|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-602 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 681.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 18 PKNTKATAKRLFSYLEQEKHKIAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQqkitsLMAGLALMAVVYVLGVG 97
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA-----LLLLLLLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 98 ATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALM 177
Cdd:COG1132 77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 178 LYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNS 257
Cdd:COG1132 157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 258 QVKAQFISGIMGPCMNAMSQVNYTLTACVGsiiafASRWGGGvpfsALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSA 337
Cdd:COG1132 237 NLRAARLSALFFPLMELLGNLGLALVLLVG-----GLLVLSG----SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 338 LAGAERVFNVMDEAEEIDDGKK-LVLDKVHGDVLVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLIT 416
Cdd:COG1132 308 LASAERIFELLDEPPEIPDPPGaVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 417 RFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYD 496
Cdd:COG1132 388 RFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 497 TMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVL 576
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVL 547
|
570 580
....*....|....*....|....*.
gi 524455117 577 ENGEIIERGTHEELLEKKGRYFELYT 602
Cdd:COG1132 548 DDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-603 |
1.23e-166 |
|
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: 492.04 E-value: 1.23e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 16 QKPKNTKATAKRLFSYLEQEKHKIAAAFVCVLVSSASTLCGSYLLRPIINGLIdstktSQQKITSLMAGLALMAVVYVLG 95
Cdd:COG2274 135 DKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVL-----PNQDLSTLWVLAIGLLLALLFE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 96 VGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFtNDVDIIGEMLNSTLVQIFSGTITLIGTLA 175
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 176 LMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLR 255
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 256 NSQVKAQFISGIMGPCMNAMSQVNYTLTACVGSIIAFASRwgggvpfsaLDIGGLTVFVNYSRQFSRPINELAQQVTNIM 335
Cdd:COG2274 369 NARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQ---------LTLGQLIAFNILSGRFLAPVAQLIGLLQRFQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 336 SALAGAERVFNVMD-EAEEIDDGKKLVLDKVHGDVLVEGVTFGYNPDKT-ILKDVSIFAHPGQKIALVGSTGAGKTTITN 413
Cdd:COG2274 440 DAKIALERLDDILDlPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLK 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 414 LITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPE 493
Cdd:COG2274 520 LLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPM 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 494 GYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAI 573
Cdd:COG2274 600 GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRI 679
|
570 580 590
....*....|....*....|....*....|
gi 524455117 574 MVLENGEIIERGTHEELLEKKGRYFELYTG 603
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
24-601 |
7.79e-150 |
|
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: 444.16 E-value: 7.79e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 24 TAKRLFSYLEQEKHKIAAAFVCVLVSSASTLCGSYLLRPIINGLidSTKTSQQKITSLMAGLALMAVVY-VLGVGATYLQ 102
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDG--FGGRDRSVLWWVPLVVIGLAVLRgICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 103 GRimisVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNW 182
Cdd:TIGR02203 79 SW----VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 183 VLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQ 262
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 263 FISGIMGPcmnaMSQVnytLTACVGSIIAFASRWGGGVpfSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAE 342
Cdd:TIGR02203 235 SAGSISSP----ITQL---IASLALAVVLFIALFQAQA--GSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 343 RVFNVMDEAEEIDDGKKlVLDKVHGDVLVEGVTFGYNP-DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNI 421
Cdd:TIGR02203 306 SLFTLLDSPPEKDTGTR-AIERARGDVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 422 NKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLS-ATDEEVRQAAKTSCADMFIKNMPEGYDTMLK 500
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 501 GDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGE 580
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|.
gi 524455117 581 IIERGTHEELLEKKGRYFELY 601
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQLH 565
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
39-344 |
6.77e-131 |
|
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: 385.60 E-value: 6.77e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSLMAG-LALMAVVYVLGVGATYLQGRIMISVSQGTLKRI 117
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRiLLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 118 REHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAK 197
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 198 IGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQ 277
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 278 VNYTLTACVGSIIAFAsrwgggvpfSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18547 241 LGYVLVAVVGGLLVIN---------GALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-601 |
4.23e-126 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 383.60 E-value: 4.23e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 21 TKATAKRLFSYLEQEKHKIAAAFVCVLVSSASTLCGSYLLRPIingLIDSTKTSQQKITSLMAgLALMAVVYVLGVgATY 100
Cdd:PRK11176 9 TWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPL---LDDGFGKADRSVLKWMP-LVVIGLMILRGI-TSF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 101 LQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYT 180
Cdd:PRK11176 84 ISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 181 NWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVK 260
Cdd:PRK11176 164 SWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 261 AQFISGIMGPCMN-----AMSQVNY---------TLTAcvGSI-IAFASRWGGGVPFSALdiggltvfVNYSRQFSRpin 325
Cdd:PRK11176 244 MVSASSISDPIIQliaslALAFVLYaasfpsvmdTLTA--GTItVVFSSMIALMRPLKSL--------TNVNAQFQR--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 326 elaqqvtnimsALAGAERVFNVMDEAEEIDDGKkLVLDKVHGDVLVEGVTFGY-NPDKTILKDVSIFAHPGQKIALVGST 404
Cdd:PRK11176 311 -----------GMAACQTLFAILDLEQEKDEGK-RVIERAKGDIEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 405 GAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSA-TDEEVRQAAKTSC 483
Cdd:PRK11176 379 GSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 484 ADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHR 563
Cdd:PRK11176 459 AMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
|
570 580 590
....*....|....*....|....*....|....*...
gi 524455117 564 LSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFELY 601
Cdd:PRK11176 539 LSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLH 576
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-600 |
1.48e-120 |
|
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: 369.92 E-value: 1.48e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 1 MPPMGPPNRNRNQKKQKPKNTKATAKRLFSYLEqeKHKIAAAFVCVLVSSASTlcgSYLLRPIINGLIDSTKTSQQKITS 80
Cdd:COG5265 1 APSARAMSAPAAPPRLDLLLRLLLLLLLPPYLR--RRRRALAALLLLLLAAAL---ALVVPPLLKDAIDALLSGAAALLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 81 LMAGLAL-MAVVYVLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDiMSRftndvDI------IG 153
Cdd:COG5265 76 VPVGLLLaYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGG-LSR-----DIergtkgIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 154 EMLNSTLVQIFSGTITLIGTLALMLYT-NWVLAVVTIVVspIIAKIG-TAIAGKSRKYFMKQQTDL-GKVNG-------- 222
Cdd:COG5265 150 FLLRFLLFNILPTLLEIALVAGILLVKyDWWFALITLVT--VVLYIAfTVVVTEWRTKFRREMNEAdSEANTravdslln 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 223 YieETVtgqkvvKVFNYEENVVNEFSELNQSLRNSQVKAQfisgimgpcmNAMSQVNYT----LTACVGSIIAFASRwgg 298
Cdd:COG5265 228 Y--ETV------KYFGNEAREARRYDEALARYERAAVKSQ----------TSLALLNFGqaliIALGLTAMMLMAAQ--- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 299 GVPFSALDIGGLtVFVN-YSRQFSRPINELAQQVTNIMSALAGAERVFNVMDEAEEIDD---GKKLVLDkvHGDVLVEGV 374
Cdd:COG5265 287 GVVAGTMTVGDF-VLVNaYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADapdAPPLVVG--GGEVRFENV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 375 TFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHL 454
Cdd:COG5265 364 SFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 455 FTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTM-----LKgdgsnLSQGQRQLLNIARAALSKAPILVL 529
Cdd:COG5265 444 FNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRvgergLK-----LSGGEKQRVAIARTLLKNPPILIF 518
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 530 DEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFEL 600
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-595 |
7.78e-118 |
|
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: 361.38 E-value: 7.78e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 26 KRLFSYLEQEKHKIAAAFVCVLVSSASTLCGSYLLRPIINGLIDStktsQQKITSLMAGLALMAVVYVLGVGATYLQGRI 105
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIG----GAPLSALLPLLGLLLAVLLLRALLAWLRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 106 MISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLA 185
Cdd:COG4988 82 AFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 186 VVTIVVSPII----AKIGTAIAGKSRKYFmKQQTDLGkvnGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNS---Q 258
Cdd:COG4988 162 LILLVTAPLIplfmILVGKGAAKASRRQW-RALARLS---GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRtmkV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 259 VKAQFISGIMgpcMNAMSQVNYTLTAcVGSIIAFAsrwGGGVPFSAldigGLTVFVnYSRQFSRPINELAQQVTNIMSAL 338
Cdd:COG4988 238 LRVAFLSSAV---LEFFASLSIALVA-VYIGFRLL---GGSLTLFA----ALFVLL-LAPEFFLPLRDLGSFYHARANGI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 339 AGAERVFNVMDEAEE-IDDGKKLVLDKVHGDVLVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITR 417
Cdd:COG4988 306 AAAEKIFALLDAPEPaAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 418 FYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDT 497
Cdd:COG4988 386 FLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDT 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 498 MLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLE 577
Cdd:COG4988 466 PLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLD 545
|
570
....*....|....*...
gi 524455117 578 NGEIIERGTHEELLEKKG 595
Cdd:COG4988 546 DGRIVEQGTHEELLAKNG 563
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
28-600 |
4.21e-117 |
|
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: 360.17 E-value: 4.21e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 28 LFSYLEQEKHKIAAAFVCVLVSSASTLCGSYLLRPII-NGLidsTKTSQQKITSLMAGLALMAVVYVLGVGATYLqgrIM 106
Cdd:TIGR02204 9 LWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIdHGF---SKDSSGLLNRYFAFLLVVALVLALGTAARFY---LV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 107 ISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTN----- 181
Cdd:TIGR02204 83 TWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSpklts 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 182 WVLAVVTIVVSPIIAkigtaIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEF-SELNQSLRNS--- 257
Cdd:TIGR02204 163 LVLLAVPLVLLPILL-----FGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFgGAVEKAYEAArqr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 258 -QVKAQFISGIMgpcmnamsqvnytlTACVGSIIAFAsrWGGG--VPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNI 334
Cdd:TIGR02204 238 iRTRALLTAIVI--------------VLVFGAIVGVL--WVGAhdVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 335 MSALAGAERVFNVMDEAEEIDDGK--KLVLDKVHGDVLVEGVTFGY--NPDKTILKDVSIFAHPGQKIALVGSTGAGKTT 410
Cdd:TIGR02204 302 QRAAGAAERLIELLQAEPDIKAPAhpKTLPVPLRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKST 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 411 ITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKN 490
Cdd:TIGR02204 382 LFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 491 MPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNA 570
Cdd:TIGR02204 462 LPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKA 541
|
570 580 590
....*....|....*....|....*....|
gi 524455117 571 DAIMVLENGEIIERGTHEELLEKKGRYFEL 600
Cdd:TIGR02204 542 DRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
367-595 |
6.13e-116 |
|
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: 344.59 E-value: 6.13e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVLVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIA 446
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 447 MVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPI 526
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 527 LVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKG 595
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
369-601 |
7.13e-116 |
|
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: 344.60 E-value: 7.13e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPDKT-ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAM 447
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 448 VLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPIL 527
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 528 VLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFELY 601
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
369-601 |
4.32e-107 |
|
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: 322.26 E-value: 4.32e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMV 448
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILV 528
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 529 LDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFELY 601
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
114-601 |
5.74e-107 |
|
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: 333.66 E-value: 5.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 114 LKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLA-------V 186
Cdd:COG4987 87 LADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALAlvlalglL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 187 VTIVVSPIIAkigtaiAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISG 266
Cdd:COG4987 167 LAGLLLPLLA------ARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 267 IMgpcmNAMSQVNYTLTACVGSIIAFASRWGGGVPFSALDIGGLTVFvnysrqfsrPINE----LAQQVTNIMSALAGAE 342
Cdd:COG4987 241 LA----QALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAL---------ALFEalapLPAAAQHLGRVRAAAR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 343 RVFNVMDEAEEIDDGKKLVLDKVHGDVLVEGVTFGY-NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNI 421
Cdd:COG4987 308 RLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 422 NKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKG 501
Cdd:COG4987 388 QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 502 DGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEI 581
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
490 500
....*....|....*....|
gi 524455117 582 IERGTHEELLEKKGRYFELY 601
Cdd:COG4987 548 VEQGTHEELLAQNGRYRQLY 567
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
372-602 |
8.25e-101 |
|
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: 306.00 E-value: 8.25e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 372 EGVTFGY--NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVL 449
Cdd:cd03249 4 KNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVL 529
Cdd:cd03249 84 QEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 530 DEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFELYT 602
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-600 |
1.39e-98 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 315.89 E-value: 1.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 5 GPPNRNRNQKKQKPKNTKATAKRLFSYLEQEKHKIAAAFVCVLVSSASTLCGSYLLRPIINGLIdsTKTSQQKITSLMAG 84
Cdd:TIGR00958 129 SSAGASEKEAEQGQSETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLG--GDKGPPALASAIFF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 85 LALMAVVYVLGVGA-----TYLQGRIMisvsqgtlKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNST 159
Cdd:TIGR00958 207 MCLLSIASSVSAGLrggsfNYTMARIN--------LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLN 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 160 LVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNY 239
Cdd:TIGR00958 279 VNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 240 EENVVNEFSE-LNQSLRNSQVKAqfisgimgpcmnaMSQVNYTLTACV-GSIIAFASRWGGG--VPFSALDIGGLTVFVN 315
Cdd:TIGR00958 359 EEGEASRFKEaLEETLQLNKRKA-------------LAYAGYLWTTSVlGMLIQVLVLYYGGqlVLTGKVSSGNLVSFLL 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 316 YSRQFSRPINELAQQVTNIMSALAGAERVFNVMDEAEEIDDGKKLVLDKVHGDVLVEGVTFGY--NPDKTILKDVSIFAH 393
Cdd:TIGR00958 426 YQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLH 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 394 PGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDE 473
Cdd:TIGR00958 506 PGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 474 EVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDAlmE 553
Cdd:TIGR00958 586 EIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--A 663
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 524455117 554 DRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFEL 600
Cdd:TIGR00958 664 SRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
286-600 |
7.67e-98 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 310.35 E-value: 7.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 286 VGSIIAFasrwgggVPFSALDIGGLTVFVNYsrqfsrpinelaqqVTNIMSALAGAERVFNVMDEAEEIDDGKKLV-LDK 364
Cdd:PRK13657 272 VGEVVAF-------VGFATLLIGRLDQVVAF--------------INQVFMAAPKLEEFFEVEDAVPDVRDPPGAIdLGR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 365 VHGDVLVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLREN 444
Cdd:PRK13657 331 VKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 445 IAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKA 524
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 525 PILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFEL 600
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-601 |
1.82e-90 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 291.24 E-value: 1.82e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 24 TAKRLFSYLEQEKHKIAAAFVCVLVSSASTLCGSYLlrpiINGLIDSTKTSQQKITSLMAGLALMAVVY-VLGVGATYLQ 102
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLL----ISYFIDNMVAKGNLPLGLVAGLAAAYVGLqLLAAGLHYAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 103 GRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEmLNSTLVQIFSGTITLIGT-LALMLYTN 181
Cdd:PRK10790 86 SLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD-LYVTVVATVLRSAALIGAmLVAMFSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 182 WVLAVVTIVVSP-------IIAKIGTAIAGKSRKYfmkqqtdLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSL 254
Cdd:PRK10790 165 WRMALVAIMIFPavlvvmvIYQRYSTPIVRRVRAY-------LADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 255 RNSQVKAQFISG-IMGPCMNAMSqvnyTLTACvGSIIAFasrwgGGVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTN 333
Cdd:PRK10790 238 YMARMQTLRLDGfLLRPLLSLFS----ALILC-GLLMLF-----GFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSM 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 334 IMSALAGAERVFNVMDEAEEI--DDGKKLVldkvHGDVLVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTI 411
Cdd:PRK10790 308 LQQAVVAGERVFELMDGPRQQygNDDRPLQ----SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 412 TNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRlSATDEEVRQAAKTSCADMFIKNM 491
Cdd:PRK10790 384 ASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 492 PEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNAD 571
Cdd:PRK10790 463 PDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEAD 542
|
570 580 590
....*....|....*....|....*....|
gi 524455117 572 AIMVLENGEIIERGTHEELLEKKGRYFELY 601
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
85-600 |
6.88e-88 |
|
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: 287.61 E-value: 6.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 85 LALMAVVYVLGVGATYLQG----RIMISVSQGTLKRIREHLFRkvqkLPVRYFDTNPTGDIMSRFTNDvDIIGEMLNSTL 160
Cdd:TIGR03796 197 LLGMGLTALLQGVLTWLQLyylrRLEIKLAVGMSARFLWHILR----LPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 161 VQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGyieETVTGQKV---VKVF 237
Cdd:TIGR03796 272 ATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTG---VAISGLQSietLKAS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 238 NYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQVNYTLTACVGSIIAFASRwgggvpfsaLDIGGLTVFVNYS 317
Cdd:TIGR03796 349 GLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQ---------LTIGMLVAFQSLM 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 318 RQFSRPINELAQQVTNIMSALAGAERVFNVMD-------EAEEIDDGKKLVLDKVHGDVLVEGVTFGYNP-DKTILKDVS 389
Cdd:TIGR03796 420 SSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRnpvdpllEEPEGSAATSEPPRRLSGYVELRNITFGYSPlEPPLIENFS 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 390 IFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLS 469
Cdd:TIGR03796 500 LTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 470 ATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMd 549
Cdd:TIGR03796 580 IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL- 658
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 550 almedR----TTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFEL 600
Cdd:TIGR03796 659 -----RrrgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
43-600 |
6.87e-87 |
|
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: 284.54 E-value: 6.87e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 43 FVCVLVSS-ASTLCGsyLLRPIINGLI------DSTKTSQQKITSLMAGLALMAVVYVLGVGATYLqgRIMISVSQGTLK 115
Cdd:TIGR03797 138 LLAILAMGlLGTLLG--MLVPIATGILigtaipDADRSLLVQIALALLAAAVGAAAFQLAQSLAVL--RLETRMDASLQA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 116 RIREHLFRkvqkLPVRYFDTNPTGDIMSRfTNDVDIIGEMLN-STLVQIFSGTITLIgTLALMLYTNWVLAVVTIVVSPI 194
Cdd:TIGR03797 214 AVWDRLLR----LPVSFFRQYSTGDLASR-AMGISQIRRILSgSTLTTLLSGIFALL-NLGLMFYYSWKLALVAVALALV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 195 IAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISgimgpcmNA 274
Cdd:TIGR03797 288 AIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIE-------NL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 275 MSQVNYTLTA-CVGSIIAFASRWGGGvpfSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERVFNVMDEAEE 353
Cdd:TIGR03797 361 LTVFNAVLPVlTSAALFAAAISLLGG---AGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 354 IDDGKKLVlDKVHGDVLVEGVTFGYNPD-KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVD 432
Cdd:TIGR03797 438 VDEAKTDP-GKLSGAIEVDRVTFRYRPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 433 IKDISLECLRENIAMVLQDTHLFTGTIMENIrYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQ 512
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQ 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 513 LLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALmeDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLE 592
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
....*...
gi 524455117 593 KKGRYFEL 600
Cdd:TIGR03797 674 REGLFAQL 681
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
27-600 |
2.79e-82 |
|
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: 269.45 E-value: 2.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 27 RLFSYLEQEKHKIAAAFVCVLVSSASTLCgsyllRPIINGLIDSTKTSQQKITSLmagLALMAVVYVLGVGATYLQGRIM 106
Cdd:TIGR01192 9 RALSYLNVHKNRVLLIVIANITLAAITIA-----EPILFGRIIDAISSKSDVLPT---LALWAGFGVFNTIAYVLVAREA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 107 ISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAV 186
Cdd:TIGR01192 81 DRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 187 VTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKA----Q 262
Cdd:TIGR01192 161 VLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVldwwA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 263 FISGimgpcMNAM-SQVNYTLTACVGSIIafasrwgggVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGA 341
Cdd:TIGR01192 241 LASG-----LNRMaSTISMMCILVIGTVL---------VIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 342 ERVFNVMDEAEEIDD-GKKLVLDKVHGDVLVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYN 420
Cdd:TIGR01192 307 EDFFDLEDSVFQREEpADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 421 INKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLK 500
Cdd:TIGR01192 387 PTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 501 GDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGE 580
Cdd:TIGR01192 467 ERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGR 546
|
570 580
....*....|....*....|
gi 524455117 581 IIERGTHEELLEKKGRYFEL 600
Cdd:TIGR01192 547 LIEKGSFQELIQKDGRFYKL 566
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
367-586 |
9.47e-77 |
|
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: 243.17 E-value: 9.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVLVEGVTFGYNPD-KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENI 445
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 446 AMVLQDTHLFTGTIMENIR-YGRlsATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKA 524
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 525 PILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGT 586
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
369-601 |
3.59e-75 |
|
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: 239.70 E-value: 3.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPD-KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAM 447
Cdd:cd03252 1 ITFEHVRFRYKPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 448 VLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPIL 527
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 528 VLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFELY 601
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
39-344 |
1.07e-74 |
|
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: 240.37 E-value: 1.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIdstKTSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIR 118
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYI---VPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 119 EHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKI 198
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 199 GTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQV 278
Cdd:cd18544 158 TYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 279 nytltaCVGSIIAFAsrwGGGVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18544 238 ------ALALVLWYG---GGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
371-580 |
1.15e-74 |
|
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: 235.74 E-value: 1.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNP-DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVL 449
Cdd:cd03228 3 FKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHLFTGTIMENIrygrlsatdeevrqaaktscadmfiknmpegydtmlkgdgsnLSQGQRQLLNIARAALSKAPILVL 529
Cdd:cd03228 83 QDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524455117 530 DEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGE 580
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-602 |
1.07e-73 |
|
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: 249.66 E-value: 1.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 14 KKQKP-KNTKATAKRLFSYLEQEKHKIA----AAFVCVLVSSAstlcGSYLLRPIINGLIDSTKTSQQKITSLMaglalM 88
Cdd:TIGR01193 132 PEYKPiKEKENSLLKFIPLITRQKKLIVniviAAIIVTLISIA----GSYYLQKIIDTYIPHKMMGTLGIISIG-----L 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 89 AVVYVLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTnDVDIIGEMLNSTLVQIFSGTI 168
Cdd:TIGR01193 203 IIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMW 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 169 TLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIagksRKYFMKQQTDLGK----VNGYIEETVTGQKVVKVFNYEENVV 244
Cdd:TIGR01193 282 ILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILF----KRTFNKLNHDAMQanavLNSSIIEDLNGIETIKSLTSEAERY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 245 N----EFSE-LNQSLRNSQVKaqfisgimgpcmnamsQVNYTLTACVGSIIAFASRWGGG--VPFSALDIGGLTVFVNYS 317
Cdd:TIGR01193 358 SkidsEFGDyLNKSFKYQKAD----------------QGQQAIKAVTKLILNVVILWTGAylVMRGKLTLGQLITFNALL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 318 RQFSRPINELAQQVTNIMSALAGAERVFNV-MDEAEEIDDGKKLVLDKVHGDVLVEGVTFGYNPDKTILKDVSIFAHPGQ 396
Cdd:TIGR01193 422 SYFLTPLENIINLQPKLQAARVANNRLNEVyLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNS 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 397 KIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYG-RLSATDEEV 475
Cdd:TIGR01193 502 KTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEI 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 476 RQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMdALMEDR 555
Cdd:TIGR01193 582 WAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDK 660
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 524455117 556 TTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFELYT 602
Cdd:TIGR01193 661 TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
57-576 |
1.41e-73 |
|
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: 244.89 E-value: 1.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 57 SYLLRPIINGLIdSTKTSQQKITSLMAGLALMAVVYVLgvgATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTN 136
Cdd:TIGR02857 23 AWLLARVVDGLI-SAGEPLAELLPALGALALVLLLRAL---LGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 137 PTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPII----AKIGTAIAGKSRKyfmk 212
Cdd:TIGR02857 99 PSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIpifmILIGWAAQAAARK---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 213 QQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRN---SQVKAQFISGIMGPCMNAMSqvnytlTACVGSI 289
Cdd:TIGR02857 175 QWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRErtmRVLRIAFLSSAVLELFATLS------VALVAVY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 290 IAFaSRWGGGVPFSAldigGLTVFVnYSRQFSRPINELAQQVTNIMSALAGAERVFNVMDEAEEIDDGKKLVLDKVHGDV 369
Cdd:TIGR02857 249 IGF-RLLAGDLDLAT----GLFVLL-LAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 370 LVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVL 449
Cdd:TIGR02857 323 EFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVL 529
Cdd:TIGR02857 403 QHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 524455117 530 DEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVL 576
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
38-344 |
5.75e-72 |
|
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: 233.13 E-value: 5.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 38 KIAAAFVCVLVSSASTLCGSYLLRPIINGLIdstktSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRI 117
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYI-----PNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 118 REHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAK 197
Cdd:cd18545 76 RQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 198 IGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQ 277
Cdd:cd18545 156 VVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISA 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 278 VNYTLtacvgsIIAFASRW-GGGvpfsALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18545 236 LGTAL------VYWYGGKLvLGG----AITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
59-601 |
1.46e-68 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 232.68 E-value: 1.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 59 LLRPIINGLI-DSTKTSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNP 137
Cdd:PRK10789 12 LIPPKVVGIIvDGVTEQHMTTGQILMWIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLSRQHPEFYLRHR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 138 TGDIMSRFTNDVDII----GEmlnstlvqifsGTITLIGTLAL------MLYT--NWVLAVVTIVVSPIIAKIGTAIAGK 205
Cdd:PRK10789 92 TGDLMARATNDVDRVvfaaGE-----------GVLTLVDSLVMgcavliVMSTqiSWQLTLLALLPMPVMAIMIKRYGDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 206 SRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSEL-----NQSLRNSQVKAQFISGIMgpcmnamsqvny 280
Cdd:PRK10789 161 LHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADaedtgKKNMRVARIDARFDPTIY------------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 281 tLTACVGSIIAFasrwGGG---VPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERVFNVMDEAEEIDDG 357
Cdd:PRK10789 229 -IAIGMANLLAI----GGGswmVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 358 KKlVLDKVHGDVLVEGVTFGY-NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDI 436
Cdd:PRK10789 304 SE-PVPEGRGELDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 437 SLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNI 516
Cdd:PRK10789 383 QLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISI 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 517 ARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGR 596
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGW 542
|
....*
gi 524455117 597 YFELY 601
Cdd:PRK10789 543 YRDMY 547
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
39-344 |
1.61e-68 |
|
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: 224.35 E-value: 1.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIdstktSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIR 118
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI-----PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 119 EHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKI 198
Cdd:cd07346 76 RDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 199 GTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQV 278
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 279 NYTLTACVGsiiafASRWGGGvpfsALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd07346 236 GTALVLLYG-----GYLVLQG----SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
367-585 |
1.49e-63 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 208.60 E-value: 1.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVLVEGVTFGYNPDKT-ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENI 445
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 446 AMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAP 525
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 526 ILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERG 585
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
360-581 |
4.56e-61 |
|
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: 202.32 E-value: 4.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 360 LVLDKVHGDVLVEGVTFGY--NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS 437
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 438 LECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIA 517
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 518 RAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEI 581
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
39-344 |
7.15e-61 |
|
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: 203.81 E-value: 7.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIdstktSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIR 118
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIF-----VEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 119 EHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKI 198
Cdd:cd18552 76 NDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 199 GTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSqv 278
Cdd:cd18552 156 IRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLG-- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 279 nytlTACVGSIIAFAsrwGGGVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18552 234 ----AIAIALVLWYG---GYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
43-600 |
1.45e-60 |
|
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: 218.66 E-value: 1.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 43 FVCvlvSSASTLCGSYLLRPIIN-GLIDSTKTSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISvsqgtlKRIREHL 121
Cdd:TIGR00957 974 FVC---NHVSALASNYWLSLWTDdPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQAS------RVLHQDL 1044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 122 FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTA 201
Cdd:TIGR00957 1045 LHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRF 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 202 IAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEEnvvnEFSELNQSLRNSQVKAQFisgimgPCMNAMSQVNYT 281
Cdd:TIGR00957 1125 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQE----RFIHQSDLKVDENQKAYY------PSIVANRWLAVR 1194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 282 LTaCVGSIIAFASRWGGGVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERVfnvmDEAEEIDDGKKLV 361
Cdd:TIGR00957 1195 LE-CVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERL----KEYSETEKEAPWQ 1269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 362 LDKVH--------GDVLVEGVTFGYNPD-KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVD 432
Cdd:TIGR00957 1270 IQETAppsgwpprGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 433 IKDISLECLRENIAMVLQDTHLFTGTIMENIR-YGRLSatDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQR 511
Cdd:TIGR00957 1350 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQYS--DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQR 1427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 512 QLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELL 591
Cdd:TIGR00957 1428 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
....*....
