|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-576 |
1.18e-151 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 447.69 E-value: 1.18e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 1 MFKKLWSLLAPFHRTFYVFILLAFLYETVQLGASYVISLVVTLFGTGVAP---WIWVVLILGLLIFDEFNMRLDNAFdWH 77
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLsalLLLLLLLLGLALLRALLSYLQRYL-LA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 78 IISKQshpIFRHLKLSAITKFLKMNIPWHHQHNSGTLVGKVGDGVWKTLDIIDVMSWEFVPTVVQTVISLIPLFIISPWV 157
Cdd:COG1132 87 RLAQR---VVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 158 ALVAIITFVLFAWLTLKGNREKQPFRSKRQDYYEEEWNKSIASVQSVETNLMFGQQPRLLNDQAVIhngiiSEALKEHRL 237
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREA-----NEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 238 GIFKYNRWRIRVLTIARRI--ILVVWI--LQLIQGSLTIAGLIFVSVLVERLFNSCWRFARLLDRAAENSEGAERLANLL 313
Cdd:COG1132 239 RAARLSALFFPLMELLGNLglALVLLVggLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 314 LEPEPIETGSiQSVPAGPI--GVSLSDVCFAYEGDyseaDGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQ 391
Cdd:COG1132 319 DEPPEIPDPP-GAVPLPPVrgEIEFENVSFSYPGD----RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 392 MGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVG 471
Cdd:COG1132 394 SGRILIDGVDIRDLTLESLRRQIGVVPQ--DTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 472 ERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQG 551
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTI-RNADRILVLDDG 550
|
570 580
....*....|....*....|....*
gi 818754182 552 KKVEEGTHEELIKSHGIYAQMVSLQ 576
Cdd:COG1132 551 RIVEQGTHEELLARGGLYARLYRLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-577 |
6.60e-122 |
|
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: 375.71 E-value: 6.60e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 2 FKKLWSLLAPFHRTFYVFILLAFLYETVQLGASYVISLVV-TLFGTGVAPWIWVVLI--LGLLIFD--------EFNMRL 70
Cdd:COG2274 144 LRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIdRVLPNQDLSTLWVLAIglLLALLFEgllrllrsYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 71 DNAFDWHIISKqshpIFRHLklsaitkfLKMNIPWHHQHNSGTLVGKVGD--GVWKTL--DIIDVMSwefvpTVVQTVIS 146
Cdd:COG2274 224 GQRIDLRLSSR----FFRHL--------LRLPLSFFESRSVGDLASRFRDveSIREFLtgSLLTALL-----DLLFVLIF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 147 LIPLFIISPWVALVAIITFVLFAWLTL-------KGNREKQPFRSKRQDYYEEewnksiaSVQSVETNLMFGQQPRLLND 219
Cdd:COG2274 287 LIVLFFYSPPLALVVLLLIPLYVLLGLlfqprlrRLSREESEASAKRQSLLVE-------TLRGIETIKALGAESRFRRR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 220 QAVIHNGIISEALKEHRLGIFkYNRWRIRVLTIARRIILVVWILQLIQGSLTIAGLIFVSVLVERLFNSCWRFARLLDRA 299
Cdd:COG2274 360 WENLLAKYLNARFKLRRLSNL-LSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRF 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 300 AENSEGAERLANLL-LEPEPIETGSIQSVPAGPIGVSLSDVCFAYEGDyseADGALHDFSLEIEPGQIVALVGQSGAGKT 378
Cdd:COG2274 439 QDAKIALERLDDILdLPPEREEGRSKLSLPRLKGDIELENVSFRYPGD---SPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 379 TIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEF 458
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQ--DVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDF 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 459 VIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTI 538
Cdd:COG2274 594 IEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI 673
|
570 580 590
....*....|....*....|....*....|....*....
gi 818754182 539 wGLADKIVVMDQGKKVEEGTHEELIKSHGIYAQMVSLQT 577
Cdd:COG2274 674 -RLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-567 |
8.54e-103 |
|
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: 321.71 E-value: 8.54e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 3 KKLWSLLAPFHRTFYVFILLAFLYETVQLGASYVISLVVT-LFGTGVAP---WIWVVLILGLLIFdefnmRLdnAFDW-- 76
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAgLIIGGAPLsalLPLLGLLLAVLLL-----RA--LLAWlr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 77 ----HIISKQshpIFRHLKLSAITKFLKMNIPWHHQHNSGTLVGKVGDGVwktlDIIDVMSWEFVPTVVQTVIS----LI 148
Cdd:COG4988 79 eraaFRAAAR---VKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV----EALDGYFARYLPQLFLAALVplliLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 149 PLFIISPWVALVAIITF---VLFAWLTLKGNREkqpfRSKRQ--------DYYEEewnksiaSVQSVETNLMFGQQPRll 217
Cdd:COG4988 152 AVFPLDWLSGLILLVTApliPLFMILVGKGAAK----ASRRQwralarlsGHFLD-------RLRGLTTLKLFGRAKA-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 218 ndqaviHNGIISEALKEHR----------------LGIFKYnrwrirvLTIArrIILVVWILQLIQGSLTIAGLIFVSVL 281
Cdd:COG4988 219 ------EAERIAEASEDFRkrtmkvlrvaflssavLEFFAS-------LSIA--LVAVYIGFRLLGGSLTLFAALFVLLL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 282 V-E-----RLFNSCWrFARLLDRAAensegAERLANLLLEPEPIETGSIQSVPA-GPIGVSLSDVCFAYEGDyseaDGAL 354
Cdd:COG4988 284 ApEfflplRDLGSFY-HARANGIAA-----AEKIFALLDAPEPAAPAGTAPLPAaGPPSIELEDVSFSYPGG----RPAL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 355 HDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNI 434
Cdd:COG4988 354 DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQ--NPYLFAGTIRENL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 435 AFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKE 514
Cdd:COG4988 432 RLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 818754182 515 IQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEELIKSHG 567
Cdd:COG4988 512 ILQALRRLAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
137-576 |
1.09e-99 |
|
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: 314.84 E-value: 1.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 137 VPTVVQTVISLIPLFII-SPWVALVAIITFVLFAWLTLKGNREKQPFRSKRQDYYEEEWNKSIASVQSVETNLMFGQQPR 215
Cdd:COG5265 160 LPTLLEIALVAGILLVKyDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 216 LLNDqavihngiISEALKEhrlgifkYNRWRIR--------------VLTIARRIILVVWILQLIQGSLTIAGLIFVSVL 281
Cdd:COG5265 240 EARR--------YDEALAR-------YERAAVKsqtslallnfgqalIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAY 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 282 VERLF------NSCWRFAR--LLDraaensegAERLANLL-LEPEPIETGSIQSVPAGPIGVSLSDVCFAYEGDYSeadg 352
Cdd:COG5265 305 LIQLYiplnflGFVYREIRqaLAD--------MERMFDLLdQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERP---- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRY 432
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQ--DTVLFNDTIAY 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITE 512
Cdd:COG5265 451 NIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 513 KEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQMVSLQ 576
Cdd:COG5265 531 RAIQAALREVARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
334-572 |
1.33e-99 |
|
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: 301.84 E-value: 1.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDyseADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03251 1 VEFKNVTFRYPGD---GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLA 493
Cdd:cd03251 78 IGLVSQ--DVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQM 572
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
334-576 |
3.83e-98 |
|
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: 297.99 E-value: 3.83e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03253 1 IEFENVTFAYDPGRP----VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLA 493
Cdd:cd03253 77 IGVVPQ--DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQMV 573
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
...
gi 818754182 574 SLQ 576
Cdd:cd03253 234 KAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
136-575 |
5.88e-96 |
|
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: 304.00 E-value: 5.88e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 136 FVPTVVQTVISL---IPLFIISPWVALV-----AIITFVLFAWLTLKGNREKQPFRSKRQDYYEEewnkSIASVQSVETN 207
Cdd:COG4987 133 LLPLLVALLVILaavAFLAFFSPALALVlalglLLAGLLLPLLAARLGRRAGRRLAAARAALRAR----LTDLLQGAAEL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 208 LMFGQQPRLLNDqavihngiISEALKehrlgifkynRWRIRVLTIARRIILVVWILQLIQGSLTIAGLIFVSVLVER--- 284
Cdd:COG4987 209 AAYGALDRALAR--------LDAAEA----------RLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAgal 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 285 --------------LFNSCWRFARLLDRAAENSEGAERLANLLLEPEPIETGSIQSVPAGPIGVSLSDVCFAYEGdysEA 350
Cdd:COG4987 271 sgpllallvlaalaLFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPG---AG 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 351 DGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESI 430
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQ--RPHLFDTTL 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAI 510
Cdd:COG4987 426 RENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAA 505
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 511 TEKEIQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEELIKSHGIYAQMVSL 575
Cdd:COG4987 506 TEQALLADLLEALAGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
334-576 |
1.88e-91 |
|
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: 280.97 E-value: 1.88e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEgdySEAD-GALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE 412
Cdd:cd03249 1 IEFKNVSFRYP---SRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 QFSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVL 492
Cdd:cd03249 78 QIGLVSQ--EPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 493 ADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQM 572
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
....
gi 818754182 573 VSLQ 576
Cdd:cd03249 235 VKAQ 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
334-567 |
1.27e-87 |
|
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: 270.64 E-value: 1.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03254 3 IEFENVNFSYDEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLA 493
Cdd:cd03254 79 IGVVLQ--DTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHG 567
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
146-576 |
2.11e-85 |
|
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: 276.58 E-value: 2.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 146 SLIPLFIISPWVAL--VAIITFVLFAWLTL-----KGNREKQPFRSKRQDYYEEewnkSIASVQSVETnlmFGQQprllN 218
Cdd:TIGR02204 149 GLIMMFITSPKLTSlvLLAVPLVLLPILLFgrrvrKLSRESQDRIADAGSYAGE----TLGAIRTVQA---FGHE----D 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 219 DQAVIHNGIISEALKEHRlgifkyNRWRIRVLTIARRIIL-------VVWI--LQLIQGSL---TIAGLIFVSVLVERLF 286
Cdd:TIGR02204 218 AERSRFGGAVEKAYEAAR------QRIRTRALLTAIVIVLvfgaivgVLWVgaHDVIAGKMsagTLGQFVFYAVMVAGSI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 287 NSCWRFARLLDRAAEnseGAERLANLLLEPEPIETGSIQSVPAGPI--GVSLSDVCFAYEG--DYSeadgALHDFSLEIE 362
Cdd:TIGR02204 292 GTLSEVWGELQRAAG---AAERLIELLQAEPDIKAPAHPKTLPVPLrgEIEFEQVNFAYPArpDQP----ALDGLNLTVR 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 363 PGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRPEAT 442
Cdd:TIGR02204 365 PGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQ--DPVLFAASVMENIRYGRPDAT 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 443 EEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI 522
Cdd:TIGR02204 443 DEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETL 522
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 818754182 523 LTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQMVSLQ 576
Cdd:TIGR02204 523 MKGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-576 |
3.60e-82 |
|
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: 268.12 E-value: 3.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 2 FKKLWSLLAPFHRTFYVFILLAFLYETVQ-LGASYVISLVVTLFGTGVAPWIWVV--LILGLLIfdefnMR-LDNAFDWH 77
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATEsTLAALLKPLLDDGFGGRDRSVLWWVplVVIGLAV-----LRgICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 78 IISKQSHPIFRHLKLSAITKFLKMNIPWHHQHNSGTLVGKVGDGVWKTLD-IIDVMSwefvpTVVQTVISLIPLFIISPW 156
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASaATDAFI-----VLVRETLTVIGLFIVLLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 157 ----VALVAIITFVLFAWLTLKGNRekqpfRSKRQDyyeEEWNKSIASVQSVETNLMFGQQPRLLndqaviHNGiisEAL 232
Cdd:TIGR02203 152 yswqLTLIVVVMLPVLSILMRRVSK-----RLRRIS---KEIQNSMGQVTTVAEETLQGYRVVKL------FGG---QAY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 233 KEHRLGiFKYNRWRIRVLTIARRIILVVWILQLIqGSLTIAGLIFVsVLVER------------LFNSCWRFARLLDRAA 300
Cdd:TIGR02203 215 ETRRFD-AVSNRNRRLAMKMTSAGSISSPITQLI-ASLALAVVLFI-ALFQAqagsltagdftaFITAMIALIRPLKSLT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 301 ENSE-------GAERLANLLLEPEPIETGS--IQSVPAGpigVSLSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVG 371
Cdd:TIGR02203 292 NVNApmqrglaAAESLFTLLDSPPEKDTGTraIERARGD---VEFRNVTFRYPGRDRPA---LDSISLVIEPGETVALVG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 372 QSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRP-EATEEEVEKAA 450
Cdd:TIGR02203 366 RSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQ--DVVLFNDTIANNIAYGRTeQADRAEIERAL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 451 HLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAII 530
Cdd:TIGR02203 444 AAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLV 523
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 818754182 531 IAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQMVSLQ 576
Cdd:TIGR02203 524 IAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
334-576 |
1.77e-78 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 247.40 E-value: 1.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03252 1 ITFEHVRFRYKPDGPVI---LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLA 493
Cdd:cd03252 78 VGVVLQ--ENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQMV 573
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
...
gi 818754182 574 SLQ 576
Cdd:cd03252 235 QLQ 237
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
334-576 |
3.71e-74 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 247.24 E-value: 3.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGdysEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:PRK11176 342 IEFRNVTFTYPG---KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAFPRPEA-TEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVL 492
Cdd:PRK11176 419 VALVSQ--NVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 493 ADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQM 572
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
....
gi 818754182 573 VSLQ 576
Cdd:PRK11176 576 HKMQ 579
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
251-548 |
2.84e-70 |
|
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: 235.26 E-value: 2.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 251 TIARRIILVVWILQLIQGSLTIAGLIFVSVLVERLFNSCWRFARLLDRAAENSEGAERLANLLLEPEPIETGSIQSVPAG 330
Cdd:TIGR02857 239 TLSVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAP 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 331 PIGVSLSDVCFAYEGdyseADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQL 410
Cdd:TIGR02857 319 ASSLEFSGVSVAYPG----RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 411 LEQFSYVPQGDdvYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARA 490
Cdd:TIGR02857 395 RDQIAWVPQHP--FLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 491 VLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVM 548
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
334-552 |
1.12e-68 |
|
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: 219.56 E-value: 1.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV---LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIafprpeateeevekaahlagihefviglkdgydtqvgergirLSGGQKQRVALARAVLA 493
Cdd:cd03228 78 IAYVPQ--DPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQGK 552
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
99-576 |
8.06e-67 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 227.54 E-value: 8.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 99 LKMNIPWHHQHNSGTLVgkvgdgvwKT-LDIIDVMSW---EFVPTVVQTVIS---LIPLFIISPW----VALVAIITFVL 167
Cdd:PRK13657 100 IQLPLAWHSQRGSGRAL--------HTlLRGTDALFGlwlEFMREHLATLVAlvvLLPLALFMNWrlslVLVVLGIVYTL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 168 FAWLTLKGNREKQpfrskrqdyyeeewnksiASVQSVETNLmFGQQPRLLNDQAVIH--NGIISE--ALKEH--RLGIFK 241
Cdd:PRK13657 172 ITTLVMRKTKDGQ------------------AAVEEHYHDL-FAHVSDAIGNVSVVQsyNRIEAEtqALRDIadNLLAAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 242 Y---NRWRI-RVL-----TIARRIILVVWILQLIQGSLTIAGLI----FVSVLVERL------FNSCW-------RFARL 295
Cdd:PRK13657 233 MpvlSWWALaSVLnraasTITMLAILVLGAALVQKGQLRVGEVVafvgFATLLIGRLdqvvafINQVFmaapkleEFFEV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 296 LD--RAAENSEGAERLANLllepepieTGSIQsvpagpigvsLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQS 373
Cdd:PRK13657 313 EDavPDVRDPPGAIDLGRV--------KGAVE----------FDDVSFSYDNSRQ----GVEDVSFEAKPGQTVAIVGPT 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 374 GAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLA 453
Cdd:PRK13657 371 GAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQ--DAGLFNRSIEDNIRVGRPDATDEEMRAAAERA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 454 GIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAH 533
Cdd:PRK13657 449 QAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 818754182 534 RLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQMVSLQ 576
Cdd:PRK13657 529 RLSTVRN-ADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
334-557 |
1.59e-65 |
|
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: 213.22 E-value: 1.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03245 3 IEFRNVSFSYPNQEIPA---LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLA 493
Cdd:cd03245 80 IGYVPQ--DVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLStIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
143-565 |
1.95e-64 |
|
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: 220.78 E-value: 1.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 143 TVISLIPLFIISPW---VALVAIITFVLFAWLTLKGNREKQpfrskrqdyyeEEWNK-SIASVQSVETNL--------Mf 210
Cdd:COG4618 143 APIFLAVLFLFHPLlglLALVGALVLVALALLNERLTRKPL-----------KEANEaAIRANAFAEAALrnaevieaM- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 211 GQQPRLLNDQAVIHNgiisEALKEHRLGifkyNRWRIRVLTIAR--RIILVVWILQL-----IQGSLTiAGLIFV-SVL- 281
Cdd:COG4618 211 GMLPALRRRWQRANA----RALALQARA----SDRAGGFSALSKflRLLLQSAVLGLgaylvIQGEIT-PGAMIAaSILm 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 282 ------VERLFNScWR---FARlldraaensEGAERLANLLLEPEPIETGSIQSVPAGPIgvSLSDVCFAYEGdysEADG 352
Cdd:COG4618 282 gralapIEQAIGG-WKqfvSAR---------QAYRRLNELLAAVPAEPERMPLPRPKGRL--SVENLTVVPPG---SKRP 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRY 432
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQ--DVELFDGTIAE 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAfpR-PEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAIT 511
Cdd:COG4618 425 NIA--RfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 512 EKEIqtnMRAILT----GKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:COG4618 503 EAAL---AAAIRAlkarGATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
306-572 |
5.35e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 206.21 E-value: 5.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 306 AERLANLLLEPEPIETGSIQSVPAGPIGVSLSDVCFAYEGdysEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVIT 385
Cdd:PRK11160 311 ARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPD---QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 386 RLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGlKDG 465
Cdd:PRK11160 388 RAWDPQQGEILLNGQPIADYSEAALRQAISVVSQ--RVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 466 YDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLStiwGLA--D 543
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLT---GLEqfD 541
|
250 260
....*....|....*....|....*....
gi 818754182 544 KIVVMDQGKKVEEGTHEELIKSHGIYAQM 572
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
266-576 |
4.80e-57 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 201.09 E-value: 4.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 266 IQGSLTIAGL----IFVSVLVERLFNSCWRFaRLLDRAaenSEGAERLANLLLEPEPIETGSiQSVPAGPIGVSLSDVCF 341
Cdd:PRK10789 247 VNGSLTLGQLtsfvMYLGLMIWPMLALAWMF-NIVERG---SAAYSRIRAMLAEAPVVKDGS-EPVPEGRGELDVNIRQF 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 342 AYEGdysEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQGD 421
Cdd:PRK10789 322 TYPQ---TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 422 dvYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILD 501
Cdd:PRK10789 399 --FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 502 EATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQMVSLQ 576
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
334-558 |
1.33e-56 |
|
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: 189.63 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEgdySEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03244 3 IEFKNVSLRYR---PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAfPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLA 493
Cdd:cd03244 80 ISIIPQ--DPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGT 558
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
306-535 |
1.97e-56 |
|
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: 198.35 E-value: 1.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 306 AERLANLLLEPEPIETGSI---QSVPAGPIGVSLSDVCFAYEGDyseaDGALHDFSLEIEPGQIVALVGQSGAGKTTIRK 382
Cdd:TIGR02868 304 AERIVEVLDAAGPVAEGSApaaGAVGLGKPTLELRDLSAGYPGA----PPVLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 383 VITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGL 462
Cdd:TIGR02868 380 TLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ--DAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRAL 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 463 KDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRL 535
Cdd:TIGR02868 458 PDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
251-573 |
8.92e-56 |
|
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: 197.80 E-value: 8.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 251 TIARRIILVVWILQLIQGSLTIAGLI----FVSVLVERLfNSCWRFARLLDRAAENSEGAERLANLLLE-PEPIETGSIQ 325
Cdd:TIGR01192 251 TISMMCILVIGTVLVIKGELSVGEVIafigFANLLIGRL-DQMSGFITQIFEARAKLEDFFDLEDSVFQrEEPADAPELP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 326 SVPAGpigVSLSDVCFayegDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDW 405
Cdd:TIGR01192 330 NVKGA---VEFRHITF----EFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTV 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 406 NGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRV 485
Cdd:TIGR01192 403 TRESLRKSIATVFQ--DAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 486 ALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:TIGR01192 481 AIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKGSFQELIQK 559
|
....*...
gi 818754182 566 HGIYAQMV 573
Cdd:TIGR01192 560 DGRFYKLL 567
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
334-552 |
8.80e-55 |
|
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: 184.98 E-value: 8.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGdySEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03248 12 VKFQNVTFAYPT--RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLA 493
Cdd:cd03248 90 VSLVGQ--EPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQGK 552
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
306-572 |
5.20e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 190.44 E-value: 5.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 306 AERLANLL-LEPEPIETGSIQSVPAGPIGVSLSDVC-FAYEGdySEADGALhdfSLEIEPGQIVALVGQSGAGKTTIRKV 383
Cdd:PRK11174 321 AESLVTFLeTPLAHPQQGEKELASNDPVTIEAEDLEiLSPDG--KTLAGPL---NFTLPAGQRIALVGPSGAGKTSLLNA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 384 ITRLAPCQmGTITVAGIDINDWNGSQLLEQFSYVpqGDDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLK 463
Cdd:PRK11174 396 LLGFLPYQ-GSLKINGIELRELDPESWRKHLSWV--GQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLP 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 464 DGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLaD 543
Cdd:PRK11174 473 QGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-D 551
|
250 260
....*....|....*....|....*....
gi 818754182 544 KIVVMDQGKKVEEGTHEELIKSHGIYAQM 572
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
150-573 |
5.53e-53 |
|
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: 192.26 E-value: 5.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 150 LFIISpwvaLVAIITFVLFAWLTlkgnreKQPFRSKRQDYYEEE--WNKSI-ASVQSVETnlmfgqqPRLLNDQAVIHNG 226
Cdd:TIGR01193 297 LFLLS----LLSIPVYAVIIILF------KRTFNKLNHDAMQANavLNSSIiEDLNGIET-------IKSLTSEAERYSK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 227 IISEAL----KEHRLGIFKYNRWRIRVLTiarRIILVVWIL-----QLIQGSLTIAGLIFVSVLVERLFNSCWRFARLLD 297
Cdd:TIGR01193 360 IDSEFGdylnKSFKYQKADQGQQAIKAVT---KLILNVVILwtgayLVMRGKLTLGQLITFNALLSYFLTPLENIINLQP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 298 RAAENSEGAERLANLLLEPEPIETGSIQSVPAGPIG-VSLSDVCFAYegdySEADGALHDFSLEIEPGQIVALVGQSGAG 376
Cdd:TIGR01193 437 KLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGdIVINDVSYSY----GYGSNILSDISLTIKMNSKTTIVGMSGSG 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 377 KTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAF-PRPEATEEEVEKAAHLAGI 455
Cdd:TIGR01193 513 KSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ--EPYIFSGSILENLLLgAKENVSQDEIWAACEIAEI 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 456 HEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMrAILTGKTAIIIAHRL 535
Cdd:TIGR01193 591 KDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRL 669
|
410 420 430
....*....|....*....|....*....|....*...
