIG----------RLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 429188963 535 ALDMDTEKRVLK--NIMSENLNKTCIVTTHRLSVLSMCHKIYRISENKVQ--LVNYE 587
Cdd:TIGR02633 433 GVDVGAKYEIYKliNQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKgdFVNHA 489
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
348-410 |
3.82e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 39.88 E-value: 3.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429188963 348 LDEEIANEIAATceengVSIKLDNIKFKYEKSGKNVLENA-----NIIANPGEIIALIGPSGEGKTTT 410
Cdd:PRK05703 175 LSPEIAEKLLKL-----LLEHMPPRERTAWRYLLELLANMipvrvEDILKQGGVVALVGPTGVGKTTT 237
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
348-410 |
4.00e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 39.85 E-value: 4.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429188963 348 LDEEIANEIAATCEENgvsIKLDNIKFK-YEKSGKNVLENANIIANPGEIIALIGPSGEGKTTT 410
Cdd:COG1419 120 VSPELARELLEKLPED---LSAEEAWRAlLEALARRLPVAEDPLLDEGGVIALVGPTGVGKTTT 180
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
50-240 |
4.80e-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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 39.42 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 50 VFLGILGVVMGLGGSVAskylIDAVTGYDS---------GGIGFIAFVMVVMAIGNLVINAVTNRISTRISIkigneira 120
Cdd:cd18783 12 LILHVLALAPPIFFQIV----IDKVLVHQSystlyvltiGVVIALLFEGILGYLRRYLLLVATTRIDARLAL-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 121 DIYDRIINTdweSMSYY--RSGDLLNRLTSDATTVSNSILGwvpSLITKTVQFCSILV---VILYYDPTMAVLAL-LSAP 194
Cdd:cd18783 80 RTFDRLLSL---PIDFFerTPAGVLTKHMQQIERIRQFLTG---QLFGTLLDATSLLVflpVLFFYSPTLALVVLaFSAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 429188963 195 IALCVSkVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSL 240
Cdd:cd18783 154 IALIIL-AFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLAL 198
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
46-302 |
5.87e-03 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 38.96 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 46 IIFYVFLGILgvvmgLGGSVA------SKYLIDavTGYDSGGIGFIAFVMV---VMAIGNLVINAVTNRISTRISIKIGN 116
Cdd:cd18571 3 LILQLLLGLL-----LGSLLQlifpflTQSIVD--KGINNKDLNFIYLILIaqlVLFLGSTSIEFIRSWILLHISSRINI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 117 EIRADIYDRIINTdweSMSYY---RSGDLLNRLtSDATTV----SNSILGWVPSLITktvqFCSILVVILYYDPTMAVLA 189
Cdd:cd18571 76 SIISDFLIKLMRL---PISFFdtkMTGDILQRI-NDHSRIesflTSSSLSILFSLLN----LIVFSIVLAYYNLTIFLIF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 190 LLSAPIALCVSKVLMKKMRNRNKEVREISSEMMSFNEETFTNLQSIKAFSLNDVFSDRLRKIQEKFKETTLEYNKFTIYT 269
Cdd:cd18571 148 LIGSVLYILWILLFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQ 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 429188963 270 SS----FMSLVGMIVTYSCfGWGVYRlwtGHITYGTM 302
Cdd:cd18571 228 QIgalfINQLKNILITFLA-AKLVID---GEITLGMM 260
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
51-254 |
7.03e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 38.69 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 51 FLGILGVVMGLGGSVASKYLIDAVTGYDSG---GIGfIAFVMVVMAIGNLVINAVTNRISTRISIKIGNEIRADIYDRII 127
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPlsdGYL-YALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429188963 128 NTDWESMSYYRSGDLLNRLTSDATTVSNSILG----WvpSLItktVQFcSILVVILYYDPTMAVLA-LLSAPIALCVSKV 202
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSfhdlW--SLP---LQI-IVALYLLYQQVGVAFLAgLVFALVLIPINKW 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 429188963 203 LMKKMrnrnkevREISSEMMSFNE-------ETFTNLQSIKAFSLNDVFSDRLRKIQEK 254
Cdd:cd18598 157 IAKRI-------GALSEKMMKHKDarvklmtEILSGIRVIKLLAWERIFKQKIEELRAK 208
|
|
| |