gi 524455117 592 EKKGRYFEL 600
Cdd:TIGR00957 1508 QQRGIFYSM 1516
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
338-601 |
5.21e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 209.68 E-value: 5.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 338 LAGAERVFNVMDEAEEIDDGKKLVLDKVHGDVLVEGVTFGYnPDKT--ILKDVSIFAHPGQKIALVGSTGAGKTTITNLI 415
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTY-PDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 416 TRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNmPEGY 495
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 496 DTMLkGDGSN-LSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIM 574
Cdd:PRK11160 466 NAWL-GEGGRqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
250 260
....*....|....*....|....*..
gi 524455117 575 VLENGEIIERGTHEELLEKKGRYFELY 601
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
366-586 |
6.27e-57 |
|
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: 190.70 E-value: 6.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 366 HGDVLVEGVTFGYNPD-KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLREN 444
Cdd:cd03369 4 HGEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 445 IAMVLQDTHLFTGTIMENI-RYGRLSatDEEVRQAAKTScadmfiknmpEGydtmlkgdGSNLSQGQRQLLNIARAALSK 523
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALRVS----------EG--------GLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 524 APILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGT 586
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
73-598 |
2.59e-55 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 203.28 E-value: 2.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 73 TSQQKITSLMAGLALmaVVYVL----GVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTND 148
Cdd:PLN03232 939 TDQSTPKSYSPGFYI--VVYALlgfgQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKD 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 149 V-DI---IGEMLNSTLVQIFS--GTITLIGT-----------LALMLYTNW---------VLAVVTIVVSPIIAKIGTAI 202
Cdd:PLN03232 1017 IgDIdrnVANLMNMFMNQLWQllSTFALIGTvstislwaimpLLILFYAAYlyyqstsreVRRLDSVTRSPIYAQFGEAL 1096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 203 AGKSRKYFMKQQTDLGKVNGyieetvtgqkvvkvfNYEENVVnEFSELN-QSLRNSQVKAQFISGIMGPCMNAMSQVNYT 281
Cdd:PLN03232 1097 NGLSSIRAYKAYDRMAKING---------------KSMDNNI-RFTLANtSSNRWLTIRLETLGGVMIWLTATFAVLRNG 1160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 282 LTAcvgSIIAFASRWGggvpfsaldiggltVFVNYSRQFSRPINELAQQVTNIMSALAGAERVFNVMD---EAEEIDDGK 358
Cdd:PLN03232 1161 NAE---NQAGFASTMG--------------LLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDlpsEATAIIENN 1223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 359 KLVLD-KVHGDVLVEGVTFGYNPD-KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDI 436
Cdd:PLN03232 1224 RPVSGwPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF 1303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 437 SLECLRENIAMVLQDTHLFTGTIMENIRYGRlSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNI 516
Cdd:PLN03232 1304 GLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSL 1382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 517 ARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGR 596
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
..
gi 524455117 597 YF 598
Cdd:PLN03232 1463 AF 1464
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
40-344 |
1.03e-54 |
|
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: 187.64 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 40 AAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQqkitsLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIRE 119
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRIIDSVIGGGLREL-----LWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 120 HLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIG 199
Cdd:cd18542 77 DLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 200 TAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQVN 279
Cdd:cd18542 157 YVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 280 YTLTACVGSIIAFASRwgggvpfsaLDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18542 237 IVLVLWVGGYLVINGE---------ITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
381-602 |
4.38e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 191.21 E-value: 4.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRF--YninKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGT 458
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 459 IMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDT 538
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 539 RTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFELYT 602
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-344 |
3.30e-52 |
|
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: 181.17 E-value: 3.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIdSTKTSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIR 118
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVL-IQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 119 EHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKI 198
Cdd:cd18563 80 RDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 199 GTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQv 278
Cdd:cd18563 160 SYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTS- 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 279 nytltacVGSIIAfasrWGGGVPF---SALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18563 239 -------LGTLIV----WYFGGRQvlsGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
26-564 |
4.53e-52 |
|
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: 187.18 E-value: 4.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 26 KRLFSYLEQEKHKIAAAF---VCVLVSSASTLCGS-YLLrpiinglidsTKTSQQKitslmAGLALM-AVVYV--LGVG- 97
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVllgALALGSAVALLGVSaWLI----------SRAAEMP-----PVLYLSvAAVAVraFGIGr 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 98 --ATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLA 175
Cdd:TIGR02868 67 avFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 176 LMLYTNWVLA-------VVTIVVSPIIAKIGTAIAGKSRKY----FMKQQTDLgkVNGYIEETVTGQKvvkvfnyeENVV 244
Cdd:TIGR02868 147 AIAVLSVPAAlilaaglLLAGFVAPLVSLRAARAAEQALARlrgeLAAQLTDA--LDGAAELVASGAL--------PAAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 245 NEFSELNQSLRNSQVKAQFISGIMgpcmNAMSQVNYTLTACVGSIIAFASRWGGGVP---FSALDIGGLTVFVNYSrqfs 321
Cdd:TIGR02868 217 AQVEEADRELTRAERRAAAATALG----AALTLLAAGLAVLGALWAGGPAVADGRLApvtLAVLVLLPLAAFEAFA---- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 322 rPINELAQQVTnimSALAGAERVFNVMDEAEEIDDG-----KKLVLDKVhgDVLVEGVTFGYNPDKTILKDVSIFAHPGQ 396
Cdd:TIGR02868 289 -ALPAAAQQLT---RVRAAAERIVEVLDAAGPVAEGsapaaGAVGLGKP--TLELRDLSAGYPGAPPVLDGVSLDLPPGE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 397 KIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRYGRLSATDEEVR 476
Cdd:TIGR02868 363 RVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELW 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 477 QAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRT 556
Cdd:TIGR02868 443 AALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRT 522
|
....*...
gi 524455117 557 TFVIAHRL 564
Cdd:TIGR02868 523 VVLITHHL 530
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
39-324 |
1.89e-51 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 178.22 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSLmagLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIR 118
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVY---SLALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 119 EHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKI 198
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 199 GTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQV 278
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 524455117 279 NYTLTACVGSIIAFAsrwgggvpfSALDIGGLTVFVNYSRQFSRPI 324
Cdd:pfam00664 238 SYALALWFGAYLVIS---------GELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-344 |
1.17e-50 |
|
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: 177.32 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSLMAGL----------ALMAVVYVLGVGATYLQGRIMIS 108
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPLLGPdplallllaaAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 109 VSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVT 188
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 189 IVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIM 268
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 269 GPCmnamsqVNYTLTACVGSIIAFASRwggGVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18564 241 SPV------VDVLVAVGTALVLWFGAW---LVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
39-344 |
6.10e-50 |
|
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: 174.54 E-value: 6.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLcgsylLRP-IINGLIDSTKTSQQKITSLMAGLALMAVVYVLGVGATYLQGRImisvSQGTLKRI 117
Cdd:cd18551 1 LILALLLSLLGTAASL-----AQPlLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRT----GERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 118 REHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAK 197
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 198 IGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQ 277
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 278 VnytltaCVGSIIAFasrwgGGVPFS--ALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18551 232 L------ALLVVLGV-----GGARVAsgALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
39-344 |
3.17e-49 |
|
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: 173.06 E-value: 3.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRpiiNGlIDSTKTSQQKITSLMAGLALMAVVyVLGVGATYLQGRIMISVSQGTLKRIR 118
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVR---YG-IDSGVRAGDLGVLLLAAAAYLAVV-LAGWVAQRAQTRLTGRTGERLLYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 119 EHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAkI 198
Cdd:cd18546 76 LRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLA-L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 199 GTAIAGK-SRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQ 277
Cdd:cd18546 155 ATRWFRRrSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGN 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 278 VNYTLTACVGsiiafASRWGGGvpfsALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18546 235 LATAAVLLVG-----AWRVAAG----TLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-344 |
4.12e-49 |
|
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: 172.72 E-value: 4.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKtSQQKITSLMAGLAlmaVVYVLGVGATYLQGRIMISVSQGTLKRIR 118
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSK-SLGLLLGLALLLL---GAYLLRALLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 119 EHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKI 198
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 199 GTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQV 278
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 279 NYTLTACVGSIIAFASRwgggvpfsaLDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18778 237 GTVLVLGFGGRLVLAGE---------LTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-592 |
7.81e-47 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 177.91 E-value: 7.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 16 QKPKNTKATAKrLFSYLEQEK-------------HK--IAAAFVCVLVSSastlcGSYLLRPIINGLIDSTKTSQQKITS 80
Cdd:PTZ00265 25 EKELNKKGTFE-LYKKIKTQKipfflpfkclpasHRklLGVSFVCATISG-----GTLPFFVSVFGVIMKNMNLGENVND 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 81 LMAGLALMAVV-YVLGVGATYlqgrIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTgdimSRFTNDVDIIGEMLNST 159
Cdd:PTZ00265 99 IIFSLVLIGIFqFILSFISSF----CMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 160 L----VQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTaIAGKSRKyfMKQQTDLGKVN---GYIEETVTGQK 232
Cdd:PTZ00265 171 IgtkfITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGV-ICNKKVK--INKKTSLLYNNntmSIIEEALVGIR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 233 VVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQVNYTLTACVGS--IIAFASR------WGGGVPFSA 304
Cdd:PTZ00265 248 TVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTriIISDLSNqqpnndFHGGSVISI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 305 LdiggLTVFVNysrQFSRPIneLAQQVTNIMSALAGAERVFNVMDE---AEEIDDGKKLvldKVHGDVLVEGVTFGYN-- 379
Cdd:PTZ00265 328 L----LGVLIS---MFMLTI--ILPNITEYMKSLEATNSLYEIINRkplVENNDDGKKL---KDIKKIQFKNVRFHYDtr 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 380 PDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITI-DGVDIKDISLECLRENIAMVLQDTHLFTGT 458
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 459 IMENIRYGRLSATDEEV------------------RQAAKTSCA----DM------------------------------ 486
Cdd:PTZ00265 476 IKNNIKYSLYSLKDLEAlsnyynedgndsqenknkRNSCRAKCAgdlnDMsnttdsneliemrknyqtikdsevvdvskk 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 487 -----FIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALM--EDRTTFV 559
Cdd:PTZ00265 556 vlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITII 635
|
650 660 670
....*....|....*....|....*....|...
gi 524455117 560 IAHRLSTIRNADAIMVLENGEIIERGTHEELLE 592
Cdd:PTZ00265 636 IAHRLSTIRYANTIFVLSNRERGSTVDVDIIGE 668
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
36-344 |
1.34e-46 |
|
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: 165.73 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 36 KHKIAAAFVCVLVSSASTLCGSYLLRPIINGLIdsTKTSQQKITSLMAGLALMAVVYVLGV-GATYLQGRIMISVSqgtl 114
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFI--TPGTLDGLTGFILLYLGLILIQALSVfLFIRLAGKIEMGVS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 115 KRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPI 194
Cdd:cd18540 75 YDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 195 IAkigtAIAGKSRKYFMKQQTDLGKVNGYI----EETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGP 270
Cdd:cd18540 155 LA----VVSIYFQKKILKAYRKVRKINSRItgafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLP 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 271 CMNAMSQVNYTLTACVGSIIAFAsrwgggvpfSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18540 231 IVLFLGSIATALVLWYGGILVLA---------GAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
367-598 |
3.72e-46 |
|
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: 163.54 E-value: 3.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVLVEGVTFGY-NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENI 445
Cdd:cd03288 18 GEIKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 446 AMVLQDTHLFTGTIMENIRYGRlSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAP 525
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 526 ILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYF 598
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
106-598 |
9.50e-46 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 174.54 E-value: 9.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 106 MISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDV-DI---IGEMLNSTLVQIFS--GTITLIG------- 172
Cdd:PLN03130 977 LIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLgDIdrnVAVFVNMFLGQIFQllSTFVLIGivstisl 1056
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 173 ----TLALMLYTNW---------VLAVVTIVVSPIIAKIGTAIAGKS--RKYfmKQQTDLGKVNGYIEETvtgqkvvkvf 237
Cdd:PLN03130 1057 waimPLLVLFYGAYlyyqstareVKRLDSITRSPVYAQFGEALNGLStiRAY--KAYDRMAEINGRSMDN---------- 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 238 NYEENVVNEFSelNQSLrnsQVKAQFISGIMgpcmnamsqVNYTLTACV------GSIIAFASRWGGGVPFsALDIGGLT 311
Cdd:PLN03130 1125 NIRFTLVNMSS--NRWL---AIRLETLGGLM---------IWLTASFAVmqngraENQAAFASTMGLLLSY-ALNITSLL 1189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 312 VFVnySRQFSRPINelaqqvtnimsALAGAERVFNVMDEAEE----IDDGKKLVLDKVHGDVLVEGVTFGYNPD-KTILK 386
Cdd:PLN03130 1190 TAV--LRLASLAEN-----------SLNAVERVGTYIDLPSEaplvIENNRPPPGWPSSGSIKFEDVVLRYRPElPPVLH 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 387 DVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIR-Y 465
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDpF 1336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 466 GRLSatDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHIN 545
Cdd:PLN03130 1337 NEHN--DADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ 1414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 524455117 546 EGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYF 598
Cdd:PLN03130 1415 KTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
69-593 |
1.15e-45 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 169.84 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 69 DSTKTSQQKITSLMAGLaLMAVVYVLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRyfdtNPTGDiMSRFTND 148
Cdd:TIGR01842 34 DRVLTSGSVPTLLMLTV-LALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLR----RGSGD-GLQALRD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 149 VDIIGEMLNST-LVQIFSGTITLIGTLALMLYTNWvLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEET 227
Cdd:TIGR01842 108 LDQLRQFLTGPgLFAFFDAPWMPIYLLVCFLLHPW-IGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 228 VTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQVNYTLTACVGSIIAFASRWGGGVPFSALDI 307
Cdd:TIGR01842 187 LRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSIL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 308 GGltvfvnysRQFSrPINELAQQVTNIMSALAGAERVFNVMDEAEEIDDgkKLVLDKVHGDVLVEGVTFGY-NPDKTILK 386
Cdd:TIGR01842 267 VG--------RALA-PIDGAIGGWKQFSGARQAYKRLNELLANYPSRDP--AMPLPEPEGHLSVENVTIVPpGGKKPTLR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 387 DVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENI-RY 465
Cdd:TIGR01842 336 GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 466 GRlSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHIN 545
Cdd:TIGR01842 416 GE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALA 494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 524455117 546 EGMDAL-MEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEK 593
Cdd:TIGR01842 495 NAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
86-593 |
1.17e-45 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 169.93 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 86 ALMAVVYVLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDImsrftNDVDIIGEMLNST------ 159
Cdd:COG4618 64 LLALGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGAAAQAL-----RDLDTLRQFLTGPglfalf 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 160 --------LVQIFS-----GTITLIGTLALMLytnwvLAVVTIVVSpiiakigtaiagksRKYFMKQQTDLGKVNGYIEE 226
Cdd:COG4618 139 dlpwapifLAVLFLfhpllGLLALVGALVLVA-----LALLNERLT--------------RKPLKEANEAAIRANAFAEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 227 TVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGpcmnAMSQ-VNYTLTACV---------------GSII 290
Cdd:COG4618 200 ALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFS----ALSKfLRLLLQSAVlglgaylviqgeitpGAMI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 291 A---FASRwgggvpfsALdiggltvfvnysrqfsRPINELAQQVTNIMSALAGAERVFNVMDEAEEidDGKKLVLDKVHG 367
Cdd:COG4618 276 AasiLMGR--------AL----------------APIEQAIGGWKQFVSARQAYRRLNELLAAVPA--EPERMPLPRPKG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 368 DVLVEGVTFGYNP-DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIA 446
Cdd:COG4618 330 RLSVENLTVVPPGsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 447 MVLQDTHLFTGTIMENI-RYGrlSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAP 525
Cdd:COG4618 410 YLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 526 ILVLDEATSSVDTRTEKHINEGMDALMEDRTT-FVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEK 593
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKARGATvVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
39-344 |
3.79e-45 |
|
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: 161.81 E-value: 3.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSLMAGLALMAVVYVLgvgaTYLQGRIMISVSQGTLKRIR 118
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIF----RFLWRYLIFGASRRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 119 EHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKI 198
Cdd:cd18541 77 NDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 199 GTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQV 278
Cdd:cd18541 157 VYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 279 NYTLTACVGSIIAFASRwgggvpfsaLDIGGLTVFVNYSRQFSRPINELAqQVTNIMS-ALAGAERV 344
Cdd:cd18541 237 SFLIVLWYGGRLVIRGT---------ITLGDLVAFNSYLGMLIWPMMALG-WVINLIQrGAASLKRI 293
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
43-343 |
6.42e-44 |
|
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: 158.77 E-value: 6.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 43 FVCVLVSSASTLCGSYLLRPIINGLIdstktSQQKITSLMAGLALMAVVYVLGVGATYL---QGRIMisvsqGTL--KRI 117
Cdd:cd18549 8 LFCAVLIAALDLVFPLIVRYIIDDLL-----PSKNLRLILIIGAILLALYILRTLLNYFvtyWGHVM-----GARieTDM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 118 REHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAK 197
Cdd:cd18549 78 RRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 198 IGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQ 277
Cdd:cd18549 158 FTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTN 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 278 VNYTLTACVGSIIAFASRwgggvpfsaLDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAER 343
Cdd:cd18549 238 LLNLVVLVAGGYFIIKGE---------ITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
355-604 |
2.39e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 167.51 E-value: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 355 DDGKKLVLDK--VHGDVLVEGVTFGY--NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNI--------- 421
Cdd:PTZ00265 1150 DNGGIRIKNKndIKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfk 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 422 ---------------------------------------------NKGKITIDGVDIKDISLECLRENIAMVLQDTHLFT 456
Cdd:PTZ00265 1230 nehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 457 GTIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSV 536
Cdd:PTZ00265 1310 MSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 537 DTRTEKHINEGMDALME--DRTTFVIAHRLSTIRNADAIMVLEN----GEIIE-RGTHEELLEKKGRYFELYTGL 604
Cdd:PTZ00265 1390 DSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYKKYVKL 1464
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-344 |
4.51e-43 |
|
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: 156.10 E-value: 4.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPII-NGLIdstKTSQQKITSLMAGLALMAVVY-VLGVGATYLQGRImisvSQGTLKR 116
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIdDALP---QGDLGLLVLLALGMVAVAVASaLLGVVQTYLSARI----GQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 117 IREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIA 196
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 197 KIGTAIAGKSRKYFMKQQTDLGKVNGYIEET--VTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGpcmna 274
Cdd:cd18550 154 LPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFF----- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 275 msqVNYTLTACVGSIIAFasrWGGGVPFS--ALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18550 229 ---AALGLFTAIGPALVY---WVGGLLVIggGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
42-344 |
1.32e-42 |
|
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: 154.95 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLIdstktsQQKITSLMAGLAL-MAVVYVLGVGATYLQGRIMISVSQGTLKRIREH 120
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAAL------GGGDTASLNQIALlLLGLFLLQAVFSFFRIYLFARVGERVVADLRKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 121 LFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAkIGT 200
Cdd:cd18576 75 LYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVV-LVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 201 AIAGKS-RKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMnamsqvn 279
Cdd:cd18576 154 VLFGRRiRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFI------- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 280 ytLTACVGSIIAFAsrWGGGVPFSA--LDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18576 227 --IFLLFGAIVAVL--WYGGRLVLAgeLTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
374-585 |
2.75e-41 |
|
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: 147.46 E-value: 2.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTFGYNP-DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISlECLRENIAMVLQDT 452
Cdd:cd03247 6 VSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 453 HLFTGTIMENIrygrlsatdeevrqaaktscadmfiknmpegydtmlkgdGSNLSQGQRQLLNIARAALSKAPILVLDEA 532
Cdd:cd03247 85 YLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 524455117 533 TSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERG 585
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
371-581 |
4.04e-40 |
|
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: 144.28 E-value: 4.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGY-NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVL 449
Cdd:cd03246 3 VENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHLFTGTIMENIrygrlsatdeevrqaaktscadmfiknmpegydtmlkgdgsnLSQGQRQLLNIARaALSKAP-ILV 528
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------LSGGQRQRLGLAR-ALYGNPrILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 524455117 529 LDEATSSVDTRTEKHINEGMDAL-MEDRTTFVIAHRLSTIRNADAIMVLENGEI 581
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
39-344 |
6.03e-40 |
|
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: 147.55 E-value: 6.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQ-QKITSLMAGLALMAVVyvLGVGATYLQGRimisVSQGTLKRI 117
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYiLRTGLLMLLLALLGLI--AGILAGYFAAK----ASQGFGRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 118 REHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAK 197
Cdd:cd18548 75 RKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 198 IGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQ 277
Cdd:cd18548 155 VVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMN 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 278 VnytltaCVGSIIAFASRWgggVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18548 235 L------AIVAILWFGGHL---INAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
39-344 |
8.88e-38 |
|
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: 141.47 E-value: 8.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQqkITSLMAGLALMAVV-YVLGVGATYLQGRimisVSQGTLKRI 117
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSA--LWPLVLLLLALGVAeAVLSFLRRYLAGR----LSLGVEHDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 118 REHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLnSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAK 197
Cdd:cd18543 75 RTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFL-AFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 198 IGtaiAGKSRKYF---MKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNA 274
Cdd:cd18543 154 VA---RRFRRRYFpasRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 275 MSQVnyTLTACVgsiiafasrWGGG--VPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18543 231 LPEL--GLAAVL---------ALGGwlVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
371-594 |
3.88e-37 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 137.85 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQ 450
Cdd:COG1122 3 LENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 --DTHLFTGTIMENIRYG--RLSATDEEVRQAAKTSCADMfiknmpeGYDTMLKGDGSNLSQGQRQLLNIArAALSKAP- 525
Cdd:COG1122 83 npDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEALELV-------GLEHLADRPPHELSGGQKQRVAIA-GVLAMEPe 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 526 ILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTI-RNADAIMVLENGEIIERGTHEELLEKK 594
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
121-598 |
9.17e-37 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 147.23 E-value: 9.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 121 LFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGT 200
Cdd:PTZ00243 1037 LLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQ 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 201 AIAGKSRKyfMKQQTDLGK--VNGYIEETVTGQKVVKVFNYEENVVNE--------FSEL---NQSLRNSQVKAQFISGI 267
Cdd:PTZ00243 1117 FYNSANRE--IRRIKSVAKspVFTLLEEALQGSATITAYGKAHLVMQEalrrldvvYSCSyleNVANRWLGVRVEFLSNI 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 268 mgpcmnamsqvnytltacVGSIIAFASRWGGGVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERVFNV 347
Cdd:PTZ00243 1195 ------------------VVTVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYY 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 348 MDEAE---------EIDDGKK-----------LVLDKVH-----------GDVLVEGVTFGYNPD-KTILKDVSIFAHPG 395
Cdd:PTZ00243 1257 TDEVPhedmpeldeEVDALERrtgmaadvtgtVVIEPASptsaaphpvqaGSLVFEGVQMRYREGlPLVLRGVSFRIAPR 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 396 QKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIRyGRLSATDEEV 475
Cdd:PTZ00243 1337 EKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEV 1415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 476 RQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVL-DEATSSVDTRTEKHINEGMDALMED 554
Cdd:PTZ00243 1416 WAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSA 1495
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 524455117 555 RTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYF 598
Cdd:PTZ00243 1496 YTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
371-596 |
3.70e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 135.76 E-value: 3.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEcLRENIAMVLQ 450
Cdd:COG4555 4 VENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENIRY-GRLSATDEEVRQAAKTSCADMFikNMPEGYDTMLKGdgsnLSQGQRQLLNIARAALSKAPILV 528
Cdd:COG4555 82 ERGLYDRlTVRENIRYfAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 529 LDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTIRN-ADAIMVLENGEIIERGTHEELLEKKGR 596
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
371-593 |
1.48e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 133.65 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEcLRENIAMVLQ 450
Cdd:COG1131 3 VRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENIRY-GRLSATDEEVRQAAKTSCADMFikNMPEGYDTMLKgdgsNLSQGQRQLLNIARAALSKAPILV 528
Cdd:COG1131 81 EPALYPDlTVRENLRFfARLYGLPRKEARERIDELLELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 529 LDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTI-RNADAIMVLENGEIIERGTHEELLEK 593
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
385-534 |
6.04e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 128.92 E-value: 6.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTG-TIMENI 463
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 464 RYGRLsatDEEVRQAAKTSCADMFIKNMPEGY--DTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATS 534
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
86-344 |
7.85e-35 |
|
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: 133.85 E-value: 7.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 86 ALMAVVYVLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFS 165
Cdd:cd18565 58 GLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 166 GTITLIGTLALMLYTNWVLAVVTIVVSPIIA----KIGTAIAgksRKYFMKQQTdLGKVNGYIEETVTGQKVVKVFNYEE 241
Cdd:cd18565 138 VVVTVLGIGAILFYLNWQLALVALLPVPLIIagtyWFQRRIE---PRYRAVREA-VGDLNARLENNLSGIAVIKAFTAED 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 242 NVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQVNYTLTACVGSIIAFAsrwgGGVPFSA-LDIGGLTVFVNYSRQF 320
Cdd:cd18565 214 FERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLD----GPPLFTGtLTVGTLVTFLFYTQRL 289
|
250 260
....*....|....*....|....