gi 818754182 536 StIWGLADKIVVMDQGKKVEEGTHEELIKSHGIYAQMV 573
Cdd:TIGR01193 670 S-VAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
334-573 |
1.95e-50 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 185.31 E-value: 1.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEAdgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVP--VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLA 493
Cdd:TIGR00958 557 VALVGQ--EPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAilTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQMV 573
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
145-564 |
3.12e-49 |
|
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: 179.08 E-value: 3.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 145 ISLIPLFIISPWVALVAII-TFVLFA------WLTLKGNREKQPFRSKRQDYYeeewNKSIASVQSVETNLMFGQ-QPRL 216
Cdd:TIGR01842 131 IYLLVCFLLHPWIGILALGgAVVLVGlallnnRATKKPLKEATEASIRANNLA----DSALRNAEVIEAMGMMGNlTKRW 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 217 LNDQavihngiiSEALKEHRLGifKYNRWRIRVLTIARRIILVVWILQL-----IQGSLTIAGLIFVSVLVERLFN---- 287
Cdd:TIGR01842 207 GRFH--------SKYLSAQSAA--SDRAGMLSNLSKYFRIVLQSLVLGLgaylaIDGEITPGMMIAGSILVGRALApidg 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 288 --SCWR--------FARLLDRAAENSEGAERLAnlLLEPE-PIETGSIQSVPAGPIGVSLSDVCFAyegdyseadgalhd 356
Cdd:TIGR01842 277 aiGGWKqfsgarqaYKRLNELLANYPSRDPAMP--LPEPEgHLSVENVTIVPPGGKKPTLRGISFS-------------- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 357 fsleIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAF 436
Cdd:TIGR01842 341 ----LQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQ--DVELFPGTVAENIAR 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 437 PRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEkeiQ 516
Cdd:TIGR01842 415 FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE---Q 491
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 818754182 517 TNMRAILT----GKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEELIK 564
Cdd:TIGR01842 492 ALANAIKAlkarGITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLA 542
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
334-564 |
3.24e-48 |
|
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: 167.51 E-value: 3.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:COG1122 1 IELENLSFSYPGGTP----ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDVYIFDESIRYNIAF-PR-----PEATEEEVEKAAHLAGIHEFviglkdgydtqvGERGI-RLSGGQKQRVA 486
Cdd:COG1122 77 VGLVFQNPDDQLFAPTVEEDVAFgPEnlglpREEIRERVEEALELVGLEHL------------ADRPPhELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 487 LArAVLADRP-ILILDEATSSVDAITEKEIqtnMRAILT----GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEE 561
Cdd:COG1122 145 IA-GVLAMEPeVLVLDEPTAGLDPRGRREL---LELLKRlnkeGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
...
gi 818754182 562 LIK 564
Cdd:COG1122 221 VFS 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
318-576 |
7.69e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 170.28 E-value: 7.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 318 PIETGSIQsvpagpigvsLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITV 397
Cdd:PRK10790 335 PLQSGRID----------IDNVSFAYRDDNL----VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 398 AGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRpEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRL 477
Cdd:PRK10790 401 DGRPLSSLSHSVLRQGVAMVQQ--DPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 478 SGGQKQRVALARaVLADRP-ILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEE 556
Cdd:PRK10790 478 SVGQKQLLALAR-VLVQTPqILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
250 260
....*....|....*....|
gi 818754182 557 GTHEELIKSHGIYAQMVSLQ 576
Cdd:PRK10790 556 GTHQQLLAAQGRYWQMYQLQ 575
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
353-566 |
1.04e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.91 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQGDDVYIfDESIRY 432
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYP-DLTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAF-------PRPEATeeevEKAAHLAgihEFViGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATS 505
Cdd:COG1131 93 NLRFfarlyglPRKEAR----ERIDELL---ELF-GLTDAADRKVGT----LSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 506 SVDAITEKEIQTNMRAILTGKTAIIIA-HRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSH 566
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLStHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
335-552 |
3.62e-42 |
|
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: 150.70 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 335 SLSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQF 414
Cdd:cd03225 1 ELKNLSFSYPDGARPA---LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 415 SYVPQGDDVYIFDESIRYNIAF-------PRPEAtEEEVEKAAHLAGIHEFViglkdgydtqvgERGI-RLSGGQKQRVA 486
Cdd:cd03225 78 GLVFQNPDDQFFGPTVEEEVAFglenlglPEEEI-EERVEEALELVGLEGLR------------DRSPfTLSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 487 LArAVLADRP-ILILDEATSSVDAITEKEIqtnMRAILT----GKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd03225 145 IA-GVLAMDPdILLLDEPTAGLDPAGRREL---LELLKKlkaeGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
307-563 |
4.78e-42 |
|
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: 158.53 E-value: 4.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 307 ERLANLLLEPEPIETGSIQSVPAGPIgVSLSDVCFAYEGDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITR 386
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAAAEPL-LEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 387 LAPCQMGTITVAGIDINDWNGSQLLE---QFSYVPQgdDVY-IFDE--SIRYNIAFP---RPEATEEEV-EKAAHLAgih 456
Cdd:COG1123 314 LLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQ--DPYsSLNPrmTVGDIIAEPlrlHGLLSRAERrERVAELL--- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 457 EFViGLkdgyDTQVGERGIR-LSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAH 533
Cdd:COG1123 389 ERV-GL----PPDLADRYPHeLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISH 463
|
250 260 270
....*....|....*....|....*....|
gi 818754182 534 RLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:COG1123 464 DLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
334-552 |
1.44e-41 |
|
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: 148.77 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGidindwngsqlleQ 413
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAFPRPEATE--EEVEKAAHLagIHEFVIgLKDGYDTQVGERGIRLSGGQKQRVALARAV 491
Cdd:cd03250 68 IAYVSQ--EPWIQNGTIRENILFGKPFDEEryEKVIKACAL--EPDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 492 LADRPILILDEATSSVDAITEKEIQTN--MRAILTGKTAIIIAHRLSTIWgLADKIVVMDQGK 552
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-552 |
3.39e-41 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 146.59 E-value: 3.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 335 SLSDVCFAYEGdysEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQF 414
Cdd:cd03246 2 EVENVSFRYPG---AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 415 SYVPQgdDVYIFDESIRYNIafprpeateeevekaahlagihefviglkdgydtqvgergirLSGGQKQRVALARAVLAD 494
Cdd:cd03246 79 GYLPQ--DDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 495 RPILILDEATSSVDAITEKEIQTNMRAI-LTGKTAIIIAHRLSTIwGLADKIVVMDQGK 552
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETL-ASADRILVLEDGR 172
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
334-566 |
7.46e-41 |
|
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: 155.06 E-value: 7.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDyseADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM---GTITVAGIDINDWNGSQL 410
Cdd:COG1123 5 LEVRDLSVRYPGG---DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 411 LEQFSYVPQGDDVYIFDESIRYNIAF-------PRPEAtEEEVEKAAHLAGIHEFViglkDGYDTQvgergirLSGGQKQ 483
Cdd:COG1123 82 GRRIGMVFQDPMTQLNPVTVGDQIAEalenlglSRAEA-RARVLELLEAVGLERRL----DRYPHQ-------LSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 484 RVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEE 561
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
....*
gi 818754182 562 LIKSH 566
Cdd:COG1123 230 ILAAP 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
334-557 |
8.59e-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: 145.92 E-value: 8.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGsQLLEQ 413
Cdd:cd03247 1 LSINNVSFSYPEQEQQV---LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIafprpeateeevekaahlagihefviglkdgydtqvgerGIRLSGGQKQRVALARAVLA 493
Cdd:cd03247 77 ISVLNQ--RPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEG 557
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
334-565 |
1.34e-40 |
|
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: 147.26 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE- 412
Cdd:cd03261 1 IELRGLTKSFGGRT-----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 --QFSYVPQG----DDVYIFDesiryNIAFPRPEAT---EEEVEKAAhLAGIHEfvIGLKDGYDTQVGErgirLSGGQKQ 483
Cdd:cd03261 76 rrRMGMLFQSgalfDSLTVFE-----NVAFPLREHTrlsEEEIREIV-LEKLEA--VGLRGAEDLYPAE----LSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 484 RVALARAVLADRPILILDEATSSVDAITEKEIQtnmRAILT-----GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGT 558
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVID---DLIRSlkkelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
....*..
gi 818754182 559 HEELIKS 565
Cdd:cd03261 221 PEELRAS 227
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
313-576 |
8.16e-40 |
|
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: 154.34 E-value: 8.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 313 LLEPEPiETGSIQSVPAGPIG-VSLSDVCFAYEgdyseADG--ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAP 389
Cdd:TIGR03797 431 ILEALP-EVDEAKTDPGKLSGaIEVDRVTFRYR-----PDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFET 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 390 CQMGTITVAGIDINDWNGSQLLEQFSYVPQGDDvyIFDESIRYNIAFPRPeATEEEVEKAAHLAGIHEFVIGLKDGYDTQ 469
Cdd:TIGR03797 505 PESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGR--LMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 470 VGERGIRLSGGQKQRVALARAvLADRP-ILILDEATSSVDAITEkEIQTNMRAILTGkTAIIIAHRLSTIWGlADKIVVM 548
Cdd:TIGR03797 582 ISEGGGTLSGGQRQRLLIARA-LVRKPrILLFDEATSALDNRTQ-AIVSESLERLKV-TRIVIAHRLSTIRN-ADRIYVL 657
|
250 260
....*....|....*....|....*...
gi 818754182 549 DQGKKVEEGTHEELIKSHGIYAQMVSLQ 576
Cdd:TIGR03797 658 DAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
334-565 |
8.09e-39 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 142.43 E-value: 8.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYeGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE- 412
Cdd:COG1127 6 IEVRNLTKSF-GDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 --QFSYVPQG----DDVYIFDesiryNIAFP---RPEATEEEVEKAAHLAgihefvigLKdgydtQVGERGIR------L 477
Cdd:COG1127 81 rrRIGMLFQGgalfDSLTVFE-----NVAFPlreHTDLSEAEIRELVLEK--------LE-----LVGLPGAAdkmpseL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 478 SGGQKQRVALARAvLADRP-ILILDEATSSVDAITEKEIQT---NMRAILtGKTAIIIAHRLSTIWGLADKIVVMDQGKK 553
Cdd:COG1127 143 SGGMRKRVALARA-LALDPeILLYDEPTAGLDPITSAVIDElirELRDEL-GLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
250
....*....|..
gi 818754182 554 VEEGTHEELIKS 565
Cdd:COG1127 221 IAEGTPEELLAS 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
353-557 |
2.05e-38 |
|
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: 141.10 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE---QFSYVPQgdDVY----- 424
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrrkEIQMVFQ--DPMsslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 ------IFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEfviGLKDGYDTQvgergirLSGGQKQRVALARAVLADRPIL 498
Cdd:cd03257 98 rmtigeQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPE---EVLNRYPHE-------LSGGQRQRVAIARALALNPKLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 499 ILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03257 168 IADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
334-565 |
2.84e-38 |
|
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: 140.90 E-value: 2.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03295 1 IEFENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDE-SIRYNIA-------FPRPEAtEEEVEKAAHLAGIHEfvIGLKDGYDTQvgergirLSGGQKQRV 485
Cdd:cd03295 77 IGYVIQ--QIGLFPHmTVEENIAlvpkllkWPKEKI-RERADELLALVGLDP--AEFADRYPHE-------LSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 486 ALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
..
gi 818754182 564 KS 565
Cdd:cd03295 225 RS 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
334-558 |
4.56e-38 |
|
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: 139.47 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:cd03369 7 IEVENLSVRYAPDLPPV---LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVYIFDESIRYNIAfPRPEATEEEVEKAahlagihefviglkdgydTQVGERGIRLSGGQKQRVALARAVLA 493
Cdd:cd03369 84 LTIIPQ--DPTLFSGTIRSNLD-PFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLaDKIVVMDQGKKVEEGT 558
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
354-505 |
5.65e-38 |
|
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: 137.01 E-value: 5.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgDDVYIFDESIRYN 433
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQ-DPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 434 IAFPRPEATEEEVEKAAHLAGIHEFViGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATS 505
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
335-552 |
8.22e-38 |
|
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: 136.99 E-value: 8.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 335 SLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQF 414
Cdd:cd00267 1 EIENLSFRYGGRT-----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 415 SYVPQgddvyifdesiryniafprpeateeevekaahlagihefviglkdgydtqvgergirLSGGQKQRVALARAVLAD 494
Cdd:cd00267 76 GYVPQ---------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 495 RPILILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
334-566 |
9.43e-38 |
|
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: 139.94 E-value: 9.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYeGDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:COG1124 2 LEVRNLSVSY-GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQgdDVY-IFD--ESIRYNIAFP-----RPEaTEEEVEKAAHLAGIHEfviGLKDGYDTQvgergirLSGGQKQRV 485
Cdd:COG1124 81 VQMVFQ--DPYaSLHprHTVDRILAEPlrihgLPD-REERIAELLEQVGLPP---SFLDRYPHQ-------LSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 486 ALARAVLADRPILILDEATSSVDAITEKEI---------QTNMrailtgkTAIIIAHRLSTIWGLADKIVVMDQGKKVEE 556
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEIlnllkdlreERGL-------TYLFVSHDLAVVAHLCDRVAVMQNGRIVEE 220
|
250
....*....|
gi 818754182 557 GTHEELIKSH 566
Cdd:COG1124 221 LTVADLLAGP 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
243-572 |
1.45e-37 |
|
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: 149.33 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 243 NRW-RIRVLTIARRIILVVWILQLIQGSLTIAGLIFVSVL--VERLFNSCWrFARLLDRAAENSEGAERLANLLlEPEPI 319
Cdd:TIGR00957 1188 NRWlAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSysLQVTFYLNW-LVRMSSEMETNIVAVERLKEYS-ETEKE 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 320 ETGSIQSV--PAG--PIG-VSLSDVCFAYEGDYseaDGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGT 394
Cdd:TIGR00957 1266 APWQIQETapPSGwpPRGrVEFRNYCLRYREDL---DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGE 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 395 ITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAfPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERG 474
Cdd:TIGR00957 1343 IIIDGLNIAKIGLHDLRFKITIIPQ--DPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGG 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 475 IRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLAdKIVVMDQGKKV 554
Cdd:TIGR00957 1420 ENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVA 1498
|
330
....*....|....*...
gi 818754182 555 EEGTHEELIKSHGIYAQM 572
Cdd:TIGR00957 1499 EFGAPSNLLQQRGIFYSM 1516
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
353-567 |
3.13e-37 |
|
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: 138.07 E-value: 3.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDInDWNGSQLLEQFSYVPQGDDVYiFDESIRY 432
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQIGVLPDERGLY-DRLTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAF------PRPEATEEEVEKAAHLAGIHEFviglkdgYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSS 506
Cdd:COG4555 94 NIRYfaelygLFDEELKKRIEELIELLGLEEF-------LDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 507 VDAITEKEIQTNMRAILT-GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSHG 567
Cdd:COG4555 163 LDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
393-575 |
6.80e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 147.10 E-value: 6.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 393 GTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGE 472
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQ--EPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGP 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 473 RGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIwGLADKIVVMDQ 550
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASI-KRSDKIVVFNN 1433
|
170 180 190
....*....|....*....|....*....|.
gi 818754182 551 ----GKKVE-EGTHEELIKSH-GIYAQMVSL 575
Cdd:PTZ00265 1434 pdrtGSFVQaHGTHEELLSVQdGVYKKYVKL 1464
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-566 |
1.99e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.99 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINdwngsQLLEQ 413
Cdd:COG1121 7 IELENLTVSYGGRP-----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDvyiFDESI-----------RYNI--AFPRPEATE-EEVEKAAHLAGIHEFViglkdgyDTQVGErgirLSG 479
Cdd:COG1121 77 IGYVPQRAE---VDWDFpitvrdvvlmgRYGRrgLFRRPSRADrEAVDEALERVGLEDLA-------DRPIGE----LSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 480 GQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGkKVEEGT 558
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGP 221
|
....*...
gi 818754182 559 HEELIKSH 566
Cdd:COG1121 222 PEEVLTPE 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
335-552 |
2.87e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.56 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 335 SLSDVCFAYEGDYSeadgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQF 414
Cdd:COG4619 2 ELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 415 SYVPQgdDVYIFDESIRYNIAFP----RPEATEEEVEKAAHLAGIHEFVIglkdgyDTQVGergiRLSGGQKQRVALARA 490
Cdd:COG4619 77 AYVPQ--EPALWGGTVRDNLPFPfqlrERKFDRERALELLERLGLPPDIL------DKPVE----RLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 491 VLADRPILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
329-565 |
1.65e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 329 AGPIgVSLSDVCFAYEGDyseADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGS 408
Cdd:PRK13635 2 KEEI-IRVEHISFRYPDA---ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 409 QLLEQFSYVPQGDDVYIFDESIRYNIAF-------PRPEATEEeVEKAAHLAGIHEFViglkdgydtqvGERGIRLSGGQ 481
Cdd:PRK13635 78 DVRRQVGMVFQNPDNQFVGATVQDDVAFglenigvPREEMVER-VDQALRQVGMEDFL-----------NREPHRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 482 KQRVALArAVLADRP-ILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGT 558
Cdd:PRK13635 146 KQRVAIA-GVLALQPdIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGT 223
|
....*..
gi 818754182 559 HEELIKS 565
Cdd:PRK13635 224 PEEIFKS 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
334-548 |
1.66e-35 |
|
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: 132.60 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYeGDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGsqlleQ 413
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDdvYIFD-ESIRYNIAFP---RPEATEEEVEKAAHLagIHEFviGLKDG---YDTQvgergirLSGGQKQRVA 486
Cdd:cd03293 75 RGYVFQQD--ALLPwLTVLDNVALGlelQGVPKAEARERAEEL--LELV--GLSGFenaYPHQ-------LSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 487 LARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVM 548
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
334-552 |
2.64e-35 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 132.23 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEADgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQL--- 410
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQ-ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 411 -LEQFSYVPQGddvY--IFDESIRYNIAFP---RPEATEEEVEKAAHLAGihefVIGLKDGYDTQVGErgirLSGGQKQR 484
Cdd:cd03255 80 rRRHIGFVFQS---FnlLPDLTALENVELPlllAGVPKKERRERAEELLE----RVGLGDRLNHYPSE----LSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 485 VALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLStIWGLADKIVVMDQGK 552
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPE-LAEYADRIIELRDGK 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
353-563 |
4.48e-35 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 131.93 E-value: 4.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQfsyvpQGDDVYIF------ 426
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA-----RRRIGMIFqhfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 427 -DESIRYNIAFPRPEATEEEVEKAAHLAGIHEFViGLKD---GYDTQvgergirLSGGQKQRVALARAVLADRPILILDE 502
Cdd:cd03258 95 sSRTVFENVALPLEIAGVPKAEIEERVLELLELV-GLEDkadAYPAQ-------LSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 503 ATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:cd03258 167 ATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
334-562 |
5.93e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 132.55 E-value: 5.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGdysEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGID-INDWNGSQLLE 412
Cdd:TIGR04520 1 IEVENVSFSYPE---SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 QFSYVPQGDDVYIFDESIRYNIAF-------PRPEaTEEEVEKAAHLAGIHEFViglkdgydtqvgERG-IRLSGGQKQR 484
Cdd:TIGR04520 78 KVGMVFQNPDNQFVGATVEDDVAFglenlgvPREE-MRKRVDEALKLVGMEDFR------------DREpHLLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 485 VALArAVLADRP-ILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEE 561
Cdd:TIGR04520 145 VAIA-GVLAMRPdIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPRE 222
|
.
gi 818754182 562 L 562
Cdd:TIGR04520 223 I 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-563 |
2.27e-34 |
|
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: 130.55 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:COG1120 2 LEAENLSVGYGGRP-----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDVyIFDESIR---------YNIAFPRPEATEEE-VEKAAHLAGIHEFViglkdgyDTQVGErgirLSGGQKQ 483
Cdd:COG1120 77 IAYVPQEPPA-PFGLTVRelvalgrypHLGLFGRPSAEDREaVEEALERTGLEHLA-------DRPVDE----LSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 484 RVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEE 561
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
..
gi 818754182 562 LI 563
Cdd:COG1120 225 VL 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
55-573 |
6.52e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 138.19 E-value: 6.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 55 VLILGLLIFDEFNMRLDNAFdWhIISKQSHPIfRHLKLSAITKFLKMNIPWHHQHNSGTL-------VGKVGDGVWKTLD 127
Cdd:PLN03232 953 IVVYALLGFGQVAVTFTNSF-W-LISSSLHAA-KRLHDAMLNSILRAPMLFFHTNPTGRVinrfskdIGDIDRNVANLMN 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 128 IIDVMSWEFVPT-VVQTVISLIPLFIISPWVALVaIITFVLFAWLTLKGNREKQPFRSKRQDYYEEEWNkSIASVQSVET 206
Cdd:PLN03232 1030 MFMNQLWQLLSTfALIGTVSTISLWAIMPLLILF-YAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALN-GLSSIRAYKA 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 207 NlmfgqqprllnDQAVIHNGIISEALKEHRLGIFKYNRW-RIRVLTIARRIILVVWILQLIQGSLTIAGLIFVSV---LV 282
Cdd:PLN03232 1108 Y-----------DRMAKINGKSMDNNIRFTLANTSSNRWlTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTmglLL 1176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 283 ERLFNSCWRFARLLDRA--AENS-EGAERLANLLLEPEpiETGSI----QSVPAGPIG--VSLSDVCFAYEgdySEADGA 353
Cdd:PLN03232 1177 SYTLNITTLLSGVLRQAskAENSlNSVERVGNYIDLPS--EATAIiennRPVSGWPSRgsIKFEDVHLRYR---PGLPPV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQGDdvYIFDESIRYN 433
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP--VLFSGTVRFN 1329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 434 IAfPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEK 513
Cdd:PLN03232 1330 ID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 514 EIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHG-IYAQMV 573
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTsAFFRMV 1468
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
334-557 |
2.98e-33 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 126.09 E-value: 2.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQllEQ 413
Cdd:cd03259 1 LELKGLSKTYGSVR-----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDVY----IFDesiryNIAFP-----RPEATEEE-VEKAAHLAGIHEFviglkdgydtqvGERGIR-LSGGQK 482
Cdd:cd03259 74 IGMVFQDYALFphltVAE-----NIAFGlklrgVPKAEIRArVRELLELVGLEGL------------LNRYPHeLSGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 483 QRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQreLGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
354-573 |
3.29e-33 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 136.06 E-value: 3.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYN 433
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQ--DPVLFDGTVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 434 IAfPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILIL-DEATSSVDAITE 512
Cdd:PTZ00243 1404 VD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALD 1482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 513 KEIQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEELI-KSHGIYAQMV 573
Cdd:PTZ00243 1483 RQIQATVMSAFSAYTVITIAHRLHTV-AQYDKIIVMDHGAVAEMGSPRELVmNRQSIFHSMV 1543
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
335-551 |
4.44e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 125.72 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 335 SLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDIndwngSQLLEQF 414
Cdd:cd03235 1 EVEDLTVSYGGHP-----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 415 SYVPQGDD--------VYIFDESIRYNIAFPRPEATEEEVEKAAHLagiHEFViGLKDGYDTQVGErgirLSGGQKQRVA 486
Cdd:cd03235 71 GYVPQRRSidrdfpisVRDVVLMGLYGHKGLFRRLSKADKAKVDEA---LERV-GLSELADRQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 487 LARAVLADRPILILDEATSSVDAITEKEIQTNMRAI-LTGKTAIIIAHRLSTIWGLADKIVVMDQG 551
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
335-557 |
5.28e-33 |
|
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: 124.47 E-value: 5.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 335 SLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQF 414
Cdd:cd03214 1 EVENLSVGYGGRT-----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 415 SYVPQgddvyifdesiryniafprpeateeevekAAHLAGIHEFViglkdgydtqvgERGIR-LSGGQKQRVALARAVLA 493
Cdd:cd03214 76 AYVPQ-----------------------------ALELLGLAHLA------------DRPFNeLSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
334-562 |
6.04e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.45 E-value: 6.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYeGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwngsqlLE- 412
Cdd:COG3842 6 LELENVSKRY-GDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG------LPp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 ---QFSYVPQGDDvyIFDE-SIRYNIAFP------RPEATEEEVEKAAHLAGIhefviglkDGYdtqvGERGIR-LSGGQ 481
Cdd:COG3842 75 ekrNVGMVFQDYA--LFPHlTVAENVAFGlrmrgvPKAEIRARVAELLELVGL--------EGL----ADRYPHqLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 482 KQRVALARAvLADRP-ILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGT 558
Cdd:COG3842 141 QQRVALARA-LAPEPrVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
....
gi 818754182 559 HEEL 562
Cdd:COG3842 220 PEEI 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
353-552 |
1.44e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 122.89 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQGDDVYifdesiry 432
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 niafprPEATEEEVekaahlagihefviglkdgydtqvgergIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITE 512
Cdd:cd03230 86 ------ENLTVREN----------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 818754182 513 KEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd03230 132 REFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
328-551 |
3.03e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.82 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 328 PAGPIGVSLSDVCFAYEGDYSEADgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDIndwng 407
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVT-ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 408 SQLLEQFSYVPQGDDVY----IFDesiryNIAF-------PRPEAtEEEVEKAAHLAGIHEFviglKDGYDTQvgergir 476
Cdd:COG1116 76 TGPGPDRGVVFQEPALLpwltVLD-----NVALglelrgvPKAER-RERARELLELVGLAGF----EDAYPHQ------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 477 LSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAH------RlstiwgLADKIVVM 548
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTHdvdeavF------LADRVVVL 212
|
...