gi 524455117 321 SRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18565 290 LWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
371-590 |
8.37e-35 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 131.15 E-value: 8.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINK-----GKITIDGVDI--KDISLECLRE 443
Cdd:cd03260 3 LRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIydLDVDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 NIAMVLQDTHLFTGTIMENIRYG-RL------SATDEEVRQAAKTscADMFiknmPEGYDtmlKGDGSNLSQGQRQLLNI 516
Cdd:cd03260 82 RVGMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRK--AALW----DEVKD---RLHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 517 ARaALSKAP-ILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLS-TIRNADAIMVLENGEIIERGTHEEL 590
Cdd:cd03260 153 AR-ALANEPeVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
42-344 |
6.39e-34 |
|
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: 130.76 E-value: 6.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLIDstKTSQQKITSLmagLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIREHL 121
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIK--GGDLDVLNEL---ALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 122 FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAkIGTA 201
Cdd:cd18557 76 FSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLL-IASK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 202 IAGKSRKYFMKQ-QTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSE-LNQSLRNSQVKAQFISGIMGpcmnamsqvn 279
Cdd:cd18557 155 IYGRYIRKLSKEvQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEaLDRSYRLARKKALANALFQG---------- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 280 ytLTACVGSIIAFASRWGGG--VPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18557 225 --ITSLLIYLSLLLVLWYGGylVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
371-580 |
7.41e-34 |
|
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: 127.97 E-value: 7.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKT-ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVL 449
Cdd:cd03225 2 LKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 Q--DTHLFTGTIMENIRYG--RLSATDEEVRQAAKTSCADMFIKNmpegydtMLKGDGSNLSQGQRQLLNIARAALSKAP 525
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEG-------LRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 526 ILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTIRN-ADAIMVLENGE 580
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
369-580 |
9.55e-34 |
|
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: 127.59 E-value: 9.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPDKT----ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdikdisleclreN 444
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 445 IAMVLQDTHLFTGTIMENIRYGrlSATDEEVRQAAKTSCA---DmfIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAAL 521
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG--KPFDEERYEKVIKACAlepD--LEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 522 SKAPILVLDEATSSVDTRTEKHINEG--MDALMEDRTTFVIAHRLSTIRNADAIMVLENGE 580
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
371-592 |
7.85e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 132.33 E-value: 7.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYN----PDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS---LECLRE 443
Cdd:COG1123 263 VRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 NIAMVLQD--THLFT-----GTIMENIR-YGRLSATD--EEVRQAAK-----TSCADMFIknmpegydtmlkgdgSNLSQ 508
Cdd:COG1123 343 RVQMVFQDpySSLNPrmtvgDIIAEPLRlHGLLSRAErrERVAELLErvglpPDLADRYP---------------HELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 509 GQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHInegMDALME-----DRTTFVIAHRLSTIRN-ADAIMVLENGEII 582
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI---LNLLRDlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
250
....*....|
gi 524455117 583 ERGTHEELLE 592
Cdd:COG1123 485 EDGPTEEVFA 494
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
42-344 |
8.45e-32 |
|
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: 124.93 E-value: 8.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYllrpIINGLIDSTKTSQQKITSLMAGL----ALMAVVYVLGVGATYLQGRIMISVSQGTLKRI 117
Cdd:cd18573 1 ALALLLVSSAVTMSVPF----AIGKLIDVASKESGDIEIFGLSLktfaLALLGVFVVGAAANFGRVYLLRIAGERIVARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 118 REHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAk 197
Cdd:cd18573 77 RKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 198 IGTAIAGKS-RKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMgpcmnams 276
Cdd:cd18573 156 VGAVFYGRYvRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLF-------- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 277 qvnYTLTACVGSIIAFASRWGGG--VPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18573 228 ---FGSTGFSGNLSLLSVLYYGGslVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
36-344 |
8.60e-32 |
|
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: 124.87 E-value: 8.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 36 KHKIAAAFVCVLVSSASTLCGSYLLRPIINGLIdstktSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLK 115
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDII-----PSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 116 RIREHLFRKVQKLPVRYFDTNPTGDIMSRFtNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPII 195
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 196 AkigtAIAGKSRKYFMKQQTDL----GKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPC 271
Cdd:cd18570 155 I----LIILLFNKPFKKKNREVmesnAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 272 MNAMSQVNYTLTACVGSIIAFASRwgggvpfsaLDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18570 231 KGLISLIGSLLILWIGSYLVIKGQ---------LSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
43-591 |
9.58e-32 |
|
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: 131.96 E-value: 9.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 43 FVCVLVSSASTLCGSYLL--RPIINGLIDS----------------TKTSQQKITSLMAGLA--LMAVVYVLGVGATYlq 102
Cdd:TIGR01271 874 LVIFLAEVAASLLGLWLItdNPSAPNYVDQqhanasspdvqkpviiTPTSAYYIFYIYVGTAdsVLALGFFRGLPLVH-- 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 103 grIMISVSqgtlKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNW 182
Cdd:TIGR01271 952 --TLLTVS----KRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQP 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 183 VLAVVTIVVSPIIAKIgtaiagksRKYFMKQQTDLGKVNG--------YIEETVTGQKVVKVFNYEenvvNEFSELNQSL 254
Cdd:TIGR01271 1026 YIFIAAIPVAVIFIML--------RAYFLRTSQQLKQLESearspifsHLITSLKGLWTIRAFGRQ----SYFETLFHKA 1093
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 255 RNSQVKAQFISgimgpcmnaMSQVNYTLTACVGSIIAFASrwggGVPFSALDIGG---------LTVFVNYSRQFSRPIN 325
Cdd:TIGR01271 1094 LNLHTANWFLY---------LSTLRWFQMRIDIIFVFFFI----AVTFIAIGTNQdgegevgiiLTLAMNILSTLQWAVN 1160
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 326 ElAQQVTNIMSALagaERVFNVMDEAEE----------IDDGKKLVLDKVH--------GDVLVEGVTFGYNPD-KTILK 386
Cdd:TIGR01271 1161 S-SIDVDGLMRSV---SRVFKFIDLPQEeprpsggggkYQLSTVLVIENPHaqkcwpsgGQMDVQGLTAKYTEAgRAVLQ 1236
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 387 DVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNiNKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIMENIR-Y 465
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpY 1315
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 466 GRLSatDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHIN 545
Cdd:TIGR01271 1316 EQWS--DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 524455117 546 EGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELL 591
Cdd:TIGR01271 1394 KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
371-580 |
3.46e-31 |
|
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: 118.89 E-value: 3.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQ 450
Cdd:cd00267 2 IENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 dthlftgtimenirygrlsatdeevrqaaktscadmfiknmpegydtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLD 530
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524455117 531 EATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTIRNA-DAIMVLENGE 580
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVtHDPELAELAaDRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
371-591 |
8.56e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 120.92 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQ 450
Cdd:COG1120 4 AENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHL-FTGTIMENIRYGR---------LSATDEE-VRQA-AKTSCADMfiKNMPegYDTmlkgdgsnLSQGQRQLLNIAR 518
Cdd:COG1120 83 EPPApFGLTVRELVALGRyphlglfgrPSAEDREaVEEAlERTGLEHL--ADRP--VDE--------LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 519 AALSKAPILVLDEATSSVDTRtekHINEGMDAL-----MEDRTTFVIAHRLS-TIRNADAIMVLENGEIIERGTHEELL 591
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLA---HQLEVLELLrrlarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
42-344 |
1.19e-30 |
|
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: 121.50 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLIDSTktSQQKITSLMAGLALMAVVYVLgvgATYLQGRIMISVSQGTLKRIREHL 121
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADG--SREAFYRAVLLLLLLSVLSGL---FSGLRGGCFSYAGTRLVRRLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 122 FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAkIGTA 201
Cdd:cd18572 76 FRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIA-LITK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 202 IAGK-SRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSE-LNQSLRNSQVKAQFISGIMGPCmnamsqvN 279
Cdd:cd18572 155 VYGRyYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERaLDKALKLSVRQALAYAGYVAVN-------T 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 280 YTLTACVGSIIAFasrwGGGVPFS-ALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18572 228 LLQNGTQVLVLFY----GGHLVLSgRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
371-592 |
1.61e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 125.40 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNP-DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNIN---KGKITIDGVDIKDISLECLRENIA 446
Cdd:COG1123 7 VRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 447 MVLQD--THLFTGTIMENIRYG--RLSATDEEVRQAAKTSCADMfiknmpeGYDTMLKGDGSNLSQGQRQLLNIARAALS 522
Cdd:COG1123 87 MVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAV-------GLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 523 KAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFV--IAHRLSTI-RNADAIMVLENGEIIERGTHEELLE 592
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVllITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
42-268 |
7.02e-30 |
|
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: 119.13 E-value: 7.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRpiinGLIDS--TKTSQQKITSLMagLALMAVVYVLGVgATYLQGRIMISVSQGTLKRIRE 119
Cdd:cd18575 1 ALIALLIAAAATLALGQGLR----LLIDQgfAAGNTALLNRAF--LLLLAVALVLAL-ASALRFYLVSWLGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 120 HLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIG 199
Cdd:cd18575 74 AVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 200 TAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQ-----SLRNSQVKAQFISGIM 268
Cdd:cd18575 154 ILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEaafaaALRRIRARALLTALVI 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
371-582 |
3.62e-29 |
|
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: 114.66 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdiKDISLECLRENIAMVLQ 450
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DT--HLFTGTIMENIRYG--RLSATDEEVRQAAKTSCADMFIKNMPEgydtmlkgdgsNLSQGQRQLLNIARAALSKAPI 526
Cdd:cd03226 79 DVdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 527 LVLDEATSSVDTRTEKHINEGMDALM-EDRTTFVIAHRLSTI-RNADAIMVLENGEII 582
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
367-594 |
5.25e-29 |
|
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: 116.49 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVLVEGVTFGYNPD-KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNInKGKITIDGVDIKDISLECLRENI 445
Cdd:cd03289 1 GQMTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 446 AMVLQDTHLFTGTIMENIR-YGRLSatDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKA 524
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 525 PILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKK 594
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
385-598 |
8.58e-28 |
|
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: 111.66 E-value: 8.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclRENIAMVLQDTHLFTG-TIMENI 463
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 464 RYGRLSATDEEVRQAAKtscadmfIKNMPE--GYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRT- 540
Cdd:cd03299 93 AYGLKKRKVDKKEIERK-------VLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTk 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 541 EKHINEGMDALMEDRTTFV-IAHRLSTIRN-ADAIMVLENGEIIERGTHEELLEKKGRYF 598
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
371-585 |
1.99e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.06 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQ 450
Cdd:cd03214 2 VENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 dthlftgtIMEnirygrlsatdeevrqaaKTSCADMFIKNMPEgydtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLD 530
Cdd:cd03214 81 --------ALE------------------LLGLAHLADRPFNE------------LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 531 EATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLS-TIRNADAIMVLENGEIIERG 585
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
371-592 |
2.85e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 110.66 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGY---NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAM 447
Cdd:COG1124 4 VRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 448 VLQDTHL-----FT--GTIMENIRYGRLSATDEEVRQAAKTScadmfikNMPEGYDTMLKGDgsnLSQGQRQLLNIARAA 520
Cdd:COG1124 84 VFQDPYAslhprHTvdRILAEPLRIHGLPDREERIAELLEQV-------GLPPSFLDRYPHQ---LSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTI-RNADAIMVLENGEIIERGTHEELLE 592
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
371-581 |
3.34e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 108.25 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEcLRENIAMVLQ 450
Cdd:cd03230 3 VRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENIRYgrlsatdeevrqaaktscadmfiknmpegydtmlkgdgsnlSQGQRQLLNIARAALSKAPILVL 529
Cdd:cd03230 81 EPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 524455117 530 DEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTIRN-ADAIMVLENGEI 581
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
371-594 |
3.73e-27 |
|
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: 109.97 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDI---KDISLECLRENIAM 447
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 448 VLQDTHLFTG-TIMENIRYGRLSAT----------DEEVRQAAKtSCADMFiknmpeGYDTMLKGDGSNLSQGQRQLLNI 516
Cdd:cd03256 83 IFQQFNLIERlSVLENVLSGRLGRRstwrslfglfPKEEKQRAL-AALERV------GLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 517 ARAALSKAPILVLDEATSSVDTRTEKHInegMDALMEDRTTF---VIA--HRLSTIR-NADAIMVLENGEIIERGTHEEL 590
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQV---MDLLKRINREEgitVIVslHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
|
....
gi 524455117 591 LEKK 594
Cdd:cd03256 233 TDEV 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
371-590 |
4.32e-27 |
|
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: 109.90 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS---LECLRENIAM 447
Cdd:cd03261 3 LRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 448 VLQDTHLFTG-TIMENI-----RYGRLSatDEEVRQAAKtSCADM-----FIKNMPegydtmlkgdgSNLSQGQRQLLNI 516
Cdd:cd03261 82 LFQSGALFDSlTVFENVafplrEHTRLS--EEEIREIVL-EKLEAvglrgAEDLYP-----------AELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 517 ARAALSKAPILVLDEATSSVDTRTEKHINEGMDAL--MEDRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
371-580 |
5.52e-27 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 107.66 E-value: 5.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEC--LRENIAMV 448
Cdd:cd03229 3 LKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFTG-TIMENIRYGrlsatdeevrqaaktscadmfiknmpegydtmlkgdgsnLSQGQRQLLNIARAALSKAPIL 527
Cdd:cd03229 82 FQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 528 VLDEATSSVDTRTEkhinEGMDALMED------RTTFVIAHRLS-TIRNADAIMVLENGE 580
Cdd:cd03229 123 LLDEPTSALDPITR----REVRALLKSlqaqlgITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
369-585 |
9.17e-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: 107.99 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclRENIAMV 448
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFTG-TIMENIRYG-RLSATDEEVRQAAKTSCADMFiknmpeGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPI 526
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlKLRGVPKAEIRARVRELLELV------GLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 527 LVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLS-TIRNADAIMVLENGEIIERG 585
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
39-344 |
1.08e-26 |
|
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: 110.26 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKiTSLMAGLALMAVVYV-LGVG---ATYLQGRIMISVSQGTL 114
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSP-DEFLDDVNKYALYFVyLGIGsfvLSYIQTACWTITGERQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 115 KRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPI 194
Cdd:cd18577 80 RRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 195 IAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNA 274
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 275 MSQVNYTLTACVGSIIAFASRWGGG----VPFSALdIGGLTvfvnysrqfsrpINELAQQVTNIMSALAGAERV 344
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGdvltVFFAVL-IGAFS------------LGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
373-585 |
1.61e-26 |
|
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: 107.98 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 373 GVTFG-YNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRE---NIAMV 448
Cdd:cd03257 8 SVSFPtGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrrkEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQD-------THlftgTIMENIRYGRLSATDEEVRQAAKTSCADMFIK-NMPEGYDTMLKGDgsnLSQGQRQLLNIARAA 520
Cdd:cd03257 88 FQDpmsslnpRM----TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvGLPEEVLNRYPHE---LSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMEDR-TTFV-IAHRLSTIRN-ADAIMVLENGEIIERG 585
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
372-583 |
2.63e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.06 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 372 EGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS---LECLRENIAMV 448
Cdd:COG2884 5 ENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFTG-TIMENIRYGrLSATDEEVRQAAKTSCA--DMF-----IKNMPEgydtmlkgdgsNLSQGQRQLLNIARAA 520
Cdd:COG2884 85 FQDFRLLPDrTVYENVALP-LRVTGKSRKEIRRRVREvlDLVglsdkAKALPH-----------ELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHInegMDALME---DRTTFVIA-HRLSTIRNADA-IMVLENGEIIE 583
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEI---MELLEEinrRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
152-600 |
3.08e-26 |
|
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: 114.66 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 152 IGEMLN--STLVQIFSGTITLIGTL-------ALMLYTNW------VLAVVTIVVspIIAKIGTAIAGKSRKYFMKQQTD 216
Cdd:TIGR00957 414 VGEIVNlmSVDAQRFMDLATYINMIwsaplqvILALYFLWlnlgpsVLAGVAVMV--LMVPLNAVMAMKTKTYQVAHMKS 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 217 LGKVNGYIEETVTGQKVVKVFNYEENvvneFSELNQSLRNSQVKAQFISGIMgpcmNAMSQVNYTLTACVGSIIAFASrW 296
Cdd:TIGR00957 492 KDNRIKLMNEILNGIKVLKLYAWELA----FLDKVEGIRQEELKVLKKSAYL----HAVGTFTWVCTPFLVALITFAV-Y 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 297 GGGVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV--FNVMDEAEEIDDGKKLVLDKVHGDVLVEGV 374
Cdd:TIGR00957 563 VTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLriFLSHEELEPDSIERRTIKPGEGNSITVHNA 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 375 TFGY-NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdikdisleclreNIAMVLQDTH 453
Cdd:TIGR00957 643 TFTWaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAW 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 454 LFTGTIMENIRYGRlsATDEEVRQAAKTSCA---DMFIknMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLD 530
Cdd:TIGR00957 710 IQNDSLRENILFGK--ALNEKYYQQVLEACAllpDLEI--LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 531 EATSSVDTRTEKHINE---GMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFEL 600
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEhviGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
372-591 |
6.92e-26 |
|
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: 106.62 E-value: 6.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 372 EGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQD 451
Cdd:cd03295 4 ENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 THLFTG-TIMENIrygRLSATDEEVRQAAKTSCADMFIK--NMPEGydTMLKGDGSNLSQGQRQLLNIARAALSKAPILV 528
Cdd:cd03295 84 IGLFPHmTVEENI---ALVPKLLKWPKEKIRERADELLAlvGLDPA--EFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 529 LDEATSSVDTRTEKHINEGMDALMED--RTTFVIAHRL-STIRNADAIMVLENGEIIERGTHEELL 591
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
371-594 |
1.41e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 106.61 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKT-ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVL 449
Cdd:PRK13632 10 VENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 Q--DTHLFTGTI-------MENIRYGRLSATDEEVRQAAKTscadmfiknmpeGYDTMLKGDGSNLSQGQRQLLNIArAA 520
Cdd:PRK13632 90 QnpDNQFIGATVeddiafgLENKKVPPKKMKDIIDDLAKKV------------GMEDYLDKEPQNLSGGQKQRVAIA-SV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 521 LSKAP-ILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA--HRLSTIRNADAIMVLENGEIIERGTHEELLEKK 594
Cdd:PRK13632 157 LALNPeIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
371-592 |
3.26e-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: 104.05 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISL-ECLRENIAMVL 449
Cdd:cd03224 3 VENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHLFTG-TIMENIRYGRLSATDEEVRQaaktscadmfikNMPEGYD------TMLKGDGSNLSQGQRQLLNIARAALS 522
Cdd:cd03224 82 EGRRIFPElTVEENLLLGAYARRRAKRKA------------RLERVYElfprlkERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 523 KAPILVLDEAT-----SSVDT--RTEKHIN-EGMDALM-EDRTTFVIAHrlstirnADAIMVLENGEIIERGTHEELLE 592
Cdd:cd03224 150 RPKLLLLDEPSeglapKIVEEifEAIRELRdEGVTILLvEQNARFALEI-------ADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
39-344 |
5.56e-25 |
|
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: 105.58 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLI-DSTKTSQQKITSLMAGLALMAVVY-VLGVGATYLQGRIMISVSQGTLKR 116
Cdd:cd18554 1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIqGSSLTLDEKVYKLFTIIGIMFFIFlILRPPVEYYRQYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 117 IREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIA 196
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 197 KIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFIsgimgpcmNAMS 276
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRW--------NAKT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 277 Q--VNyTLTACVGSIIAFASRWggGVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18554 233 FsaVN-TITDLAPLLVIGFAAY--LVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
371-591 |
1.52e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 102.86 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDislecLRENIAMVLQ 450
Cdd:COG1121 9 LENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHL---FTGTIMENI---RYG------RLSATD-EEVRQAAKTscADMfiknmpEGY-DTMLkgdgSNLSQGQRQLLNI 516
Cdd:COG1121 83 RAEVdwdFPITVRDVVlmgRYGrrglfrRPSRADrEAVDEALER--VGL------EDLaDRPI----GELSGGQQQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 517 ARAALSKAPILVLDEATSSVDTRTEKHINEGMDAL-MEDRTTFVIAHRLSTIR-NADAIMVLeNGEIIERGTHEELL 591
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
382-585 |
2.06e-24 |
|
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: 100.70 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLIT--RFYNINKGKITIDGvdiKDISLECLRENIAMVLQDTHLF-TGT 458
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDILHpTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 459 IMENIRYgrlsatdeevrqAAKtscadmfiknmpegydtmLKGdgsnLSQGQRQLLNIARAALSKAPILVLDEATSSVDT 538
Cdd:cd03213 99 VRETLMF------------AAK------------------LRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 524455117 539 RTEKHInegMDALM----EDRTTFVIAHRLST--IRNADAIMVLENGEIIERG 585
Cdd:cd03213 145 SSALQV---MSLLRrladTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
375-591 |
7.33e-24 |
|
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: 100.35 E-value: 7.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 375 TFGYNPDKTI-LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS---LECLRENIAMVLQ 450
Cdd:cd03258 10 VFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKARRRIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENIRYGRLSATDEEVRQAAKtscadmfIKNMPEGYDTMLKGDG--SNLSQGQRQLLNIARAALSKAPIL 527
Cdd:cd03258 90 HFNLLSSrTVFENVALPLEIAGVPKAEIEER-------VLELLELVGLEDKADAypAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 528 VLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEELL 591
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
42-344 |
8.57e-24 |
|
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: 101.94 E-value: 8.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSLMAGLALM-AVVYVLGVGATYLQGRIMISVSQGTLKRIREH 120
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLIlLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 121 LFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAkIGT 200
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLS-IGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 201 AIAGKS-RKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSE-LNQSLrNSQVKAQFISGIMGPCMNAMSQv 278
Cdd:cd18780 160 VIYGKYvRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEkINESY-LLGKKLARASGGFNGFMGAAAQ- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 279 nytltacvGSIIAFAsrWGGG--VPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18780 238 --------LAIVLVL--WYGGrlVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
371-582 |
9.63e-24 |
|
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: 99.53 E-value: 9.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIsleclRENIAMVLQ 450
Cdd:cd03235 2 VEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHL---FTGTIMENIRYGRLS----------ATDEEVRQAAKTscADMF-IKNMPEGydtmlkgdgsNLSQGQRQLLNI 516
Cdd:cd03235 76 RRSIdrdFPISVRDVVLMGLYGhkglfrrlskADKAKVDEALER--VGLSeLADRQIG----------ELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 517 ARAALSKAPILVLDEATSSVDTRTEKHINEGMDAL-MEDRTTFVIAHRLSTI-RNADAIMVLeNGEII 582
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLL-NRTVV 210
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
29-354 |
1.19e-23 |
|
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: 101.76 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 29 FSYLEQEKHKIAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSLMAGLALM-AVVYVLgvgATYLQGRIMI 107
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVlAIVAGI---AYFLQGYLFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 108 SVSQGTLKRIREHLFRKVQKLPVRYFD--TNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLA 185
Cdd:cd18578 78 IAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 186 VVTIVVSPIIakigtAIAGKSRKYFMKQQTDLGK-----VNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVK 260
Cdd:cd18578 158 LVGLATVPLL-----LLAGYLRMRLLSGFEEKNKkayeeSSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 261 AQFISGImgpcMNAMSQvnytltACVGSIIAFASRWG------GGVPFSALdiggLTVF--VNYSRQFsrpINELAQQVT 332
Cdd:cd18578 233 RALISGL----GFGLSQ------SLTFFAYALAFWYGgrlvanGEYTFEQF----FIVFmaLIFGAQS---AGQAFSFAP 295
|
330 340
....*....|....*....|..
gi 524455117 333 NIMSALAGAERVFNVMDEAEEI 354
Cdd:cd18578 296 DIAKAKAAAARIFRLLDRKPEI 317
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
371-592 |
1.97e-23 |
|
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: 99.29 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECL-RENIAMVL 449
Cdd:COG0410 6 VENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHLFTG-TIMENIRYGRLSATDEEVRQAAKTSCADMFiknmPEGYDtMLKGDGSNLSQGQRQLLNIARAALSKAPILV 528
Cdd:COG0410 85 EGRRIFPSlTVEENLLLGAYARRDRAEVRADLERVYELF----PRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 529 LDEAT-----SSVDT--RTEKHIN-EGMDALM-EDRTTFV--IAHRlstirnadaIMVLENGEIIERGTHEELLE 592
Cdd:COG0410 160 LDEPSlglapLIVEEifEIIRRLNrEGVTILLvEQNARFAleIADR---------AYVLERGRIVLEGTAAELLA 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
371-581 |
2.21e-23 |
|
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: 98.72 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKT---ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECL----RE 443
Cdd:cd03255 3 LKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 NIAMVLQDTHLFTG-TIMENIRY-----GRLSATDEE-VRQAAKTSCADMFIKNMPegydtmlkgdgSNLSQGQRQLLNI 516
Cdd:cd03255 83 HIGFVFQSFNLLPDlTALENVELplllaGVPKKERRErAEELLERVGLGDRLNHYP-----------SELSGGQQQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 517 ARAALSKAPILVLDEATSSVDTRTEKHInegMDALME----DRTTFVIA-HRLSTIRNADAIMVLENGEI 581
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEV---MELLRElnkeAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
46-334 |
7.47e-23 |
|
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: 99.12 E-value: 7.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 46 VLVSSASTLCGsyLLRPIING-LIDS--TKTSQQKITSLMAGLALMAVVYVLgvgATYLQGRIMISVSQGTLKRIREHLF 122
Cdd:cd18555 8 LLLSLLLQLLT--LLIPILTQyVIDNviVPGNLNLLNVLGIGILILFLLYGL---FSFLRGYIIIKLQTKLDKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 123 RKVQKLPVRYFDTNPTGDIMSRFtNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAI 202
Cdd:cd18555 83 EHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 203 AGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGpcmNAMSQVNYTL 282
Cdd:cd18555 162 RKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILN---SISSSIQFIA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 283 TA---CVGSIIAFASRwgggvpfsaLDIGGLTVFVNYSRQFSRPINELAQQVTNI 334
Cdd:cd18555 239 PLlilWIGAYLVINGE---------LTLGELIAFSSLAGSFLTPIVSLINSYNQF 284
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
371-589 |
1.73e-22 |
|
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: 96.74 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVT--FGynpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDislecLREN---- 444
Cdd:cd03219 3 VRGLTkrFG---GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-----LPPHeiar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 445 --IAMVLQDTHLFTG-TIMENIRYGRLSAT------------DEEVRQAAKtSCADMFiknmpeGYDTMLKGDGSNLSQG 509
Cdd:cd03219 75 lgIGRTFQIPRLFPElTVLENVMVAAQARTgsglllararreEREARERAE-ELLERV------GLADLADRPAGELSYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 510 QRQLLNIARAALSKAPILVLDEATSSVdTRTEKhinEGMDALMED-----RTTFVIAHRLSTIRN-ADAIMVLENGEIIE 583
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGL-NPEET---EELAELIRElrergITVLLVEHDMDVVMSlADRVTVLDQGRVIA 223
|
....*.
gi 524455117 584 RGTHEE 589
Cdd:cd03219 224 EGTPDE 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
385-590 |
1.85e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDG--VDIKDIsLECLRENIAMVLQDTHLFTG-TIME 461
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 NIRYGRLSAT-----DEEVRQAAKTSCADMfikNMPEGYDTMLkgdgSNLSQGQRQLLNIARAALSKAPILVLDEATSSV 536
Cdd:COG1129 99 NIFLGREPRRgglidWRAMRRRARELLARL---GLDIDPDTPV----GDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 537 dTRTE-KHINEGMDALMEDRTTFV-IAHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:COG1129 172 -TEREvERLFRIIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
371-595 |
2.01e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.81 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNP----DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDI--KDISLECLREN 444
Cdd:PRK13637 5 IENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 445 IAMVLQ--DTHLFTGTIMENIRYG--RLSATDEEVRQAAKTScadMFIKNMPegYDTMLKGDGSNLSQGQRQLLNIARAA 520
Cdd:PRK13637 85 VGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA---MNIVGLD--YEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTI-RNADAIMVLENGEIIERGTHEEL------L 591
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVfkevetL 239
|
....
gi 524455117 592 EKKG 595
Cdd:PRK13637 240 ESIG 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
371-583 |
2.48e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 95.88 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDK---TILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS---LECLR-E 443
Cdd:COG1136 7 LRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLRrR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 NIAMVLQDTHLFTG-TIMENI----RYGRLSAtdEEVRQAAKTSCADM----FIKNMPegydtmlkgdgSNLSQGQRQLL 514
Cdd:COG1136 87 HIGFVFQFFNLLPElTALENValplLLAGVSR--KERRERARELLERVglgdRLDHRP-----------SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 515 NIARAALSKAPILVLDEATSSVDTRTEKHInegMDALM----EDRTTFVIA-HRLSTIRNADAIMVLENGEIIE 583
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEV---LELLRelnrELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
371-593 |
6.76e-22 |
|
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: 95.79 E-value: 6.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVT--FGYNPDKTI---------------------LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKIT 427
Cdd:cd03294 3 IKGLYkiFGKNPQKAFkllakgkskeeilkktgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 428 IDGVDIKDISLECLRE----NIAMVLQDTHLFTG-TIMENIRYG-RLSATDEEVRQAAKTscadmfiknmpEGYDTM-LK 500
Cdd:cd03294 83 IDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTVLENVAFGlEVQGVPRAEREERAA-----------EALELVgLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 501 GDG----SNLSQGQRQLLNIARAALSKAPILVLDEATSSVD--TRTEkhinegM-DALME-----DRTTFVIAHRLS-TI 567
Cdd:cd03294 152 GWEhkypDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplIRRE------MqDELLRlqaelQKTIVFITHDLDeAL 225
|
250 260
....*....|....*....|....*.
gi 524455117 568 RNADAIMVLENGEIIERGTHEELLEK 593
Cdd:cd03294 226 RLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
39-346 |
1.11e-21 |
|
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: 95.65 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSLMAGLALMAVVyVLGVGATYLQGRIMISVSqgtlKRIR 118
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASV-LLVLLRWLLFVLAGLRAS----RRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 119 EHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKI 198
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 199 gtaiagksRKYFMK-----QQTDL---GKVNGYIEETVTGQKVVKVFNYEENVVNEFSELnqsLRNSQvKAQFISGImgp 270
Cdd:cd18580 156 --------QRYYLRtsrqlRRLESesrSPLYSHFSETLSGLSTIRAFGWQERFIEENLRL---LDASQ-RAFYLLLA--- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 271 CMNAMSQVNYTLTACVGSIIAFASRWGGGVPFSALdiGGLTvfVNYSRQFSRPINELAQQVTNIMSALAGAERVFN 346
Cdd:cd18580 221 VQRWLGLRLDLLGALLALVVALLAVLLRSSISAGL--VGLA--LTYALSLTGSLQWLVRQWTELETSMVSVERILE 292
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
395-585 |
2.09e-21 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 92.94 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 395 GQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKdiSLECLRENIAMVLQDTHLFTG-TIMENIRYGR---LSA 470
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGLGLspgLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 471 TDEEvRQAAKTSCADMfiknmpeGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRtekhINEGMDA 550
Cdd:cd03298 102 TAED-RQAIEVALARV-------GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA----LRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 524455117 551 LMED------RTTFVIAHRLSTIRN-ADAIMVLENGEIIERG 585
Cdd:cd03298 170 LVLDlhaetkMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
371-573 |
2.46e-21 |
|
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: 92.54 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEcLRENIAMVLQ 450
Cdd:COG4133 5 AENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENIRY----GRLSATDEEVRQAAK----TSCADMFIKNmpegydtmlkgdgsnLSQGQRQLLNIARAAL 521
Cdd:COG4133 83 ADGLKPElTVRENLRFwaalYGLRADREAIDEALEavglAGLADLPVRQ---------------LSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 524455117 522 SKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTIRNADAI 573
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
371-589 |
2.82e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 93.56 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVT--FGYNpdkTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISL-ECLRENIAM 447
Cdd:COG0411 7 VRGLTkrFGGL---VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 448 VLQDTHLFTG-TIMENIRYGRLSAT-----------------DEEVRQAAKtSCADMFiknmpeGYDTMLKGDGSNLSQG 509
Cdd:COG0411 84 TFQNPRLFPElTVLENVLVAAHARLgrgllaallrlprarreEREARERAE-ELLERV------GLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 510 QRQLLNIARAALSKAPILVLDEATSSVdTRTEKHinEGMDALME-----DRTTFVIAHRLSTIRN-ADAIMVLENGEIIE 583
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGL-NPEETE--ELAELIRRlrderGITILLIEHDMDLVMGlADRIVVLDFGRVIA 233
|
....*.
gi 524455117 584 RGTHEE 589
Cdd:COG0411 234 EGTPAE 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
358-591 |
4.05e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 358 KKLVLDKVhgdvlveGVTFGynpdktiLKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS 437
Cdd:PRK10070 31 KEQILEKT-------GLSLG-------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 438 LECLRE----NIAMVLQDTHLFTG-TIMENIRYGRLSA--TDEEVRQAAKTSCADMFIKNMPEGYDTMLKGdgsnlsqGQ 510
Cdd:PRK10070 97 DAELREvrrkKIAMVFQSFALMPHmTVLDNTAFGMELAgiNAEERREKALDALRQVGLENYAHSYPDELSG-------GM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 511 RQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALM--EDRTTFVIAHRL-STIRNADAIMVLENGEIIERGTH 587
Cdd:PRK10070 170 RQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTP 249
|
....
gi 524455117 588 EELL 591
Cdd:PRK10070 250 DEIL 253
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
371-607 |
4.67e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGY-NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVL 449
Cdd:PRK13635 8 VEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QD-THLFTGTI--------MENIRYGRLSATdEEVRQAAKTSCADMFIKNMPegydtmlkgdgSNLSQGQRQLLNIArAA 520
Cdd:PRK13635 88 QNpDNQFVGATvqddvafgLENIGVPREEMV-ERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIA-GV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 521 LSKAP-ILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELlekkgry 597
Cdd:PRK13635 155 LALQPdIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI------- 227
|
250
....*....|
gi 524455117 598 FELYTGLKEL 607
Cdd:PRK13635 228 FKSGHMLQEI 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
371-591 |
5.91e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.13 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAhpGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclRENIAMVLQ 450
Cdd:COG3840 4 LDDLTYRYG-DFPLRFDLTIAA--GERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENIRYG-----RLSATD-EEVRQAA-KTSCADMfIKNMPEgydtmlkgdgsNLSQGQRQLLNIARAALS 522
Cdd:COG3840 79 ENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALeRVGLAGL-LDRLPG-----------QLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 523 KAPILVLDEATSSVDT--RTEkhinegMDALMED------RTTFVIAHRLS-TIRNADAIMVLENGEIIERGTHEELL 591
Cdd:COG3840 147 KRPILLLDEPFSALDPalRQE------MLDLVDElcrergLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
374-591 |
7.27e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 7.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTFGynpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTH 453
Cdd:PRK09536 11 VEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 454 L---FTG-TIME------NIRYGRLSATDEE-VRQAAKTSCADMFIKNmpegydtmlkgDGSNLSQGQRQLLNIARAALS 522
Cdd:PRK09536 88 LsfeFDVrQVVEmgrtphRSRFDTWTETDRAaVERAMERTGVAQFADR-----------PVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 523 KAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLS-TIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
369-593 |
8.53e-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: 91.53 E-value: 8.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclRENIAMV 448
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFTG-TIMENIRYG-RLSATDEEVRQAAKTSCADMFikNMpEGYdtmLKGDGSNLSQGQRQLLNIARAALSKAPI 526
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlRLKKLPKAEIKERVAEALDLV--QL-EGY---ANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 527 LVLDEATSSVDTRTEKHINEGMDALMED-RTTFV-IAHRLS-TIRNADAIMVLENGEIIERGTHEELLEK 593
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVfVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
381-581 |
1.76e-20 |
|
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: 90.28 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDI--KDISLECLRENIAMVLQDTHLFTG- 457
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 TIMENIRYG---RLSATDEEVRQAAKTSCADMFIKNMPEGYDtmlkgdgSNLSQGQRQLLNIARAALSKAPILVLDEATS 534
Cdd:cd03262 92 TVLENITLApikVKGMSKAEAEERALELLEKVGLADKADAYP-------AQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 524455117 535 SVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTIRN-ADAIMVLENGEI 581
Cdd:cd03262 165 ALDPELVGEVLDVMKDLAEEGMTMVVVtHEMGFAREvADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
371-592 |
1.77e-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: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKTILK---DVSIFAHPGQKIALVGSTGAGKTTITNLITRFY---NINKGKITIDGVDIKDISLECLRE- 443
Cdd:COG0444 4 VRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKELRKi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 ---NIAMVLQD--THL---FT-GT-IMENIRYGRLsATDEEVRQAAKT-------SCADMFIKNMP-Egydtmlkgdgsn 505
Cdd:COG0444 84 rgrEIQMIFQDpmTSLnpvMTvGDqIAEPLRIHGG-LSKAEARERAIEllervglPDPERRLDRYPhE------------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 506 LSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDR-TTFV-IAHRLSTIRN-ADAIMVLENGEII 582
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILfITHDLGVVAEiADRVAVMYAGRIV 230
|
250
....*....|
gi 524455117 583 ERGTHEELLE 592
Cdd:COG0444 231 EEGPVEELFE 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
369-584 |
1.81e-20 |
|
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: 90.22 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGY---NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclrenI 445
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 446 AMVLQDTHLFT-GTIMENIRYG----RLSATD--EEVRQAAKTSCADMFIKNMPegydtmlkgdgSNLSQGQRQLLNIAR 518
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqGVPKAEarERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 519 AALSKAPILVLDEATSSVD--TRTEKHiNEGMDALMEDRTTFV-IAHRLS-TIRNADAIMVLEN--GEIIER 584
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDalTREQLQ-EELLDIWRETGKTVLlVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
369-593 |
3.01e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.40 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYnPD--KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFY---NINKGKITIDGVDIKDISLECLRE 443
Cdd:PRK13640 6 VEFKHVSFTY-PDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 NIAMVLQ--DTHLFTGTIMENIRYGRlsatdeEVRQAAKTSCADMFIKNMPE-GYDTMLKGDGSNLSQGQRQLLNIARAA 520
Cdd:PRK13640 85 KVGIVFQnpDNQFVGATVGDDVAFGL------ENRAVPRPEMIKIVRDVLADvGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEK 593
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
384-608 |
4.49e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 94.98 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 384 ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdikdisleclreNIAMVLQDTHLFTGTIMENI 463
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 464 RYGrLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKH 543
Cdd:TIGR01271 508 IFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 544 INEG-MDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFELYTGLKELD 608
Cdd:TIGR01271 587 IFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFD 652
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
42-344 |
4.60e-20 |
|
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: 90.83 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLIdsTKTSQQKITslMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLkRIREHL 121
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIV--IEKSQDKFS--RAIIIMGLLAIASSVAAGIRGGLFTLAMARLNI-RIRNLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 122 FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTA 201
Cdd:cd18784 76 FRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 202 IAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSE-LNQSLRNSQVKAQFISGIMgpCMNAMSQVny 280
Cdd:cd18784 156 YGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEkLKDTYKLKIKEALAYGGYV--WSNELTEL-- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 281 tltacvgsIIAFASRWGGG--VPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18784 232 --------ALTVSTLYYGGhlVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
369-581 |
5.34e-20 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 88.85 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDisLECLRENIAMV 448
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD--LPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFTG-TIMENIRYG------RLSATDEEVRQAAKTSCADMFIKNMPegydtmlkgdgSNLSQGQRQLLNIARAAL 521
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 522 SKAPILVLDEATSSVD------TRTE-KHINEGMDAlmedrTTFVIAH-RLSTIRNADAIMVLENGEI 581
Cdd:cd03301 147 REPKVFLMDEPLSNLDaklrvqMRAElKRLQQRLGT-----TTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
78-334 |
5.93e-20 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 90.60 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 78 ITSLMAGLALMAVvyvLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFtNDVDIIGEMLN 157
Cdd:cd18567 41 LTVLAIGFGLLLL---LQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 158 STLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVF 237
Cdd:cd18567 117 TGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 238 NYEENVVNEFSELNQSLRNSQVKAQFISgimgpcmNAMSQVNYTLTACVG-SIIAFASRwgggvpfSALD----IGGLTV 312
Cdd:cd18567 197 GREAEREARWLNLLVDAINADIRLQRLQ-------ILFSAANGLLFGLENiLVIYLGAL-------LVLDgeftVGMLFA 262
|
250 260
....*....|....*....|..
gi 524455117 313 FVNYSRQFSRPINELAQQVTNI 334
Cdd:cd18567 263 FLAYKDQFSSRASSLIDKLFEL 284
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
378-591 |
6.00e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.72 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 378 YNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGV------DIKDISLECLRENIAMVLQD 451
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 THLFTG-TIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLD 530
Cdd:PRK14246 99 PNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 531 EATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTI-RNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
371-582 |
6.18e-20 |
|
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: 87.10 E-value: 6.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDG--VDIKDISlECLRENIAMV 448
Cdd:cd03216 3 LRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPR-DARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQdthlftgtimenirygrlsatdeevrqaaktscadmfiknmpegydtmlkgdgsnLSQGQRQLLNIARAALSKAPILV 528
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 529 LDEATSSVDTRTEKHINEGMDALMEDRTTFV-IAHRLSTIRN-ADAIMVLENGEII 582
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
384-608 |
1.55e-19 |
|
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: 89.15 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 384 ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdikdisleclreNIAMVLQDTHLFTGTIMENI 463
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 464 RYGrLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKH 543
Cdd:cd03291 119 IFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 544 INEG-MDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKKGRYFELYTGLKELD 608
Cdd:cd03291 198 IFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFD 263
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
371-591 |
3.36e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.38 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQ 450
Cdd:PRK11231 5 TENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 dtHLFTG---TIMENIRYGR---------LSATDEE-VRQA-AKTSCADMFIKNMpegydtmlkgdgSNLSQGQRQLLNI 516
Cdd:PRK11231 84 --HHLTPegiTVRELVAYGRspwlslwgrLSAEDNArVNQAmEQTRINHLADRRL------------TDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 517 ARAALSKAPILVLDEATSSVDTrteKHINEGMDaLM-----EDRTTFVIAHRLS-TIRNADAIMVLENGEIIERGTHEEL 590
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDI---NHQVELMR-LMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEV 225
|
.
gi 524455117 591 L 591
Cdd:PRK11231 226 M 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
376-592 |
8.20e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.91 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 376 FGynpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKD--ISLECLRENIAMVLQDTH 453
Cdd:PRK09493 11 FG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 454 LFTG-TIMENIRYGRL---SATDEEVRQAAKTSCADMFIKNMPEGYDtmlkgdgSNLSQGQRQLLNIARAALSKAPILVL 529
Cdd:PRK09493 88 LFPHlTALENVMFGPLrvrGASKEEAEKQARELLAKVGLAERAHHYP-------SELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 530 DEATSSVDTRTEKHINEGMDALMEDRTTFVI-AHRLSTIRN-ADAIMVLENGEIIERGTHEELLE 592
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
367-593 |
1.91e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.05 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVLVEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclRENIA 446
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 447 MVLQD----THLftgTIMENIRYG----RLSAT--DEEVRQAAKtscadmfiknmpegydtMLKGDG------SNLSQGQ 510
Cdd:COG3839 79 MVFQSyalyPHM---TVYENIAFPlklrKVPKAeiDRRVREAAE-----------------LLGLEDlldrkpKQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 511 RQLLNIARAALSKAPILVLDEATSSVD------TRTE-KHINEgmdalmEDRTTFVIA-HRLS---TIrnADAIMVLENG 579
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHR------RLGTTTIYVtHDQVeamTL--ADRIAVMNDG 210
|
250
....*....|....
gi 524455117 580 EIIERGTHEELLEK 593
Cdd:COG3839 211 RIQQVGTPEELYDR 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
377-585 |
2.74e-18 |
|
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: 84.12 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 377 GYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdiKDISLecLRENIAMVLQdthlFT 456
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSL--LGLGGGFNPE----LT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 457 GtiMENIR-YGRLS-ATDEEVRQAAKtscadmFIKN---MPEGYDTMLKgdgsNLSQGQRQLLNIARAALSKAPILVLDE 531
Cdd:cd03220 101 G--RENIYlNGRLLgLSRKEIDEKID------EIIEfseLGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 532 ATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTIRN-ADAIMVLENGEIIERG 585
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
369-585 |
3.65e-18 |
|
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: 83.57 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPDKTI---LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLReNI 445
Cdd:cd03266 2 ITADALTKRFRDVKKTvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 446 AMVLQDTHLFTG-TIMENIRY-GRLSATDEEVRQAAKTSCADMFikNMPEGYDTMLKGdgsnLSQGQRQLLNIARAALSK 523
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfAGLYGLKGDELTARLEELADRL--GMEELLDRRVGG----FSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 524 APILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTI-RNADAIMVLENGEIIERG 585
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
379-590 |
5.37e-18 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 82.94 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 379 NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEClRENIAMVLQDTHLFTG- 457
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA-RQSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 TIMENIR-YGRL-----SATDEEVRQAAK----TSCADMFIKnmpegydtmlkgdgsNLSQGQRQLLNIARAALSKAPIL 527
Cdd:cd03263 91 TVREHLRfYARLkglpkSEIKEEVELLLRvlglTDKANKRAR---------------TLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 528 VLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
374-581 |
7.14e-18 |
|
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: 82.46 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDI---SLECLRENIAMVLQ 450
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLF-TGTIMENIRYGrLSATDEEVRQAAKTSCADMFIKNMPEGYDTMlkgdGSNLSQGQRQLLNIARAALSKAPILVL 529
Cdd:cd03292 86 DFRLLpDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 524455117 530 DEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADA--IMVLENGEI 581
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
42-344 |
7.50e-18 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 84.47 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLidsTKTSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIREHL 121
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDAL---SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 122 FRKVQKLPVRYFDTNPTGD---IMSRFTNDVDIIgemLNSTLVQIFSGTITLIGTLALMLYT-NWVLAVVTIVVspIIAK 197
Cdd:cd18582 78 FRHLHSLSLRFHLSRKTGAlsrAIERGTRGIEFL---LRFLLFNILPTILELLLVCGILWYLyGWSYALITLVT--VALY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 198 IG-TAIAGKSRKYFMKQQTDL-GKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQfisgimgpcmNAM 275
Cdd:cd18582 153 VAfTIKVTEWRTKFRREMNEAdNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQ----------TSL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 276 SQVNYT----LTACVGSIIAFASRwggGVPFSALDIGGLtVFVN-YSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18582 223 ALLNIGqaliISLGLTAIMLLAAQ---GVVAGTLTVGDF-VLVNtYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
382-591 |
1.11e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHL-FTGTIM 460
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 461 ENIRYGRL------SATDEEVRQA-AKTSCADMFIKNMPEgydtmlkgdgsnLSQGQRQLLNIAR--AALSKA----PIL 527
Cdd:PRK13548 95 EVVAMGRAphglsrAEDDALVAAAlAQVDLAHLAGRDYPQ------------LSGGEQQRVQLARvlAQLWEPdgppRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 528 VLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA--HRLS-TIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
371-591 |
1.26e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYnPDKT-ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS-LECLRENIAMV 448
Cdd:PRK13644 4 LENVSYSY-PDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQ--DTHLFTGTIMENIRYG--RLSATDEEVRQAAKTSCADMfiknmpeGYDTMLKGDGSNLSQGQRQLLNIARAALSKA 524
Cdd:PRK13644 83 FQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEI-------GLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 525 PILVLDEATSSVDTRTEKHINEGMDALMEDRTTFV-IAHRLSTIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
369-598 |
2.49e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 81.62 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclRENIAMV 448
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFTG-TIMENIRYG--------RLSAT--DEEVRQAAKTSCADMFIKNMPegydtmlkgdgSNLSQGQRQLLNIA 517
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGlrvkprseRPPEAeiRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 518 RAALSKAPILVLDEATSSVDTRTEKHINEGMDALMED---RTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEKK 594
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
....
gi 524455117 595 GRYF 598
Cdd:cd03296 229 ASPF 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
387-590 |
2.58e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.24 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 387 DVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRE---NIAMVLQDTH--L---FT-- 456
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPYasLnprMTvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 457 GTIMENIRYGRLsATDEEVRQAAktscADMfiknM------PEGYDT---MLKGdgsnlsqGQRQLLNIARA-ALSkaP- 525
Cdd:COG4608 116 DIIAEPLRIHGL-ASKAERRERV----AEL----LelvglrPEHADRyphEFSG-------GQRQRIGIARAlALN--Pk 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 526 ILVLDEATSSVDTRTEKHI-NegmdaLMED-----RTTFV-IAHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVlN-----LLEDlqdelGLTYLfISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
42-344 |
2.78e-17 |
|
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: 82.53 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIrehL 121
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSL---I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 122 FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNStLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTA 201
Cdd:cd18579 79 YRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLF-LHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 202 IAGKSRKYFMK--QQTD--LGKVNgyieETVTGQKVVKVFNYEENvvneFSELNQSLRNSQVKAQFISGIMGPCMNAMSQ 277
Cdd:cd18579 158 LAKLISKLRKKlmKATDerVKLTN----EILSGIKVIKLYAWEKP----FLKRIEELRKKELKALRKFGYLRALNSFLFF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 278 VNYTLTACVgsiiAFASRWGGGVPFSAldiggLTVFVNYS--RQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18579 230 STPVLVSLA----TFATYVLLGNPLTA-----AKVFTALSlfNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
378-601 |
2.83e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.75 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 378 YNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNIN-----KGKITIDGVDIKDISLEC--LRENIAMVLQ 450
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTGTIMENIRYG-RLSAT-DEEV-RQAAKTSCADMFIKNmpEGYDtMLKGDGSNLSQGQRQLLNIARAALSKAPIL 527
Cdd:PRK14239 94 QPNPFPMSIYENVVYGlRLKGIkDKQVlDEAVEKSLKGASIWD--EVKD-RLHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 528 VLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRL---STIRNADAIMVleNGEIIERG-THEELLEKKGRYFELY 601
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRISDRTGFFL--DGDLIEYNdTKQMFMNPKHKETEDY 246
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
383-591 |
4.05e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.82 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 383 TILKDVSIFAHPGQKIALVGSTGAGKTTitnLItRfyNIN------KGKITIDGVDIKDIS---LECLRENIAMVLQDTH 453
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKST---LI-R--CINllerptSGSVLVDGVDLTALSereLRAARRKIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 454 LFTG-TIMENIRYG-RLSATDEEVRQA------------AKtscADMFiknmPegydtmlkgdgSNLSQGQRQLLNIARA 519
Cdd:COG1135 93 LLSSrTVAENVALPlEIAGVPKAEIRKrvaellelvglsDK---ADAY----P-----------SQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 520 aLSKAP-ILVLDEATSSVDTRTE-------KHINEGMDAlmedrTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:COG1135 155 -LANNPkVLLCDEATSALDPETTrsildllKDINRELGL-----TIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDV 228
|
.
gi 524455117 591 L 591
Cdd:COG1135 229 F 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
371-598 |
4.63e-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: 80.65 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDI-KDISLECLRENIAMVL 449
Cdd:TIGR03410 3 VSNLNVYYG-QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHLFTG-TIMENIRYGrLSATDEEVRqaaktscadmfiKNMPEGYD------TMLKGDGSNLSQGQRQLLNIARAALS 522
Cdd:TIGR03410 82 QGREIFPRlTVEENLLTG-LAALPRRSR------------KIPDEIYElfpvlkEMLGRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 523 KAPILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEELLEKKGRYF 598
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDKVRRY 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
358-592 |
5.24e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.07 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 358 KKLVLDKVHGDVLVE--GVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKD 435
Cdd:PRK09452 2 KKLNKQPSSLSPLVElrGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 436 ISLEclRENIAMVLQDTHLFTG-TIMENIRYG-RLSATDEE-----VRQAAKTSCADMFIKNMPegydtmlkgdgSNLSQ 508
Cdd:PRK09452 81 VPAE--NRHVNTVFQSYALFPHmTVFENVAFGlRMQKTPAAeitprVMEALRMVQLEEFAQRKP-----------HQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 509 GQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALmeDRT---TFV-IAH-RLSTIRNADAIMVLENGEIIE 583
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKAL--QRKlgiTFVfVTHdQEEALTMSDRIVVMRDGRIEQ 225
|
....*....