gi 818754182 549 DQG 551
Cdd:COG1116 213 SAR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
353-552 |
3.62e-32 |
|
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: 121.91 E-value: 3.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLleqfsyvPQGDDV-YIFDE--- 428
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP-------PLRRRIgMVFQDfal 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 ----SIRYNIAFPrpeateeevekaahlagihefviglkdgydtqvgergirLSGGQKQRVALARAVLADRPILILDEAT 504
Cdd:cd03229 88 fphlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 818754182 505 SSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd03229 129 SALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
334-562 |
4.03e-32 |
|
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: 123.44 E-value: 4.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM-----GTITVAGIDINDWNGS 408
Cdd:cd03260 1 IELRDLNVYYGDKH-----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 409 --QLLEQFSYVPQGDDVyiFDESIRYNIAFP-------RPEATEEEVEKAAHLAGIHEFViglKDGYDtqvgerGIRLSG 479
Cdd:cd03260 76 vlELRRRVGMVFQKPNP--FPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEV---KDRLH------ALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 480 GQKQRVALARAvLADRP-ILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGT 558
Cdd:cd03260 145 GQQQRLCLARA-LANEPeVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
....
gi 818754182 559 HEEL 562
Cdd:cd03260 224 TEQI 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
353-563 |
5.70e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 126.35 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTT-IRkVITRLAPCQMGTITVAGIDINDWNGSQLLE---QFSYVPQGDDVY---- 424
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTlIR-CINLLERPTSGSVLVDGVDLTALSERELRAarrKIGMIFQHFNLLssrt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 IFDesiryNIAFP-------RPEATEeeveKAAHLAgihEFViGL---KDGYDTQvgergirLSGGQKQRVALARAvLAD 494
Cdd:COG1135 99 VAE-----NVALPleiagvpKAEIRK----RVAELL---ELV-GLsdkADAYPSQ-------LSGGQKQRVGIARA-LAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 495 RP-ILILDEATSSVDAITekeiqTnmRAILT---------GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:COG1135 158 NPkVLLCDEATSALDPET-----T--RSILDllkdinrelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVF 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
300-573 |
1.29e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 131.01 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 300 AENSEGA-ERLANLL-LEPE-PIETGSIQSVPAGPIG--VSLSDVCFAYEgdySEADGALHDFSLEIEPGQIVALVGQSG 374
Cdd:PLN03130 1199 AENSLNAvERVGTYIdLPSEaPLVIENNRPPPGWPSSgsIKFEDVVLRYR---PELPPVLHGLSFEISPSEKVGIVGRTG 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 375 AGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQGDdvYIFDESIRYNIAfPRPEATEEEVEKAAHLAG 454
Cdd:PLN03130 1276 AGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAP--VLFSGTVRFNLD-PFNEHNDADLWESLERAH 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 455 IHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHR 534
Cdd:PLN03130 1353 LKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHR 1432
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 818754182 535 LSTIWGlADKIVVMDQGKKVEEGTHEELI-KSHGIYAQMV 573
Cdd:PLN03130 1433 LNTIID-CDRILVLDAGRVVEFDTPENLLsNEGSAFSKMV 1471
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
334-556 |
2.75e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 121.30 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEADgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQL--- 410
Cdd:COG1136 5 LELRNLTKSYGTGEGEVT-ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 411 -LEQFSYVPQgdDVYIFDE-SIRYNIAFP---RPEATEEEVEKAAHLAgihEFViGLKDGYDTQVGErgirLSGGQKQRV 485
Cdd:COG1136 84 rRRHIGFVFQ--FFNLLPElTALENVALPlllAGVSRKERRERARELL---ERV-GLGDRLDHRPSQ----LSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 486 ALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAH--RLStiwGLADKIVVMDQGKKVEE 556
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHdpELA---ARADRVIRLRDGRIVSD 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
353-565 |
3.27e-31 |
|
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: 123.62 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM---GTITVAGIDINDWNGSQLLE----QFSYVPQ------ 419
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQMIFQdpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 420 ------GDdvyIFDESIRYNIAFPRPEAtEEEVEKAAHLAGI-----------HEFviglkdgydtqvgergirlSGGQK 482
Cdd:COG0444 100 npvmtvGD---QIAEPLRIHGGLSKAEA-RERAIELLERVGLpdperrldrypHEL-------------------SGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 483 QRVALARAVLADRPILILDEATSSVDAITE-------KEIQTNMrailtGKTAIIIAHRLSTIWGLADKIVVMDQGKKVE 555
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQaqilnllKDLQREL-----GLAILFITHDLGVVAEIADRVAVMYAGRIVE 231
|
250
....*....|
gi 818754182 556 EGTHEELIKS 565
Cdd:COG0444 232 EGPVEELFEN 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
262-572 |
9.58e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 128.32 E-value: 9.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 262 ILQLIQGSLTIA----GLIFVSVLVERLFnscwRFARLLDRAAENSEGAERLANLLLEPE-------PIETGsiqsVPAg 330
Cdd:PLN03130 544 VFTLLGGDLTPAraftSLSLFAVLRFPLF----MLPNLITQAVNANVSLKRLEELLLAEErvllpnpPLEPG----LPA- 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 331 pigVSLSDVCFAYEgdySEAD-GALHDFSLEIEPGQIVALVGQSGAGKTT-IRKVITRLAPCQMGTITVAGidindwngs 408
Cdd:PLN03130 615 ---ISIKNGYFSWD---SKAErPTLSNINLDVPVGSLVAIVGSTGEGKTSlISAMLGELPPRSDASVVIRG--------- 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 409 qlleQFSYVPQGDdvYIFDESIRYNIAFPRPeATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALA 488
Cdd:PLN03130 680 ----TVAYVPQVS--WIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMA 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 489 RAVLADRPILILDEATSSVDAITEKEI-QTNMRAILTGKTAIIIA---HRLSTIwglaDKIVVMDQGKKVEEGTHEELIK 564
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTnqlHFLSQV----DRIILVHEGMIKEEGTYEELSN 828
|
....*...
gi 818754182 565 SHGIYAQM 572
Cdd:PLN03130 829 NGPLFQKL 836
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
334-552 |
1.93e-30 |
|
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: 118.51 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDW-----NGS 408
Cdd:cd03301 1 VELENVTKRFGNVT-----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkdrDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 409 QLLEQFSYVPQgddvyifdESIRYNIAFP------RPEATEEEVEKAAHLAGIHEfvigLKDGYDTQvgergirLSGGQK 482
Cdd:cd03301 76 MVFQNYALYPH--------MTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEH----LLDRKPKQ-------LSGGQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 483 QRVALARAVLADRPILILDEATSSVDAitekEIQTNMRAILT------GKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd03301 137 QRVALGRAIVREPKVFLMDEPLSNLDA----KLRVQMRAELKrlqqrlGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
353-563 |
5.60e-30 |
|
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: 118.90 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE-----------QFSYVPQgd 421
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkismvfqSFALLPH-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 422 dvyifdESIRYNIAFP-----RPEATEEEV-EKAAHLAGIHefviGLKDGYDTQvgergirLSGGQKQRVALARAVLADR 495
Cdd:cd03294 117 ------RTVLENVAFGlevqgVPRAEREERaAEALELVGLE----GWEHKYPDE-------LSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 496 PILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
354-565 |
1.57e-29 |
|
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: 116.67 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQllEQFSYVPQgdDVYIFDE-SIRY 432
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQ--NYALFPHmTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAF-------PRPEaTEEEVEKAAHLAGIHEfvigLKDGYDTqvgergiRLSGGQKQRVALARAVLADRPILILDEATS 505
Cdd:cd03299 91 NIAYglkkrkvDKKE-IERKVLEIAEMLGIDH----LLNRKPE-------TLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 506 SVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:cd03299 159 ALDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
347-562 |
2.05e-29 |
|
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: 116.51 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPqgddvYIF 426
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIG-----MIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 427 DEsirYNI----------------------AFPRPeATEEEVEKAAHLAgihEFViGLKDGYDTQVGErgirLSGGQKQR 484
Cdd:cd03256 85 QQ---FNLierlsvlenvlsgrlgrrstwrSLFGL-FPKEEKQRALAAL---ERV-GLLDKAYQRADQ----LSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 485 VALARAvLADRPILIL-DEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEE 561
Cdd:cd03256 153 VAIARA-LMQQPKLILaDEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
.
gi 818754182 562 L 562
Cdd:cd03256 232 L 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
326-573 |
3.83e-29 |
|
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: 116.16 E-value: 3.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 326 SVPAGPIG----VSLSDVCFAYEgdySEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGID 401
Cdd:cd03288 8 SSNSGLVGlggeIKIHDLCVRYE---NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 402 INDWNGSQLLEQFSYVPQgdDVYIFDESIRYNIAfPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQ 481
Cdd:cd03288 85 ISKLPLHTLRSRLSIILQ--DPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 482 KQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEE 561
Cdd:cd03288 162 RQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPEN 240
|
250
....*....|...
gi 818754182 562 LI-KSHGIYAQMV 573
Cdd:cd03288 241 LLaQEDGVFASLV 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
334-562 |
4.77e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.25 E-value: 4.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwngsqlLE- 412
Cdd:COG3839 4 LELENVSKSYGGVE-----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD------LPp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 ---QFSYVPQGDDVY----IFDesiryNIAFP-----RPEAT-EEEVEKAAHLAGIHEfvigLKDGYDTQvgergirLSG 479
Cdd:COG3839 73 kdrNIAMVFQSYALYphmtVYE-----NIAFPlklrkVPKAEiDRRVREAAELLGLED----LLDRKPKQ-------LSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 480 GQKQRVALARAVLADRPILILDEATSSVDAitekEIQTNMRAIL------TGKTAIIIAHRLSTIWGLADKIVVMDQGKK 553
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDA----KLRVEMRAEIkrlhrrLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
....*....
gi 818754182 554 VEEGTHEEL 562
Cdd:COG3839 213 QQVGTPEEL 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
335-552 |
6.57e-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: 113.89 E-value: 6.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 335 SLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWngsQLLEQF 414
Cdd:cd03226 1 RIENISFSYKKGTE----ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 415 SYVPQGDDVYIFDESIRYNIAF--PRPEATEEEVEKAAHLAGIHEFViglkdgydtqvgERGIR-LSGGQKQRVALARAV 491
Cdd:cd03226 74 GYVMQDVDYQLFTDSVREELLLglKELDAGNEQAETVLKDLDLYALK------------ERHPLsLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 492 LADRPILILDEATSSVDAITEKEIQTNMRAI-LTGKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
334-565 |
8.13e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 8.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:PRK13632 8 IKVENVSFSYPNSENNA---LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDVYIFDESIRYNIAFP------RPEATEEEVEKAAHLAGIHEFvigLKdgYDTQvgergiRLSGGQKQRVAL 487
Cdd:PRK13632 85 IGIIFQNPDNQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDY---LD--KEPQ------NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 488 ArAVLADRP-ILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWgLADKIVVMDQGKKVEEGTHEELIK 564
Cdd:PRK13632 154 A-SVLALNPeIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN 231
|
.
gi 818754182 565 S 565
Cdd:PRK13632 232 N 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
353-562 |
1.44e-28 |
|
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: 113.37 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQgDDVyIFDE-SIR 431
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQ-FDA-LFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 YNIAF-------PRPEAtEEEVEKAAHlagihefVIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEAT 504
Cdd:cd03263 94 EHLRFyarlkglPKSEI-KEEVELLLR-------VLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 505 SSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
353-562 |
2.03e-28 |
|
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: 112.91 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-FSYVPQGDDvyIFDE-SI 430
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRR--IFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNI---AFPRPEATEEEVekaahLAGIHEFVIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSSV 507
Cdd:cd03224 93 EENLllgAYARRRAKRKAR-----LERVYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 508 DAITEKEIQTNMRAILTGKTAIIIA-HRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:cd03224 164 APKIVEEIFEAIRELRDEGVTILLVeQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
334-561 |
3.30e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.45 E-value: 3.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE- 412
Cdd:COG2884 2 IRFENVSKRYPGGRE----ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 --QFSYVPQgDDVYIFDESIRYNIAFP------RPEATEEEVEKAAHLagihefvIGLKDGYDTQVGErgirLSGGQKQR 484
Cdd:COG2884 78 rrRIGVVFQ-DFRLLPDRTVYENVALPlrvtgkSRKEIRRRVREVLDL-------VGLSDKAKALPHE----LSGGEQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 485 VALARAVLADRPILILDEATSSVDAITEKEIqtnMRAIL----TGKTaIIIA-HRLSTIWGLADKIVVMDQGKKVEEGTH 559
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEI---MELLEeinrRGTT-VLIAtHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
..
gi 818754182 560 EE 561
Cdd:COG2884 222 GV 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
353-562 |
5.51e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.86 E-value: 5.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVItrlapcqmgtitvAGIDIND-----WNGSQLleqFSYVPQGD-DV-YI 425
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRII-------------AGLETPDsgrivLNGRDL---FTNLPPRErRVgFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 FDE-------SIRYNIAF------PRPEATEEEVE---KAAHLAGihefvigLKDGYDTQvgergirLSGGQKQRVALAR 489
Cdd:COG1118 81 FQHyalfphmTVAENIAFglrvrpPSKAEIRARVEellELVQLEG-------LADRYPSQ-------LSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 490 AvLADRP-ILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:COG1118 147 A-LAVEPeVLLLDEPFGALDAKVRKELRRWLRRLHdeLGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
353-561 |
5.81e-28 |
|
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: 112.82 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE-------QfsyVPQgddvyI 425
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARlgiartfQ---NPR-----L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 FDE-SIRYNIA-----------------FPRPEATEEEV-EKAAHLAgihEFViGLKDGYDTQVGErgirLSGGQKQRVA 486
Cdd:COG0411 91 FPElTVLENVLvaaharlgrgllaallrLPRARREEREArERAEELL---ERV-GLADRADEPAGN----LSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 487 LARAvLADRP-ILILDEATSSVdaiTEKEIQTNMRAIL-----TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHE 560
Cdd:COG0411 163 IARA-LATEPkLLLLDEPAAGL---NPEETEELAELIRrlrdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
.
gi 818754182 561 E 561
Cdd:COG0411 239 E 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
295-573 |
7.33e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 119.31 E-value: 7.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 295 LLDRAAENSEGAERLANLLLEPEPIETGSIQSVPAGPiGVSLSDVCFAYegDYSEADGALHDFSLEIEPGQIVALVGQSG 374
Cdd:PLN03232 577 LLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAP-AISIKNGYFSW--DSKTSKPTLSDINLEIPVGSLVAIVGGTG 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 375 AGKTT-IRKVITRLAPCQMGTITVAGidindwngsqlleQFSYVPQGDdvYIFDESIRYNIAFPRPEATEEEVEKAAHLA 453
Cdd:PLN03232 654 EGKTSlISAMLGELSHAETSSVVIRG-------------SVAYVPQVS--WIFNATVRENILFGSDFESERYWRAIDVTA 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 454 GIHEfvIGLKDGYD-TQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDA-ITEKEIQTNMRAILTGKTAIII 531
Cdd:PLN03232 719 LQHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLV 796
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 818754182 532 AHRLSTIwGLADKIVVMDQGKKVEEGTHEELIKSHGIYAQMV 573
Cdd:PLN03232 797 TNQLHFL-PLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
314-573 |
1.55e-27 |
|
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: 118.51 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 314 LEPEPIETGSIQsvPAGPIGVSLSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMG 393
Cdd:TIGR00957 619 LEPDSIERRTIK--PGEGNSITVHNATFTWARDLPPT---LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 394 TITVAGidindwngsqlleQFSYVPQgdDVYIFDESIRYNIAFPRP--EATEEEVEKAAHLAGIHEFvigLKDGYDTQVG 471
Cdd:TIGR00957 694 HVHMKG-------------SVAYVPQ--QAWIQNDSLRENILFGKAlnEKYYQQVLEACALLPDLEI---LPSGDRTEIG 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 472 ERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNM---RAILTGKTAIIIAHRLSTIwGLADKIVVM 548
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYL-PQVDVIIVM 834
|
250 260
....*....|....*....|....*
gi 818754182 549 DQGKKVEEGTHEELIKSHGIYAQMV 573
Cdd:TIGR00957 835 SGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
334-562 |
1.58e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 111.30 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE- 412
Cdd:COG3638 3 LELRNLSKRYPGGTP----ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 --QFSYVPQGddvyifdesirYN------------------IAFPR---PEATEEEVEKAAHLagIHEFviGLKDgydtQ 469
Cdd:COG3638 79 rrRIGMIFQQ-----------FNlvprlsvltnvlagrlgrTSTWRsllGLFPPEDRERALEA--LERV--GLAD----K 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 470 VGERGIRLSGGQKQRVALARAvLADRPILIL-DEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIV 546
Cdd:COG3638 140 AYQRADQLSGGQQQRVAIARA-LVQEPKLILaDEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRYADRII 218
|
250
....*....|....*.
gi 818754182 547 VMDQGKKVEEGTHEEL 562
Cdd:COG3638 219 GLRDGRVVFDGPPAEL 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
353-564 |
3.63e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDIND--WNGSQLLEQFSYVPQGDDVYIFDESI 430
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPEYQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNIAF-PR-----PEATEEEVEKAAHLAGIHefviglkdgYDTQVGERGIRLSGGQKQRVALArAVLADRP-ILILDEA 503
Cdd:PRK13637 102 EKDIAFgPInlglsEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIA-GVVAMEPkILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 504 TSSVDAITEKEIQTNMRAILTGK--TAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIK 564
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
354-563 |
7.05e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.72 E-value: 7.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgddVYIFDE--SIR 431
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ---HHLTPEgiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 YNIAFPRP----------EATEEEVEKAAHLAGIHEFViglkdgyDTQVGErgirLSGGQKQRVALARAVLADRPILILD 501
Cdd:PRK11231 95 ELVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 502 EATSSVDAITEKEIQTNMRAILT-GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
354-552 |
8.88e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 107.64 E-value: 8.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVIT-RLAPCQM-GTITVAGIDINDWNGSQLLeqfSYVPQgDDVYIFDESIR 431
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGVsGEVLINGRPLDKRSFRKII---GYVPQ-DDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 YNIAFprpeateeevekAAHLAGIhefviglkdgydtqvgergirlSGGQKQRVALARAVLADRPILILDEATSSVDAIT 511
Cdd:cd03213 101 ETLMF------------AAKLRGL----------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 818754182 512 EKEIQTNMRAI-LTGKTAIIIAHRLST-IWGLADKIVVMDQGK 552
Cdd:cd03213 147 ALQVMSLLRRLaDTGRTIICSIHQPSSeIFELFDKLLLLSQGR 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
334-557 |
1.04e-26 |
|
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: 107.96 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEgdyseaDGALHdFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQllEQ 413
Cdd:cd03298 1 VRLDKIRFSYG------EQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDVYIfDESIRYNIAF---PRPEATEEE---VEKAAHLAGIHEFVIGLKDgydtqvgergiRLSGGQKQRVAL 487
Cdd:cd03298 72 VSMLFQENNLFA-HLTVEQNVGLglsPGLKLTAEDrqaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 488 ARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHaeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
353-563 |
1.32e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 108.16 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLE---QFSYVPQgddvyifdes 429
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKlrrKVGMVFQ---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 iRYNIaFP-------------------RPEATE---EEVEKaahlagihefvIGLKDgydtQVGERGIRLSGGQKQRVAL 487
Cdd:COG1126 85 -QFNL-FPhltvlenvtlapikvkkmsKAEAEEramELLER-----------VGLAD----KADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 488 ARAvLADRPILIL-DEATSSVDAITEKEIQTNMRAI-LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:COG1126 148 ARA-LAMEPKVMLfDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
353-565 |
1.32e-26 |
|
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: 108.29 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-----FSyVPQgddvyIFD 427
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigrtFQ-IPR-----LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 428 E-SIRYNI-------------AFPRPEATEEEVEKAAHLAgihEFViGLKDGYDTQVGErgirLSGGQKQRVALARAvLA 493
Cdd:cd03219 89 ElTVLENVmvaaqartgsgllLARARREEREARERAEELL---ERV-GLADLADRPAGE----LSYGQQRRLEIARA-LA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 494 DRP-ILILDEATSSVdaiTEKEIQTNMRAILT----GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:cd03219 160 TDPkLLLLDEPAAGL---NPEETEELAELIRElrerGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
347-562 |
2.63e-26 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 107.77 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPqgddvYIF 426
Cdd:TIGR02315 11 YPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRIG-----MIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 427 DE-------SIRYNIAFPRPEA-----------TEEEVEKAahLAGIHEFviGLKDGYDTQVGErgirLSGGQKQRVALA 488
Cdd:TIGR02315 86 QHynlierlTVLENVLHGRLGYkptwrsllgrfSEEDKERA--LSALERV--GLADKAYQRADQ----LSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 489 RAvLADRPILIL-DEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:TIGR02315 158 RA-LAQQPDLILaDEPIASLDPKTSKQVMDYLKRINKedGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
353-562 |
2.64e-26 |
|
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: 107.38 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-FSYVPQGDDvyIFDE-SI 430
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRR--IFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNI---AFPRP-----EATEEEV--------EKAAHLAGihefviglkdgydtqvgergiRLSGGQKQRVALARAVLAD 494
Cdd:COG0410 96 EENLllgAYARRdraevRADLERVyelfprlkERRRQRAG---------------------TLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 495 RPILILDEAT-----SSVDAITE--KEIQTnmrailTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:COG0410 155 PKLLLLDEPSlglapLIVEEIFEiiRRLNR------EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
354-563 |
4.26e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.10 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLL---------EQFSYVPQgddvy 424
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqeagmvfQQFYLFPH----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 ifdESIRYNIAF-PRP--EATEEEVEKAAH--LAGihefvIGLKDGYDTQVGErgirLSGGQKQRVALARAvLADRPILI 499
Cdd:PRK09493 92 ---LTALENVMFgPLRvrGASKEEAEKQARelLAK-----VGLAERAHHYPSE----LSGGQQQRVAIARA-LAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 500 L-DEATSSVDAITEKEIQTNMRAILT-GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:PRK09493 159 LfDEPTSALDPELRHEVLKVMQDLAEeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
353-562 |
4.69e-26 |
|
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: 106.65 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQllEQFSYVPQgdDVYIFDE-SIR 431
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQ--HYALFRHmTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 YNIAF-----PRPEATEEEvEKAAHLAGIHEFV--IGLKDGYDTQvgergirLSGGQKQRVALARAvLADRP-ILILDEA 503
Cdd:cd03296 93 DNVAFglrvkPRSERPPEA-EIRAKVHELLKLVqlDWLADRYPAQ-------LSGGQRQRVALARA-LAVEPkVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 504 TSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
354-532 |
4.74e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 105.64 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQGDDVYIF---DESI 430
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPEltvRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNIAFPRPEATEEEVEKAAHLAGIHEFViglkdgyDTQVGergiRLSGGQKQRVALARAVLADRPILILDEATSSVDAI 510
Cdd:COG4133 97 RFWAALYGLRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180
....*....|....*....|..
gi 818754182 511 TEKEIQTNMRAILTGKTAIIIA 532
Cdd:COG4133 166 GVALLAELIAAHLARGGAVLLT 187
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
334-562 |
5.20e-26 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 106.55 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQllEQ 413
Cdd:cd03300 1 IELENVSKFYGGFV-----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDVY----IFDesiryNIAFP-----RPEAT-EEEVEKAAHLAGIHEFviglkdgydtqvGERGIR-LSGGQK 482
Cdd:cd03300 74 VNTVFQNYALFphltVFE-----NIAFGlrlkkLPKAEiKERVAEALDLVQLEGY------------ANRKPSqLSGGQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 483 QRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHE 560
Cdd:cd03300 137 QRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
..