gi 524455117 584 RGTHEELLE 592
Cdd:PRK09452 226 DGTPREIYE 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
355-592 |
5.46e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.71 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 355 DDGKKLVLDKVhgdvlVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITrFYNIN----KGKITIDG 430
Cdd:TIGR00955 16 QDGSWKQLVSR-----LRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 431 vdiKDISLECLRENIAMVLQDtHLFTGT--------IMENIRYGRLSATDEEvRQAAK--------TSCADMFIknmpeG 494
Cdd:TIGR00955 90 ---MPIDAKEMRAISAYVQQD-DLFIPTltvrehlmFQAHLRMPRRVTKKEK-RERVDevlqalglRKCANTRI-----G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 495 YDTMLKGdgsnLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLST--IRNAD 571
Cdd:TIGR00955 160 VPGRVKG----LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFD 235
|
250 260
....*....|....*....|.
gi 524455117 572 AIMVLENGEIIERGTHEELLE 592
Cdd:TIGR00955 236 KIILMAEGRVAYLGSPDQAVP 256
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
369-579 |
5.78e-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: 80.07 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECL----REN 444
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 445 IAMVLQDTHLFTGTIMENIRYGrlSATDEEVRQAAKTSCA-DMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSK 523
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 524 APILVLDEATSSVDTRTEKHI-NEGMDALMED--RTTFVIAHRLSTIRNADAIMVLENG 579
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLmQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
373-590 |
8.81e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 373 GVTFgynPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISL-ECLRENIAMVLQD 451
Cdd:PRK11288 11 GKTF---PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 THLFTG-TIMENIRYGRLSATDEEVRQAAKTSCADMFIKNMPEGYD--TMLKgdgsNLSQGQRQLLNIARAALSKAPILV 528
Cdd:PRK11288 88 LHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLK----YLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 529 LDEATSSVDTRTEKHINEGMDALM-EDRTTFVIAHRLSTI-RNADAIMVLENGEIIErgTHEEL 590
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRaEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
374-608 |
1.06e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.52 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTF--GYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQD 451
Cdd:COG1101 9 KTFnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 THLFTG---TIMENI--------RYGRLSATDEEVRQAAKTSCADMfikNMpeGYDTMLKGDGSNLSQGQRQLLNIARAA 520
Cdd:COG1101 89 PMMGTApsmTIEENLalayrrgkRRGLRRGLTKKRRELFRELLATL---GL--GLENRLDTKVGLLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLS-TIRNADAIMVLENGEII--------ERGTHEE 589
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRIIldvsgeekKKLTVED 243
|
250
....*....|....*....
gi 524455117 590 LLEKkgryFELYTGLKELD 608
Cdd:COG1101 244 LLEL----FEEIRGEELAD 258
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
116-599 |
1.43e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 83.87 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 116 RIREHL----FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIgEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVV 191
Cdd:PLN03232 371 RLRSTLvaaiFHKSLRLTHEARKNFASGKVTNMITTDANAL-QQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLI 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 192 SPIIAKIGTAIAGKSRKYFMK--QQTDlgKVNGYIEETVTGQKVVKVFNYEENvvneFSELNQSLRNSQV----KAQFIS 265
Cdd:PLN03232 450 LFLLIPLQTLIVRKMRKLTKEglQWTD--KRVGIINEILASMDTVKCYAWEKS----FESRIQGIRNEELswfrKAQLLS 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 266 GIMGPCMNAMSQVnytltACVGSIIAFASRWGGGVPFSALDIGGLTVFVNYsrqfsrPINELAQQVTNIMSALAGAERVF 345
Cdd:PLN03232 524 AFNSFILNSIPVV-----VTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRS------PLNMLPNLLSQVVNANVSLQRIE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 346 NVMDEAEEIDdGKKLVLDKVHGDVLVEGVTFGYNP--DKTILKDVSIFAHPGQKIALVGSTGAGKTT-ITNLITRFYNIN 422
Cdd:PLN03232 593 ELLLSEERIL-AQNPPLQPGAPAISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSlISAMLGELSHAE 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 423 KGKITIDGvdikdisleclreNIAMVLQDTHLFTGTIMENIRYGRLSATDEEVRQAAKTSCA---DMFiknmpEGYDTML 499
Cdd:PLN03232 672 TSSVVIRG-------------SVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQhdlDLL-----PGRDLTE 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 500 KGD-GSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHI-NEGMDALMEDRTTFVIAHRLSTIRNADAIMVLE 577
Cdd:PLN03232 734 IGErGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVS 813
|
490 500
....*....|....*....|..
gi 524455117 578 NGEIIERGTHEElLEKKGRYFE 599
Cdd:PLN03232 814 EGMIKEEGTFAE-LSKSGSLFK 834
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
372-591 |
1.49e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 79.74 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 372 EGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGK-ITI-----DGVDIKDislecLRENI 445
Cdd:COG1119 7 RNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerrGGEDVWE-----LRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 446 AMV---LQDTHL------------FTGTIMeniRYGRLsaTDEEVRQAAKtsCADMF----IKNMPegYDTmlkgdgsnL 506
Cdd:COG1119 81 GLVspaLQLRFPrdetvldvvlsgFFDSIG---LYREP--TDEQRERARE--LLELLglahLADRP--FGT--------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 507 SQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDR-TTFV-IAHRLSTIrnADAI---MVLENGEI 581
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEI--PPGIthvLLLKDGRV 221
|
250
....*....|
gi 524455117 582 IERGTHEELL 591
Cdd:COG1119 222 VAAGPKEEVL 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
372-594 |
1.92e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 372 EGVTFGYNPDKTI----LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIK----DISLECLRE 443
Cdd:PRK13641 6 ENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 NIAMVLQ--DTHLFTGTIMENIRYG--RLSATDEEVRQAAKTscadmFIKNMPEGYDTMLKGDgSNLSQGQRQLLNIARA 519
Cdd:PRK13641 86 KVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDEAKEKALK-----WLKKVGLSEDLISKSP-FELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 520 ALSKAPILVLDEATSSVDTRTEKHINE-GMDALMEDRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEELLEKK 594
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQlFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
392-591 |
4.31e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.70 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 392 AHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclRENIAMVLQDTHLFTG-TIMENIRYG---- 466
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGlnpg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 467 -RLSATD-EEVRQAAKTSCADMFIKNMPegydtmlkgdgSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDT--RTEk 542
Cdd:PRK10771 100 lKLNAAQrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPalRQE- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 543 hinegMDALMED------RTTFVIAHRLS-TIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK10771 168 -----MLTLVSQvcqerqLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
384-591 |
4.82e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.47 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 384 ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDI-------------SLECLRENIAMVLQ 450
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENIRYGR---LSATDEEVRQAAKTSCADMFIKNMPEG-YDtmlkgdgSNLSQGQRQLLNIARAALSKAP 525
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPiqvLGLSKQEARERAVKYLAKVGIDERAQGkYP-------VHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 526 ILVLDEATSSVDTRTEKHINEGMDALMED-RTTFVIAHRLSTIRNADA-IMVLENGEIIERGTHEELL 591
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
371-594 |
5.53e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.62 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQ 450
Cdd:PRK13647 7 VEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 --DTHLFTGTIMENIRYG----RLSATDEEVRQAAKTSCADMF-IKNMPEgydtmlkgdgSNLSQGQRQLLNIARAALSK 523
Cdd:PRK13647 87 dpDDQVFSSTVWDDVAFGpvnmGLDKDEVERRVEEALKAVRMWdFRDKPP----------YHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 524 APILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLS-TIRNADAIMVLENGEIIERGTHEELLEKK 594
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
371-600 |
6.56e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.23 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKT--ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMV 448
Cdd:PRK13650 7 VKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQ--DTHLFTGTIMENIRYG------RLSATDEEVRQAAKTSCADMFIKNMPegydtmlkgdgSNLSQGQRQLLNIARAA 520
Cdd:PRK13650 87 FQnpDNQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 521 LSKAPILVLDEATSSVD-------TRTEKHINEGMDAlmedrTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEK 593
Cdd:PRK13650 156 AMRPKIIILDEATSMLDpegrlelIKTIKGIRDDYQM-----TVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
....*..
gi 524455117 594 KGRYFEL 600
Cdd:PRK13650 231 GNDLLQL 237
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
394-585 |
1.06e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 76.18 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 394 PGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKD----ISLECLRENIAMVLQDTHLFTG-TIMENIRYGRL 468
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 469 SATDEEVRQaaktsCADMFIKNMpeGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGM 548
Cdd:cd03297 102 RKRNREDRI-----SVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 524455117 549 DALMED--RTTFVIAHRLSTI-RNADAIMVLENGEIIERG 585
Cdd:cd03297 175 KQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
369-590 |
1.06e-15 |
|
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: 76.25 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEcLRENIAMV 448
Cdd:cd03265 1 IEVENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHL---FTGTimENIR-YGRLsatdeevrQAAKTSCADMFIKNMPEGYDTMLKGDG--SNLSQGQRQLLNIARAALS 522
Cdd:cd03265 79 FQDLSVddeLTGW--ENLYiHARL--------YGVPGAERRERIDELLDFVGLLEAADRlvKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 523 KAPILVLDEATSSVDTRTEKHINEGMDALME--DRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
375-590 |
1.19e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 375 TFGYNpdkTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclRENIAMVLQDTHL 454
Cdd:PRK11432 15 RFGSN---TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 455 FTG-TIMENIRYG--RLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGdgsnlsqGQRQLLNIARAALSKAPILVLDE 531
Cdd:PRK11432 90 FPHmSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISG-------GQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 532 ATSSVDTRTEKHINEGMDALME--DRTTFVIAHRLS-TIRNADAIMVLENGEIIERGTHEEL 590
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
378-592 |
1.23e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.19 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 378 YNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNIN-----KGKITIDGVDI--KDISLECLRENIAMVLQ 450
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENI----RYGRLSAT----DEEVRQAAKTSCADMFIKNMpegydtmLKGDGSNLSQGQRQLLNIARAAL 521
Cdd:PRK14267 93 YPNPFPHlTIYDNVaigvKLNGLVKSkkelDERVEWALKKAALWDEVKDR-------LNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 522 SKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHR-LSTIRNADAIMVLENGEIIERGTHEELLE 592
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
368-593 |
1.26e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 368 DVL-VEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIdGVDIKdisleclrenIA 446
Cdd:COG0488 314 KVLeLEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 447 MVLQDTHLFTG--TIMENIRYGRLSATDEEVRQAaktsCADMfiknmpegydtMLKGDG-----SNLSQGQRQLLNIARA 519
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGY----LGRF-----------LFSGDDafkpvGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 520 ALSKAPILVLDEATSSVDTRTekhINEGMDALME-DRTTFVIAH-R--LSTIrnADAIMVLENGEIIER-GTHEELLEK 593
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIET---LEALEEALDDfPGTVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
376-583 |
1.41e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.03 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 376 FGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLE---CLRENIAMVLQDT 452
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 453 -------HLFTGTIMENIRYgrLSATDEEVRQAAKTSCADMFikNMPEGYDTMLKGdgsNLSQGQRQLLNIARAALSKAP 525
Cdd:PRK10419 99 isavnprKTVREIIREPLRH--LLSLDKAERLARASEMLRAV--DLDDSVLDKRPP---QLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 526 ILVLDEATSSVDtrteKHINEGMDALMEDR-----TTFV-IAHRLSTI-RNADAIMVLENGEIIE 583
Cdd:PRK10419 172 LLILDEAVSNLD----LVLQAGVIRLLKKLqqqfgTACLfITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
348-593 |
1.80e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 348 MDEAEEIDD-GKKLVLDKVHGDVLVEGVTFGYNP---DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINK 423
Cdd:COG1134 1 MSSMIEVENvSKSYRLYHEPSRSLKELLLRRRRTrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 424 GKITIDGvdikdisleclreNIAMVL-------QDthlFTGtiMENIR-YGR-LSATDEEVRQAAKtSCAD-----MFIk 489
Cdd:COG1134 81 GRVEVNG-------------RVSALLelgagfhPE---LTG--RENIYlNGRlLGLSRKEIDEKFD-EIVEfaelgDFI- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 490 NMPegydtmLKgdgsNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTIR 568
Cdd:COG1134 141 DQP------VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVR 210
|
250 260
....*....|....*....|....*.
gi 524455117 569 N-ADAIMVLENGEIIERGTHEELLEK 593
Cdd:COG1134 211 RlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
376-590 |
1.99e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 76.65 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 376 FGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTitnLITRFYNI---NKGKITIDGVDIK--DISLECLRENIAMVLQ 450
Cdd:PRK13639 9 YSYPDGTEALKGINFKAEKGEMVALLGPNGAGKST---LFLHFNGIlkpTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 --DTHLFTGTIMENIRYG--RLSATDEEVRQAAKTSCADMFIknmpEGYDtmlKGDGSNLSQGQRQLLNIARAALSKAPI 526
Cdd:PRK13639 86 npDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEALKAVGM----EGFE---NKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 527 LVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTI-RNADAIMVLENGEIIERGTHEEL 590
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
375-585 |
2.00e-15 |
|
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: 75.33 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 375 TFGynpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISlECLRENIAMVlqDTHL 454
Cdd:cd03268 9 TYG---KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALI--EAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 455 FTG--TIMENIRYgrlSATDEEVRQAAKTSCADMFiknmpeGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEA 532
Cdd:cd03268 83 FYPnlTARENLRL---LARLLGIRKKRIDEVLDVV------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 533 TSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLSTIRN-ADAIMVLENGEIIERG 585
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
339-579 |
2.42e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.08 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 339 AGAERV---FNVMDEAEEIDDGKKLVLDKVHGDVLVEGVTFgYNPD-KTILKDVSIFAHPGQKIALVGSTGAGKTTITNL 414
Cdd:COG4178 330 ATVDRLagfEEALEAADALPEAASRIETSEDGALALEDLTL-RTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 415 ITRFYNINKGKITI-DGVDIkdisleclreniaMVL-QDTHLFTGTIMENIRY--GRLSATDEEVRQAAKTSCADMFIKN 490
Cdd:COG4178 409 IAGLWPYGSGRIARpAGARV-------------LFLpQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAER 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 491 MPEGYDTmlkgdGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHinegMDALMEDR---TTFV-IAHRLST 566
Cdd:COG4178 476 LDEEADW-----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA----LYQLLREElpgTTVIsVGHRSTL 546
|
250
....*....|...
gi 524455117 567 IRNADAIMVLENG 579
Cdd:COG4178 547 AAFHDRVLELTGD 559
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
374-593 |
2.81e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTFGYNPDKTI-LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQD- 451
Cdd:PRK13648 13 VSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 THLFTGTIME-NIRYG---RLSATDEEVRQAAKT-SCADMFIKNMPEGYdtmlkgdgsNLSQGQRQLLNIARAALSKAPI 526
Cdd:PRK13648 93 DNQFVGSIVKyDVAFGlenHAVPYDEMHRRVSEAlKQVDMLERADYEPN---------ALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 527 LVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLEK 593
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
42-255 |
3.73e-15 |
|
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: 76.29 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLIdstkTSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIREHL 121
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVF----LEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 122 FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIF-SGTITLIgTLALMLYTNWVLAVVTIVVSPII----A 196
Cdd:cd18584 77 LARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVlAAIVPLL-ILVAVFPLDWVSALILLVTAPLIplfmI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 197 KIGTAIAGKSRkyfmKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLR 255
Cdd:cd18584 156 LIGKAAQAASR----RQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYR 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
368-606 |
6.41e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.44 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 368 DVLVEGVTFGYNP----DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITI------DGVDIKDis 437
Cdd:PRK13634 2 DITFQKVEHRYQYktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKK-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 438 LECLRENIAMVLQ--DTHLFTGTIMENIRYGRLS--ATDEEVRQAAKTSCAdmfIKNMPEGYdtmLKGDGSNLSQGQRQL 513
Cdd:PRK13634 80 LKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEEL---LARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 514 LNIArAALSKAP-ILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEE 589
Cdd:PRK13634 154 VAIA-GVLAMEPeVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPRE 232
|
250
....*....|....*..
gi 524455117 590 LLEKKGRYFELYTGLKE 606
Cdd:PRK13634 233 IFADPDELEAIGLDLPE 249
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
116-599 |
7.38e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 78.63 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 116 RIREHL----FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNStLVQIFSGTITLIGTLALMLYTNWVLAVVTIVV 191
Cdd:PLN03130 371 RLRSTLvaavFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQ-LHTLWSAPFRIIIAMVLLYQQLGVASLIGSLM 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 192 SPIIAKIGTAIAGKSRKYFMK--QQTDlgKVNGYIEETVTGQKVVKVFNYEenvvNEFSELNQSLRNSQV----KAQFIS 265
Cdd:PLN03130 450 LVLMFPIQTFIISKMQKLTKEglQRTD--KRIGLMNEVLAAMDTVKCYAWE----NSFQSKVQTVRDDELswfrKAQLLS 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 266 GIMGPCMNAMSQVNYTLTACVGSIIafasrwgGGVPFSALDIGGLTVFvnysrQFSR-PINELAQQVTNIMSALAGAERV 344
Cdd:PLN03130 524 AFNSFILNSIPVLVTVVSFGVFTLL-------GGDLTPARAFTSLSLF-----AVLRfPLFMLPNLITQAVNANVSLKRL 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 345 FNVMdEAEEIDDGKKLVLDKVHGDVLVEGVTFGYNP--DKTILKDVSIFAHPGQKIALVGSTGAGKTT-ITNLITRFYNI 421
Cdd:PLN03130 592 EELL-LAEERVLLPNPPLEPGLPAISIKNGYFSWDSkaERPTLSNINLDVPVGSLVAIVGSTGEGKTSlISAMLGELPPR 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 422 NKGKITIDGvdikdisleclreNIAMVLQDTHLFTGTIMENIRYGrlsATDEEVR--QAAKTSCADMFIKNMPEGYDTML 499
Cdd:PLN03130 671 SDASVVIRG-------------TVAYVPQVSWIFNATVRDNILFG---SPFDPERyeRAIDVTALQHDLDLLPGGDLTEI 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 500 KGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHI-NEGMDALMEDRTTFVIAHRLSTIRNADAIMVLEN 578
Cdd:PLN03130 735 GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHE 814
|
490 500
....*....|....*....|.
gi 524455117 579 GEIIERGTHEELLeKKGRYFE 599
Cdd:PLN03130 815 GMIKEEGTYEELS-NNGPLFQ 834
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
382-592 |
8.57e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNiNKGKITIDGVDIKDIS---LECLRENIAMVLQDTH----- 453
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPNsslnp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 454 -LFTGTIMEN---IRYGRLSATDEEVRqaaktscadmFIKNMPE-GYDTMLKGD-GSNLSQGQRQLLNIARAALSKAPIL 527
Cdd:PRK15134 378 rLNVLQIIEEglrVHQPTLSAAQREQQ----------VIAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 528 VLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEELLE 592
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
381-595 |
9.01e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 73.33 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRF--YNINKGKITIDGVDIKDISL-ECLRENIAMVLQDTHLFTG 457
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 TIMENirygrlsatdeevrqaaktscadmFIKNMPEGydtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLDEATSSVD 537
Cdd:cd03217 92 VKNAD------------------------FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 538 TRTEKHINEGMDALMEDRTTF-VIAH--RLSTIRNADAIMVLENGEIIERGTHE--ELLEKKG 595
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
371-533 |
1.03e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvDIKdisleclrenIAMVLQ 450
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENIRYG--RLSATDEEVRQA-AKTSCADMFIKNMPE---------GYD------TMLKGDG-------- 503
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGdaELRALEAELEELeAKLAEPDEDLERLAElqeefealgGWEaearaeEILSGLGfpeedldr 148
|
170 180 190
....*....|....*....|....*....|..
gi 524455117 504 --SNLSQGQRQLLNIARAALSKAPILVLDEAT 533
Cdd:COG0488 149 pvSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
385-594 |
1.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.40 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDI------KDIslECLRENIAMVLQ--DTHLFT 456
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDI--KQIRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 457 GTIMENIRYG--RLSATDEEVRQAAKTSCA------DMFIKNMPEgydtmlkgdgsnLSQGQRQLLNIARAALSKAPILV 528
Cdd:PRK13649 101 ETVLKDVAFGpqNFGVSQEEAEALAREKLAlvgiseSLFEKNPFE------------LSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 529 LDEATSSVDTRTEKHINEGMDALMEDRTTFV-IAHRLSTIRN-ADAIMVLENGEIIERGT------HEELLEKK 594
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKpkdifqDVDFLEEK 242
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
371-594 |
1.29e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.50 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDG--VDIKDISLECLRENIAMV 448
Cdd:PRK13636 8 VEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQ--DTHLFTGTIMENIRYG--RLSATDEEVRQ-----AAKTSCADMfiKNMPEGYdtmlkgdgsnLSQGQRQLLNIARA 519
Cdd:PRK13636 88 FQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKrvdnaLKRTGIEHL--KDKPTHC----------LSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 520 ALSKAPILVLDEATSSVDTrteKHINEGMDALME-----DRTTFVIAHRLSTIR-NADAIMVLENGEIIERGTHEELLEK 593
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDP---MGVSEIMKLLVEmqkelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
.
gi 524455117 594 K 594
Cdd:PRK13636 233 K 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-591 |
1.53e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTFGynpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNIN-----KGKITIDGVDIKDISLECLRENIAMV 448
Cdd:PRK14247 11 VSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTH-LFTGTIMENIRYG----RLSATDEE----VRQAAKTSCADMFIKNMpegydtmLKGDGSNLSQGQRQLLNIARA 519
Cdd:PRK14247 88 FQIPNpIPNLSIFENVALGlklnRLVKSKKElqerVRWALEKAQLWDEVKDR-------LDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 520 ALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAH-RLSTIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
371-585 |
1.58e-14 |
|
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: 72.61 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYnPDKTILKDVSIFAHPGQkIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDiSLECLRENIAMVLQ 450
Cdd:cd03264 3 LENLTKRY-GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENIRY----GRLSATDEEVRqaaktscADMFIK--NMPEGYDTMLKGdgsnLSQGQRQLLNIARAALSK 523
Cdd:cd03264 80 EFGVYPNfTVREFLDYiawlKGIPSKEVKAR-------VDEVLElvNLGDRAKKKIGS----LSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 524 APILVLDEATSSVD----TRTEKHINEgmdaLMEDRTTFVIAHRLSTIRN-ADAIMVLENGEIIERG 585
Cdd:cd03264 149 PSILIVDEPTAGLDpeerIRFRNLLSE----LGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
371-592 |
1.71e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.18 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIkDISLECLRENIAMVLQ 450
Cdd:COG1118 5 VRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 D----THLftgTIMENIRYG-RLSATDEEVRQAAKTSCADM-----FIKNMPegydtmlkgdgSNLSQGQRQLLNIARAA 520
Cdd:COG1118 83 HyalfPHM---TVAENIAFGlRVRPPSKAEIRARVEELLELvqlegLADRYP-----------SQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMED--RTT-FVI-----AHRLstirnADAIMVLENGEIIERGTHEELLE 592
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTvFVThdqeeALEL-----ADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
385-591 |
1.82e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDI-SLECLRENIAMVLQDTHLFTG-TIMEN 462
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 463 IRYGRLSATDEEVRQAAKtSCADMFiknmPEGYDTMLKGDGSnLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEK 542
Cdd:PRK11614 101 LAMGGFFAERDQFQERIK-WVYELF----PRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524455117 543 HINEGMDALMED-RTTFVIAHRLS-TIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK11614 175 QIFDTIEQLREQgMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
377-586 |
2.02e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.84 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 377 GYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS---LECLRENIAMVLQDTH 453
Cdd:PRK11153 13 QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 454 LFTG-TIMENIRYG-RLSATD-EEVRQ-----------AAKtscADMFiknmPegydtmlkgdgSNLSQGQRQLLNIARA 519
Cdd:PRK11153 93 LLSSrTVFDNVALPlELAGTPkAEIKArvtellelvglSDK---ADRY----P-----------AQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 520 ALSKAPILVLDEATSSVDTRTE-------KHINEGMDAlmedrTTFVIAHRLSTIRN-ADAIMVLENGEIIERGT 586
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTrsilellKDINRELGL-----TIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
371-591 |
2.19e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.25 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYN-----INKGKITIDGVdiKDIS-----LEC 440
Cdd:PRK11264 6 VKNLVKKFH-GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDTA--RSLSqqkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 441 LRENIAMVLQDTHLFTG-TIMENIRYGRLsATDEEVRQAAKTSCADMFIKNMPEGYDTMLKgdgSNLSQGQRQLLNIARA 519
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHrTVLENIIEGPV-IVKGEPKEEATARARELLAKVGLAGKETSYP---RRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 520 ALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVI-AHRLSTIRN-ADAIMVLENGEIIERGTHEELL 591
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
371-601 |
2.65e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.74 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKtILKDVSIFAHPGQKIALVGSTGAGKTTitnLItRFYNI----NKGKITIDG--------VDIKDISL 438
Cdd:PRK11124 5 LNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSS---LL-RVLNLlempRSGTLNIAGnhfdfsktPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 439 ecLRENIAMVLQDTHLFTG-TIMEN-----IRYgrLSATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGdgsnlsqGQRQ 512
Cdd:PRK11124 80 --LRRNVGMVFQQYNLWPHlTVQQNlieapCRV--LGLSKDQALARAEKLLERLRLKPYADRFPLHLSG-------GQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 513 LLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVI-AHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIvTHEVEVARKtASRVVYMENGHIVEQGDASCF 228
|
250
....*....|.