gi 818754182 561 EL 562
Cdd:cd03300 217 EI 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
353-558 |
8.83e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.73 E-value: 8.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE---------QFSYVPQGDDV 423
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrqigmifQHFNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 yiFDesiryNIAFPRPEATEEEVEKAAHLAGIHEFViGL---KDGYDTQvgergirLSGGQKQRVALARAvLADRP-ILI 499
Cdd:PRK11153 100 --FD-----NVALPLELAGTPKAEIKARVTELLELV-GLsdkADRYPAQ-------LSGGQKQRVAIARA-LASNPkVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 500 LDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGT 558
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
354-562 |
1.52e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.60 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNG--------SQLLEQFSYVPQGDDVYI 425
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 FDESIRYNIAFP---RPEATEEEVEKAAHL---AGIHefviGLKDGYDTqvgergiRLSGGQKQRVALARAvLADRPILI 499
Cdd:PRK11264 99 HRTVLENIIEGPvivKGEPKEEATARARELlakVGLA----GKETSYPR-------RLSGGQQQRVAIARA-LAMRPEVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 500 L-DEATSSVDAITEKEIQTNMRAILTGK-TAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK11264 167 LfDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
353-557 |
2.40e-25 |
|
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: 103.99 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQGDDVYifDE-SIR 431
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLY--DRlTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 YNIAF------PRPEATEEEVEKAAHLAGIHEFViglkdgyDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATS 505
Cdd:cd03266 97 ENLEYfaglygLKGDELTARLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818754182 506 SVDAITEKEIQTNMRAILT-GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03266 166 GLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
354-552 |
3.12e-25 |
|
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: 103.53 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIE---PGQIVALVGQSGAGKTTIRKVITRLApcqmgTITVAGIDIND--WNGSQLleQFSYVPQGDDV-YIFD 427
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLE-----KPDGGTIVLNGtvLFDSRK--KINLPPQQRKIgLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 428 E-------SIRYNIAF--PRPEATEEEVEKAAHLAgihefVIGLkdgydTQVGERGI-RLSGGQKQRVALARAVLADRPI 497
Cdd:cd03297 83 QyalfphlNVRENLAFglKRKRNREDRISVDELLD-----LLGL-----DHLLNRYPaQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 498 LILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
353-554 |
5.64e-25 |
|
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: 101.35 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINdwngsqlleqfsyvpqgddvyifdesiry 432
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 niaFPRPeateeeveKAAHLAGIhEFViglkdgydTQvgergirLSGGQKQRVALARAVLADRPILILDEATSsvdAITE 512
Cdd:cd03216 66 ---FASP--------RDARRAGI-AMV--------YQ-------LSVGERQMVEIARALARNARLLILDEPTA---ALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 818754182 513 KEIQT------NMRAilTGKTAIIIAHRLSTIWGLADKIVVMDQGKKV 554
Cdd:cd03216 116 AEVERlfkvirRLRA--QGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
335-562 |
6.47e-25 |
|
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: 103.37 E-value: 6.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 335 SLSDVCFAYEGdySEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ- 413
Cdd:TIGR03410 2 EVSNLNVYYGQ--SHI---LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDvyIFDE-SIRYNI---AFPRPEATEEEVEKAAHLagiheFVIgLKDgydtQVGERGIRLSGGQKQRVALAR 489
Cdd:TIGR03410 77 IAYVPQGRE--IFPRlTVEENLltgLAALPRRSRKIPDEIYEL-----FPV-LKE----MLGRRGGDLSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 490 AvLADRP-ILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:TIGR03410 145 A-LVTRPkLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
353-557 |
9.69e-25 |
|
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: 102.30 E-value: 9.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDIND----WN--GSqLLEQFSYVPQ---GDDV 423
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKnieaLRriGA-LIEAPGFYPNltaRENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 YIFDESIRyniafpRPEATEEEVEKaahlagihefVIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEA 503
Cdd:cd03268 94 RLLARLLG------IRKKRIDEVLD----------VVGLKDSAKKKVKG----FSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 504 TSSVDAITEKEiqtnMRAIL-----TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03268 154 TNGLDPDGIKE----LRELIlslrdQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
336-566 |
1.58e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.14 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 336 LSDVCFAYEGDyseadgALHdFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQ----LL 411
Cdd:COG3840 4 LDDLTYRYGDF------PLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvsML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 412 EQ----FSYVpqgddvyifdeSIRYNIAF---PRPEATEEEVEKAAHLA---GIHefviGLKDGYDTQvgergirLSGGQ 481
Cdd:COG3840 77 FQennlFPHL-----------TVAQNIGLglrPGLKLTAEQRAQVEQALervGLA----GLLDRLPGQ-------LSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 482 KQRVALARAVLADRPILILDEATSSVDAITEKEiqtnMRAIL------TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVE 555
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQE----MLDLVdelcreRGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
250
....*....|.
gi 818754182 556 EGTHEELIKSH 566
Cdd:COG3840 211 DGPTAALLDGE 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
354-563 |
1.78e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.89 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgddvyifdesiRYN 433
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQ-----------HSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 434 IAFP----------------RPEATEEEVEKAAHLAGIHEFviglkdgydtqvGERGIR-LSGGQKQRVALARaVLA--- 493
Cdd:COG4559 86 LAFPftveevvalgraphgsSAAQDRQIVREALALVGLAHL------------AGRSYQtLSGGEQQRVQLAR-VLAqlw 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 494 -----DRPILILDEATSSVDaitekeI---QTNMRAI--LT--GKTAIIIAHRLStiwgL----ADKIVVMDQGKKVEEG 557
Cdd:COG4559 153 epvdgGPRWLFLDEPTSALD------LahqHAVLRLArqLArrGGGVVAVLHDLN----LaaqyADRILLLHQGRLVAQG 222
|
....*.
gi 818754182 558 THEELI 563
Cdd:COG4559 223 TPEEVL 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-562 |
1.94e-24 |
|
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: 107.08 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQmGTITVAGIDINDWNGSQLLE---QFSYVPQgdDVY----- 424
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPlrrRMQVVFQ--DPFgslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 ------IFDESIRYNiafpRPEATEEEVEKAA-------HLAG------IHEFviglkdgydtqvgergirlSGGQKQRV 485
Cdd:COG4172 378 rmtvgqIIAEGLRVH----GPGLSAAERRARVaealeevGLDPaarhryPHEF-------------------SGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 486 ALARAvLADRP-ILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:COG4172 435 AIARA-LILEPkLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
338-533 |
2.30e-24 |
|
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: 101.33 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 338 DVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQ--LLEQFS 415
Cdd:cd03292 5 NVTKTYPNGTA----ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 416 YVPQGDDVYIFDESIRYNIAFP------RPEATEEEVEKAAHLagihefvIGLKDGYDTQVGErgirLSGGQKQRVALAR 489
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAlevtgvPPREIRKRVPAALEL-------VGLSHKHRALPAE----LSGGEQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 818754182 490 AVLADRPILILDEATSSVDAITEKEIQTNMRAI-LTGKTAIIIAH 533
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
353-552 |
3.57e-24 |
|
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: 100.68 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDIND--WNGSQLLEQFSYVPQgddvyifdesi 430
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQ----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNIaFPRPEATE--------------EEVEKAA--HLAgihefVIGLKDgydtQVGERGIRLSGGQKQRVALARAVLAD 494
Cdd:cd03262 84 QFNL-FPHLTVLEnitlapikvkgmskAEAEERAleLLE-----KVGLAD----KADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 495 RPILILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAeEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
354-561 |
3.99e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVIT-RLAPCQmGTITVAGIDINDWNGSQL------LEQFSyvpqgddvyif 426
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDS-GEVRLNGRPLADWSPAELarrravLPQHS----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 427 desiryNIAFP----------------RPEATEEEVEKAAHLAGIHEFviglkdgydtqvGERGIR-LSGGQKQRVALAR 489
Cdd:PRK13548 86 ------SLSFPftveevvamgraphglSRAEDDALVAAALAQVDLAHL------------AGRDYPqLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 490 aVLA-------DRPILILDEATSSVDaitekeI---QTNMR-----AILTGKTAIIIAHRLstiwGLA----DKIVVMDQ 550
Cdd:PRK13548 148 -VLAqlwepdgPPRWLLLDEPTSALD------LahqHHVLRlarqlAHERGLAVIVVLHDL----NLAaryaDRIVLLHQ 216
|
250
....*....|.
gi 818754182 551 GKKVEEGTHEE 561
Cdd:PRK13548 217 GRLVADGTPAE 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
354-556 |
4.73e-24 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 101.81 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGS---------QLLEQFSYV---PQGD 421
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafrrdvQLVFQDSPSavnPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 422 DVYIFDESIRYniaFPRPEATEEEvEKAAHLAGIHEFVIGLKDGYDTQvgergirLSGGQKQRVALARAVLADRPILILD 501
Cdd:TIGR02769 107 VRQIIGEPLRH---LTSLDESEQK-ARIAELLDMVGLRSEDADKLPRQ-------LSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 502 EATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEE 556
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
353-557 |
6.30e-24 |
|
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: 99.96 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGqIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQGDDVYifdESIRy 432
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVY---PNFT- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 niafprpeaTEEEVEKAAHLAGIH------------EFViGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILIL 500
Cdd:cd03264 89 ---------VREFLDYIAWLKGIPskevkarvdevlELV-NLGDRAKKKIGS----LSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 501 DEATSSVDaITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03264 155 DEPTAGLD-PEERIRFRNLLSELgEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
356-576 |
9.88e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 106.65 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRL-APCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDESIRYNI 434
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLyDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQ--DPLLFSNSIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 435 AFP-----RPEATEEEVEK---------------AAHLAG-------------------------------------IHE 457
Cdd:PTZ00265 481 KYSlyslkDLEALSNYYNEdgndsqenknkrnscRAKCAGdlndmsnttdsneliemrknyqtikdsevvdvskkvlIHD 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 458 FVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAiLTG---KTAIIIAHR 534
Cdd:PTZ00265 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN-LKGnenRITIIIAHR 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 535 LSTIwGLADKIVVMDQGKK-----------------------------------------------VEEGTHEELIKS-H 566
Cdd:PTZ00265 640 LSTI-RYANTIFVLSNRERgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyiIEQGTHDALMKNkN 718
|
330
....*....|
gi 818754182 567 GIYAQMVSLQ 576
Cdd:PTZ00265 719 GIYYTMINNQ 728
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
338-564 |
1.07e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.93 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 338 DVCFAYE-GDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDIND----WNgsqLLE 412
Cdd:PRK13633 9 NVSYKYEsNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeenlWD---IRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 QFSYVPQGDDVYIFDESIRYNIAF-PR-----PEATEEEVEKAAHLAGIHEFviglKDgYDTQVgergirLSGGQKQRVA 486
Cdd:PRK13633 86 KAGMVFQNPDNQIVATIVEEDVAFgPEnlgipPEEIRERVDESLKKVGMYEY----RR-HAPHL------LSGGQKQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 487 LArAVLADRP-ILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELI 563
Cdd:PRK13633 155 IA-GILAMRPeCIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
.
gi 818754182 564 K 564
Cdd:PRK13633 233 K 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
354-574 |
1.41e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.02 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVItrlapcqMGTITVAgidindwNGSQLLEQ-FSYVPQgdDVYIFDESIRY 432
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSL-------LSQFEIS-------EGRVWAERsIAYVPQ--QAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAFPRPEaTEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDA-IT 511
Cdd:PTZ00243 740 NILFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVG 818
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 512 EKEIQTNMRAILTGKTAIIIAHRLStIWGLADKIVVMDQGKKVEEGTHEELIKShGIYAQMVS 574
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVH-VVPRADYVVALGDGRVEFSGSSADFMRT-SLYATLAA 879
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
353-570 |
2.11e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDIND----------------WNGSQLLEQFSY 416
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelitnpyskkiKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 417 VPQGDDVYIFDESIRYNIAFPrPEATEEEVEKAAHLAGIHEFVIGLKDGYDtqvgERG-IRLSGGQKQRVALArAVLADR 495
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSYL----ERSpFGLSGGQKRRVAIA-GILAIQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 496 P-ILILDEATSSVDAITEKEIqtnMRAILT----GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSHGIYA 570
Cdd:PRK13631 195 PeILIFDEPTAGLDPKGEHEM---MQLILDakanNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
127-535 |
2.43e-23 |
|
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: 105.38 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 127 DIIDVMSWEFVPTVVQTVISLIPLFIISPWVALVAIITFVLFAWLTLKGNREKQPFRSKRQDYYEEEWNKSIASVQSVET 206
Cdd:TIGR01271 997 DMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWT 1076
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 207 NLMFGQQPRLlndQAVIHngiisEALKEHRLGIFKYN---RW---RIRVLTI-----------------ARRIILVVWIL 263
Cdd:TIGR01271 1077 IRAFGRQSYF---ETLFH-----KALNLHTANWFLYLstlRWfqmRIDIIFVfffiavtfiaigtnqdgEGEVGIILTLA 1148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 264 QLIQGSLTIAglIFVSVLVERLFNSCWRFARLLDRAAENSE-----GAERLANLLLepepIETGSIQSVPAGPIGVSLSD 338
Cdd:TIGR01271 1149 MNILSTLQWA--VNSSIDVDGLMRSVSRVFKFIDLPQEEPRpsgggGKYQLSTVLV----IENPHAQKCWPSGGQMDVQG 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 339 VCFAYEgdySEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQmGTITVAGIDINDWNGSQLLEQFSYVP 418
Cdd:TIGR01271 1223 LTAKYT---EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIP 1298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 419 QgdDVYIFDESIRYNIAfPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPIL 498
Cdd:TIGR01271 1299 Q--KVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
410 420 430
....*....|....*....|....*....|....*..
gi 818754182 499 ILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRL 535
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
331-565 |
4.65e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 331 PIGVSLSDVCFayeGDYSEADGAlhdfSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQL 410
Cdd:PRK09536 3 MIDVSDLSVEF---GDTTVLDGV----DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 411 LEQFSYVPQGDDVYiFDESIRYNIAFPRP----------EATEEEVEKAAHLAGIHEFViglkdgyDTQVGErgirLSGG 480
Cdd:PRK09536 76 SRRVASVPQDTSLS-FEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFA-------DRPVTS----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 481 QKQRVALARAVLADRPILILDEATSSVDaiTEKEIQT---NMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLD--INHQVRTlelVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
....*...
gi 818754182 558 THEELIKS 565
Cdd:PRK09536 222 PPADVLTA 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
354-565 |
6.43e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 100.57 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIE---PGQ-IVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwnGSQLL------EQFSYVPQgdDV 423
Cdd:TIGR02142 9 LGDFSLDADftlPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD--SRKGIflppekRRIGYVFQ--EA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 YIFD-----ESIRYNIAFPRPEATEEEVEKAAHLAGIHEFViglkdgydtqvgERGI-RLSGGQKQRVALARAVLADRPI 497
Cdd:TIGR02142 85 RLFPhlsvrGNLRYGMKRARPSERRISFERVIELLGIGHLL------------GRLPgRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 498 LILDEATSSVDAITEKEIQTNMRAiLTGKTAI---IIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLER-LHAEFGIpilYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
354-557 |
8.82e-23 |
|
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: 96.96 E-value: 8.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQ---MGTITVAGIDINDwngSQLLEQFSYVPQGDD------VY 424
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKP---DQFQKCVAYVRQDDIllpgltVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 ifdESIRY--NIAFPRPEATEEEVEKAAhlagihefVIGLKDGYDTQVGERGIR-LSGGQKQRVALARAVLADRPILILD 501
Cdd:cd03234 100 ---ETLTYtaILRLPRKSSDAIRKKRVE--------DVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 502 EATSSVDAITEKE-IQTNMRAILTGKTAIIIAHR-LSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03234 169 EPTSGLDSFTALNlVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
347-574 |
9.91e-23 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 98.39 E-value: 9.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADGA-LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQmGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYI 425
Cdd:cd03289 12 YTEGGNAvLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQ--KVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 FDESIRYNIAfPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATS 505
Cdd:cd03289 89 FSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 506 SVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELIKSHGIYAQMVS 574
Cdd:cd03289 168 HLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
255-534 |
1.02e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.19 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 255 RIILVV-WILQL---IQGSLTIAGLIFVSVLVERLFNSC-W------RFARLldRAaenseGAERLANLL-----LEPEP 318
Cdd:COG4178 277 QLAVIFpILVAApryFAGEITLGGLMQAASAFGQVQGALsWfvdnyqSLAEW--RA-----TVDRLAGFEealeaADALP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 319 IETGSIQSVPAGpiGVSLSDVCFAyegdysEADGA--LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTIT 396
Cdd:COG4178 350 EAASRIETSEDG--ALALEDLTLR------TPDGRplLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 397 V-AGIDIndwngsQLLEQFSYVPQGddvyifdeSIRYNIAFPRPEA--TEEEVEKAAHLAGIHEFVIGLKDGYDtqvgeR 473
Cdd:COG4178 422 RpAGARV------LFLPQRPYLPLG--------TLREALLYPATAEafSDAELREALEAVGLGHLAERLDEEAD-----W 482
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 474 GIRLSGGQKQRVALARAVLAdRP-ILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHR 534
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLH-KPdWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
295-566 |
2.06e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.75 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 295 LLDRAaeNSEGAERLANLLLEPEPIETGS--IQSVPAG--PIGVSLSDVCFAYeGDYSEADGalhdFSLEIEPGQIVALV 370
Cdd:PRK13536 1 LLTRA--VAEEAPRRLELSPIERKHQGISeaKASIPGSmsTVAIDLAGVSKSY-GDKAVVNG----LSFTVASGECFGLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 371 GQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQGDDVYIfDESIRYN-IAFPRP-EATEEEVEk 448
Cdd:PRK13536 74 GPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLDL-EFTVRENlLVFGRYfGMSTREIE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 449 aAHLAGIHEFViGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILT-GKT 527
Cdd:PRK13536 151 -AVIPSLLEFA-RLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKT 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 818754182 528 AIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSH 566
Cdd:PRK13536 225 ILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
354-562 |
2.16e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.00 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQllEQFSYVPQGDDVY----IFDes 429
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFrhmtVFD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 iryNIAF-----PRPEATEEEVEKA-----------AHLAgihefviglkDGYDTQvgergirLSGGQKQRVALARAVLA 493
Cdd:PRK10851 94 ---NIAFgltvlPRRERPNAAAIKAkvtqllemvqlAHLA----------DRYPAQ-------LSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
353-562 |
5.23e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 97.11 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE---QFSYVPQgdDVY----- 424
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQ--DPYaslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 ------IFDESIRYNIAFPRPEAtEEEVEKAAHLAGI---------HEFviglkdgydtqvgergirlSGGQKQRVALAR 489
Cdd:COG4608 111 rmtvgdIIAEPLRIHGLASKAER-RERVAELLELVGLrpehadrypHEF-------------------SGGQRQRIGIAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 490 AvLADRP-ILILDEATSSVDaiteKEIQT---NMRAILT---GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:COG4608 171 A-LALNPkLIVCDEPVSALD----VSIQAqvlNLLEDLQdelGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
334-565 |
6.89e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.59 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDyseADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:PRK13648 8 IVFKNVSFQYQSD---ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDVYIFDESIRYNIAF-------PRpEATEEEVEKAAHLAGIHEfviglKDGYDTQvgergiRLSGGQKQRVA 486
Cdd:PRK13648 85 IGIVFQNPDNQFVGSIVKYDVAFglenhavPY-DEMHRRVSEALKQVDMLE-----RADYEPN------ALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 487 LArAVLADRP-ILILDEATSSVDAITEKEIQTNMRAILTGK--TAIIIAHRLSTIWGlADKIVVMDQGKKVEEGTHEELI 563
Cdd:PRK13648 153 IA-GVLALNPsVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
..
gi 818754182 564 KS 565
Cdd:PRK13648 231 DH 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
332-558 |
7.73e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.58 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 332 IGVSLSDVCFAYEGDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINdwNGS--- 408
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT--STSknk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 409 ---QLLEQFSYVPQGDDVYIFDESIRYNIAFPrPE---ATEEEVEKAA----HLAGIHEfviglkDGYDTQVGErgirLS 478
Cdd:PRK13649 79 dikQIRKKVGLVFQFPESQLFEETVLKDVAFG-PQnfgVSQEEAEALAreklALVGISE------SLFEKNPFE----LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 479 GGQKQRVALArAVLADRP-ILILDEATSSVDAITEKEIQTNMRAI-LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEE 556
Cdd:PRK13649 148 GGQMRRVAIA-GILAMEPkILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
..
gi 818754182 557 GT 558
Cdd:PRK13649 227 GK 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
353-564 |
8.01e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-FSYVPQgdDVYIFDE-SI 430
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQ--ELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNIAFPRP---------EATEEEVEKAAHLAGIHEFViglkdgyDTQVGErgirLSGGQKQRVALARAVLADRPILILD 501
Cdd:COG1129 97 AENIFLGREprrgglidwRAMRRRARELLARLGLDIDP-------DTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 502 EATSSvdaITEKEIQTNMRAILT----GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG-----THEELIK 564
Cdd:COG1129 166 EPTAS---LTEREVERLFRIIRRlkaqGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
354-551 |
1.02e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 94.07 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwngsqlleqfsyvPQGDDVYIFDE----- 428
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-------------PGPDRMVVFQNysllp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 --SIRYNIAFP----RPEATEEEVEKAA--HLAgihefVIGLKDGYDTQVGErgirLSGGQKQRVALARAvLADRP-ILI 499
Cdd:TIGR01184 68 wlTVRENIALAvdrvLPDLSKSERRAIVeeHIA-----LVGLTEAADKRPGQ----LSGGMKQRVAIARA-LSIRPkVLL 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 818754182 500 LDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVMDQG 551
Cdd:TIGR01184 138 LDEPFGALDALTRGNLQEELMQIWeeHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
354-564 |
2.24e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.20 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM---GTITVAGIDINDWngsQLLEQFSYVPQgDDVYIFDESI 430
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAK---EMRAISAYVQQ-DDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNIAF------PRPEATEEEVEKAAHLagIHEfvIGLKDGYDTQVGERGIR--LSGGQKQRVALARAVLADRPILILDE 502
Cdd:TIGR00955 117 REHLMFqahlrmPRRVTKKEKRERVDEV--LQA--LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 503 ATSSVDAITEKE-IQTNMRAILTGKTAIIIAHR-LSTIWGLADKIVVMDQGKKVEEGTHEELIK 564
Cdd:TIGR00955 193 PTSGLDSFMAYSvVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
325-562 |
3.48e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.18 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 325 QSVPAGPIGVSLSDVCFAYeGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITR---LAP-CQM-GTITVAG 399
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY-GDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPgARVeGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 400 IDINDwngsqlleqfsyvPQGDDVYI-------------FDESIRYNIAF-PR------PEATEEEVEKAAHLAGIHEFV 459
Cdd:COG1117 78 EDIYD-------------PDVDVVELrrrvgmvfqkpnpFPKSIYDNVAYgLRlhgiksKSELDEIVEESLRKAALWDEV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 460 iglKDgydtQVGERGIRLSGGQKQRVALARAvLADRP-ILILDEATSSVDAITEKEIQTNMRAiLTGKTAIII------- 531
Cdd:COG1117 145 ---KD----RLKKSALGLSGGQQQRLCIARA-LAVEPeVLLMDEPTSALDPISTAKIEELILE-LKKDYTIVIvthnmqq 215
|
250 260 270
....*....|....*....|....*....|.
gi 818754182 532 AHRLStiwglaDKIVVMDQGKKVEEGTHEEL 562
Cdd:COG1117 216 AARVS------DYTAFFYLGELVEFGPTEQI 240
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
356-565 |
6.04e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.72 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQGDDVYIfDESIRYNIA 435
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQFDNLDP-DFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 436 -----FPRPEATEEEVekaahLAGIHEFViGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSSVDAI 510
Cdd:PRK13537 103 vfgryFGLSAAAARAL-----VPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 511 TEKEIQTNMRAILT-GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:PRK13537 173 ARHLMWERLRSLLArGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
354-564 |
8.64e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.97 E-value: 8.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQF----SYVPQGDDVYIFDES 429
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLrkkvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 IRYNIAF-PRP-EATEEEVEKAAhLAGIHefviglKDGYDTQVGERG-IRLSGGQKQRVALArAVLADRP-ILILDEATS 505
Cdd:PRK13641 103 VLKDVEFgPKNfGFSEDEAKEKA-LKWLK------KVGLSEDLISKSpFELSGGQMRRVAIA-GVMAYEPeILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 506 SVDAITEKEiqtnMRAIL-----TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIK 564
Cdd:PRK13641 175 GLDPEGRKE----MMQLFkdyqkAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
354-565 |
2.87e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.53 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQGDDVyifdeSIRYN 433
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI-----NSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 434 IA-------FP----RP-EATEEEVEKAAHLAGIHEfvigLKDGY-DTqvgergirLSGGQKQRVALArAVLA-DRPILI 499
Cdd:COG4604 92 VRelvafgrFPyskgRLtAEDREIIDEAIAYLDLED----LADRYlDE--------LSGGQRQRAFIA-MVLAqDTDYVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 500 LDEATSSVDAITEKEIqtnMRAI--LT---GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:COG4604 159 LDEPLNNLDMKHSVQM---MKLLrrLAdelGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITP 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
335-548 |
3.34e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.31 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 335 SLSDVCFAYEGDySEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwngsqlleqf 414
Cdd:COG4525 5 TVRHVSVRYPGG-GQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 415 syvPQGDDVYIFDE-------SIRYNIAFPRPEATeeeVEKAAHLAGIHEFV--IGLKDgydtqVGERGI-RLSGGQKQR 484
Cdd:COG4525 74 ---PGADRGVVFQKdallpwlNVLDNVAFGLRLRG---VPKAERRARAEELLalVGLAD-----FARRRIwQLSGGMRQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 485 VALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVM 548
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
350-552 |
3.42e-20 |
|
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: 88.26 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 350 ADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-FSYVP-----QGddv 423
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrkrEG--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 yIF-DESIRYNIAFPRpeateeevekaahlagihefviglkdgydtqvgergiRLSGGQKQRVALARAVLADRPILILDE 502
Cdd:cd03215 89 -LVlDLSVAENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 818754182 503 ATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
306-562 |
4.01e-20 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 94.09 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 306 AERLANLLLEPEPIETGSIQSVPAGPIG----VSLSDVCFAYEGDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIR 381
Cdd:COG4615 296 LRKIEELELALAAAEPAAADAAAPPAPAdfqtLELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 382 KVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYIFDEsirynIAFPRPEATEEEVEKAAHLAGIHEFViG 461
Cdd:COG4615 376 KLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFS--DFHLFDR-----LLGLDGEADPARARELLERLELDHKV-S 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 462 LKDGYDTQvgergIRLSGGQKQRVALARAVLADRPILILDEATSSVD----AITEKEIQTNMRAIltGKTAIIIAH--RL 535
Cdd:COG4615 448 VEDGRFST-----TDLSQGQRKRLALLVALLEDRPILVFDEWAADQDpefrRVFYTELLPELKAR--GKTVIAISHddRY 520
|
250 260
....*....|....*....|....*..
gi 818754182 536 stiWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:COG4615 521 ---FDLADRVLKMDYGKLVELTGPAAL 544
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
354-562 |
4.47e-20 |
|
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: 90.69 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVIT-RLAPCQmGTITVAGidindwngsqlleQFSYVPQGDdvYIFDESIRY 432
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSE-GKIKHSG-------------RISFSSQFS--WIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAF--PRPEATEEEVEKAAHLagiHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAI 510
Cdd:cd03291 117 NIIFgvSYDEYRYKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818754182 511 TEKEI-QTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:cd03291 194 TEKEIfESCVCKLMANKTRILVTSKMEHL-KKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
353-562 |
7.82e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 88.20 E-value: 7.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQG----------DD 422
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDlsvddeltgwEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 423 VYIFDESirYNIafPRPEATE--EEVEKAahlagihefvIGLKDGYDTQVGergiRLSGGQKQRVALARAVLADRPILIL 500
Cdd:cd03265 94 LYIHARL--YGV--PGAERREriDELLDF----------VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 501 DEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
354-558 |
1.72e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.59 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLlEQFsyvpQGDDVYIFDES---- 429
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQR-KAF----RRDIQMVFQDSisav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 -----IRYNIAFP-RPEATEEEVEKAAHLAGIHEFViGLKDGYDTQvgeRGIRLSGGQKQRVALARAvLADRP-ILILDE 502
Cdd:PRK10419 103 nprktVREIIREPlRHLLSLDKAERLARASEMLRAV-DLDDSVLDK---RPPQLSGGQLQRVCLARA-LAVEPkLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 503 ATSSVDAItekeIQTNMRAIL------TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGT 558
Cdd:PRK10419 178 AVSNLDLV----LQAGVIRLLkklqqqFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
338-562 |
3.30e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 338 DVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYV 417
Cdd:PRK13652 8 DLCYSYSGSKE----ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 418 PQGDDVYIFDESIRYNIAFP------RPEATEEEVEKAAHLAGIHEfviglkdgYDTQVGERgirLSGGQKQRVALArAV 491
Cdd:PRK13652 84 FQNPDDQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEE--------LRDRVPHH---LSGGEKKRVAIA-GV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 492 LADRP-ILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK13652 152 IAMEPqVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-562 |
3.64e-19 |
|
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: 90.90 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAP----CQMGTITVAGIDINDWNGSQLLEQfsyvpQGDDV-YIF- 426
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERELRRI-----RGNRIaMIFq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 427 ----------------DESIRYNIAFPRPEATEEEVEkAAHLAGIHEFVIGLKDgYDTQvgergirLSGGQKQRVALARA 490
Cdd:COG4172 100 epmtslnplhtigkqiAEVLRLHRGLSGAAARARALE-LLERVGIPDPERRLDA-YPHQ-------LSGGQRQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 491 vLADRP-ILILDEATSSVDAITEKEI---------QTNMrAILtgktaiIIAHRLSTIWGLADKIVVMDQGKKVEEGTHE 560
Cdd:COG4172 171 -LANEPdLLIADEPTTALDVTVQAQIldllkdlqrELGM-ALL------LITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242
|
..
gi 818754182 561 EL 562
Cdd:COG4172 243 EL 244
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-567 |
4.00e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 88.24 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNgsqlLEQFSYVPqgddvyifDE---- 428
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLP--------EErgly 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 ---SIRYNIAF-------PRPEATEeeveKAAHLagIHEFviGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPIL 498
Cdd:COG4152 84 pkmKVGEQLVYlarlkglSKAEAKR----RADEW--LERL--GLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 499 ILDEATSSVDAI-TE--KEIQTNMRAilTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSHG 567
Cdd:COG4152 152 ILDEPFSGLDPVnVEllKDVIRELAA--KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
319-561 |
4.09e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.24 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 319 IETGSIQSVPAGPIgVSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVA 398
Cdd:PRK09452 1 SKKLNKQPSSLSPL-VELRGISKSFDGKE-----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 399 GIDINDWNGSQ-----LLEQFSYVPQgddVYIFDesiryNIAF-------PRPEaTEEEVEKAAHLAGIHEFviglkdgy 466
Cdd:PRK09452 75 GQDITHVPAENrhvntVFQSYALFPH---MTVFE-----NVAFglrmqktPAAE-ITPRVMEALRMVQLEEF-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 467 dtqvGERGIR-LSGGQKQRVALARAVLaDRP-ILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLA 542
Cdd:PRK09452 138 ----AQRKPHqLSGGQQQRVAIARAVV-NKPkVLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHDQEEALTMS 212
|
250
....*....|....*....
gi 818754182 543 DKIVVMDQGKKVEEGTHEE 561
Cdd:PRK09452 213 DRIVVMRDGRIEQDGTPRE 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
334-562 |
5.44e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.48 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEADgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ 413
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYT--LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 414 FSYVPQGDDVYIFDESIRYNIAF-------PRPEaTEEEVEKAAHLAGIHEFviglKDgydtqvgERGIRLSGGQKQRVA 486
Cdd:PRK13650 83 IGMVFQNPDNQFVGATVEDDVAFglenkgiPHEE-MKERVNEALELVGMQDF----KE-------REPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 487 LARAVlADRP-ILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK13650 151 IAGAV-AMRPkIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
351-562 |
5.73e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.12 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 351 DG--ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQ-----LLEQFSYVPQgddv 423
Cdd:PRK11607 30 DGqhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpinmMFQSYALFPH---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 yifdESIRYNIAF-------PRPEATEEeVEKAAHLAGIHEFViglkdgydtqvGERGIRLSGGQKQRVALARAvLADRP 496
Cdd:PRK11607 106 ----MTVEQNIAFglkqdklPKAEIASR-VNEMLGLVHMQEFA-----------KRKPHQLSGGQRQRVALARS-LAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 497 -ILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK11607 169 kLLLLDEPMGALDKKLRDRMQLEVVDILerVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
354-565 |
7.20e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 85.67 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDW---NGSQLleQFSYVPQgdDVYIF-DES 429
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmhKRARL--GIGYLPQ--EASIFrKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 IRYNI---AFPRPEATEEEVEKAAHLagIHEFVIG-LKDgydtqvgERGIRLSGGQKQRVALARAVLADRPILILDEATS 505
Cdd:cd03218 92 VEENIlavLEIRGLSKKEREEKLEEL--LEEFHIThLRK-------SKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 506 SVDAITEKEIQtNMRAILTGK-TAIIIA-HRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:cd03218 163 GVDPIAVQDIQ-KIIKILKDRgIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
334-565 |
7.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.14 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDIN----DWNGSQ 409
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 410 LLEQFSYVPQGDDVYIFDESIRYNIAFPrPEATEEEVEKAAHLAgiHEFVIGLkdGYDTQVGERG-IRLSGGQKQRVALA 488
Cdd:PRK13646 83 VRKRIGMVFQFPESQLFEDTVEREIIFG-PKNFKMNLDEVKNYA--HRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 489 RAVLADRPILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
350-560 |
8.36e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.84 E-value: 8.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 350 ADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAG------IDINDWNGSQLLEQFSYVPQgddv 423
Cdd:PRK11124 14 AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQ---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 yifdesiRYNIaFPRPEATEEEVEKAAHLAGIHEfviglkdgydTQVGERGIR-----------------LSGGQKQRVA 486
Cdd:PRK11124 90 -------QYNL-WPHLTVQQNLIEAPCRVLGLSK----------DQALARAEKllerlrlkpyadrfplhLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 487 LARAVLADRPILILDEATSSVDAitekEIQTNMRAIL-----TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHE 560
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDP----EITAQIVSIIrelaeTGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
353-565 |
8.68e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 8.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE-----------QFSYVPQgd 421
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkkiamvfqSFALMPH-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 422 dVYIFDES-IRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDgydtqvgergiRLSGGQKQRVALARAVLADRPILIL 500
Cdd:PRK10070 121 -MTVLDNTaFGMELAGINAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 501 DEATSSVDAITEKEIQTNMRAILTG--KTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
350-562 |
1.03e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 350 ADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAG--IDINdwNGSQLLEQ-FSYVP-----QGd 421
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIR--SPRDAIRAgIAYVPedrkgEG- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 422 dvyIF-DESIRYNIAFPRPEA--------TEEEVEKAAHLagIHEFviGLK-DGYDTQVGErgirLSGGQKQRVALARAV 491
Cdd:COG1129 341 ---LVlDLSIRENITLASLDRlsrgglldRRRERALAEEY--IKRL--RIKtPSPEQPVGN----LSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 492 LADRPILILDEATSSVDAITEKEIQTNMRAiLT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRE-LAaeGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
353-557 |
1.25e-18 |
|
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: 85.46 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFSYVPQGDDVYIFD----E 428
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVFGQKTQLWWDlpviD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRYNIAFPR--PEATEEEVEKAAHLAGIHEFViglkdgyDTQVgeRgiRLSGGQKQRVALARAVLADRPILILDEATSS 506
Cdd:cd03267 115 SFYLLAAIYDlpPARFKKRLDELSELLDLEELL-------DTPV--R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818754182 507 VDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03267 184 LDVVAQENIRNFLKEYnrERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
334-568 |
1.26e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEgDYSEAdgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITR-LAPCQM--GTITVAGIDINDWNGSQL 410
Cdd:PRK13640 6 VEFKHVSFTYP-DSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNpnSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 411 LEQFSYVPQGDDVYIFDESIRYNIAF-------PRPEaTEEEVEKAAHLAGIHEFViglkdgyDTQVGErgirLSGGQKQ 483
Cdd:PRK13640 83 REKVGIVFQNPDNQFVGATVGDDVAFglenravPRPE-MIKIVRDVLADVGMLDYI-------DSEPAN----LSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 484 RVALArAVLADRP-ILILDEATSSVDAITEKEIQTNMRAILTGK--TAIIIAHRLSTIwGLADKIVVMDQGKKVEEGT-- 558
Cdd:PRK13640 151 RVAIA-GILAVEPkIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSpv 228
|
250
....*....|....
gi 818754182 559 ----HEELIKSHGI 568
Cdd:PRK13640 229 eifsKVEMLKEIGL 242
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
347-562 |
1.58e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQGDDVYIF 426
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 427 DESIRYNIAF-P-----RPEATEEEVEKAAHLAGIHEFviGLKDGYdtqvgergiRLSGGQKQRVALArAVLADRP-ILI 499
Cdd:PRK13647 94 SSTVWDDVAFgPvnmglDKDEVERRVEEALKAVRMWDF--RDKPPY---------HLSYGQKKRVAIA-GVLAMDPdVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 500 LDEATSSVDAITEKEIqtnmRAIL-----TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK13647 162 LDEPMAYLDPRGQETL----MEILdrlhnQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
333-560 |
1.82e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.70 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 333 GVSLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINdwngsQLLE 412
Cdd:PRK15056 6 GIVVNDVTVTWRNGHT----ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 Q--FSYVPQGDDV----YIFDESI----RYNIA--FPRPEATEEEVEKAAhLAGIhefviGLKDGYDTQVGErgirLSGG 480
Cdd:PRK15056 77 KnlVAYVPQSEEVdwsfPVLVEDVvmmgRYGHMgwLRRAKKRDRQIVTAA-LARV-----DMVEFRHRQIGE----LSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 481 QKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADkIVVMDQGKKVEEGTH 559
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPT 225
|
.
gi 818754182 560 E 560
Cdd:PRK15056 226 E 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
334-564 |
1.93e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLL-- 411
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIkp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 412 --EQFSYVPQGDDVYIFDESIRYNIAFPrPE---ATEEEVEKAAhlAGIHEFViglkdGYDTQVGERG-IRLSGGQKQRV 485
Cdd:PRK13643 82 vrKKVGVVFQFPESQLFEETVLKDVAFG-PQnfgIPKEKAEKIA--AEKLEMV-----GLADEFWEKSpFELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 486 ALArAVLADRP-ILILDEATSSVDAITEKEIQTNMRAI-LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:PRK13643 154 AIA-GILAMEPeVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
.
gi 818754182 564 K 564
Cdd:PRK13643 233 Q 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
353-551 |
2.50e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.75 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwngsqlleqfsyvPQGDDVYIFDE---- 428
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-------------PGAERGVVFQNegll 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 ---SIRYNIAFPRPEATeeeVEKAAHLAGIHEFV--IGLkDGYdtqvGERGI-RLSGGQKQRVALARAVLADRPILILDE 502
Cdd:PRK11248 83 pwrNVQDNVAFGLQLAG---VEKMQRLEIAHQMLkkVGL-EGA----EKRYIwQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 818754182 503 ATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVVMDQG 551
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWqeTGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
354-562 |
2.50e-18 |
|
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: 89.20 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVIT-RLAPCQmGTITVAGidindwngsqlleQFSYVPQGDdvYIFDESIRY 432
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSE-GKIKHSG-------------RISFSPQTS--WIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAF--PRPEATEEEVEKAAHLagiHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAI 510
Cdd:TIGR01271 506 NIIFglSYDEYRYTSVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818754182 511 TEKEI-QTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:TIGR01271 583 TEKEIfESCLCKLMSNKTRILVTSKLEHL-KKADKILLLHEGVCYFYGTFSEL 634
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
357-566 |
2.91e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.25 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 357 FSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQ----LLEQ----FSYVpqgddvyifde 428
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvsMLFQennlFSHL----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRYNIAF---PRPEATEEEVEKAAHLAGihefVIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATS 505
Cdd:PRK10771 87 TVAQNIGLglnPGLKLNAAQREKLHAIAR----QMGIEDLLARLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 506 SVDAITEKEIQTNMRAILTGK--TAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSH 566
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
353-551 |
3.87e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 83.64 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITV----AGIDINDWNGSQLLE----QFSYVPQgddvy 424
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREILAlrrrTIGYVSQ----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 iFDESIryniafPRpEATEEEVEKAAhlagihefvigLKDGYDTQVGER---------GI--RL--------SGGQKQRV 485
Cdd:COG4778 101 -FLRVI------PR-VSALDVVAEPL-----------LERGVDREEARArarellarlNLpeRLwdlppatfSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 486 ALARAVLADRPILILDEATSSVDAIT-EKEIQTnMRAILTGKTAII-IAHRLSTIWGLADKIVVMDQG 551
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANrAVVVEL-IEEAKARGTAIIgIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
353-562 |
5.78e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITR---LAPcqmgTITVAGIdiNDWNGSQLleqfsYVPQGDDVYI---- 425
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNP----EVTITGS--IVYNGHNI-----YSPRTDTVDLrkei 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 ---------FDESIRYNIAF-------PRPEATEEEVEKAAHLAGIHEFViglKDG-YDTQVGergirLSGGQKQRVALA 488
Cdd:PRK14239 89 gmvfqqpnpFPMSIYENVVYglrlkgiKDKQVLDEAVEKSLKGASIWDEV---KDRlHDSALG-----LSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 489 RaVLADRP-ILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK14239 161 R-VLATSPkIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
356-563 |
6.53e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEiePGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSY-VPQgdDVYIF-DESIRYN 433
Cdd:PRK15439 31 DFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYlVPQ--EPLLFpNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 434 IAF--PRPEATEEEVEKAAHLAGIHefvigLKdgYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSSVDAIT 511
Cdd:PRK15439 107 ILFglPKRQASMQKMKQLLAALGCQ-----LD--LDSSAGS----LEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 512 EKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGK-----KVEEGTHEELI 563
Cdd:PRK15439 176 TERLFSRIRELLaQGVGIVFISHKLPEIRQLADRISVMRDGTialsgKTADLSTDDII 233
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
333-560 |
6.89e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 333 GVSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGI------DINDWN 406
Cdd:COG4161 2 SIQLKNINCFYGSHQ-----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 407 GSQLLEQFSYVPQgddvyifdesiRYN-----------IAFP---RPEATEEEVEKAAHLagihefvigLKDGYDTQVGE 472
Cdd:COG4161 77 IRLLRQKVGMVFQ-----------QYNlwphltvmenlIEAPckvLGLSKEQAREKAMKL---------LARLRLTDKAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 473 R-GIRLSGGQKQRVALARAVLADRPILILDEATSSVD-AITEK--EIQTNMRAilTGKTAIIIAHRLSTIWGLADKIVVM 548
Cdd:COG4161 137 RfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpEITAQvvEIIRELSQ--TGITQVIVTHEVEFARKVASQVVYM 214
|
250
....*....|..
gi 818754182 549 DQGKKVEEGTHE 560
Cdd:COG4161 215 EKGRIIEQGDAS 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
356-556 |
7.37e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.70 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQfsyVPQGDDVyifdesirynia 435
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDA---IGRKGDF------------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 436 fprPEATEeevekAAHLAGIHEFVIGLKDgYDtqvgergiRLSGGQKQRVALARAvLADRP-ILILDEATSSVDAITEKE 514
Cdd:COG2401 113 ---KDAVE-----LLNAVGLSDAVLWLRR-FK--------ELSTGQKFRFRLALL-LAERPkLLVIDEFCSHLDRQTAKR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 818754182 515 IQTNMRAIL--TGKTAIIIAHRLSTIWGLA-DKIVVMDQGKKVEE 556
Cdd:COG2401 175 VARNLQKLArrAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
353-557 |
1.42e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQmGTITVAGIDINDWNGSQLL---EQFSYV---------PQG 420
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLLpvrHRIQVVfqdpnsslnPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 421 DDVYIFDESIRYNIAFPRPEATEEEVEKAAHLAGIhefviglkdgyDTQVGER-GIRLSGGQKQRVALARAVLADRPILI 499
Cdd:PRK15134 380 NVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGL-----------DPETRHRyPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 500 LDEATSSVDAITEKEIQTNMRAIL-TGKTA-IIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQqKHQLAyLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
334-565 |
1.61e-17 |
|
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: 82.44 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITR-LAPCQMGTITVAGIDINDWNGSQLLE 412
Cdd:COG1119 4 LELRNVTVRRGGKT-----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 QFSYV-PQGDDVYIFDESIR-------YNIAFPRPEATEEEVEKAAHLAGIhefvIGLKDGYDTQVGErgirLSGGQKQR 484
Cdd:COG1119 79 RIGLVsPALQLRFPRDETVLdvvlsgfFDSIGLYREPTDEQRERARELLEL----LGLAHLADRPFGT----LSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 485 VALARAVLADRPILILDEATSSVDAITEKEIQTNMRAI-LTGKTAII-IAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVlVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
...
gi 818754182 563 IKS 565
Cdd:COG1119 231 LTS 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
347-563 |
1.71e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADG--ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQF-SYVPQGDDV 423
Cdd:PRK13644 9 YSYPDGtpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLvGIVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 YIFDESIRYNIAF-PR-----PEATEEEVEKAAHLAGIHEFviglkdgydtqvGERGIR-LSGGQKQRVALArAVLADRP 496
Cdd:PRK13644 89 QFVGRTVEEDLAFgPEnlclpPIEIRKRVDRALAEIGLEKY------------RHRSPKtLSGGQGQCVALA-GILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 497 -ILILDEATSSVDAITEKEIQTNMRAI-LTGKTAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:PRK13644 156 eCLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-562 |
2.54e-17 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 83.61 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIE---PGQ-IVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGidiNDWNGSQlleqfsyvpQGDDV------ 423
Cdd:COG4148 11 RGGFTLDVDftlPGRgVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG---EVLQDSA---------RGIFLpphrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 --YIFDES-----------IRYNIAFPRPEATEEEVEKAAHLAGIHEFViglkdgydtqvgERGI-RLSGGQKQRVALAR 489
Cdd:COG4148 79 igYVFQEArlfphlsvrgnLLYGRKRAPRAERRISFDEVVELLGIGHLL------------DRRPaTLSGGERQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 490 AVLADRPILILDEATSSVDAITEKEIQTNMRAiLTGKTAI---IIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:COG4148 147 ALLSSPRLLLMDEPLAALDLARKAEILPYLER-LRDELDIpilYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
353-557 |
2.76e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 80.79 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITvagidindWNGSQL----LEQFSYVPQGDDVYIfDE 428
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL--------FDGKPLdiaaRNRIGYLPEERGLYP-KM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRYNIAF-------PRPEA---TEEEVEKaahlagihefvIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPIL 498
Cdd:cd03269 86 KVIDQLVYlaqlkglKKEEArrrIDEWLER-----------LELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 499 ILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
356-564 |
2.88e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.62 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwngsqlleqfSYVPQGDDVYIFDE------- 428
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH----------RSIQQRDICMVFQSyalfphm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRYNIAF-------PRPEaTEEEVEKAAHLAGIhefvIGLKDGYDTQVgergirlSGGQKQRVALARAVLADRPILILD 501
Cdd:PRK11432 94 SLGENVGYglkmlgvPKEE-RKQRVKEALELVDL----AGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 502 EATSSVDA-----ITEK--EIQTNMrailtGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIK 564
Cdd:PRK11432 162 EPLSNLDAnlrrsMREKirELQQQF-----NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
354-565 |
3.85e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQ------GDDVYIFD 427
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQqlpaaeGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 428 ESIRY--NIAFPRPEATE-EEVEKAAHLAGIHEFVIGLKDGydtqvgergirLSGGQKQRVALARAVLADRPILILDEAT 504
Cdd:PRK10575 107 AIGRYpwHGALGRFGAADrEKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 505 SSVDAITEKE----IQTNMRaiLTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:PRK10575 176 SALDIAHQVDvlalVHRLSQ--ERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
353-562 |
4.71e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.99 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDI----NDWNGSQLLEQFSYVPQGDDVYIFDE 428
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKVGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRYNIAF-------PRPEAtEEEVEKAAHLAGIHEFVIGlKDGYDtqvgergirLSGGQKQRVALArAVLADRP-ILIL 500
Cdd:PRK13634 102 TVEKDICFgpmnfgvSEEDA-KQKAREMIELVGLPEELLA-RSPFE---------LSGGQMRRVAIA-GVLAMEPeVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 501 DEATSSVDAITEKEIQtNMRAIL---TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK13634 170 DEPTAGLDPKGRKEMM-EMFYKLhkeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
353-557 |
4.81e-17 |
|
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: 80.27 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVagidindwngsqlleqfsyvpQGDDVYIFDesirY 432
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV---------------------RGRVSSLLG----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAFpRPEATEEE-------------VEKAAHLAGIHEFViGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILI 499
Cdd:cd03220 92 GGGF-NPELTGREniylngrllglsrKEIDEKIDEIIEFS-ELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 500 LDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLkQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
354-565 |
6.59e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.46 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDW-------NGsqlleqFSYVPQgdDVYIF 426
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkrarLG------IGYLPQ--EASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 427 -DESIRYNI-AF--PRPEATEEEVEKAAHLagIHEFVIG-LKDgydtqvgERGIRLSGGQKQRVALARAvLADRP-ILIL 500
Cdd:COG1137 91 rKLTVEDNIlAVleLRKLSKKEREERLEEL--LEEFGIThLRK-------SKAYSLSGGERRRVEIARA-LATNPkFILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 501 DEATSSVDAITEKEIQtNMRAILTGK-TAIIIA-HRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:COG1137 161 DEPFAGVDPIAVADIQ-KIIRHLKERgIGVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNN 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
326-558 |
6.99e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 80.17 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 326 SVPAGPIgVSLSDVCFAYegdySEADGA---LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDI 402
Cdd:COG4181 2 SSSSAPI-IELRGLTKTV----GTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 403 NDWNGSQLLeQFsyvpQGDDV-YIFD-----------EsiryNIAFPRPEATEEEVEKAAH--LAGIhefviGLK---DG 465
Cdd:COG4181 77 FALDEDARA-RL----RARHVgFVFQsfqllptltalE----NVMLPLELAGRRDARARARalLERV-----GLGhrlDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 466 YDTQvgergirLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAiLT---GKTAIIIAHRLStiwgLA 542
Cdd:COG4181 143 YPAQ-------LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFE-LNrerGTTLVLVTHDPA----LA 210
|
250
....*....|....*....