gi 524455117 591 LEKKGRYFELY 601
Cdd:PRK11124 229 TQPQTEAFKNY 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
385-593 |
3.15e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.23 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEC---LRENIAMVLQDThlftgtime 461
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNP--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 nirYGRL------SATDEE--------VRQAAKTSCADMFIKN--MPEGYDT---MLKGdgsnlsqGQRQLLNIARAALS 522
Cdd:PRK11308 102 ---YGSLnprkkvGQILEEpllintslSAAERREKALAMMAKVglRPEHYDRyphMFSG-------GQRQRIAIARALML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 523 KAPILVLDEATSSVDTRTEKHI-NEGMDALMEDRTTFV-IAHRLSTIRN-ADAIMVLENGEIIERGTHEELLEK 593
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVlNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-591 |
3.47e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.21 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTFGYnPDKTILKDVSIfAHPGQKI-ALVGSTGAGKTTITNLITRFYNI-----NKGKITIDGVDI---KDIsLEcLREN 444
Cdd:PRK14271 27 LTLGF-AGKTVLDQVSM-GFPARAVtSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDV-LE-FRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 445 IAMVLQDTHLFTGTIMENIRYGRLS---ATDEEVRQAAKTSCADMfikNMPEGYDTMLKGDGSNLSQGQRQLLNIARAAL 521
Cdd:PRK14271 103 VGMLFQRPNPFPMSIMDNVLAGVRAhklVPRKEFRGVAQARLTEV---GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 522 SKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLS-TIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
374-590 |
3.75e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.91 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQ--D 451
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 THLFTGTIMENIRYGRLS-ATDEEVRQAAKTSCADMFiknmpeGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLD 530
Cdd:PRK13652 89 DQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 531 EATSSVDTRTEKHINEGMDALMEDRTTFVI--AHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
78-344 |
5.48e-14 |
|
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: 73.01 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 78 ITSLMAGLALMAVVyvLGVGATYLQGRIMISVSQGTLKRIREHLFRkvqkLPVRYFDTNPTGDIMSRFtNDVDIIGEMLN 157
Cdd:cd18782 44 IGVVMLVAALLEAV--LTALRTYLFTDTANRIDLELGGTIIDHLLR----LPLGFFDKRPVGELSTRI-SELDTIRGFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 158 STLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIgTAIAGKS-RKYFMKQQTDLGKVNGYIEETVTGQKVVKV 236
Cdd:cd18782 117 GTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLL-TFLFGPIlRRQIRRRAEASAKTQSYLVESLTGIQTVKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 237 FNYEENVVNEFSE-LNQSLRNSqVKAQFISGIMGPCMNAMSQVNYTLTACVGSIIAFAsrwgggvpfSALDIGGLTVFVN 315
Cdd:cd18782 196 QNAELKARWRWQNrYARSLGEG-FKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLR---------GELTLGQLIAFRI 265
|
250 260
....*....|....*....|....*....
gi 524455117 316 YSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18782 266 LSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
371-592 |
5.61e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.81 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPdKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISL-ECLRENIAMVL 449
Cdd:cd03218 3 AENLSKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHLFTG-TIMENIRYGRLSATDEEVRQAAKtscadmfIKNMPE--GYDTMLKGDGSNLSQGQRQLLNIARAALSKAPI 526
Cdd:cd03218 82 QEASIFRKlTVEENILAVLEIRGLSKKEREEK-------LEELLEefHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 527 LVLDEATSSVDTRTEKHI--------NEGMDALMED---RTTFVIAHRlstirnadaIMVLENGEIIERGTHEELLE 592
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIqkiikilkDRGIGVLITDhnvRETLSITDR---------AYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
385-586 |
7.28e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNI-----NKGKITIDGVDI--KDISLECLRENIAMVLQDTHLFTG 457
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 TIMENIRYG-RLSA----TDEEV----RQAAktscadmfiknMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILV 528
Cdd:PRK14243 106 SIYDNIAYGaRINGykgdMDELVerslRQAA-----------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 529 LDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGT 586
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
385-592 |
8.33e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 74.34 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTT----ITNLITrfyniNKGKITIDGVDIKDIS---LECLRENIAMVLQDTHlftG 457
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPF---G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 ------TIMENIRYG----RLSATDEEVRQAAktscADMFIK-NMPEgyDTMlkgdgsN-----LSQGQRQLLNIARAAL 521
Cdd:COG4172 374 slsprmTVGQIIAEGlrvhGPGLSAAERRARV----AEALEEvGLDP--AAR------HrypheFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 522 SKAPILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEELLE 592
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
373-603 |
1.01e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.56 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 373 GVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDiSLECLRENIAMVLQ-D 451
Cdd:PRK13536 46 GVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 THLFTGTIMENI----RYGRLSATDEEVrqaaktscadmFIKNMPEGYDTMLKGDG--SNLSQGQRQLLNIARAALSKAP 525
Cdd:PRK13536 124 NLDLEFTVRENLlvfgRYFGMSTREIEA-----------VIPSLLEFARLESKADArvSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 526 ILVLDEATSSVDTRTEKHINEGMDALM-EDRTTFVIAHRLSTI-RNADAIMVLENG-EIIERGTHEELLEKKG-RYFELY 601
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPHALIDEHIGcQVIEIY 272
|
..
gi 524455117 602 TG 603
Cdd:PRK13536 273 GG 274
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
384-590 |
1.26e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.42 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 384 ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdiKDISLECLRE-NIAMVLQDTHLFTG-TIME 461
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSRLHARDrKVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 NIRYG--------RLSAtdEEVRQAAkTSCADMF-IKNMPEGYDtmlkgdgSNLSQGQRQLLNIARAALSKAPILVLDEA 532
Cdd:PRK10851 94 NIAFGltvlprreRPNA--AAIKAKV-TQLLEMVqLAHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 533 TSSVDTRTEKHINEGMDALMED---RTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEEL 590
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
369-563 |
2.75e-13 |
|
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: 67.95 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIdgvdikdisleCLRENIAMV 448
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFTGTIMENIRYgrlsatdeevrqaaktscadmfiknmPEGydtmlkgdgSNLSQGQRQLLNIARAALSKAPILV 528
Cdd:cd03223 70 PQRPYLPLGTLREQLIY--------------------------PWD---------DVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 524455117 529 LDEATSSVDTRTEKHInegMDALMEDRTTFV-IAHR 563
Cdd:cd03223 115 LDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
380-562 |
2.78e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 380 PDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEclReniAMVLQDTHLFT-GT 458
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--R---GVVFQNEGLLPwRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 459 IMENIRYG-RLSATDEEVRQAaktSCADMFIKNMPEGYDtmlKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVD 537
Cdd:PRK11248 87 VQDNVAFGlQLAGVEKMQRLE---IAHQMLKKVGLEGAE---KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*..
gi 524455117 538 TRTEKHINEGMDALMED--RTTFVIAH 562
Cdd:PRK11248 161 AFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
388-590 |
4.47e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 388 VSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDI-SLECLRENIAMVLQDTHLFTG-TIMEN--- 462
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLFREmTVIENllv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 463 -----IRYGRLS----------ATDEEVRQAAK-------TSCAdmfikNMPEGydtmlkgdgsNLSQGQRQLLNIARAA 520
Cdd:PRK11300 104 aqhqqLKTGLFSgllktpafrrAESEALDRAATwlervglLEHA-----NRQAG----------NLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
379-540 |
4.51e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 68.84 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 379 NPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLIT---RFYNINKGKITIDGvdiKDISLECLRENIAMVLQDTHLF 455
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 456 TG-TIMENIRYGRLSATDEEVRQAAKTSCADMFIknMPEGYDTMLKGDG-SNLSQGQRQLLNIARAALSKAPILVLDEAT 533
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVL--LRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
....*..
gi 524455117 534 SSVDTRT 540
Cdd:cd03234 172 SGLDSFT 178
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
80-267 |
4.98e-13 |
|
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: 70.06 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 80 SLMAGLALMAVVYVLGVGATYLQGRI-MISVSQGTlKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNS 158
Cdd:cd18590 34 AFTSAIGLMCLFSLGSSLSAGLRGGLfMCTLSRLN-LRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 159 TLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFN 238
Cdd:cd18590 113 NANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFK 192
|
170 180
....*....|....*....|....*....
gi 524455117 239 YEENVVNEFSELNQSLRNSQVKAQFISGI 267
Cdd:cd18590 193 AEEEEACRYSEALERTYNLKDRRDTVRAV 221
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
93-329 |
4.99e-13 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 69.84 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 93 VLGVGAtylqgrIMISVSQGTLKRIREH----------------LFRKVQKLPVRYFDTNPTGDIMSRFtNDVDIIGEML 156
Cdd:cd18588 43 VLAIGL------LVVALFEAVLSGLRTYlfshttnridaelgarLFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 157 NSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYfMKQQTDLGKVN-GYIEETVTGQKVVK 235
Cdd:cd18588 116 TGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRR-LEEKFQRGAENqSFLVETVTGIETVK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 236 VFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQVNYTLTACVGSIIAFASRwgggvpfsaLDIGGLTVFVN 315
Cdd:cd18588 195 SLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGE---------LTIGQLIAFNM 265
|
250
....*....|....
gi 524455117 316 YSRQFSRPINELAQ 329
Cdd:cd18588 266 LAGQVSQPVLRLVQ 279
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
112-344 |
5.77e-13 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 69.81 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 112 GTLKRIREHL----FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVV 187
Cdd:cd18589 62 ITMSRIHSRLqglvFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 188 TIVVSPIIAKIgTAIAGKSRKYFMKQ-QTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSE-LNQSLRnsqvkaqfis 265
Cdd:cd18589 142 TALGLPLLLLV-PKFVGKFQQSLAVQvQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQrLQKTYR---------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 266 gimgpcMNAMSQVNYTLTACVGSIIAFASRWG----GG--VPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALA 339
Cdd:cd18589 211 ------LNKKEAAAYAVSMWTSSFSGLALKVGilyyGGqlVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVG 284
|
....*
gi 524455117 340 GAERV 344
Cdd:cd18589 285 SSEKI 289
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
115-265 |
6.33e-13 |
|
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: 69.87 E-value: 6.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 115 KRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGE----MLNSTLVQIFSgtitLIGTLALMLYTNWVLAVVTIV 190
Cdd:cd18605 75 RRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDslpfILNILLAQLFG----LLGYLVVICYQLPWLLLLLLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 191 VSPIIAKIgtaiagksRKYFMK--------QQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELnqsLRNSQvKAQ 262
Cdd:cd18605 151 LAFIYYRI--------QRYYRAtsrelkrlNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEK---LENNQ-RAQ 218
|
...
gi 524455117 263 FIS 265
Cdd:cd18605 219 LAS 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
372-581 |
8.50e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.98 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 372 EGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDI---KDISLECLRENIAMV 448
Cdd:PRK10908 5 EHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFTG-TIMENIRYGRL--SATDEEVRQAAKTSCADMFIKNMPEGYDTMLKGdgsnlsqGQRQLLNIARAALSKAP 525
Cdd:PRK10908 85 FQDHHLLMDrTVYDNVAIPLIiaGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSG-------GEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 526 ILVLDEATSSVDtrteKHINEGMDALMED-----RTTFVIAHRLSTI-RNADAIMVLENGEI 581
Cdd:PRK10908 158 VLLADEPTGNLD----DALSEGILRLFEEfnrvgVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
371-591 |
9.34e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.97 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKTI--LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMV 448
Cdd:PRK13642 7 VENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQ--DTHLFTGTIMENIRYGRLSA---TDEEVRQAAKTscadMFIKNMPEgYDTMlkgDGSNLSQGQRQLLNIARAALSK 523
Cdd:PRK13642 87 FQnpDNQFVGATVEDDVAFGMENQgipREEMIKRVDEA----LLAVNMLD-FKTR---EPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 524 APILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
385-579 |
1.27e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLREN-IAMVLQDTHLFTG-TIMEN 462
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 463 IRYGRLSatdeeVRQAAKTSCADMfiKNMPEGYDTMLKGDG---------SNLSQGQRQLLNIARAALSKAPILVLDEAT 533
Cdd:PRK09700 101 LYIGRHL-----TKKVCGVNIIDW--REMRVRAAMMLLRVGlkvdldekvANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 524455117 534 SSVDTRTEKHINEGMDALMEDRTTFV-IAHRLSTIRN-ADAIMVLENG 579
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
400-590 |
1.40e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.11 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 400 LVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEC----------------LRENIAMVLQ--DTHLFTGTIME 461
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 NIRYG--RLSATDEEVRQAAKTSCADMFIKnmpegyDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTR 539
Cdd:PRK13631 137 DIMFGpvALGVKKSEAKKLAKFYLNKMGLD------DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 524455117 540 TEKHINEG-MDALMEDRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:PRK13631 211 GEHEMMQLiLDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
387-592 |
3.38e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.32 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 387 DVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISleCLRENIAMVLQDTHLFTG-TIMENIRY 465
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFPHmTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 466 G----RLSATDEEVRQAAKTSCADM--FIKNMPEgydtmlkgdgsNLSQGQRQLLNIARaALSKAP-ILVLDEATSSVDT 538
Cdd:PRK11607 115 GlkqdKLPKAEIASRVNEMLGLVHMqeFAKRKPH-----------QLSGGQRQRVALAR-SLAKRPkLLLLDEPMGALDK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 539 RTEKHIN-EGMDALMEDRTTFV-IAH-RLSTIRNADAIMVLENGEIIERGTHEELLE 592
Cdd:PRK11607 183 KLRDRMQlEVVDILERVGVTCVmVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
385-607 |
3.56e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDI----KDISLECLRENIAMVLQ--DTHLFTGT 458
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 459 IMENIRYG--RLSATDEEVRQAAKTSCADM-FIKNmpegydtMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSS 535
Cdd:PRK13646 103 VEREIIFGpkNFKMNLDEVKNYAHRLLMDLgFSRD-------VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 536 VDTRTEKHINEGMDALMED--RTTFVIAHRLSTI-RNADAIMVLENGEIIERGTHEELLEKKGRYFELYTGLKEL 607
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDKKKLADWHIGLPEI 250
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
377-576 |
4.21e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.33 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 377 GYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITrfyninkgkitidGVdIKDISLECLRE---NIAMVLQDTH 453
Cdd:NF040873 1 GY-GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLA-------------GV-LRPTSGTVRRAggaRVAYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 454 L---FTGTIMENIRYG---------RLSATDeevRQAAKTSCADMfiknmpeGYDTMLKGDGSNLSQGQRQLLNIARAAL 521
Cdd:NF040873 66 VpdsLPLTVRDLVAMGrwarrglwrRLTRDD---RAAVDDALERV-------GLADLAGRQLGELSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 522 SKAPILVLDEATSSVDTRTEKHINEGMDALMED-RTTFVIAHRLSTIRNADAIMVL 576
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
371-591 |
4.34e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.60 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKtILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNIN-----KGKITIDGVDI--KDISLECLRE 443
Cdd:PRK14258 10 VNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNRLRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 NIAMVLQDTHLFTGTIMENIRYG-RLSA------TDEEVRQAAKTscADMF--IKNMpegydtmLKGDGSNLSQGQRQLL 514
Cdd:PRK14258 89 QVSMVHPKPNLFPMSVYDNVAYGvKIVGwrpkleIDDIVESALKD--ADLWdeIKHK-------IHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 515 NIARAALSKAPILVLDEATSSVDTRTEKHINEGMDA--LMEDRTTFVIAHRLSTI-RNADAIMVLEN-----GEIIERGT 586
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLVEFGL 239
|
....*
gi 524455117 587 HEELL 591
Cdd:PRK14258 240 TKKIF 244
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
78-327 |
5.55e-12 |
|
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: 66.92 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 78 ITSLMAGLALMAVVYVLGVgatYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLN 157
Cdd:cd18561 35 IMPPLAGIAGVIVLRAALL---WLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 158 STLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPII----AKIGTAIAGKSRKYFMKqqtdLGKVNGYIEETVTGQKV 233
Cdd:cd18561 112 RYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIplspALWDRLAKDTGRRHWAA----YGRLSAQFLDSLQGMTT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 234 VKVFNYEENVVNEFSELNQSLRNSQVK----AQFISGIMGpcmnamsqvNYTLTACVGSIIAFASRWGGGvpfsALDIGG 309
Cdd:cd18561 188 LKAFGASKRRGNELAARAEDLRQATMKvlavSLLSSGIMG---------LATALGTALALGVGALRVLGG----QLTLSS 254
|
250
....*....|....*...
gi 524455117 310 LTVFVNYSRQFSRPINEL 327
Cdd:cd18561 255 LLLILFLSREFFRPLRDL 272
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
381-576 |
6.71e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIM 460
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 461 ENIRYG---RLSATDEevrqaaKTSCADMFIKNMPEgydTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVD 537
Cdd:PRK10247 99 DNLIFPwqiRNQQPDP------AIFLDDLERFALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 524455117 538 TRTEKHINEGMDALMEDRTTFVI--AHRLSTIRNADAIMVL 576
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITL 210
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
68-196 |
8.73e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 66.47 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 68 IDSTKTSQQKITSLMAGLALMAVVYVLGVGATYLQGRIM-ISVSqgtlKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFT 146
Cdd:cd18602 39 ITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAgLRAA----RRLHDRMLRNIVRAPMRFFDTTPIGRILNRFS 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 524455117 147 NDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIvvsPIIA 196
Cdd:cd18602 115 SDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALI---PIII 161
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
394-589 |
9.19e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.82 E-value: 9.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 394 PGQKI-ALVGSTGAGKTTITNLITRFYNINKGKITIDG---VDI-KDISLECLRENIAMVLQDTHLFTG-TIMENIRYGr 467
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAeKGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 468 lsatdeevrqaaktsCAdmfiKNMPE---------GYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVD- 537
Cdd:PRK11144 101 ---------------MA----KSMVAqfdkivallGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDl 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 538 ----------TRTEKHINEGMdalmedrttFVIAHRLSTI-RNADAIMVLENGEIIERGTHEE 589
Cdd:PRK11144 162 prkrellpylERLAREINIPI---------LYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
371-585 |
1.02e-11 |
|
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: 64.61 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVT--FGynpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDG--VDIKDisleclRENIA 446
Cdd:cd03269 3 VENVTkrFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA------RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 447 MVLQDTHLFTG-TIMENIRY-GRLSATDeevRQAAKTSCADMFiknmpEGYDTMLKGDGS--NLSQGQRQLLNIARAALS 522
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYlAQLKGLK---KEEARRRIDEWL-----ERLELSEYANKRveELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 523 KAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVI-AHRLSTI-RNADAIMVLENGEIIERG 585
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
46-261 |
1.07e-11 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 66.03 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 46 VLVSSASTLCGsyLLRPIING-LIDSTKTSQQkiTSLMAGLALMAVVYVLGVGAT---------YLQGRIMISVSQGTLk 115
Cdd:cd18779 8 LLASLLLQLLG--LALPLLTGvLVDRVIPRGD--RDLLGVLGLGLAALVLTQLLAgllrshlllRLRTRLDTQLTLGFL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 116 rirEHLFRkvqkLPVRYFDTNPTGDIMSRFtNDVDIIGEML-NSTLVQIFSGTItLIGTLALMLYTNWVLAVVTIVVSpi 194
Cdd:cd18779 83 ---EHLLR----LPYRFFQQRSTGDLLMRL-SSNATIRELLtSQTLSALLDGTL-VLGYLALLFAQSPLLGLVVLGLA-- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 195 IAKIGTAIAGKSRKYFMKQQ--TDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFS-----ELNQSLRNSQVKA 261
Cdd:cd18779 152 ALQVALLLATRRRVRELMARelAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSnlfvdQLNASLRRGRLDA 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
384-590 |
1.51e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 384 ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS-LECLRENIAMVLQDTHLFTG-TIME 461
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 NIRYGRLSATDEEVRQAAKtscadmfIKNMPEGYDtmLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSS---VDT 538
Cdd:PRK15439 106 NILFGLPKRQASMQKMKQL-------LAALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASltpAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 524455117 539 RTE-KHINEgmdALMEDRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEEL 590
Cdd:PRK15439 177 ERLfSRIRE---LLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
39-204 |
1.73e-11 |
|
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: 65.18 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 39 IAAAFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSL--MAGLALMAVVYVL-GVGATYLQGRIMISVSqgtlK 115
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLyyLGIYALISLLSVLlGTLRYLLFFFGSLRAS----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 116 RIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVV---- 191
Cdd:cd18604 77 KLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLaaly 156
|
170 180 190
....*....|....*....|....*....|....*
gi 524455117 192 ----------------------SPIIAKIGTAIAG 204
Cdd:cd18604 157 vyigrlylrasrelkrlesvarSPILSHFGETLAG 191
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
92-312 |
1.99e-11 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 65.38 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 92 YVLGVGAT-----YLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSG 166
Cdd:cd18558 64 YYLIIGAIvlitaYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 167 TITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNE 246
Cdd:cd18558 144 IATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETR 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 247 FSELNQSLRNSQVKAQFISGIMGPCMNAMSQVNYTLTACVGSIIAFASRWGGG----VPFSALdIGGLTV 312
Cdd:cd18558 224 YAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGevltVFFSVL-IGAFSA 292
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
381-540 |
2.19e-11 |
|
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: 63.03 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNIN--KGKITIDGVDIKdislECLRENIAMVLQ-DTHLFTG 457
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD----KNFQRSTGYVEQqDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 TIMENIRYgrlSAtdeevrqaaktscadmfiknmpegydtMLKGdgsnLSQGQRQLLNIARAALSKAPILVLDEATSSVD 537
Cdd:cd03232 95 TVREALRF---SA---------------------------LLRG----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
...
gi 524455117 538 TRT 540
Cdd:cd03232 141 SQA 143
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
372-583 |
2.48e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 372 EGVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQD 451
Cdd:PRK10522 326 RNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 THLFTGTIMEniryGRLSATDEEVRQ-------AAKTSCADMFIKNMpegydtmlkgdgsNLSQGQRQLLNIARAALSKA 524
Cdd:PRK10522 406 FHLFDQLLGP----EGKPANPALVEKwlerlkmAHKLELEDGRISNL-------------KLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 525 PILVLDEATSSVDTRTEKHINEGMDALMED--RTTFVIAHRLSTIRNADAIMVLENGEIIE 583
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
372-593 |
4.38e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 372 EGVTFGYNPDKTI----LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS----LECLRE 443
Cdd:PRK13643 5 EKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 NIAMVLQ--DTHLFTGTIMENIRYG--RLSATDEEvrqAAKTSCADMFIKNMPEGYdtmLKGDGSNLSQGQRQLLNIARA 519
Cdd:PRK13643 85 KVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEK---AEKIAAEKLEMVGLADEF---WEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 520 ALSKAPILVLDEATSSVDTRTEKHINEGMDALMED-RTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEELLEK 593
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
369-593 |
5.09e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.57 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPD-----KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS-LECLR 442
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 443 ENIAMVLQ--DTHLFTGTIMENIRYG--RLSATDEEVRQAAKTSCADMfikNMPE--GYDTMLkgdgsnLSQGQRQLLNI 516
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIRERVDESLKKV---GMYEyrRHAPHL------LSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 517 ARAALSKAPILVLDEATSSVDTRTEKhinEGMDALME-----DRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRR---EVVNTIKElnkkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIF 232
|
..
gi 524455117 592 EK 593
Cdd:PRK13633 233 KE 234
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
120-268 |
5.19e-11 |
|
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: 63.73 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 120 HLFRKVQKLPVRYFDTNPTGDIMSRFtNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIg 199
Cdd:cd18568 80 DFYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLL- 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 200 TAIAGKSRKYFMKQQTDLG-KVNGYIEETVTGQKVVKVFNYEENVV----NEFSE-LNQSLRNSQ--VKAQFISGIM 268
Cdd:cd18568 158 TLLSSPKLKRNSREIFQANaEQQSFLVEALTGIATIKALAAERPIRwrweNKFAKaLNTRFRGQKlsIVLQLISSLI 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
367-606 |
5.68e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.87 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVLVEGVTFGYNpDKT-----ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKiTIDG-----VDIKDI 436
Cdd:PRK13645 5 KDIILDNVSYTYA-KKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGdyaipANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 437 -SLECLRENIAMVLQ--DTHLFTGTIMENIRYG--RLSATDEEVRQAAKTScadMFIKNMPEGYdtmLKGDGSNLSQGQR 511
Cdd:PRK13645 83 kEVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYKKVPEL---LKLVQLPEDY---VKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 512 QLLNIARAALSKAPILVLDEATSSVDTRTEK---HINEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERG--- 585
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGspf 236
|
250 260
....*....|....*....|....*...
gi 524455117 586 ---THEELLEK----KGRYFELYTGLKE 606
Cdd:PRK13645 237 eifSNQELLTKieidPPKLYQLMYKLKN 264
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
374-592 |
5.99e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 65.09 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTFG-YNPDKTILKDVSIFAHPGQKIALVGSTGAGKT----TITNLITRFYNINKGKITIDGVDIKDISLECLRE----N 444
Cdd:COG4172 14 VAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 445 IAMVLQD--THL---FT-GT-IMENIR-YGRLSatdeevRQAAKTSCADMF----IKNmPEgydTMLKGDGSNLSQGQRQ 512
Cdd:COG4172 94 IAMIFQEpmTSLnplHTiGKqIAEVLRlHRGLS------GAAARARALELLervgIPD-PE---RRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 513 LLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFV--IAHRLSTIRN-ADAIMVLENGEIIERGTHEE 589
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALllITHDLGVVRRfADRVAVMRQGEIVEQGPTAE 243
|
...
gi 524455117 590 LLE 592
Cdd:COG4172 244 LFA 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
385-592 |
6.54e-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: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDG--VDIKDiSLECLRENIAMVLQDTHLF-TGTIME 461
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRS-PRDAIALGIGMVHQHFMLVpNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 NIRYGR---------LSATDEEVRQAAKTscadmfiknmpegY------DTMLkgdgSNLSQGQRQLLNIARAALSKAPI 526
Cdd:COG3845 100 NIVLGLeptkggrldRKAARARIRELSER-------------YgldvdpDAKV----EDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 527 LVLDEATsSVDTRTEKhinegmDALM--------EDRTTFVIAHRLSTIR-NADAIMVLENGEIIERG-----THEELLE 592
Cdd:COG3845 163 LILDEPT-AVLTPQEA------DELFeilrrlaaEGKSIIFITHKLREVMaIADRVTVLRRGKVVGTVdtaetSEEELAE 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
381-542 |
6.67e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdiKDISLECLRENIAMV-----LQDtHLf 455
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLghrnaMKP-AL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 456 tgTIMENIRYGR--LSATDEEVRQAAktscADM---FIKNMPEGYdtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLD 530
Cdd:PRK13539 89 --TVAENLEFWAafLGGEELDIAAAL----EAVglaPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
|
170
....*....|..
gi 524455117 531 EATSSVDTRTEK 542
Cdd:PRK13539 153 EPTAALDAAAVA 164
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
371-580 |
1.19e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 59.77 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdikdisleclRENIAMVLQ 450
Cdd:cd03221 3 LENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 dthlftgtimenirygrlsatdeevrqaaktscadmfiknmpegydtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLD 530
Cdd:cd03221 71 -------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524455117 531 EATSSVDTRTEKHINEGMDALmeDRTTFVIAHRLSTIRN-ADAIMVLENGE 580
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEY--PGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
86-249 |
1.31e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 62.72 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 86 ALMAVVYVLGVGATYLQGRIMISVSQgtlkRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFS 165
Cdd:cd18601 67 GLTAATFVFGFLRSLLFFHVAVSASK----NLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 166 GTITLIGTLALMLYTN-WVLavvtIVVSPIIakigtAIAGKSRKYFMKQQTDLGKVNG--------YIEETVTGQKVVKV 236
Cdd:cd18601 143 LLLQVVGVVLLAVVVNpWVL----IPVIPLV-----ILFLFLRRYYLKTSREVKRIEGttrspvfsHLSSTLQGLWTIRA 213
|
170
....*....|...
gi 524455117 237 FNYEENVVNEFSE 249
Cdd:cd18601 214 YSAQERFQEEFDA 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
381-540 |
2.43e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRfyNINKGKITIDGVDIKDISL-ECLRENIAMVLQ-DTHLFTGT 458
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLdSSFQRSIGYVQQqDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 459 IMENIRYG---RLSAtdeEVRQAAKTSCADMFIK--NMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILV-LDEA 532
Cdd:TIGR00956 853 VRESLRFSaylRQPK---SVSKSEKMEYVEEVIKllEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
....*...
gi 524455117 533 TSSVDTRT 540
Cdd:TIGR00956 930 TSGLDSQT 937
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
382-563 |
3.30e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.36 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYninKGKITIDGVDIKDISLEclREniamvlqdthlftGTIME 461
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTPVAGCVDVPDNQFG--RE-------------ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 NIryGRLSATDE--EVRQAAKTSCADMFIKNMPEgydtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLDEATSSVDTR 539
Cdd:COG2401 105 AI--GRKGDFKDavELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 524455117 540 TEKHINEGM-DALMEDRTTFVIA-HR 563
Cdd:COG2401 171 TAKRVARNLqKLARRAGITLVVAtHH 196
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
42-343 |
3.33e-10 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 61.47 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLidsTKTSQQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIREHL 121
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNAL---TLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 122 FRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLA-LMLYTNWVLAVVTIvVSPIIAKIGT 200
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVvFAFHFGAWLALIVF-LSVLLYGVFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 201 AIAGKSRKYFMKQQTDL-GKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFISGImgpcMNAMSQVN 279
Cdd:cd18560 157 IKVTEWRTKFRRAANKKdNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSL----LNVGQQLI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 280 YTLTACVGSIIAfASRWGGGvpfsALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAER 343
Cdd:cd18560 233 IQLGLTLGLLLA-GYRVVDG----GLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMEN 291
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
385-592 |
3.67e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdiKDISLECLREN----IAMVLQDTHLFTG-TI 459
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELNLIPQlTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 460 MENIRYGRlsatdEEVRQAAKTSCADMFIK--------NMPEGYDTMLkgdgSNLSQGQRQLLNIARAALSKAPILVLDE 531
Cdd:PRK10762 97 AENIFLGR-----EFVNRFGRIDWKKMYAEadkllarlNLRFSSDKLV----GELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 532 ATSSV-DTRTE---KHINEGMDalmEDRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEELLE 592
Cdd:PRK10762 168 PTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIFEiCDDVTVFRDGQFIAEREVADLTE 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
369-588 |
4.08e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.05 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPDKTILKDVSiFAHPGQKIA-LVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKdislECLREN-IA 446
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDAS-FTVPGGSIAaLVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 447 MVLQDTH-------LFTGTIMENiRYG------RLSATDEEVRQAA--KTSCADMFIKNMPEgydtmlkgdgsnLSQGQR 511
Cdd:PRK15056 82 YVPQSEEvdwsfpvLVEDVVMMG-RYGhmgwlrRAKKRDRQIVTAAlaRVDMVEFRHRQIGE------------LSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 512 QLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALM-EDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHE 588
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
380-590 |
4.49e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.48 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 380 PDKTILKDVSIFAHPGQKIALVGSTGAGKT----TITNLITRFYNINKGKITIDGvdiKDISLECLR-ENIAmvlqdthl 454
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG---KPVAPCALRgRKIA-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 455 ftgTIMENIRygrlSATD----------EEVRQAAKTSCADMFIKNMP----EGYDTMLKGDGSNLSQGQRQLLNIARAA 520
Cdd:PRK10418 83 ---TIMQNPR----SAFNplhtmhtharETCLALGKPADDATLTAALEavglENAARVLKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRT--TFVIAHRLSTI-RNADAIMVLENGEIIERGTHEEL 590
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
385-540 |
7.72e-10 |
|
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: 59.37 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITID----GVDIKDIS----LECLRENIAMVLQdthlFT 456
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreiLALRRRTIGYVSQ----FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 457 GTImeniryGRLSATD---------EEVRQAAKTSCADMFIK-NMPEgydtmlkgdgsNL--------SQGQRQLLNIAR 518
Cdd:COG4778 103 RVI------PRVSALDvvaepllerGVDREEARARARELLARlNLPE-----------RLwdlppatfSGGEQQRVNIAR 165
|
170 180
....*....|....*....|..
gi 524455117 519 AALSKAPILVLDEATSSVDTRT 540
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAAN 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
385-582 |
8.69e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIK-DISLECLRENIAMVLQDTHLFTG-TIMEN 462
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 463 IRYGR-----LSATDEEVRQAAKTSCADMFIKNMPegydtmlKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVD 537
Cdd:PRK10982 94 MWLGRyptkgMFVDQDKMYRDTKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 524455117 538 TRTEKHINEGMDALMEDRTTFV-IAHRLSTIRN-ADAIMVLENGEII 582
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVyISHKMEEIFQlCDEITILRDGQWI 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-600 |
8.86e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 8.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVT--FGynpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISleclRENIA-- 446
Cdd:COG4152 4 LKGLTkrFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 447 ---------MvlqdthlftgTIMENIRY-GRLSATDeevRQAAKTSCADMFIK-NMPEGYDTMLKgdgsNLSQGQRQLLN 515
Cdd:COG4152 77 peerglypkM----------KVGEQLVYlARLKGLS---KAEAKRRADEWLERlGLGDRANKKVE----ELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 516 IARAALSKAPILVLDEATSSVDTrtekhINEGM--DALME--DRTTFVI--AHRLSTI-RNADAIMVLENGEIIERGTHE 588
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDP-----VNVELlkDVIRElaAKGTTVIfsSHQMELVeELCDRIVIINKGRKVLSGSVD 214
|
250
....*....|...
gi 524455117 589 ELLEK-KGRYFEL 600
Cdd:COG4152 215 EIRRQfGRNTLRL 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
385-581 |
9.58e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 58.21 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS-LECLRENIAMVLQDTH---LFTG-TI 459
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDRKregLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 460 MENIRYGRLsatdeevrqaaktscadmfiknmpegydtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLDEATSSVDTR 539
Cdd:cd03215 96 AENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 524455117 540 TEKHINEGMDALMEDRTTFVIahrLST-----IRNADAIMVLENGEI 581
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
382-591 |
9.65e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.52 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISL-ECLRENIAMVLQDTHLFTgtim 460
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFR---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 461 enirygRLSATDE-----EVRQ-AAKTSCADMFIKNMPEGYDTMLKGD-GSNLSQGQRQLLNIARAALSKAPILVLDEAT 533
Cdd:PRK10895 92 ------RLSVYDNlmavlQIRDdLSAEQREDRANELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 534 SSVD-------TRTEKHINE-GMDALMED---RTTFVIAHRlstirnadaIMVLENGEIIERGTHEELL 591
Cdd:PRK10895 166 AGVDpisvidiKRIIEHLRDsGLGVLITDhnvRETLAVCER---------AYIVSQGHLIAHGTPTEIL 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
388-586 |
1.78e-09 |
|
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: 61.18 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 388 VSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIkDISLECLRENIAMVLQDTHLFTG-TIMENIR-Y 465
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILfY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 466 GRLSATDEEVRQaaktscadMFIKNMPEgyDTML----KGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTE 541
Cdd:TIGR01257 1028 AQLKGRSWEEAQ--------LEMEAMLE--DTGLhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 524455117 542 KHINEGMDALMEDRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGT 586
Cdd:TIGR01257 1098 RSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
385-592 |
2.04e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS---LECLRENIAMVLQDT-------HL 454
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyasldprQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 455 FTGTIMENIRYGRLSATDEEVRQAAktscadmfiknmpegydTMLKGDG----------SNLSQGQRQLLNIARAALSKA 524
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARVA-----------------WLLERVGllpehawrypHEFSGGQRQRICIARALALNP 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 525 PILVLDEATSSVDTRTEKH-INEGMDALMEDRTTFV-IAHRLSTI-RNADAIMVLENGEIIERGTHEELLE 592
Cdd:PRK10261 483 KVIIADEAVSALDVSIRGQiINLLLDLQRDFGIAYLfISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
385-591 |
2.53e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.65 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDG--VDIKDISLECLRenIAMVLQDThlfTGTIMEN 462
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQR--IRMIFQDP---STSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 463 IRYGRL--------SATDEEVRQAAKTSCADM--FIKNMPEGYDTMLkgdgsnlSQGQRQLLNIARAALSKAPILVLDEA 532
Cdd:PRK15112 104 QRISQIldfplrlnTDLEPEQREKQIIETLRQvgLLPDHASYYPHML-------APGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 533 TSSVDTRTEKHINEGMDALMEDRT---TFVIAHRLSTIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGisyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
91-187 |
2.55e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 58.64 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 91 VYV-LGVG---ATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSG 166
Cdd:cd18606 40 IYAgLGVLqaiFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYT 119
|
90 100
....*....|....*....|..
gi 524455117 167 TITLIGTLALML-YTNWVLAVV 187
Cdd:cd18606 120 LSSIIGTFILIIiYLPWFAIAL 141
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
63-252 |
2.85e-09 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 58.71 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 63 IINGLIDSTKTSQQKITSLMAGLAL-MAVVYVLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDI 141
Cdd:cd18574 22 LVNVISRSLKETNGDFIEDLKKPALkLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 142 MSRFTNDVdiigEMLNSTLVQIFS----GTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDL 217
Cdd:cd18574 102 VNRLTADV----QEFKSSFKQCVSqglrSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQV 177
|
170 180 190
....*....|....*....|....*....|....*
gi 524455117 218 GKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQ 252
Cdd:cd18574 178 AKATGVADEALGNIRTVRAFAMEDRELELYEEEVE 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
383-560 |
3.02e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 383 TILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLE---CLR-ENIAMVLQDTHLF-TG 457
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIpTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 TIMENIRYGRL--SATDEEVRQAAKTSCADMfiknmpeGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSS 535
Cdd:PRK10584 104 NALENVELPALlrGESSRQSRNGAKALLEQL-------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180
....*....|....*....|....*
gi 524455117 536 VDTRTEKHINEGMDALMEDRTTFVI 560
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLI 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
385-582 |
3.15e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNIN--KGKITIDGVDIKDISL-ECLRENIAMVLQDTHLFTG-TIM 460
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 461 ENIRYGRlsatdeEVRQAAKTSCADMFIKnmpegYDTMLKGDG---------SNLSQGQRQLLNIARAALSKAPILVLDE 531
Cdd:PRK13549 101 ENIFLGN------EITPGGIMDYDAMYLR-----AQKLLAQLKldinpatpvGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 532 ATSSVdtrTEKHINEGMDALMEDRTTFV----IAHRLSTIRN-ADAIMVLENGEII 582
Cdd:PRK13549 170 PTASL---TESETAVLLDIIRDLKAHGIaciyISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
380-582 |
3.31e-09 |
|
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: 56.89 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 380 PDKTILKDVSIFAHPGQKIALVGSTGAGKTT----ITNLITRFYNINkGKITIDGVDIKDISLECLRENIAMVLQDTHLF 455
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 456 TGTIMENIRYGRLSATDEEVRqaaktscadmfiknmpegydtmlkgdgsNLSQGQRQLLNIARAALSKAPILVLDEATSS 535
Cdd:cd03233 97 TLTVRETLDFALRCKGNEFVR----------------------------GISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524455117 536 VDTRTEKHINEGMDAL--MEDRTTFVIAHRLS-TIRNA-DAIMVLENGEII 582
Cdd:cd03233 149 LDSSTALEILKCIRTMadVLKTTTFVSLYQASdEIYDLfDKVLVLYEGRQI 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
369-581 |
6.02e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.99 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIsleclRENIAMV 448
Cdd:PRK11247 13 LLLNAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQDTHLFT-GTIMENIRYGRLSATDEEVRQA-AKTSCADMfIKNMPegydtmlkgdgSNLSQGQRQLLNIARAALSKAPI 526
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLKGQWRDAALQAlAAVGLADR-ANEWP-----------AALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 527 LVLDEATSSVD--TRTEkhinegMDALMEDR------TTFVIAHRLS-TIRNADAIMVLENGEI 581
Cdd:PRK11247 155 LLLDEPLGALDalTRIE------MQDLIESLwqqhgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
384-582 |
6.49e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 384 ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECL----RENIAMVLQDTHLFTG-T 458
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 459 IMENIRYGRLSATDEEVRQAAKtscADMFIKNMpeGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDT 538
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLR---AQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 524455117 539 RTEKhinEGMDALMEDR----TTFVIAHRLSTIRNADAIMVLENGEII 582
Cdd:PRK10535 178 HSGE---EVMAILHQLRdrghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
105-267 |
6.69e-09 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits 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. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 57.56 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 105 IMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNStLVQIFSGTITLIGTLALMLYTNW-- 182
Cdd:cd18553 77 LLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVIQS-FLFILSEIFVILFIYSLLLYVNWki 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 183 --VLAVVTIVVSPIIAKIgtaIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVK 260
Cdd:cd18553 156 tlVLTLFLGLNVFFITKI---VSKKIKKQGKKREESQKKFYKILSETFGNFKIIKLKSNEKEILKNFSQASLKFAKANII 232
|
....*..
gi 524455117 261 AQFISGI 267
Cdd:cd18553 233 NQTLQTV 239
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
384-565 |
7.26e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.75 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 384 ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEC---LREN-IAMVLQDTHLFTG-T 458
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 459 IMENIRYGRLSATDEevRQAAKTSCADMFiknMPEGYDTMLKGDGSNLSQGQRQLLNIARaALSKAPILVL-DEATSSVD 537
Cdd:PRK11629 104 ALENVAMPLLIGKKK--PAEINSRALEML---AAVGLEHRANHRPSELSGGERQRVAIAR-ALVNNPRLVLaDEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 524455117 538 TRTEKHINEGMDAL-MEDRTTF-VIAHRLS 565
Cdd:PRK11629 178 ARNADSIFQLLGELnRLQGTAFlVVTHDLQ 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
381-590 |
7.42e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.73 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIslECLRENIAMVLQDTHLFTG-TI 459
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMVFQSYALYPHlSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 460 MENIRYG-RLSAT-----DEEVRQAAKTSCADMFIKNMPEGydtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLDEAT 533
Cdd:PRK11000 93 AENMSFGlKLAGAkkeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 534 SSVD-----------TRTEKHINEGMDALMEDRttfVIAHRLstirnADAIMVLENGEIIERGTHEEL 590
Cdd:PRK11000 162 SNLDaalrvqmrieiSRLHKRLGRTMIYVTHDQ---VEAMTL-----ADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
367-590 |
7.44e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVL-VEGVTFGYNPDK---TILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDG----------VD 432
Cdd:PRK10261 10 RDVLaVENLNIAFMQEQqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 433 IKDISLECLRE----NIAMVLQD--THL---FT--GTIMENIRYGRLSATDEEVRQAAKTscadMFIKNMPEGyDTMLKG 501
Cdd:PRK10261 90 LSEQSAAQMRHvrgaDMAMIFQEpmTSLnpvFTvgEQIAESIRLHQGASREEAMVEAKRM----LDQVRIPEA-QTILSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 502 DGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFV--IAHRLSTIRN-ADAIMVLEN 578
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEiADRVLVMYQ 244
|
250
....*....|..
gi 524455117 579 GEIIERGTHEEL 590
Cdd:PRK10261 245 GEAVETGSVEQI 256
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
372-591 |
8.42e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 372 EGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQD 451
Cdd:PRK10253 11 EQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 -THLFTGTIMENIRYGRL---------SATDEEVRQAA--KTSCADMFIKNMpegyDTmlkgdgsnLSQGQRQLLNIARA 519
Cdd:PRK10253 90 aTTPGDITVQELVARGRYphqplftrwRKEDEEAVTKAmqATGITHLADQSV----DT--------LSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 520 ALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDR--TTFVIAHRLS-TIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
381-592 |
9.60e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.12 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLEClRENIAMVLQDTHL---FTg 457
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVPQFDNLdpdFT- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 tIMENI----RYGRLSATDEEVRqaaktscadmfIKNMPEGYDTMLKGDG--SNLSQGQRQLLNIARAALSKAPILVLDE 531
Cdd:PRK13537 97 -VRENLlvfgRYFGLSAAAARAL-----------VPPLLEFAKLENKADAkvGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 532 ATSSVDTRTEKHINEGMDALM-EDRTTFVIAHRLSTI-RNADAIMVLENGEIIERGTHEELLE 592
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
381-591 |
1.52e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTtITNL-ITRF-------YNinKGKITIDGVDIKDISLECLR----ENIAMV 448
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKS-VTALsILRLlpsppvvYP--SGDIRFHGESLLHASEQTLRgvrgNKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 449 LQD-----THLFTgtiMENIRYGRLSATDEEVRQAAKT---SCADMF-IKNMPegydTMLKGDGSNLSQGQRQLLNIARA 519
Cdd:PRK15134 98 FQEpmvslNPLHT---LEKQLYEVLSLHRGMRREAARGeilNCLDRVgIRQAA----KRLTDYPHQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 520 ALSKAPILVLDEATSSVDTRTEKHInegMDALME-----DRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEELL 591
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQI---LQLLRElqqelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF 245
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
88-329 |
1.79e-08 |
|
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: 55.99 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 88 MAVVYVLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMsRFTNDVDIIGEMLNSTLVQIFSGT 167
Cdd:cd18783 48 VVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLT-KHMQQIERIRQFLTGQLFGTLLDA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 168 ITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYEENVVNEF 247
Cdd:cd18783 127 TSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREW 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 248 SELNQSLRNSQVKAQFISGIMGPCMNAMSQVNYTLTACVGSIIAFAsrwgggvpfSALDIGGLTVFVNYSRQFSRPINEL 327
Cdd:cd18783 207 DERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFA---------GSLTVGALIAFNMLAGRVAGPLVQL 277
|
..
gi 524455117 328 AQ 329
Cdd:cd18783 278 AG 279
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
371-592 |
1.89e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.95 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQ 450
Cdd:PRK10575 14 LRNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLFTG-TIMENI---RY------GRLSATD-EEVRQAAKTSCADMFIKNMPEgydtmlkgdgsNLSQGQRQLLNIARA 519
Cdd:PRK10575 93 QLPAAEGmTVRELVaigRYpwhgalGRFGAADrEKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 520 ALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA--HRLS-TIRNADAIMVLENGEIIERGTHEELLE 592
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
381-595 |
1.91e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRF--YNINKGKITIDGVDIKDISLEcLRENIAMVLQDTHLFTGT 458
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 459 IMENIRYGRLSATDEEVRQ--------------AAKTSCADM---FI-KNMPEGYdtmlkgdgsnlSQGQRQLLNIARAA 520
Cdd:CHL00131 98 GVSNADFLRLAYNSKRKFQglpeldplefleiiNEKLKLVGMdpsFLsRNVNEGF-----------SGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFV-IAH--RLSTIRNADAIMVLENGEIIERGTHE--ELLEKKG 595
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKG 246
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
382-591 |
2.57e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLI---------TRFYNInKGKITIDGVDIKDIS---LECLRENIAMVL 449
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaPRGARV-TGDVTLNGEPLAAIDaprLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHLFtgTIMENIRYGRLSatdeEVRQAAKTSCADMFIKNMP---EGYDTMLKGDGSNLSQGQRQLLNIARA------- 519
Cdd:PRK13547 93 QPAFAF--SAREIVLLGRYP----HARRAGALTHRDGEIAWQAlalAGATALVGRDVTTLSGGELARVQFARVlaqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 520 --ALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA--HRLS-TIRNADAIMVLENGEIIERGTHEELL 591
Cdd:PRK13547 167 hdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
375-582 |
2.79e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 375 TFGynpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFY--NINKGKITIDGVDIKDISL-ECLRENIAMVLQD 451
Cdd:TIGR02633 10 TFG---GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIrDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 452 THLFTG-TIMENI-------RYGRLSATDEEVRQAAKTsCADMFIKNMPegyDTMLKGDgsnLSQGQRQLLNIARAALSK 523
Cdd:TIGR02633 87 LTLVPElSVAENIflgneitLPGGRMAYNAMYLRAKNL-LRELQLDADN---VTRPVGD---YGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524455117 524 APILVLDEATSSVdtrTEKHINEGMDALMEDRTTFV----IAHRLSTIRN-ADAIMVLENGEII 582
Cdd:TIGR02633 160 ARLLILDEPSSSL---TEKETEILLDIIRDLKAHGVacvyISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
382-592 |
2.80e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDgvdikdisleclrENIAMVLQDTHLFTGTIME 461
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 NIRYgrlsaTDEE----VRQAAKTSCADMFIKNMPEGYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVD 537
Cdd:PTZ00243 740 NILF-----FDEEdaarLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 538 TRTEKHI-NEGMDALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGTHEELLE 592
Cdd:PTZ00243 815 AHVGERVvEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
85-344 |
3.53e-08 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 55.17 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 85 LALMAVVYVLGVGATYLQGRIM------ISVSQGTlkRIREHLFRkvqkLPVRYFDTNPTGDIMSR-FTNDVdiIGEMLN 157
Cdd:cd18569 45 LLGMALTALLQGLLTWLQQYYLlrletkLALSSSS--RFFWHVLR----LPVEFFSQRYAGDIASRvQSNDR--VANLLS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 158 STLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYieeTVTGQKV---V 234
Cdd:cd18569 117 GQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGT---TMSGLQMietL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 235 KVFNYEENVVNEFSELNQSLRNSQVKAQFISGIMGPCMNAMSQVNYTLTACVGSIIAFAsrwgggvpfSALDIGGLTVFV 314
Cdd:cd18569 194 KASGAESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMD---------GALTIGMLVAFQ 264
|
250 260 270
....*....|....*....|....*....|
gi 524455117 315 NYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18569 265 SLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
373-595 |
3.78e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.01 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 373 GVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDG--VDIKDISLECLRENIAMVLQ 450
Cdd:PRK13638 6 DLWFRYQ-DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 D--THLFTGTIMENIRYG--RLSATDEEVRQ---AAKTSCADMFIKNMPEgydtmlkgdgSNLSQGQRQLLNIARAALSK 523
Cdd:PRK13638 85 DpeQQIFYTDIDSDIAFSlrNLGVPEAEITRrvdEALTLVDAQHFRHQPI----------QCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 524 APILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVI-AHRLSTIRN-ADAIMVLENGEIIERG------THEELLEKKG 595
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
371-593 |
4.27e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 55.96 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLI--TRFYNINKGKI---------------------- 426
Cdd:TIGR03269 3 VKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 427 -----------TIDGVDIKDISLECLRENIAMVLQDTHLFTG--TIMENIRYGRLSA---TDEEVRQAAKtscadmFIKN 490
Cdd:TIGR03269 82 cpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEIgyeGKEAVGRAVD------LIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 491 MPEGYDTMlkGDGSNLSQGQRQLLNIARAaLSKAPILVL-DEATSSVDTRTEKHINEGMDALM--EDRTTFVIAHRLSTI 567
Cdd:TIGR03269 156 VQLSHRIT--HIARDLSGGEKQRVVLARQ-LAKEPFLFLaDEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|....*..
gi 524455117 568 RN-ADAIMVLENGEIIERGTHEELLEK 593
Cdd:TIGR03269 233 EDlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
106-263 |
4.60e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 54.79 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 106 MISVSQGTL---KRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNW 182
Cdd:cd18603 62 SLALALGCVrasRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 183 VLAVVTIVVSPIIAKIgtaiagksRKYFMKQQTDLGK--------VNGYIEETVTGQKVVKVFnyeeNVVNEFSELNQSL 254
Cdd:cd18603 142 IFLVVIIPLAILYFFI--------QRFYVATSRQLKRlesvsrspIYSHFSETLQGASTIRAY----GVQERFIRESDRR 209
|
....*....
gi 524455117 255 RNSQVKAQF 263
Cdd:cd18603 210 VDENQRAYY 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
381-585 |
5.28e-08 |
|
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: 53.88 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLReNIAMVL----------- 449
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVFgqktqlwwdlp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 -QDTHLFTGTIMeNIRYGRLSATDEEvrqaaktsCADMFikNMPEGYDTMLKgdgsNLSQGQRQLLNIARAALSKAPILV 528
Cdd:cd03267 112 vIDSFYLLAAIY-DLPPARFKKRLDE--------LSELL--DLEELLDTPVR----QLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 529 LDEATSSVDTRTEKHINEGMDALMEDRTTFVI--AHRLSTI-RNADAIMVLENGEIIERG 585
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
84-344 |
6.94e-08 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 54.53 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 84 GLALMAVVYVLGVGATYLQGRIMISVSQGTLK---RIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNStL 160
Cdd:cd18559 37 GQVYLSVLGALAILQGITVFQYSMAVSIGGIFasrAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQ-V 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 161 VQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVVKVFNYE 240
Cdd:cd18559 116 IKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 241 EnvvnEFSELNQSLRNSQVKAQfisgimgPCMNAMSQVNYTLTACVGSIIAFASRWGGGVPFSALDIGGLTVFvnYSRQF 320
Cdd:cd18559 196 E----AFIRQVDAKRDNELAYL-------PSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVF--YSLAL 262
|
250 260
....*....|....*....|....*...
gi 524455117 321 SR----PINELAQQVTNIMSALAGAERV 344
Cdd:cd18559 263 TTylnwPLNMSPEVITNIVAAEVSLERS 290
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
382-531 |
8.26e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.49 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDI-----------------------KDISL 438
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarlgigylpqeasifRKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 439 EclrENIAMVLQDTHLftgtimenirygrlsatDEEVRQAAKTSCADMF----IKNMPegydtmlkgdGSNLSQGQRQLL 514
Cdd:COG1137 96 E---DNILAVLELRKL-----------------SKKEREERLEELLEEFgithLRKSK----------AYSLSGGERRRV 145
|
170
....*....|....*....