gi 818754182 543 ---DKIVVMDQGKKVEEGT 558
Cdd:COG4181 211 arcDRVLRLRAGRLVEDTA 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
354-554 |
8.66e-17 |
|
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: 79.23 E-value: 8.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM---GTITVAGIDiNDWNGSQLLEQFSYVPQgDDVYIfdesi 430
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIP-YKEFAEKYPGEIIYVSE-EDVHF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 ryniafprPEAT-EEEVEKAAHLAGiHEFViglkdgydtqvgeRGIrlSGGQKQRVALARAVLADRPILILDEATSSVDA 509
Cdd:cd03233 96 --------PTLTvRETLDFALRCKG-NEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 818754182 510 ITEKEIQTNMRAI--LTGKTAIIIAHRLS-TIWGLADKIVVMDQGKKV 554
Cdd:cd03233 152 STALEILKCIRTMadVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
354-549 |
1.06e-16 |
|
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: 77.58 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTItvagiDINDWNGSQLLEQFSYVPQGddvyifdeSIRYN 433
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----GMPEGEDLLFLPQRPYLPLG--------TLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 434 IAFPRpeateeevekaahlagihefviglkdgydtqvgerGIRLSGGQKQRVALARAVLAdRP-ILILDEATSSVDAITE 512
Cdd:cd03223 84 LIYPW-----------------------------------DDVLSGGEQQRLAFARLLLH-KPkFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*...
gi 818754182 513 KEIqtnMRAILTGKTAII-IAHRlSTIWGLADKIVVMD 549
Cdd:cd03223 128 DRL---YQLLKELGITVIsVGHR-PSLWKFHDRVLDLD 161
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
351-561 |
1.06e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 351 DGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQmGTITVAGIDINDWNGSQLLEQFSYVPQGDD------VY 424
Cdd:COG4138 9 AGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHRAYLSQQQSppfampVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 IFdesirynIAFPRP-EATEEEVEKA-AHLAGihefVIGLKDGYDTQVGergiRLSGGQKQRVALARAVL----ADRP-- 496
Cdd:COG4138 88 QY-------LALHQPaGASSEAVEQLlAQLAE----ALGLEDKLSRPLT----QLSGGEWQRVRLAAVLLqvwpTINPeg 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 497 -ILILDEATSSVD----AITEKEIQTNMRAiltGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEE 561
Cdd:COG4138 153 qLLLLDEPMNSLDvaqqAALDRLLRELCQQ---GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
353-568 |
1.71e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.15 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLL-EQFSYVPQGDDVY---IFDE 428
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMrEAVAIVPEGRRVFsrmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRYNIAFPRPEATEEEVEKaahlagihefVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVD 508
Cdd:PRK11614 100 NLAMGGFFAERDQFQERIKW----------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 509 AITEKEIQTNMRAILT-GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSHGI 568
Cdd:PRK11614 170 PIIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
353-566 |
2.36e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGidindwNGSQLLEqfsyVPQGddvyiFD----- 427
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLE----LGAG-----FHpeltg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 428 -ESIRYNIA---FPRPEaTEEEVEKAAHLAGIHEFViglkdgyDTQVGergiRLSGGQKQRVALARAVLADRPILILDEA 503
Cdd:COG1134 106 rENIYLNGRllgLSRKE-IDEKFDEIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 504 TSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSH 566
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELReSGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
347-562 |
2.71e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADG--ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDInDWNGSQLLE---QFSYVPQGD 421
Cdd:PRK13639 9 YSYPDGteALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEvrkTVGIVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 422 DVYIFDESIRYNIAFPrP---EATEEEVEKAAHLAgihefvigLK----DGYDTQVGERgirLSGGQKQRVALArAVLAD 494
Cdd:PRK13639 88 DDQLFAPTVEEDVAFG-PlnlGLSKEEVEKRVKEA--------LKavgmEGFENKPPHH---LSGGQKKRVAIA-GILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 495 RP-ILILDEATSSVDAITEKEIqtnMRAIL----TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK13639 155 KPeIIVLDEPTSGLDPMGASQI---MKLLYdlnkEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
353-566 |
4.91e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 78.34 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVagidindwNGSQLleQFsyvpqGDDVY-------I 425
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILI--------NGHKL--EY-----GDYKYrckhirmI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 FDESiryNIAF-PR------------------PEATEEEVEKAAHLAGIH----EFVIGLkdgydtqvgergirLSGGQK 482
Cdd:COG4167 93 FQDP---NTSLnPRlnigqileeplrlntdltAEEREERIFATLRLVGLLpehaNFYPHM--------------LSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 483 QRVALARAVLADRPILILDEATSSVDAITEK-------EIQTNMrailtGKTAIIIAHRLSTIWGLADKIVVMDQGKKVE 555
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSqiinlmlELQEKL-----GISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|...
gi 818754182 556 EGTHEE------------LIKSH 566
Cdd:COG4167 231 YGKTAEvfanpqhevtkrLIESH 253
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
354-508 |
6.20e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQGDdvYIFDESIRYN 433
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP--TLFGDTVYDN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 434 IAFPRpEATEEEVEKAAHLAGIHEFviglkdGYDTQVGERGIR-LSGGQKQRVALARAVLADRPILILDEATSSVD 508
Cdd:PRK10247 101 LIFPW-QIRNQQPDPAIFLDDLERF------ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-573 |
6.64e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.98 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITR-LAPCQmGTITVAGIDINDwNGSQLLEQFSYV-----------PQG 420
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPTS-GEVRVLGYVPFK-RRKEFARRIGVVfgqrsqlwwdlPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 421 DDVYIFDEsIrYNIafPRPEAtEEEVEKAAHLAGIHEFViglkdgyDTQVgeRgiRLSGGQKQRVALARAVLADRPILIL 500
Cdd:COG4586 115 DSFRLLKA-I-YRI--PDAEY-KKRLDELVELLDLGELL-------DTPV--R--QLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 501 DEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSHGIYAQMV 573
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIV 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
356-552 |
8.32e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-FSYVPQGDDVY--IFDESIRY 432
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARgLVYLPEDRQSSglYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NI---AFPRPEATEEEVEKAAHLAGIHEfVIGLK-DGYDTQVGergiRLSGGQKQRVALARAVLADRPILILDEATSSVD 508
Cdd:PRK15439 361 NVcalTHNRRGFWIKPARENAVLERYRR-ALNIKfNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 818754182 509 AITEKEIQTNMRAILTGKTAII-IAHRLSTIWGLADKIVVMDQGK 552
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQMADRVLVMHQGE 480
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
334-562 |
9.05e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.97 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYegdyseADG--ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAG--IDINDWNGSQ 409
Cdd:PRK13636 6 LKVEELNYNY------SDGthALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 410 LLEQFSYVPQGDDVYIFDESIRYNIAF-------PRPEaTEEEVEKAAHLAGIHEfvigLKDGyDTQVgergirLSGGQK 482
Cdd:PRK13636 80 LRESVGMVFQDPDNQLFSASVYQDVSFgavnlklPEDE-VRKRVDNALKRTGIEH----LKDK-PTHC------LSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 483 QRVALArAVLADRP-ILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTH 559
Cdd:PRK13636 148 KRVAIA-GVLVMEPkVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
...
gi 818754182 560 EEL 562
Cdd:PRK13636 227 KEV 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
353-573 |
9.90e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 9.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINdwngsQLLEQFSYVPQGDDVY----IFDE 428
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN-----KLDHKLAAQLGIGIIYqelsVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 -SIRYNIAFPRPEATE----------EEVEKAAHLAGIhefvIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPI 497
Cdd:PRK09700 95 lTVLENLYIGRHLTKKvcgvniidwrEMRVRAAMMLLR----VGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 498 LILDEATSSvdaITEKEIQtNMRAILT-----GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEElIKSHGIYAQM 572
Cdd:PRK09700 167 IIMDEPTSS---LTNKEVD-YLFLIMNqlrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD-VSNDDIVRLM 241
|
.
gi 818754182 573 V 573
Cdd:PRK09700 242 V 242
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
353-548 |
1.23e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.35 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGidindwnGSQLleqfSYVPQGDDVyifDESiry 432
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-------GARV----AYVPQRSEV---PDS--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 niaFPrpeATEEEV---------------EKAAHLAGIHEFV-IGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRP 496
Cdd:NF040873 70 ---LP---LTVRDLvamgrwarrglwrrlTRDDRAAVDDALErVGLADLAGRQLGE----LSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818754182 497 ILILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIwGLADKIVVM 548
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELV-RRADPCVLL 191
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-565 |
1.57e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.06 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPcqmgtiTVAGIDindWNGSQLLEQFSYVPQGDdvyIFDESIRYN 433
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMND------KVSGYR---YSGDVLLGGRSIFNYRD---VLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 434 IAFPRPEATEEEVEKAAhLAGI--HEFV---------------IGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRP 496
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNV-LAGVraHKLVprkefrgvaqarlteVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 497 ILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
353-562 |
1.60e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAG--IDINDwngsqlleqfsyvPQgddvyifdESI 430
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRS-------------PR--------DAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RY-------------------NIA---------FPRPEATEEEVEKaahLAGIHEFVIGLkdgyDTQVGErgirLSGGQK 482
Cdd:COG3845 79 ALgigmvhqhfmlvpnltvaeNIVlgleptkggRLDRKAARARIRE---LSERYGLDVDP----DAKVED----LSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 483 QRVALARAVLADRPILILDEATsSVdaITEKEIQT------NMRAilTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEE 556
Cdd:COG3845 148 QRVEILKALYRGARILILDEPT-AV--LTPQEADElfeilrRLAA--EGKSIIFITHKLREVMAIADRVTVLRRGKVVGT 222
|
250
....*....|.
gi 818754182 557 G-----THEEL 562
Cdd:COG3845 223 VdtaetSEEEL 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
358-532 |
2.09e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 358 SLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwngSQLLEQFSYVPQGDDVYifDE-SIRYNIAF 436
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD---PDVAEACHYLGHRNAMK--PAlTVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 437 PRP--EATEEEVEKAAHLAGIHEfVIGLKDGYdtqvgergirLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKE 514
Cdd:PRK13539 97 WAAflGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170
....*....|....*...
gi 818754182 515 IQTNMRAILTGKTAIIIA 532
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAA 183
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
354-509 |
2.27e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.21 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVIT-RLAP--CQMGTITVAGIDINDwnGSQLLEQFSYVPQgdDVYIFDE-S 429
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPafSASGEVLLNGRRLTA--LPAEQRRIGILFQ--DDLLFPHlS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 IRYNIAFPRPEATEEEVEKAAHLAGIHEfvIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSSVDA 509
Cdd:COG4136 93 VGENLAFALPPTIGRAQRRARVEQALEE--AGLAGFADRDPAT----LSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
353-571 |
2.28e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.31 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDI--NDWNGSQLLEQ-----F-----SYVPQG 420
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkADPEAQKLLRQkiqivFqnpygSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 421 DDVYIFDESIRYNIAFPRPEATEEEVEKAAHlagihefvIGLK-DGYDtqvgergiR----LSGGQKQRVALARAVLADR 495
Cdd:PRK11308 110 KVGQILEEPLLINTSLSAAERREKALAMMAK--------VGLRpEHYD--------RyphmFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 496 PILILDEATSSVDAitekEIQT---NMRAILT---GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEElikshgIY 569
Cdd:PRK11308 174 DVVVADEPVSALDV----SVQAqvlNLMMDLQqelGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ------IF 243
|
..
gi 818754182 570 AQ 571
Cdd:PRK11308 244 NN 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
336-562 |
2.36e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.97 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 336 LSDVCFAYEGDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITV------AGI----DINDw 405
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLkkikEVKR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 406 ngsqLLEQFSYVPQGDDVYIFDESIRYNIAFPrP----EATEEEVEKAAHLAGIhefvIGLKDGYdtqVGERGIRLSGGQ 481
Cdd:PRK13645 88 ----LRKEIGLVFQFPEYQLFQETIEKDIAFG-PvnlgENKQEAYKKVPELLKL----VQLPEDY---VKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 482 KQRVALARAVLADRPILILDEATSSVDAITEKEIqTNMRAILT---GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGT 558
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF-INLFERLNkeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
....
gi 818754182 559 HEEL 562
Cdd:PRK13645 235 PFEI 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
353-562 |
2.53e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSyvpqgDDVYIFDESI-- 430
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS-----DIQMIFQDPLas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 ---RYN----IAFP----RPEATEEEVE---KAAHL-AGI---------HEFviglkdgydtqvgergirlSGGQKQRVA 486
Cdd:PRK15079 111 lnpRMTigeiIAEPlrtyHPKLSRQEVKdrvKAMMLkVGLlpnlinrypHEF-------------------SGGQCQRIG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 487 LARAVLADRPILILDEATSSVDAITE-------KEIQTNMrailtGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTH 559
Cdd:PRK15079 172 IARALILEPKLIICDEPVSALDVSIQaqvvnllQQLQREM-----GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTY 246
|
...
gi 818754182 560 EEL 562
Cdd:PRK15079 247 DEV 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
365-558 |
3.42e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.29 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 365 QIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDInDWNGSQLLEQFSYVPQGDDVY---IFDESIRYNIAFPRPEA 441
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFhhlTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 442 TEEEVEKAAHL--AGIHEfviglkdgydtQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNM 519
Cdd:TIGR01257 1036 EEAQLEMEAMLedTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....*....
gi 818754182 520 RAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGT 558
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
353-562 |
3.89e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.28 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTT-IRKVITRLAPCQmGTITVAGIDINDWNGSQLLE------------------- 412
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfIEHLNALLLPDT-GTIEWIFKDEKNKKKTKEKEkvleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 -----QFSYVPQGDDVYIFDESIRYNIAF-PRPEATE-EEVEKAAhlAGIHEFViGLKDGYdtqVGERGIRLSGGQKQRV 485
Cdd:PRK13651 101 keirrRVGVVFQFAEYQLFEQTIEKDIIFgPVSMGVSkEEAKKRA--AKYIELV-GLDESY---LQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 486 ALArAVLADRP-ILILDEATSSVDAITEKEiqtnMRAILT-----GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG-T 558
Cdd:PRK13651 175 ALA-GILAMEPdFLVFDEPTAGLDPQGVKE----ILEIFDnlnkqGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGdT 249
|
....
gi 818754182 559 HEEL 562
Cdd:PRK13651 250 YDIL 253
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
354-554 |
5.14e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.23 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLL----EQFSYVPQgddvyifdes 429
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlrrEHFGFIFQ---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 iRY----------NIAFPrpeATEEEVEKAAHLAGIHEFVIGLkdGYDTQVGERGIRLSGGQKQRVALARAVLADRPILI 499
Cdd:PRK10535 94 -RYhllshltaaqNVEVP---AVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 500 LDEATSSVDAITEKEIQtnmrAIL-----TGKTAIIIAHRlSTIWGLADKIVVMDQGKKV 554
Cdd:PRK10535 168 ADEPTGALDSHSGEEVM----AILhqlrdRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
354-562 |
5.51e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.01 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRL-APCQmGTITVAGIDIN------------DWNGSQLLE-QFSYVPQ 419
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLeKPSE-GSIVVNGQTINlvrdkdgqlkvaDKNQLRLLRtRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 420 GDDVYIFDESIRYNIAFP-------RPEATEEEVEKAAHLaGIHEfviglkdgydTQVGERGIRLSGGQKQRVALARAVL 492
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPiqvlglsKQEARERAVKYLAKV-GIDE----------RAQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818754182 493 ADRPILILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-565 |
5.84e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGI------DINDWNGSQLLEQFSYVPQG 420
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 421 DDVYIfDESIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGL-KDGYDtQVGERGIRLSGGQKQRVALARAVLADRPILI 499
Cdd:PRK14246 99 PNPFP-HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 500 LDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
334-565 |
6.29e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.51 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEgdySEAD-GALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE 412
Cdd:PRK13642 5 LEVENLVFKYE---KESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 QFSYVPQGDDVYIFDESIRYNIAF-------PRPEATEEeVEKAAHLAGIHEFVIglkdgydtqvgERGIRLSGGQKQRV 485
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVAFgmenqgiPREEMIKR-VDEALLAVNMLDFKT-----------REPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 486 ALArAVLADRP-ILILDEATSSVDAITEKEIqtnMRAILTGK-----TAIIIAHRLSTIwGLADKIVVMDQGKKVEEGTH 559
Cdd:PRK13642 150 AVA-GIIALRPeIIILDESTSMLDPTGRQEI---MRVIHEIKekyqlTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAP 224
|
....*.
gi 818754182 560 EELIKS 565
Cdd:PRK13642 225 SELFAT 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
307-561 |
7.45e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 307 ERLANLLLEPEPIETGSI-----QSVPAGPIGVSLSDVCFAYEGDYseadgALHDFSLEIEPGQIVALVGQSGAGKTTIR 381
Cdd:COG0488 284 KALEKLEREEPPRRDKTVeirfpPPERLGKKVLELEGLSKSYGDKT-----LLDDLSLRIDRGDRIGLIGPNGAGKSTLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 382 KVIT-RLAPCQmGTITVagidindwnGSQLleQFSYVPQGDDVYIFDESIRYNIAFPRPEATEEEVekAAHLAGiheFvi 460
Cdd:COG0488 359 KLLAgELEPDS-GTVKL---------GETV--KIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEV--RGYLGR---F-- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 461 gLKDGYD--TQVGergiRLSGGQKQRVALARAVLADRPILILDEAT-----SSVDAITEkeiqtnmrAILT--GkTAIII 531
Cdd:COG0488 420 -LFSGDDafKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTnhldiETLEALEE--------ALDDfpG-TVLLV 485
|
250 260 270
....*....|....*....|....*....|....
gi 818754182 532 AH-R--LSTIwglADKIVVMDQGKKVE-EGTHEE 561
Cdd:COG0488 486 SHdRyfLDRV---ATRILEFEDGGVREyPGGYDD 516
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
361-557 |
1.01e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.84 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 361 IEPGQIVALVGQSGAGKTTIRKVIT----RLAPCQMGTITVAGIDINDwngsqLLEQFsyvpQGDDVYI----------- 425
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEE-----IKKHY----RGDVVYNaetdvhfphlt 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 ----FDESIRYNIAFPRPEATEEEvEKAAHLAGIHEFVIGLKDGYDTQVGERGIR-LSGGQKQRVALARAVLADRPILIL 500
Cdd:TIGR00956 155 vgetLDFAARCKTPQNRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 501 DEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLS-TIWGLADKIVVMDQGKKVEEG 557
Cdd:TIGR00956 234 DNATRGLDSATALEFIRALKTSanILDTTPLVAIYQCSqDAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
356-563 |
1.13e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.77 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWN-GSQLLEQFSYVPQGDDVY----IFDE-- 428
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFrrlsVYDNlm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 ---SIRYNIafprpeATEEEVEKAAHLagIHEFVIG-LKDGYdtqvgerGIRLSGGQKQRVALARAVLADRPILILDEAT 504
Cdd:PRK10895 101 avlQIRDDL------SAEQREDRANEL--MEEFHIEhLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 505 SSVDAITE---KEIQTNMRAilTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:PRK10895 166 AGVDPISVidiKRIIEHLRD--SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
353-563 |
1.89e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.99 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKT--------------TIRKVITRLAPCQmgtiTVAGIDINDWNGSQLLE-QFSYV 417
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSvlmhvlrgmdqyepTSGRIIYHVALCE----KCGYVERPSKVGEPCPVcGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 418 PQGDDVYIFDESIRYN------IAFPRPEATEEE------VEKAAHLAGiHEFVIGLKDGYD----TQVGERGIR----L 477
Cdd:TIGR03269 91 PEEVDFWNLSDKLRRRirkriaIMLQRTFALYGDdtvldnVLEALEEIG-YEGKEAVGRAVDliemVQLSHRITHiardL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 478 SGGQKQRVALARAvLADRPILIL-DEATSSVDAITEKEIQTNMR--AILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKV 554
Cdd:TIGR03269 170 SGGEKQRVVLARQ-LAKEPFLFLaDEPTGTLDPQTAKLVHNALEeaVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
....*....
gi 818754182 555 EEGTHEELI 563
Cdd:TIGR03269 249 EEGTPDEVV 257
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
353-544 |
1.92e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.66 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRL----APCQM-GTITVAGIDIND--WNGSQLLEQFSYVPQGDdvYI 425
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndliPGFRVeGKVTFHGKNLYApdVDPVEVRRRIGMVFQKP--NP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 FDESIRYNIAF-PRPEA----TEEEVEKAAHLAGIHEFViglKDgydtQVGERGIRLSGGQKQRVALARAVLADRPILIL 500
Cdd:PRK14243 103 FPKSIYDNIAYgARINGykgdMDELVERSLRQAALWDEV---KD----KLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 818754182 501 DEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLADK 544
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDM 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
354-504 |
2.28e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVA-GIDIndwngsqlleqfSYVPQ----GDDVYIFDE 428
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRI------------GYLPQepplDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SI-----------RYNIAFPRPEATEEEVEKAAHLagIHEFVIglKDGY--------------------DTQVGErgirL 477
Cdd:COG0488 82 VLdgdaelraleaELEELEAKLAEPDEDLERLAEL--QEEFEA--LGGWeaearaeeilsglgfpeedlDRPVSE----L 153
|
170 180
....*....|....*....|....*..
gi 818754182 478 SGGQKQRVALARAVLADRPILILDEAT 504
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-562 |
6.61e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.87 E-value: 6.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 358 SLEIEPGQIVALVGQSGAGKTTIRKVITRL-----APCQMGTITVAGIDINDWNGSQLLEQFSYVPQGDDVyIFDESIRY 432
Cdd:PRK14247 23 NLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNP-IPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAF--------PRPEATEEEVEKAAHLAGIHEFViglKDGYDTQVGergiRLSGGQKQRVALARAVLADRPILILDEAT 504
Cdd:PRK14247 102 NVALglklnrlvKSKKELQERVRWALEKAQLWDEV---KDRLDAPAG----KLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 505 SSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
353-573 |
7.15e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ--------FSYVPqgddvy 424
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgvaiiyqeLHLVP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 ifDESIRYNI---AFP-------RPEATEEEVEKAAHLagihefviGLKDGYDTQVGergiRLSGGQKQRVALARAVLAD 494
Cdd:PRK11288 93 --EMTVAENLylgQLPhkggivnRRLLNYEAREQLEHL--------GVDIDPDTPLK----YLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 495 RPILILDEATSSVDAiteKEIQTNMRAILT----GKTAIIIAHRLSTIWGLADKIVVMDQGKKVE------EGTHEELIk 564
Cdd:PRK11288 159 ARVIAFDEPTSSLSA---REIEQLFRVIRElraeGRVILYVSHRMEEIFALCDAITVFKDGRYVAtfddmaQVDRDQLV- 234
|
....*....