gi 524455117 515 NIARaALSKAP--ILvLDE 531
Cdd:COG1137 146 EIAR-ALATNPkfIL-LDE 162
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
373-546 |
8.84e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 373 GVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITnlitrfyninkgKItIDGVDiKDISLECLRE---NIAMVL 449
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RI-MAGVD-KDFNGEARPQpgiKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 450 QDTHL-FTGTIMENIRYGRLSATD-----EEVRQAAKTSCADM--FIKNMPEGYDTMLKGDG------------------ 503
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAEIKDaldrfNEISAKYAEPDADFdkLAAEQAELQEIIDAADAwdldsqleiamdalrcpp 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524455117 504 -----SNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRT----EKHINE 546
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
381-595 |
9.48e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLIT--RFYNINKGKITIDGVDIKDISLECLR-ENIAMVLQ------- 450
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQypveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 -DTHLFTGTIMENIRygrlsatdeEVRQAAKTSCADM--FIK------NMPEgyDTMLKGDGSNLSQGQRQLLNIARAAL 521
Cdd:PRK09580 93 vSNQFFLQTALNAVR---------SYRGQEPLDRFDFqdLMEekiallKMPE--DLLTRSVNVGFSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 522 SKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRLSTIRN---ADAIMVLENGEIIERGTHE--ELLEKKG 595
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSGDFTlvKQLEEQG 240
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
376-540 |
1.26e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 376 FGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDiSLECLRENIAMVLQDTHLF 455
Cdd:PRK13540 9 FDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 456 TG-TIMENIRYG-RLSATDEEVRQAAKTSCADMFIkNMPEGYdtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLDEAT 533
Cdd:PRK13540 87 PYlTLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
....*..
gi 524455117 534 SSVDTRT 540
Cdd:PRK13540 156 VALDELS 162
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
374-590 |
2.28e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.19 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 374 VTFGyNPDK--TILKDVSIFAHPGQKIALVGSTGAGKT----TITNLITRFYNInKGKITIDGVDIKDIS---LECLR-E 443
Cdd:PRK09473 20 VTFS-TPDGdvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGREILNLPekeLNKLRaE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 444 NIAMVLQD--THL---------FTGTIMENIRYGRLSATDEEVR--QAAKtscadmfiknMPEGYDTMlKGDGSNLSQGQ 510
Cdd:PRK09473 98 QISMIFQDpmTSLnpymrvgeqLMEVLMLHKGMSKAEAFEESVRmlDAVK----------MPEARKRM-KMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 511 RQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTT--FVIAHRLSTIRN-ADAIMVLENGEIIERGTH 587
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKVLVMYAGRTMEYGNA 246
|
...
gi 524455117 588 EEL 590
Cdd:PRK09473 247 RDV 249
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
382-599 |
2.54e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLI---TRFYNINK-GKITIDGVDIKDISLECLRENIAMVLQDTHLFTG 457
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasnTDGFHIGVeGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 TIMENIRYG--------RLSATDEEVRQAAKTSCAdMFIKNMPEGYDT-----MLKGdgsnLSQGQRQLLNIARAALSKA 524
Cdd:TIGR00956 154 TVGETLDFAarcktpqnRPDGVSREEYAKHIADVY-MATYGLSHTRNTkvgndFVRG----VSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 525 PILVLDEATSSVDTRTE----KHINEGMDALmeDRTTFVIAHRLStiRNA----DAIMVLENGEIIERGTHEELLEkkgr 596
Cdd:TIGR00956 229 KIQCWDNATRGLDSATAlefiRALKTSANIL--DTTPLVAIYQCS--QDAyelfDKVIVLYEGYQIYFGPADKAKQ---- 300
|
...
gi 524455117 597 YFE 599
Cdd:TIGR00956 301 YFE 303
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
378-592 |
2.73e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 53.27 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 378 YNPDKTILK---DVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITI----DGVDIKDISLEC---LRENIAM 447
Cdd:TIGR03269 290 ISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrgrAKRYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 448 VLQDTHLFT-GTIMENIRYG-RLSATDE-EVRQAAKTSCADMFIKNMPEgydTMLKGDGSNLSQGQRQLLNIARAALSKA 524
Cdd:TIGR03269 370 LHQEYDLYPhRTVLDNLTEAiGLELPDElARMKAVITLKMVGFDEEKAE---EILDKYPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524455117 525 PILVLDEATSSVDTRTEKHINEG-MDALMEDRTTFVI-AHRLSTIRN-ADAIMVLENGEIIERGTHEELLE 592
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSiLKAREEMEQTFIIvSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
75-292 |
2.99e-07 |
|
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: 52.59 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 75 QQKITSLMAGLALMAVVYVLGVGATYLQGRIMISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFtNDVDIIGE 154
Cdd:cd18566 35 NESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 155 MLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDLGKVNGYIEETVTGQKVV 234
Cdd:cd18566 114 FLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524455117 235 KVFNYEENVVNEFSEL-NQSLRNS----------QVKAQFISGIMGPCM---NAMSQVNYTLTacVGSIIAF 292
Cdd:cd18566 194 KAMAMEPQMLRRYERLqANAAYAGfkvakinavaQTLGQLFSQVSMVAVvafGALLVINGDLT--VGALIAC 263
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
382-548 |
3.06e-07 |
|
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: 51.34 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 382 KTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQDTHLFTGTIME 461
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 NIRYGRLSATDEEVRQAAKTSCADMFiKNMPEGYdtmlkgdgsnLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTE 541
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
....*..
gi 524455117 542 KHINEGM 548
Cdd:cd03231 162 ARFAEAM 168
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
381-599 |
3.99e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLIT-RFYNIN-KGKITIDGvdiKDISLECLREnIAMVLQDTHLFTG- 457
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILKR-TGFVTQDDILYPHl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 TIMENI-------------RYGRLSATDEEVRQAAKTSCADMFIKNmpegydTMLKGdgsnLSQGQRQLLNIARAALSKA 524
Cdd:PLN03211 156 TVRETLvfcsllrlpksltKQEKILVAESVISELGLTKCENTIIGN------SFIRG----ISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 525 PILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIA-HRLST--IRNADAIMVLENGEIiergtheeLLEKKGR----Y 597
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSrvYQMFDSVLVLSEGRC--------LFFGKGSdamaY 297
|
..
gi 524455117 598 FE 599
Cdd:PLN03211 298 FE 299
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
385-593 |
5.23e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGvdikDISLeclrenIAMVLQDTHLFTGtiMENIR 464
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSV------IAISAGLSGQLTG--IENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 465 YGRLSA--TDEEVR----QAAKTSCADMFIKNMPEGYdtmlkgdgsnlSQGQRQLLNIARAALSKAPILVLDEATSSVD- 537
Cdd:PRK13546 108 FKMLCMgfKRKEIKamtpKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGDq 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 538 TRTEKHINEGMDALMEDRTTFVIAHRLSTIRN-ADAIMVLENGEIIERGTHEELLEK 593
Cdd:PRK13546 177 TFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
369-608 |
5.24e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 369 VLVEGVTFGYNPDKTiLKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFynINKGKITIDGVDIKDISLECL------- 441
Cdd:PRK09984 5 IRVEKLAKTFNQHQA-LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTVQREgrlardi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 442 ---RENIAMVLQDTHLFTG-TIMENIRYGRLSATdeevrqAAKTSCADMFIKNMPEGYDTMLKGDG---------SNLSQ 508
Cdd:PRK09984 82 rksRANTGYIFQQFNLVNRlSVLENVLIGALGST------PFWRTCFSWFTREQKQRALQALTRVGmvhfahqrvSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 509 GQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGM-DALMEDRTTFVIA-HRLS-TIRNADAIMVLENGEIIERG 585
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrDINQNDGITVVVTlHQVDyALRYCERIVALRQGHVFYDG 235
|
250 260
....*....|....*....|...
gi 524455117 586 THEELleKKGRYFELYTGLKELD 608
Cdd:PRK09984 236 SSQQF--DNERFDHLYRSINRVE 256
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
381-538 |
5.68e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 50.56 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYN---INKGKITIDGVDIKDISLEclRENIAMVLQDTHLFTG 457
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 458 -TIMENIRYGRLSATDEEVRQAAktscadmfIKNMPE--GYDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATS 534
Cdd:COG4136 91 lSVGENLAFALPPTIGRAQRRAR--------VEQALEeaGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
....
gi 524455117 535 SVDT 538
Cdd:COG4136 163 KLDA 166
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
85-250 |
8.43e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 51.02 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 85 LALMAVVYVLGVGATYLQGRIMISVSqgtlKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIF 164
Cdd:cd18599 65 GGSILVILLLSLIRGFVFVKVTLRAS----SRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 165 SGTITLIGTLALMLYT-NWVLAVVTIVVspiiakigtAIAGKSRKYFMKQQTDLGKVN--------GYIEETVTGQKVVK 235
Cdd:cd18599 141 QNVLLVVFSLIIIAIVfPWFLIALIPLA---------IIFVFLSKIFRRAIRELKRLEnisrsplfSHLTATIQGLSTIH 211
|
170
....*....|....*
gi 524455117 236 VFNYEENVVNEFSEL 250
Cdd:cd18599 212 AFNKEKEFLSKFKKL 226
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
122-268 |
8.95e-07 |
|
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: 50.90 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 122 FRKVQKLPVRYFDTNPTGDIMSRfTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTIvvspiiakIGTA 201
Cdd:cd18571 82 LIKLMRLPISFFDTKMTGDILQR-INDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFL--------IGSV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 202 IAGKSRKYFMKQQTDL--------GKVNGYIEETVTGQKVVKVFNYE-------ENVVNEFSELN-QSLRNSQVK---AQ 262
Cdd:cd18571 153 LYILWILLFLKKRKKLdykrfdlsSENQSKLIELINGMQEIKLNNSErqkrwewERIQAKLFKINiKSLKLDQYQqigAL 232
|
....*.
gi 524455117 263 FISGIM 268
Cdd:cd18571 233 FINQLK 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
379-537 |
1.10e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 379 NPDKTILKDVSIFAHPGQKIALVGSTGAGKT-TITNLITRFYNINKGKITIDG--VDIKDiSLECLRENIAMVLQDTHLF 455
Cdd:PRK13549 272 NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGkpVKIRN-PQQAIAQGIAMVPEDRKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 456 tG--TIM---ENI------RYGRLSATDEevrqAAKTSCADMFIKNMP-EGYDTMLKGdgSNLSQGQRQLLNIARAALSK 523
Cdd:PRK13549 351 -GivPVMgvgKNItlaaldRFTGGSRIDD----AAELKTILESIQRLKvKTASPELAI--ARLSGGNQQKAVLAKCLLLN 423
|
170
....*....|....
gi 524455117 524 APILVLDEATSSVD 537
Cdd:PRK13549 424 PKILILDEPTRGID 437
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
367-590 |
1.26e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVL--VEGVTfgynpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDG--VDIKDISlECLR 442
Cdd:COG1129 253 GEVVleVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPR-DAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 443 ENIAMVLQDTH---LFTG-TIMENI---------RYGRLSATDEevRQAAKTSCADMFIKnMPEGYDTMlkgdgSNLSQG 509
Cdd:COG1129 327 AGIAYVPEDRKgegLVLDlSIRENItlasldrlsRGGLLDRRRE--RALAEEYIKRLRIK-TPSPEQPV-----GNLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 510 QRQLLNIARAALSKAPILVLDEATSSVD--TRTE--KHINE----GMDALMedrttfviahrLST-----IRNADAIMVL 576
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIRElaaeGKAVIV-----------ISSelpelLGLSDRILVM 467
|
250
....*....|....
gi 524455117 577 ENGEIIERGTHEEL 590
Cdd:COG1129 468 REGRIVGELDREEA 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
394-586 |
1.29e-06 |
|
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: 48.52 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 394 PGQKIALVGSTGAGKTTITNLITRFYNINKGK-ITIDGVDIKDISLECLREniamvlqdthlftgtimenirygrlsatd 472
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 473 eevrqaaktscadmfiknmpegydTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMD--- 549
Cdd:smart00382 52 ------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 524455117 550 ----ALMEDRTTFVIAHRLSTIRNADAIMVLENGEIIERGT 586
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
42-344 |
2.11e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 49.76 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 42 AFVCVLVSSASTLCGSYLLRPIINGLIDSTKTSQQKITSLMAGLA----LMAVVYVLGVGATYLQGRIMISVSQGTLKRI 117
Cdd:cd18597 2 AGLLKLLADVLQVLSPLLLKYLINFVEDAYLGGPPPSIGYGIGYAiglfLLQLLSSLLLNHFFYRSMLTGAQVRAALTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 118 rehLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIgEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVTI----VVSP 193
Cdd:cd18597 82 ---IYRKSLRLSGKSRHEFPNGKITNLMSTDLSRI-DFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIgvliLSIP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 194 IIAKIGTAIAgKSRKYFMKqQTDlgKVNGYIEETVTGQKVVKVFNYEENvvneFSELNQSLRNSQVKAQFISGIMGPCMN 273
Cdd:cd18597 158 LQGFLMKKLF-KLRKKANK-ITD--KRVKLTQEILQGIRVIKFYAWEDA----FLERITEIRKKELKYVRKLQILRSILT 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524455117 274 AMSQVNYTLTACVGSIIAFASrwGG----GVPFSAldiggLTVFvNYSRQfsrPINELAQQVTNIMSALAGAERV 344
Cdd:cd18597 230 AVAFSLPVLASMLSFITYYAT--GHtldpANIFSS-----LALF-NVLRM---PLMFLPLALSSLADALVALKRI 293
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
371-585 |
2.91e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.15 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 371 VEGVTFGYNPDKTiLKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDISLECLRENIAMVLQ 450
Cdd:PRK11701 9 VRGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 451 DTHLftGTIMENIRYG-------------RLSATDE----EVRQAAKTSCADMFI-----KNMPEGYdtmlkgdgsnlSQ 508
Cdd:PRK11701 88 RTEW--GFVHQHPRDGlrmqvsaggnigeRLMAVGArhygDIRATAGDWLERVEIdaariDDLPTTF-----------SG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 509 GQRQLLNIARaALSKAPILVL-DEATSSVDTRTEKHINEGMDALMEDRTTFVI--AHRLSTIRN-ADAIMVLENGEIIER 584
Cdd:PRK11701 155 GMQQRLQIAR-NLVTHPRLVFmDEPTGGLDVSVQARLLDLLRGLVRELGLAVVivTHDLAVARLlAHRLLVMKQGRVVES 233
|
.
gi 524455117 585 G 585
Cdd:PRK11701 234 G 234
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
63-344 |
6.44e-06 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 48.29 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 63 IINGLIDSTKTSQQKITSLMAGLALMAVVYVLGVGATYLQgrimISVSQGTLKRIREHLFRKVQKLPVRYFDTNPTGDIM 142
Cdd:cd18583 22 IVDSLSGGSGKSPWKEIGLYVLLRFLQSGGGLGLLRSWLW----IPVEQYSYRALSTAAFNHVMNLSMDFHDSKKSGEVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 143 sRFTNDVDIIGEMLNSTLVQIFSGTITL---IGTLALM--LYTNWVLAVVTIVVSPIIAKIGTAIAGKSRKYFMKQQTDL 217
Cdd:cd18583 98 -KAIEQGSSINDLLEQILFQIVPMIIDLviaIVYLYYLfdPYMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 218 GKVNgyieETVTGQKVVKVFNyeeNVVNEFSELNQSLRNSQvKAQF---ISGIMgpcMNAMSQVNYTLTACVGSIIAfAS 294
Cdd:cd18583 177 SILT----ESLLNWETVKYFN---REPYEKERYREAVKNYQ-KAERkylFSLNL---LNAVQSLILTLGLLAGCFLA-AY 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 524455117 295 RwgggVPFSALDIGGLTVFVNYSRQFSRPINELAQQVTNIMSALAGAERV 344
Cdd:cd18583 245 Q----VSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
341-591 |
7.36e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 341 AERVFNVMDEAEEIDD--GKKLV-----LDKVHGDVL--VEGVTfgyNPDktiLKDVSIFAHPGQKIALVGSTGAGKTTI 411
Cdd:PRK10762 221 AEREVADLTEDSLIEMmvGRKLEdqyprLDKAPGEVRlkVDNLS---GPG---VNDVSFTLRKGEILGVSGLMGAGRTEL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 412 TNLITRFYNINKGKITIDGVDIKDIS-LECLRENIAMVLQDTH---LFTG-TIMEN-----IRYgrLSATDEEVRQAAKT 481
Cdd:PRK10762 295 MKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRKrdgLVLGmSVKENmsltaLRY--FSRAGGSLKHADEQ 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 482 SCADMFIKNMPEGYDTMLKGDGsNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHI--------NEGMDALMe 553
Cdd:PRK10762 373 QAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIyqlinqfkAEGLSIIL- 450
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 524455117 554 drttfVIAHRLSTIRNADAIMVLENGEI-----IERGTHEELL 591
Cdd:PRK10762 451 -----VSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
385-583 |
1.56e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 385 LKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNIN--KGKITIDG--VDIKDISlECLRENIAMVLQDTHLFTG-TI 459
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGevCRFKDIR-DSEALGIVIIHQELALIPYlSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 460 MENIRYGRLSAT------DEEVRQAAktscaDMFIK-NMPEGYDTMLKgdgsNLSQGQRQLLNIARaALSK-APILVLDE 531
Cdd:NF040905 96 AENIFLGNERAKrgvidwNETNRRAR-----ELLAKvGLDESPDTLVT----DIGVGKQQLVEIAK-ALSKdVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 532 ATSSVDTRTEKHInegMDALMEDR----TTFVIAHRLSTIRN-ADAIMVLENGEIIE 583
Cdd:NF040905 166 PTAALNEEDSAAL---LDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
326-572 |
2.86e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 326 ELAQQVtnIMSALAGAERVFNV-MDEAEEIDDGKKLVLDKVHgdVLVEGVTFGYNpDKTILKDVSIFAHPGQKIALVGST 404
Cdd:PRK10938 221 EILQQA--LVAQLAHSEQLEGVqLPEPDEPSARHALPANEPR--IVLNNGVVSYN-DRPILHNLSWQVNPGEHWQIVGPN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 405 GAGKTTITNLIT----RFYNiNK----GKITIDGVDIKDIsleclRENIAMVLQDTHL---------------FTGTIme 461
Cdd:PRK10938 296 GAGKSTLLSLITgdhpQGYS-NDltlfGRRRGSGETIWDI-----KKHIGYVSSSLHLdyrvstsvrnvilsgFFDSI-- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 462 niryGRLSATDEEVRQAAKTSCAdmfIKNMPegyDTMLKGDGSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTE 541
Cdd:PRK10938 368 ----GIYQAVSDRQQKLAQQWLD---ILGID---KRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 524455117 542 KHINEGMDALMEDRTT---FV----------IAHRLSTIRNADA 572
Cdd:PRK10938 438 QLVRRFVDVLISEGETqllFVshhaedapacITHRLEFVPDGDI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
373-411 |
4.76e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 4.76e-05
10 20 30
....*....|....*....|....*....|....*....
gi 524455117 373 GVTFGYNPDKTILKDVSIFAHPGQKIALVGSTGAGKTTI 411
Cdd:PRK11819 11 RVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTL 49
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
394-564 |
1.33e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.39 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 394 PGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKdISLECLRENIAMVLQ-DT--HLFTGTimENIR-YGRLS 469
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQfDAidDLLTGR--EHLYlYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 470 AT-DEEVRQAAKTSCADMFIKNmpegYDTMLKGdgsNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHI-NEG 547
Cdd:TIGR01257 2041 GVpAEEIEKVANWSIQSLGLSL----YADRLAG---TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTI 2113
|
170
....*....|....*..
gi 524455117 548 MDALMEDRTTFVIAHRL 564
Cdd:TIGR01257 2114 VSIIREGRAVVLTSHSM 2130
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
346-414 |
1.53e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 1.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524455117 346 NVMDEAE-EIDDGK---KLVLDkvhgdvlVEGVTFGYnPDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNL 414
Cdd:PRK11147 300 EVMGTAKmQVEEASrsgKIVFE-------MENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKL 364
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
369-426 |
2.30e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 2.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 524455117 369 VLVEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKI 426
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
384-539 |
4.16e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.91 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 384 ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDisLECLRENIAMVLQDTHLFTG-TIMEN 462
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIAMVFQNYALYPHmSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 463 IRYG----RLSAT--DEEVRQAAKTSCADMFIKNMPegydtmlkgdgSNLSQGQRQLLNIARAALSKAPILVLDEATSSV 536
Cdd:PRK11650 97 MAYGlkirGMPKAeiEERVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
...
gi 524455117 537 DTR 539
Cdd:PRK11650 166 DAK 168
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
367-566 |
4.57e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 43.00 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 367 GDVLVE--GVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIdGVDIKDISLECLREN 444
Cdd:TIGR03719 319 GDKVIEaeNLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 445 iamvLQDTHlftgTIMENIRYGrlsaTDE----EVRQAAKTSCADMFIKnmpeGYDTMLKgdGSNLSQGQRQLLNIARAA 520
Cdd:TIGR03719 397 ----LDPNK----TVWEEISGG----LDIiklgKREIPSRAYVGRFNFK----GSDQQKK--VGQLSGGERNRVHLAKTL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 524455117 521 LSKAPILVLDEATSSVDTRTEKHINEGMDALMEdrTTFVIAH------RLST 566
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdrwfldRIAT 508
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
384-539 |
4.96e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 384 ILKDVSIFAHPGQKIALVGSTGAGKTTITNLITrfyninkGKIT---IDGvDIKDISLECLRENIAMV-----LQDTHLF 455
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA-------GRKTggyIEG-DIRISGFPKKQETFARIsgyceQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 456 TGTIMENIRYGRLSATDEEVRQAAKTSCAD--MFIKNMPEGYDTMLKGDG-SNLSQGQRQLLNIARAALSKAPILVLDEA 532
Cdd:PLN03140 967 QVTVRESLIYSAFLRLPKEVSKEEKMMFVDevMELVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*..
gi 524455117 533 TSSVDTR 539
Cdd:PLN03140 1047 TSGLDAR 1053
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
58-294 |
5.95e-04 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 42.24 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 58 YLLRPIINGLIDSTKTSQQKITSLMAGLALMAVVYVLG-----VGATYLQGRIMISVSqgTLkrirehLFRKVQKLPVRY 132
Cdd:cd18594 18 LLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLhhpyfFGLHRYGMQLRIALS--SL------IYKKTLKLSSSA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 133 FDTNPTGDIMSRFTNDVDIIGEMLnSTLVQIFSGTITLIGTLALMLYT--NWVLAVVTIV--VSPIIAKIGTAIAgKSRK 208
Cdd:cd18594 90 LSKITTGHIVNLLSNDVQKFDEVL-VYLHFLWIAPLQVIVLTGLLWREigPSSLAGLGVLllLLPLQAYLGKLFA-KYRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 209 YFMKQQTDLGKVngyIEETVTGQKVVKVFNYEENvvneFSELNQSLRNSQVKAQFisgimgpCMNAMSQVNYTLTACVGS 288
Cdd:cd18594 168 KTAGLTDERVKI---MNEIISGMRVIKMYTWEES----FAKLIENIRKKELKLIR-------KAAYIRAFNMAFFFFSPT 233
|
....*.
gi 524455117 289 IIAFAS 294
Cdd:cd18594 234 LVSFAT 239
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
503-595 |
1.17e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 503 GSNLSQGQRQLLNIARAALSKAPILVLDEATSSVDTRTEKHINEGMDALMEDRTTFVIAHRL--STIRNADAIMVLENGE 580
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVIDRGR 221
|
90
....*....|....*
gi 524455117 581 IIERGTHEELLEKKG 595
Cdd:NF000106 222 VIADGKVDELKTKVG 236
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
397-452 |
1.19e-03 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 40.35 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 524455117 397 KIALVGSTGAGKTTITN-LITRFYNINKGKITIdGVDIKDISLECLRENIAMVLQDT 452
Cdd:COG1100 5 KIVVVGTGGVGKTSLVNrLVGDIFSLEKYLSTN-GVTIDKKELKLDGLDVDLVIWDT 60
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
114-267 |
1.98e-03 |
|
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: 40.54 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 114 LKRIREHLFRKVQKLPVRYFDTNPTGDIMSRFTNDVDIIGEMLNSTLVQIFSGTITLIGTLALMLYTNWVLAVVT----- 188
Cdd:cd18585 67 LSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILlagll 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 189 ---IVVSPIIAKIGTAIAGKSRkyfmKQQTDLgkvNGYIEETVTGQKVVKVFNYEENVVNEFSELNQSLRNSQVKAQFIS 265
Cdd:cd18585 147 lagVVIPLLFYRLGKKIGQQLV----QLRAEL---RTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLS 219
|
..
gi 524455117 266 GI 267
Cdd:cd18585 220 GL 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
504-580 |
2.81e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 504 SNLSQGQRQLLNIArAALSK-APILVLDEATSSVD-------TRTEKHINEGMDAlmedrTTFVIAHRLSTIRN-ADAIM 574
Cdd:PRK13409 452 KDLSGGELQRVAIA-ACLSRdADLYLLDEPSAHLDveqrlavAKAIRRIAEEREA-----TALVVDHDIYMIDYiSDRLM 525
|
....*.
gi 524455117 575 VLEnGE 580
Cdd:PRK13409 526 VFE-GE 530
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
381-594 |
2.93e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.54 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 381 DKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKITIDGVDIKDIS-LECLRENIAMVLQ---DTHLFT 456
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 457 G-TIMENI------RYGRLSAT-----DEEVRQAAKTSCADMFIK------NMPEgydtmlkgdgsnLSQGQRQLLNIAR 518
Cdd:PRK09700 355 NfSIAQNMaisrslKDGGYKGAmglfhEVDEQRTAENQRELLALKchsvnqNITE------------LSGGNQQKVLISK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 519 AALSKAPILVLDEATSSVDTRTEKHINEGMDALMED-RTTFVIAHRLSTIRNA-DAIMVLENGEIIERGTH-EELLEKK 594
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNrDDMSEEE 501
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
395-429 |
3.43e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 40.26 E-value: 3.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 524455117 395 GQKIALVGSTGAGKTT-ITNLITRFYNINKGK----ITID 429
Cdd:PRK05703 221 GGVVALVGPTGVGKTTtLAKLAARYALLYGKKkvalITLD 260
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
371-426 |
5.93e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 5.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 524455117 371 VEGVTFGYNpDKTILKDVSIFAHPGQKIALVGSTGAGKTTITNLITRFYNINKGKI 426
Cdd:PRK10636 315 MEKVSAGYG-DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
386-581 |
8.15e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 39.26 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 386 KDVSIFAHPGQKIALVGSTGAGKTtitNLITRFYNINK---GKITIDGVDIKDIS-LECLRENIAMVLQDTH---LF--- 455
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRT---ELAETLYGLRPargGRIMLNGKEINALStAQRLARGLVYLPEDRQssgLYlda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524455117 456 -----TGTIMEN-----IRYGRLSATDEEVRQAAKTSCADmfiKNMPEGydtmlkgdgsNLSQGQRQLLNIARAaLSKAP 525
Cdd:PRK15439 357 plawnVCALTHNrrgfwIKPARENAVLERYRRALNIKFNH---AEQAAR----------TLSGGNQQKVLIAKC-LEASP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524455117 526 -ILVLDEATSSVDTRTEKHINEGMDALMEDRTTFV-IAHRLSTIRN-ADAIMVLENGEI 581
Cdd:PRK15439 423 qLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| |