gi 818754182 565 shgiyAQMV 573
Cdd:PRK11288 235 -----QAMV 238
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
354-551 |
1.02e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 70.44 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIrkVITRLAPCQmgtiTVAG--------IDINDWNGSQLLEQFSYVPQGDDVYI 425
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQ----TLEGkvhwsnknESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 FDESIRYNIAFPRPeATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATS 505
Cdd:cd03290 91 LNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 818754182 506 SVDA-ITEKEIQTNMRAILTG--KTAIIIAHRLSTIwGLADKIVVMDQG 551
Cdd:cd03290 170 ALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
333-562 |
1.18e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 333 GVSLSDVCFAYegdyseadGALH---DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQ 409
Cdd:PRK11000 3 SVTLRNVTKAY--------GDVViskDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 410 llEQFSYVPQGDDVY----IFDesiryNIAFprpeateeevekAAHLAGIHEFVIglkDGYDTQVGE----------RGI 475
Cdd:PRK11000 75 --RGVGMVFQSYALYphlsVAE-----NMSF------------GLKLAGAKKEEI---NQRVNQVAEvlqlahlldrKPK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 476 RLSGGQKQRVALARAVLADRPILILDEATSSVDAitekEIQTNMRAILT------GKTAIIIAHRLSTIWGLADKIVVMD 549
Cdd:PRK11000 133 ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA----ALRVQMRIEISrlhkrlGRTMIYVTHDQVEAMTLADKIVVLD 208
|
250
....*....|...
gi 818754182 550 QGKKVEEGTHEEL 562
Cdd:PRK11000 209 AGRVAQVGKPLEL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
353-563 |
1.22e-13 |
|
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: 73.68 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDinDW----------NGSQ------LLEQFSY 416
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGD--EWvdmtkpgpdgRGRAkryigiLHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 417 VPQGDDVYIFDESIryNIAFPRpeatEEEVEKAAHLAGihefVIGLKDGYDTQVGER-GIRLSGGQKQRVALARAVLADR 495
Cdd:TIGR03269 377 YPHRTVLDNLTEAI--GLELPD----ELARMKAVITLK----MVGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 496 PILILDEATSSVDAITEKEIQTN-MRA-ILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSiLKArEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
354-552 |
1.22e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVagidindwnGSQLLEQfsyvPQGDDVYIFDE----- 428
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA---------GTAPLAE----AREDTRLMFQDarllp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 --SIRYNIAFP-----RPEATE--EEVekaahlagihefviGLKDgydtQVGERGIRLSGGQKQRVALARAvLADRP-IL 498
Cdd:PRK11247 95 wkKVIDNVGLGlkgqwRDAALQalAAV--------------GLAD----RANEWPAALSGGQKQRVALARA-LIHRPgLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 499 ILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
358-532 |
1.27e-13 |
|
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: 69.83 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 358 SLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITvagidindWNGSQLLEQFSYVPQGDdVYIFDE-------SI 430
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL--------LNGGPLDFQRDSIARGL-LYLGHApgikttlSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNIAFPRPEATEEEVEKAAHLAGIHEFviglkdgYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSSVDAI 510
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALARVGLNGF-------EDRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|..
gi 818754182 511 TEKEIQTNMRAILTGKTAIIIA 532
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLT 181
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
308-555 |
1.70e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.08 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 308 RLANLLLEPePIETGSIQSVPAGPIGVSLSDVCFAYEgdysEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRL 387
Cdd:PRK10522 298 KLNKLALAP-YKAEFPRPQAFPDWQTLELRNVTFAYQ----DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 388 APCQMGTITVAGIDINDWNGSQLLEQFSYVpqGDDVYIFDESIRyniafprPEATEEEVEKA----AHLAGIHEfvIGLK 463
Cdd:PRK10522 373 YQPQSGEILLDGKPVTAEQPEDYRKLFSAV--FTDFHLFDQLLG-------PEGKPANPALVekwlERLKMAHK--LELE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 464 DGYDTQvgergIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRlSTIWGL 541
Cdd:PRK10522 442 DGRISN-----LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISHD-DHYFIH 515
|
250
....*....|....
gi 818754182 542 ADKIVVMDQGKKVE 555
Cdd:PRK10522 516 ADRLLEMRNGQLSE 529
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
353-565 |
1.74e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.86 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVItrlapcqMG------TITVagiDINDWNGSQLLeQFSYVPQ----GDD 422
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI-------CGitkdnwHVTA---DRFRWNGIDLL-KLSPRERrkiiGRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 423 V-YIFDESIRY----------------NIAFP-----RPEATEEEVEKAAHLAGI--HEFVIglkDGYDTQvgergirLS 478
Cdd:COG4170 91 IaMIFQEPSSCldpsakigdqlieaipSWTFKgkwwqRFKWRKKRAIELLHRVGIkdHKDIM---NSYPHE-------LT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 479 GGQKQRVALARAvLADRP-ILILDEATSSVDAITEKEI--------QTNMRAILtgktaiIIAHRLSTIWGLADKIVVMD 549
Cdd:COG4170 161 EGECQKVMIAMA-IANQPrLLIADEPTNAMESTTQAQIfrllarlnQLQGTSIL------LISHDLESISQWADTITVLY 233
|
250
....*....|....*.
gi 818754182 550 QGKKVEEGTHEELIKS 565
Cdd:COG4170 234 CGQTVESGPTEQILKS 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
355-562 |
2.20e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 355 HDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQmgTITVAGIDINdWNGSQLL---EQFSYVPQGDDV-YIFDE-- 428
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSP--PVVYPSGDIR-FHGESLLhasEQTLRGVRGNKIaMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 -------SIRYNIAFP-------RPEATEEEVEKAAHLAGIHEFVIGLKDgYDTQvgergirLSGGQKQRVALARAVLAD 494
Cdd:PRK15134 103 vslnplhTLEKQLYEVlslhrgmRREAARGEILNCLDRVGIRQAAKRLTD-YPHQ-------LSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 495 RPILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
333-562 |
2.40e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.41 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 333 GVSLSDVCFAYEGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwngsqlLE 412
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ----VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE------LE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 qfsyvPQGDDV-YIFDE-------SIRYNIA-------FPRPEaTEEEVEKAAHLAGIHEFViglkdgydtqvgERGIR- 476
Cdd:PRK11650 73 -----PADRDIaMVFQNyalyphmSVRENMAyglkirgMPKAE-IEERVAEAARILELEPLL------------DRKPRe 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 477 LSGGQKQRVALARAVLADRPILILDEATSSVDAiteK-------EIQTNMRAILTgkTAIIIAHRLSTIWGLADKIVVMD 549
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA---KlrvqmrlEIQRLHRRLKT--TSLYVTHDQVEAMTLADRVVVMN 209
|
250
....*....|....
gi 818754182 550 QGkKVEE-GTHEEL 562
Cdd:PRK11650 210 GG-VAEQiGTPVEV 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
353-552 |
3.30e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQ---LLEQFSYVPQgDDVYIFDES 429
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQ-DHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 IRYNIAFPR--PEATEEEVEKAAHlAGIHEfvIGLKDgydtQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSV 507
Cdd:PRK10908 96 VYDNVAIPLiiAGASGDDIRRRVS-AALDK--VGLLD----KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 818754182 508 D-AITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:PRK10908 169 DdALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
349-562 |
3.41e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.73 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 349 EADGAL-HDFSLEIEPGQIVALVGQSGAGKTT------------IRKVITRL-------APCQMGTITVAGIDINDWNGs 408
Cdd:PRK10418 13 QAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLtcaaalgilpagVRQTAGRVlldgkpvAPCALRGRKIATIMQNPRSA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 409 qlleqFSYVPQGDDVYIfdESIRyniafprpeATEEEVEKAAHLAGIHEfvIGLKDGydtqvgERGIRL-----SGGQKQ 483
Cdd:PRK10418 92 -----FNPLHTMHTHAR--ETCL---------ALGKPADDATLTAALEA--VGLENA------ARVLKLypfemSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 484 RVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEE 561
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
.
gi 818754182 562 L 562
Cdd:PRK10418 228 L 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-562 |
9.39e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDyseadGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDInDWNGSQLL-- 411
Cdd:PRK13638 2 LATSDLWFRYQDE-----PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLal 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 412 -EQFSYVPQGDDVYIFDESIRYNIAFPRPEATEEEVEKAAHLagihefviglkDGYDTQVGERGIR------LSGGQKQR 484
Cdd:PRK13638 76 rQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRV-----------DEALTLVDAQHFRhqpiqcLSHGQKKR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 485 VALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILT-GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
353-573 |
1.03e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCqmGT-----------ITVAGIDINDWNGSQLLEQ-FSYVPQ- 419
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH--GTyegeiifegeeLQASNIRDTERAGIAIIHQeLALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 420 --GDDVYIFDESIR-----YNIAFPRPEATEEEVekaahlagihefviGLKDGYDTQVGErgirLSGGQKQRVALARAVL 492
Cdd:PRK13549 98 svLENIFLGNEITPggimdYDAMYLRAQKLLAQL--------------KLDINPATPVGN----LGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 493 ADRPILILDEATSSvdaITEKEIQTNMRAI----LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSHgI 568
Cdd:PRK13549 160 KQARLLILDEPTAS---LTESETAVLLDIIrdlkAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDD-I 235
|
....*
gi 818754182 569 YAQMV 573
Cdd:PRK13549 236 ITMMV 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
353-557 |
1.54e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQfsyvpQGDDVYIFDE---- 428
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAL-----RRDIQFIFQDpyas 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 -----SIRYNIAFP-RPEATEEEVEKAAHLAGIHEFViGLKDgydtqvgERGIR----LSGGQKQRVALARAVLADRPIL 498
Cdd:PRK10261 414 ldprqTVGDSIMEPlRVHGLLPGKAAAARVAWLLERV-GLLP-------EHAWRypheFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 499 ILDEATSSVDAITEKEIqTNMRAILT---GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEG 557
Cdd:PRK10261 486 IADEAVSALDVSIRGQI-INLLLDLQrdfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
347-549 |
2.25e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 67.05 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADGALHDFSLEIEPG-----QIVALVGQSGAGKTT-IRKVITRLAPcQMGTITVAGIDIndwngsqlleqfSYVPQg 420
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTfIKMLAGVLKP-DEGDIEIELDTV------------SYKPQ- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 421 ddvYI---FDESIRYNIAFPRPEATEE-----EVEKAAHLAGIhefviglkdgYDTQVGErgirLSGGQKQRVALARAVL 492
Cdd:cd03237 69 ---YIkadYEGTVRDLLSSITKDFYTHpyfktEIAKPLQIEQI----------LDREVPE----LSGGELQRVAIAACLS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 493 ADRPILILDEATSSVDA----ITEKEIQtnmRAIL-TGKTAIIIAHRLSTIWGLADKIVVMD 549
Cdd:cd03237 132 KDADIYLLDEPSAYLDVeqrlMASKVIR---RFAEnNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
356-562 |
2.25e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLE---QFSYVPQG----DDVYIFDe 428
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkRMSMLFQSgalfTDMNVFD- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 siryNIAFPRPEATE--EEVEKAAHLAGIHefVIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSS 506
Cdd:PRK11831 104 ----NVAYPLREHTQlpAPLLHSTVMMKLE--AVGLRGAAKLMPSE----LSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 507 VDAITE----KEIQTNMRAIltGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK11831 174 QDPITMgvlvKLISELNSAL--GVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-554 |
2.66e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.03 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQgdDVYI---FDES 429
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQ--DPMMgtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 IRYN--IAFPR-----------PEATEEEVEKAAHLAgihefvIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRP 496
Cdd:COG1101 99 IEENlaLAYRRgkrrglrrgltKKRRELFRELLATLG------LGLENRLDTKVGL----LSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 497 ILILDEATSSVD--------AITEKEIQTNmrailtGKTAIIIAHRLSTIWGLADKIVVMDQGKKV 554
Cdd:COG1101 169 LLLLDEHTAALDpktaalvlELTEKIVEEN------NLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
358-533 |
2.80e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.84 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 358 SLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGsQLLEQFSYVPQGDDVYIfDESIRYNIAFP 437
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPGLKP-ELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 438 RPEATEEEVEKAAHLAgihefVIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQT 517
Cdd:TIGR01189 98 AAIHGGAQRTIEDALA-----AVGLTGFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170
....*....|....*..
gi 818754182 518 NMRAIL-TGKTAIIIAH 533
Cdd:TIGR01189 169 LLRAHLaRGGIVLLTTH 185
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
353-562 |
3.38e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGsQLLEQFSYVPQGDDVYIFDE---- 428
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQIARMGVVRTFQHVRLFREmtvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 ---------SIRYNI--------AFPRPEAteEEVEKAAHLAGihefVIGLKDGYDTQVGErgirLSGGQKQRVALARAV 491
Cdd:PRK11300 99 enllvaqhqQLKTGLfsgllktpAFRRAES--EALDRAATWLE----RVGLLEHANRQAGN----LAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 492 LADRPILILDEATSSVDAITEKEIQtNMRAILT---GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELD-ELIAELRnehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
361-557 |
3.91e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 361 IEPGQIVALVGQSGAGKTTIRKVIT-RL-APCQMGTITVAGIDINdwngSQLLEQFSYVPQgDDVYIFDESIRYNIAF-- 436
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAgRIqGNNFTGTILANNRKPT----KQILKRTGFVTQ-DDILYPHLTVRETLVFcs 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 437 ----PRPEATEEEVEKAAHLagIHEfvIGLKDGYDTQVGERGIR-LSGGQKQRVALARAVLADRPILILDEATSSVDAIT 511
Cdd:PLN03211 166 llrlPKSLTKQEKILVAESV--ISE--LGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 818754182 512 E-KEIQTNMRAILTGKTAIIIAHRLST-IWGLADKIVVMDQGKKVEEG 557
Cdd:PLN03211 242 AyRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
353-563 |
4.20e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINdWNG---SQ------LLEQFSYVPQgddv 423
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNGpksSQeagigiIHQELNLIPQ---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 yifdESIRYNI--------AFPRPEATEEEVEKAAHLAGihefvIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADR 495
Cdd:PRK10762 94 ----LTIAENIflgrefvnRFGRIDWKKMYAEADKLLAR-----LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 496 PILILDEATssvDAITEKEIQTNMRAI----LTGKTAIIIAHRLSTIWGLADKIVVMDQGK-----KVEEGTHEELI 563
Cdd:PRK10762 161 KVIIMDEPT---DALTDTETESLFRVIrelkSQGRGIVYISHRLKEIFEICDDVTVFRDGQfiaerEVADLTEDSLI 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
353-573 |
4.64e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.31 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM--GTITVAGIDINDWN-------GSQLLEQ-FSYVPQ--- 419
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNirdteraGIVIIHQeLTLVPElsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 420 ------GDDVYIFDESIRYNIAFPRPEATEEEVEkaahlagihefvigLKDGYDTQ-VGERGirlsGGQKQRVALARAVL 492
Cdd:TIGR02633 96 aeniflGNEITLPGGRMAYNAMYLRAKNLLRELQ--------------LDADNVTRpVGDYG----GGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 493 ADRPILILDEATSSvdaITEKEIQTNMRAI----LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVeeGTHE-ELIKSHG 567
Cdd:TIGR02633 158 KQARLLILDEPSSS---LTEKETEILLDIIrdlkAHGVACVYISHKLNEVKAVCDTICVIRDGQHV--ATKDmSTMSEDD 232
|
....*.
gi 818754182 568 IYAQMV 573
Cdd:TIGR02633 233 IITMMV 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
354-566 |
8.11e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.82 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIE---PGQ-IVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwngsqlLEQFSYVPQ-----GddvY 424
Cdd:PRK11144 10 LGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD------AEKGICLPPekrriG---Y 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 IFDE-------SIRYNIAFPRPEATEEEVEKAAHLAGIHEfvigLKDGYDtqvgergIRLSGGQKQRVALARAVLADRPI 497
Cdd:PRK11144 81 VFQDarlfphyKVRGNLRYGMAKSMVAQFDKIVALLGIEP----LLDRYP-------GSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 498 LILDEATSSVDAITEKEI----QTNMRAIltgKTAII-IAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSH 566
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELlpylERLAREI---NIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
355-509 |
1.02e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 355 HDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITvagidindWNGSQLLEQfsyvpqgddvyifDESIRYNI 434
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL--------WQGEPIRRQ-------------RDEYHQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 435 AFprpeateeevekAAHLAGIHE---------FVIGLKDGYDT--------QVGERGI------RLSGGQKQRVALARAV 491
Cdd:PRK13538 77 LY------------LGHQPGIKTeltalenlrFYQRLHGPGDDealwealaQVGLAGFedvpvrQLSAGQQRRVALARLW 144
|
170
....*....|....*...
gi 818754182 492 LADRPILILDEATSSVDA 509
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDK 162
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-543 |
1.30e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.06 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQmGTITVAG--------IDINDWNGSQLLEQFSYV- 417
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNLNRLRRQVSMVh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 418 PQGDdvyIFDESIRYNIAFP------RPEATEEEVEKAAHLAGihefviGLKDGYDTQVGERGIRLSGGQKQRVALARAV 491
Cdd:PRK14258 95 PKPN---LFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 492 LADRPILILDEATSSVDAITEKEIQT-----NMRAILtgkTAIIIAHRLSTIWGLAD 543
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESliqslRLRSEL---TMVIVSHNLHQVSRLSD 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
346-558 |
1.31e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.12 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 346 DYSEADGALHDFSLEIEPGQI-----VALVGQSGAGKTTIRKVIT-RLAPCQmGTITvAGIDIndwngsqlleqfSYVPQ 419
Cdd:COG1245 343 EYPDLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAgVLKPDE-GEVD-EDLKI------------SYKPQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 420 gddvYI---FDESIRYNIAFPRPEATEEEVEKaahlagiHEFV--IGLKDGYDTQVGErgirLSGGQKQRVALARAVLAD 494
Cdd:COG1245 409 ----YIspdYDGTVEEFLRSANTDDFGSSYYK-------TEIIkpLGLEKLLDKNVKD----LSGGELQRVAIAACLSRD 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 495 RPILILDEATSSVDA----ITEKEIQTNMRAilTGKTAIIIAHRLSTIWGLADKIVVMDqGKKVEEGT 558
Cdd:COG1245 474 ADLYLLDEPSAHLDVeqrlAVAKAIRRFAEN--RGKTAMVVDHDIYLIDYISDRLMVFE-GEPGVHGH 538
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
354-563 |
1.37e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDIN-----------------DWNGSQL------ 410
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqdglangivyiseDRKRDGLvlgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 411 --------LEQFSYVP----QGDDVYIFDESIR-YNIAFPRPEATeeevekaahlagihefvIGLkdgydtqvgergirL 477
Cdd:PRK10762 348 kenmsltaLRYFSRAGgslkHADEQQAVSDFIRlFNIKTPSMEQA-----------------IGL--------------L 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 478 SGGQKQRVALARAvLADRP-ILILDEATSSVDAITEKEI-QTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGK--- 552
Cdd:PRK10762 397 SGGNQQKVAIARG-LMTRPkVLILDEPTRGVDVGAKKEIyQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRisg 475
|
250
....*....|...
gi 818754182 553 --KVEEGTHEELI 563
Cdd:PRK10762 476 efTREQATQEKLM 488
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
350-561 |
1.73e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 350 ADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQmGTITVAGIDINDWNGSQLLEQFSYVPQGD------DV 423
Cdd:PRK03695 8 VSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELARHRAYLSQQQtppfamPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 YIFdesirynIAFPRPEATEEEVEKAAhlagIHEFV--IGLKDGYDTQVGergiRLSGGQKQRVALARAVLADRP----- 496
Cdd:PRK03695 87 FQY-------LTLHQPDKTRTEAVASA----LNEVAeaLGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQVWPdinpa 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 497 --ILILDEATSSVDAITEKEIQTNMRAILT-GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEE 561
Cdd:PRK03695 152 gqLLLLDEPMNSLDVAQQAALDRLLSELCQqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
334-565 |
2.33e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSEADgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAG----------IDIN 403
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIA-AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 404 DWNGSQLleqfSYVPQGDDVYIFDESI-RYNIAFPRPEATEEEVeKAAHLAGIHEFVIGLKDGYD--------TQVGERG 474
Cdd:PRK10261 92 EQSAAQM----RHVRGADMAMIFQEPMtSLNPVFTVGEQIAESI-RLHQGASREEAMVEAKRMLDqvripeaqTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 475 IRLSGGQKQRVALARAvLADRP-ILILDEATSSVDAITEKEIQTNMRAILTGKT--AIIIAHRLSTIWGLADKIVVMDQG 551
Cdd:PRK10261 167 HQLSGGMRQRVMIAMA-LSCRPaVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQG 245
|
250
....*....|....
gi 818754182 552 KKVEEGTHEELIKS 565
Cdd:PRK10261 246 EAVETGSVEQIFHA 259
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
345-565 |
2.68e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 65.15 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 345 GDYSEADGALHDFSLEIEPGQIVALVGQSGAGKTtirkvITRLAPcqMGTITVAGIDIND---WNGSQLL-----EQFSY 416
Cdd:PRK11022 14 GDESAPFRAVDRISYSVKQGEVVGIVGESGSGKS-----VSSLAI--MGLIDYPGRVMAEkleFNGQDLQrisekERRNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 417 VpqGDDV-YIFDESIR-----YNIAFPRPEATEeeVEKAAHLAGIHEFVIGLKdgydTQVGergI------------RLS 478
Cdd:PRK11022 87 V--GAEVaMIFQDPMTslnpcYTVGFQIMEAIK--VHQGGNKKTRRQRAIDLL----NQVG---IpdpasrldvyphQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 479 GGQKQRVALARAVLADRPILILDEATSSVDAITEKEI---------QTNMRAILtgktaiiIAHRLSTIWGLADKIVVMD 549
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIielllelqqKENMALVL-------ITHDLALVAEAAHKIIVMY 228
|
250
....*....|....*.
gi 818754182 550 QGKKVEEGTHEELIKS 565
Cdd:PRK11022 229 AGQVVETGKAHDIFRA 244
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
334-552 |
3.17e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 61.31 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 334 VSLSDVCFAYEGDYSeadgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVIT-RLAPCQmGTITVAGIdindwngsqllE 412
Cdd:cd03221 1 IELENLSKTYGGKLL-----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDE-GIVTWGST-----------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 413 QFSYVPQgddvyifdesiryniafprpeateeevekaahlagihefviglkdgydtqvgergirLSGGQKQRVALARAVL 492
Cdd:cd03221 64 KIGYFEQ---------------------------------------------------------LSGGEKMRLALAKLLL 86
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 493 ADRPILILDEATS-----SVDAITE--KEIQtnmrailtgKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:cd03221 87 ENPNLLLLDEPTNhldleSIEALEEalKEYP---------GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
354-536 |
3.54e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGidindwngsQLLEQFSYVPQGD-------DVYIF 426
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG---------QPMSKLSSAAKAElrnqklgFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 427 -----DESIRYNIAFP-------RPEATEEEVEKaahLAGIhefviglkdGYDTQVGERGIRLSGGQKQRVALARAvLAD 494
Cdd:PRK11629 96 hhllpDFTALENVAMPlligkkkPAEINSRALEM---LAAV---------GLEHRANHRPSELSGGERQRVAIARA-LVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 818754182 495 RPILIL-DEATSSVDAITEKEI-----QTNMR---AILTGKTAIIIAHRLS 536
Cdd:PRK11629 163 NPRLVLaDEPTGNLDARNADSIfqllgELNRLqgtAFLVVTHDLQLAKRMS 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
346-549 |
3.74e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 346 DYSEADGALHDFSLEIEPGQI-----VALVGQSGAGKTTIRKVItrlapcqmgtitvAGIdINDWNGSQLLE-QFSYVPQ 419
Cdd:PRK13409 342 EYPDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLL-------------AGV-LKPDEGEVDPElKISYKPQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 420 gddvYIFDESiryniafprpeatEEEVEkaAHLAGI----------HEFV--IGLKDGYDTQVGErgirLSGGQKQRVAL 487
Cdd:PRK13409 408 ----YIKPDY-------------DGTVE--DLLRSItddlgssyykSEIIkpLQLERLLDKNVKD----LSGGELQRVAI 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 488 ARAVLADRPILILDEATSSVDAitEKEIQTNmRAI-----LTGKTAIIIAHRLSTIWGLADKIVVMD 549
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDV--EQRLAVA-KAIrriaeEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
336-567 |
5.08e-11 |
|
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: 66.19 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 336 LSDVCFAYEGDYSEAdgaLHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDwNGSQLLEQFS 415
Cdd:TIGR01257 1940 LNELTKVYSGTSSPA---VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 416 YVPQGDDVYIFDESIRYNIAFPRPEAT-EEEVEKAAHLaGIHEfvIGLKDGYDTQVGErgirLSGGQKQRVALARAVLAD 494
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRGVpAEEIEKVANW-SIQS--LGLSLYADRLAGT----YSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 495 RPILILDEATSSVDAITEKEI-QTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKSHG 567
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
353-565 |
8.47e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAG--IDINDWN-GSQLLEQF------SYVPQGDDV 423
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSyRSQRIRMIfqdpstSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 YIFDESIRYNIAFpRPEATEEEVEKAAHLAGIhefvigLKD--GYDTQVgergirLSGGQKQRVALARAVLADRPILILD 501
Cdd:PRK15112 108 QILDFPLRLNTDL-EPEQREKQIIETLRQVGL------LPDhaSYYPHM------LAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 502 EATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
359-554 |
1.45e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 359 LEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAgidiNDWNGSQLlEQ----------FSYVPQG-------- 420
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARL-QQdpprnvegtvYDFVAEGieeqaeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 421 -------DDVyIFDESIRyNIAfpRPEATEEEVEkaaHLAG------IHEFVIGLKDGYDTQVGErgirLSGGQKQRVAL 487
Cdd:PRK11147 99 kryhdisHLV-ETDPSEK-NLN--ELAKLQEQLD---HHNLwqlenrINEVLAQLGLDPDAALSS----LSGGWLRKAAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 488 ARAVLADRPILILDEATS--SVDAITEKEiqtnmRAILTGKTAII-IAHRLSTIWGLADKIVVMDQGKKV 554
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNhlDIETIEWLE-----GFLKTFQGSIIfISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
356-552 |
1.70e-10 |
|
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: 63.69 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM-GTITVAGIDINDWNGSQLLEQ-FSYVPQG--DDVYIFDESIR 431
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDIRNPAQAIRAgIAMVPEDrkRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 YNIAFP--RPEATEEEVEKAAHLAGIHEFVIGLK---DGYDTQVGergiRLSGGQKQRVALARAVLADRPILILDEATSS 506
Cdd:TIGR02633 358 KNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKvktASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 818754182 507 VDAITEKEIQTNMRAILT-GKTAIIIAHRLSTIWGLADKIVVMDQGK 552
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
347-562 |
2.17e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.43 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 347 YSEADG---ALHDFSLEIEPGQIVALVGQSGAGKT-TIRKVITRLApcQMGTITVAGIdindWNGSQLL----------- 411
Cdd:PRK09473 22 FSTPDGdvtAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLA--ANGRIGGSAT----FNGREILnlpekelnklr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 412 -EQFSYVPQ------------GD---DVYI----------FDESIRYNIAFPRPEAteeevEKAAHLAGiHEFviglkdg 465
Cdd:PRK09473 96 aEQISMIFQdpmtslnpymrvGEqlmEVLMlhkgmskaeaFEESVRMLDAVKMPEA-----RKRMKMYP-HEF------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 466 ydtqvgergirlSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTG-KTAII-IAHRLSTIWGLAD 543
Cdd:PRK09473 163 ------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDLGVVAGICD 230
|
250
....*....|....*....
gi 818754182 544 KIVVMDQGKKVEEGTHEEL 562
Cdd:PRK09473 231 KVLVMYAGRTMEYGNARDV 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
354-567 |
2.36e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 60.23 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVI--------TRlapcqmGTITVAGIDINDwngsqlLEQfsyvpqgddvyi 425
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkyevTE------GEILFKGEDITD------LPP------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 fDESIRYNI--AFPRPEATEeevekaahlaGIH--EFVIGLKDGydtqvgergirLSGGQKQRVALARAVLADRPILILD 501
Cdd:cd03217 72 -EERARLGIflAFQYPPEIP----------GVKnaDFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 502 EATSSVDAITEKEIQTNMRAILT-GKTAIIIAHR---LSTIwgLADKIVVMDQGKKVEEGTHE--ELIKSHG 567
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREeGKSVLIITHYqrlLDYI--KPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
355-563 |
2.68e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 355 HDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQ------LLEQFSYVPQGDDVYIFDE 428
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarrigLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRY--NIAFPRPEATEEE-VEKAAHLAGIHEFViglKDGYDTqvgergirLSGGQKQRVALARAVLADRPILILDEATS 505
Cdd:PRK10253 104 RGRYphQPLFTRWRKEDEEaVTKAMQATGITHLA---DQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 506 SVDaITEkeiQTNMRAILT------GKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELI 563
Cdd:PRK10253 173 WLD-ISH---QIDLLELLSelnrekGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
353-562 |
4.06e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-FSYVP---QGDDVyIFDE 428
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPedrLGRGL-VPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRYNIAFPRpeATEEEVEKAAHL--AGIHEFVIGLKDGYD-------TQVGergiRLSGGQKQRVALARAVLADRPILI 499
Cdd:COG3845 352 SVAENLILGR--YRRPPFSRGGFLdrKAIRAFAEELIEEFDvrtpgpdTPAR----SLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818754182 500 LDEATSSVD--AITE--KEIqTNMRAilTGKTAIIIAHRLSTIWGLADKIVVMDQGK-----KVEEGTHEEL 562
Cdd:COG3845 426 AAQPTRGLDvgAIEFihQRL-LELRD--AGAAVLLISEDLDEILALSDRIAVMYEGRivgevPAAEATREEI 494
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
363-554 |
5.28e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 363 PGQIVALVGQSGAGKTTIRKVIT-RLApcqMGTITvAGIDINdwNGSQLLEQFS----YVPQgDDVYI----FDESIRYN 433
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAeRVT---TGVIT-GGDRLV--NGRPLDSSFQrsigYVQQ-QDLHLptstVRESLRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 434 IAFPRP-EATEEE----VEKAAHLAGIHEFViglkdgyDTQVGERGIRLSGGQKQRVALArAVLADRP--ILILDEATSS 506
Cdd:TIGR00956 861 AYLRQPkSVSKSEkmeyVEEVIKLLEMESYA-------DAVVGVPGEGLNVEQRKRLTIG-VELVAKPklLLFLDEPTSG 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 818754182 507 VDAITEKEIQTNMRAIL-TGKTAIIIAHRLS-TIWGLADKIVVMDQGKKV 554
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLAdHGQAILCTIHQPSaILFEEFDRLLLLQKGGQT 982
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
353-555 |
9.26e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPcqMGTitvagidindWNGSQLLE----QFSYVPQGDD---VYI 425
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HGS----------YEGEILFDgevcRFKDIRDSEAlgiVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 426 FDE-------SIRYNIAFPRPEAT------EEEVEKAAHLAGIhefvIGLKDGYDTQVGERGIrlsgGQKQRVALARAVL 492
Cdd:NF040905 84 HQElalipylSIAENIFLGNERAKrgvidwNETNRRARELLAK----VGLDESPDTLVTDIGV----GKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 493 ADRPILILDEATSsvdAITEKEIQTNMRAILT----GKTAIIIAHRLSTIWGLADKIVVMDQGKKVE 555
Cdd:NF040905 156 KDVKLLILDEPTA---ALNEEDSAALLDLLLElkaqGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
355-552 |
1.09e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 355 HDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAP--CQmGTITVAG--IDINdwNGSQLLEQ-FSYVPQGDDVY--IFD 427
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrWE-GEIFIDGkpVKIR--NPQQAIAQgIAMVPEDRKRDgiVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 428 ESIRYNIAFP--RPEATEEEVEKAAHLAGIHEFVIGLKdgYDTQVGERGI-RLSGGQKQRVALARAVLADRPILILDEAT 504
Cdd:PRK13549 356 MGVGKNITLAalDRFTGGSRIDDAAELKTILESIQRLK--VKTASPELAIaRLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 818754182 505 SSVDAITEKEIQTNMRAILTGKTAII-IAHRLSTIWGLADKIVVMDQGK 552
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQGVAIIvISSELPEVLGLSDRVLVMHEGK 482
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
353-562 |
1.29e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.26 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRK----VIT--RLAPCQM----GTITVAGIDINDWNGSQ-----LLEQFSYV 417
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITgdKSAGSHIellgRTVQREGRLARDIRKSRantgyIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 418 PQ---GDDVYI--------FDESIRYniaFPRpeATEEEVEKAAHLAGIHEFViglkdgydtqvGERGIRLSGGQKQRVA 486
Cdd:PRK09984 99 NRlsvLENVLIgalgstpfWRTCFSW---FTR--EQKQRALQALTRVGMVHFA-----------HQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 487 LARAVLADRPILILDEATSSVDAITEKEIQTNMRAI--LTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEEL 562
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-565 |
1.65e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM-----GTITVAGIDI--NDWNGSQLLEQFSYVPQGDDVY-- 424
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFph 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 --IFDE---SIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGYDTQvgergirLSGGQKQRVALARAvLADRP-IL 498
Cdd:PRK14267 100 ltIYDNvaiGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARA-LAMKPkIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 499 ILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGKKVEEGTHEELIKS 565
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
354-508 |
3.15e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.82 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITvagidindwNGSQLleQFSYVPQgddvyifdeSIRYN 433
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL--RIGYVPQ---------KLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 434 IAFP---------RPEATEEEV------EKAAHLagiHEFVIGlkdgydtqvgergiRLSGGQKQRVALARAVLADRPIL 498
Cdd:PRK09544 80 TTLPltvnrflrlRPGTKKEDIlpalkrVQAGHL---IDAPMQ--------------KLSGGETQRVLLARALLNRPQLL 142
|
170
....*....|
gi 818754182 499 ILDEATSSVD 508
Cdd:PRK09544 143 VLDEPTQGVD 152
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
358-571 |
4.11e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 358 SLEIEPGQIVALVGQSGAGKTTIRKVItrlapcqmgtitvAGIDINDWNGSQllEQFSYvpqgDDVYIFDES-------I 430
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAI-------------CGVTKDNWRVTA--DRMRF----DDIDLLRLSprerrklV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNIA--FPRPEATEEEVEKAAH--------------------------LAGIHEfvIGLKDGYDTqVGERGIRLSGGQK 482
Cdd:PRK15093 88 GHNVSmiFQEPQSCLDPSERVGRqlmqnipgwtykgrwwqrfgwrkrraIELLHR--VGIKDHKDA-MRSFPYELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 483 QRVALARAvLADRP-ILILDEATSSVDAITEKEI--------QTNMRAILtgktaiIIAHRLSTIWGLADKIVVMDQGKK 553
Cdd:PRK15093 165 QKVMIAIA-LANQPrLLIADEPTNAMEPTTQAQIfrlltrlnQNNNTTIL------LISHDLQMLSQWADKINVLYCGQT 237
|
250
....*....|....*....
gi 818754182 554 VEEGTHEELIKS-HGIYAQ 571
Cdd:PRK15093 238 VETAPSKELVTTpHHPYTQ 256
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
353-557 |
8.01e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.86 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVI-TRLAPcQMGTITVAGIDindwnGSQLleqfsyvpqgdDVYIFDESIR 431
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAP-DAGEVHYRMRD-----GQLR-----------DLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 Y--------------------------NIAFP------------RPEATE--EEVEKAAhlagihefviglkdgydTQVG 471
Cdd:PRK11701 84 RrllrtewgfvhqhprdglrmqvsaggNIGERlmavgarhygdiRATAGDwlERVEIDA-----------------ARID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 472 ERGIRLSGGQKQRVALARaVLADRPILIL-DEATSSVDAITEKEIQTNMRAILT--GKTAIIIAHRLSTIWGLADKIVVM 548
Cdd:PRK11701 147 DLPTTFSGGMQQRLQIAR-NLVTHPRLVFmDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLLAHRLLVM 225
|
....*....
gi 818754182 549 DQGKKVEEG 557
Cdd:PRK11701 226 KQGRVVESG 234
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
354-558 |
8.78e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.76 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM--------GTITVAGIDINDWNGSQLLEQFSYVPQ-GDDVY 424
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 425 IFdeSIRYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLKDGyDTQVGERGIRLSGGQKQRVALARAVLADRP-------- 496
Cdd:PRK13547 97 AF--SAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqpp 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 497 -ILILDEATSSVDAITEKEIQTNMRAIL----TGKTAIIiaHRLSTIWGLADKIVVMDQGKKVEEGT 558
Cdd:PRK13547 174 rYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIV--HDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
352-564 |
9.14e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 352 GALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-FSYVPQG--DDVYIFDE 428
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITESrrDNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRYNIAFPRP--------------EATEEEV-EKAAHLAGIHEFVIglkdgyDTQVGErgirLSGGQKQRVALARAVLA 493
Cdd:PRK09700 357 SIAQNMAISRSlkdggykgamglfhEVDEQRTaENQRELLALKCHSV------NQNITE----LSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 494 DRPILILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGK------KVEEGTHEELIK 564
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVCDRIAVFCEGRltqiltNRDDMSEEEIMA 504
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
359-515 |
1.86e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.17 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 359 LEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQ-----------LLEQFSYVPQgddvyifd 427
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvgfVFQSFMLIPT-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 428 ESIRYNIAFP---RPEATEEEVEKAAHLAGihefVIGLkdgydtqvGER----GIRLSGGQKQRVALARAVLADRPILIL 500
Cdd:PRK10584 103 LNALENVELPallRGESSRQSRNGAKALLE----QLGL--------GKRldhlPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170
....*....|....*
gi 818754182 501 DEATSSVDAITEKEI 515
Cdd:PRK10584 171 DEPTGNLDRQTGDKI 185
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
354-554 |
1.86e-08 |
|
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: 54.56 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTI------RK---VITrlapcqmGTITVagidindwNGSQLLEQFS----YVPQg 420
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLldvlagRKtagVIT-------GEILI--------NGRPLDKNFQrstgYVEQ- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 421 DDVYIfdesiryniafprPEAT-EEEVEKAAHLagihefviglkdgydtqvgeRGirLSGGQKQRVALARAVLADRPILI 499
Cdd:cd03232 87 QDVHS-------------PNLTvREALRFSALL--------------------RG--LSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 500 LDEATSSVDAITEKEIqtnMRAI----LTGKTAIIIAHRLS-TIWGLADKIVVMDQGKKV 554
Cdd:cd03232 132 LDEPTSGLDSQAAYNI---VRFLkklaDSGQAILCTIHQPSaSIFEKFDRLLLLKRGGKT 188
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
363-554 |
3.37e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 363 PGQIVALVGQSGAGKTTIRKVitrLAPCQMGTITVAGIDINDWNGSQllEQFS----YVPQGD----DVYIfDESIRYNi 434
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDV---LAGRKTGGYIEGDIRISGFPKKQ--ETFArisgYCEQNDihspQVTV-RESLIYS- 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 435 AFPR--PEATEEE----VEKAAHLagihefvIGLKDGYDTQVGERGIR-LSGGQKQRVALARAVLADRPILILDEATSSV 507
Cdd:PLN03140 978 AFLRlpKEVSKEEkmmfVDEVMEL-------VELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 818754182 508 DAiteKEIQTNMRAIL----TGKTAIIIAHRLST-IWGLADKIVVMDQGKKV 554
Cdd:PLN03140 1051 DA---RAAAIVMRTVRntvdTGRTVVCTIHQPSIdIFEAFDELLLMKRGGQV 1099
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
354-564 |
3.63e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.95 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTtirkvitRLApcqM------------GTITVAGIDINDWNGSQLLEQ-FSYVPQG 420
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRT-------ELA---MsvfgrsygrnisGTVFKDGKEVDVSTVSDAIDAgLAYVTED 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 421 DDVY--IFDESIRYNIAfprpeateeevekAAHLAGIHEFVIgLKDGYDTQVGER-----GIR----------LSGGQKQ 483
Cdd:NF040905 346 RKGYglNLIDDIKRNIT-------------LANLGKVSRRGV-IDENEEIKVAEEyrkkmNIKtpsvfqkvgnLSGGNQQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 484 RVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMDQGKKV-----EEG 557
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKGVIVISSELPELLGMCDRIYVMNEGRITgelprEEA 491
|
....*..
gi 818754182 558 THEELIK 564
Cdd:NF040905 492 SQERIMR 498
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
353-564 |
4.86e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-FSYVPQGDDVyIFDESIR 431
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNL-VLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 YNIAFPRPEATEEEVEKAAhlagIHEFVIGLKDGYDTQVG--ERGIRLSGGQKQRVALARAVLADRPILILDEATSSvda 509
Cdd:PRK10982 92 DNMWLGRYPTKGMFVDQDK----MYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS--- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 510 ITEKEIQTNMRAILT----GKTAIIIAHRLSTIWGLADKIVVMDQGK-----KVEEGTHEELIK 564
Cdd:PRK10982 165 LTEKEVNHLFTIIRKlkerGCGIVYISHKMEEIFQLCDEITILRDGQwiatqPLAGLTMDKIIA 228
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
45-282 |
6.01e-08 |
|
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: 54.46 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 45 GTGVAPWIWVVLILGL----------LIFDEFNMRLDNafdwHIISKQSHPIFRHLklsaitkflkMNIP--WHHQHNSG 112
Cdd:cd18583 29 GSGKSPWKEIGLYVLLrflqsggglgLLRSWLWIPVEQ----YSYRALSTAAFNHV----------MNLSmdFHDSKKSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 113 tlvgkvgdGVWKTLD----IIDVMSW---EFVPTVVQTVISLIPLFII-SPWVALVAIITFVLFAWLTLKGNREKQPFRS 184
Cdd:cd18583 95 --------EVLKAIEqgssINDLLEQilfQIVPMIIDLVIAIVYLYYLfDPYMGLIVAVVMVLYVWSTIKLTSWRTKLRR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 185 KRQDYYEEEWNKSIASVQSVETNLMFGQQP----RLlndqavihngiiSEALKEHRLGIFKYNRWRIrvltiarriilvv 260
Cdd:cd18583 167 DMIDADREERSILTESLLNWETVKYFNREPyekeRY------------REAVKNYQKAERKYLFSLN------------- 221
|
250 260
....*....|....*....|..
gi 818754182 261 wILQLIQGSLTIAGLIFVSVLV 282
Cdd:cd18583 222 -LLNAVQSLILTLGLLAGCFLA 242
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
16-288 |
1.34e-07 |
|
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: 53.03 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 16 FYVFILLAFLYETVQLGASYVISLVV-TLFGTGVAPW----IWVVLILGLLIFDEFNMRLDNAFDWHIISKQShpifRHL 90
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdVLLPDGDPETqalnVYSLALLLLGLAQFILSFLQSYLLNHTGERLS----RRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 91 KLSAITKFLKMNIPWHHQHNSGTLVGKVGDGVwktlDIIDVMSWEFVPTVVQTVISLIPLFII----SPWVALVAIITFV 166
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDT----SKIRDGLGEKLGLLFQSLATIVGGIIVmfyyGWKLTLVLLAVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 167 LFAWLTLKGNREKQPFRSKRQDYYEEEWNKSIASVQSVETNLMFGQQPRLLNdqavihngIISEALKEHRLGIFKYNRWR 246
Cdd:pfam00664 153 LYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELE--------KYDKALEEALKAGIKKAVAN 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 818754182 247 IRVLTIARRIILVVWIL-------QLIQGSLTIAGLIFVSVLVERLFNS 288
Cdd:pfam00664 225 GLSFGITQFIGYLSYALalwfgayLVISGELSVGDLVAFLSLFAQLFGP 273
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
353-508 |
3.53e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTI-------RKVitrlapcQMGTITVAGIDINDWNG-SQLLEQFSYVPQ--GDD 422
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLlsliagaRKI-------QQGRVEVLGGDMADARHrRAVCPRIAYMPQglGKN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 423 VYiFDESIRYNIAF-------PRPE----------ATeeevekaahlaGIHEFViglkdgyDTQVGergiRLSGGQKQRV 485
Cdd:NF033858 89 LY-PTLSVFENLDFfgrlfgqDAAErrrridellrAT-----------GLAPFA-------DRPAG----KLSGGMKQKL 145
|
170 180
....*....|....*....|...
gi 818754182 486 ALARAVLADRPILILDEATSSVD 508
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
353-564 |
4.31e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 353 ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQ-FSYVPQ---GDDVYIFdE 428
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgFALVTEerrSTGIYAY-L 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 429 SIRYN--IAFPRPEATEEEVEKAAHLAGIHEFVIGLKD----GYDTQVGErgirLSGGQKQRVALARAVLADRPILILDE 502
Cdd:PRK10982 342 DIGFNslISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRvktpGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818754182 503 ATSSVDAITEKEI-QTNMRAILTGKTAIIIAHRLSTIWGLADKIVVMDQGK-----KVEEGTHEELIK 564
Cdd:PRK10982 418 PTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvagivDTKTTTQNEILR 485
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
315-537 |
4.91e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 315 EPEPIETGSIQsVPAGP-IG---VSLSDVCFAYeGDYSEADgalhDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPC 390
Cdd:TIGR03719 301 FQKRNETAEIY-IPPGPrLGdkvIEAENLTKAF-GDKLLID----DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 391 QMGTITVagidindwnGSQLleQFSYVPQGDDVYIFDESIRyniafprpeateEEVEkaahlAGIHEFVIGLKD------ 464
Cdd:TIGR03719 375 DSGTIEI---------GETV--KLAYVDQSRDALDPNKTVW------------EEIS-----GGLDIIKLGKREipsray 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 465 -------GYDTQ--VGErgirLSGGQKQRVALARAVLADRPILILDEATSSVDaitekeIQTnMR----AILT-GKTAII 530
Cdd:TIGR03719 427 vgrfnfkGSDQQkkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD------VET-LRaleeALLNfAGCAVV 495
|
250
....*....|...
gi 818754182 531 IAH------RLST 537
Cdd:TIGR03719 496 ISHdrwfldRIAT 508
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
363-545 |
7.39e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 363 PGQIVALVGQSGAGKTTI-RKVITRLAPCQMGTITVAGIDINDWNGSQLLEqfsyvpqgddvyifdesiryniafprpea 441
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLaRALARELGPPGGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 442 teeevekaahlagihefviglkdgydTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRA 521
Cdd:smart00382 52 --------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEEL 105
|
170 180 190
....*....|....*....|....*....|.
gi 818754182 522 IL-------TGKTAIIIAHRLSTIWGLADKI 545
Cdd:smart00382 106 RLllllkseKNLTVILTTNDEKDLGPALLRR 136
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
328-561 |
8.70e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 328 PAGPIGVSLSDVcfayegdysEADGALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAG--IDINDw 405
Cdd:PRK11288 252 PLGEVRLRLDGL---------KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRS- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 406 ngsqlleqfsyvPQgddvyifdESIRYNIAFPrPE-----------ATEEEVEKAAHLAGIHEFVIgLKDGYDTQVGERG 474
Cdd:PRK11288 322 ------------PR--------DAIRAGIMLC-PEdrkaegiipvhSVADNINISARRHHLRAGCL-INNRWEAENADRF 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 475 IR---------------LSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQtnmrAIL-----TGKTAIIIAHR 534
Cdd:PRK11288 380 IRslniktpsreqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIY----NVIyelaaQGVAVLFVSSD 455
|
250 260
....*....|....*....|....*..
gi 818754182 535 LSTIWGLADKIVVMDQGKKVEEGTHEE 561
Cdd:PRK11288 456 LPEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
352-508 |
9.92e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 352 GALHdfsLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDINDWNGSQLLEQFSYVPQGDDvyifDESIR 431
Cdd:PRK13543 28 GPLD---FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKA----DLSTL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818754182 432 YNIAFprpeATEEEVEKAAHLAGIHEFVIGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPILILDEATSSVD 508
Cdd:PRK13543 101 ENLHF----LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
357-548 |
1.00e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 357 FSLEI-EPGQIVALVGQSGAGKTTIRKVIT-RLAPCQMGTITVAGID--INDWNGSQLLEQFSYVPQGDdvyifdesIR- 431
Cdd:PRK13409 91 YGLPIpKEGKVTGILGPNGIGKTTAVKILSgELIPNLGDYEEEPSWDevLKRFRGTELQNYFKKLYNGE--------IKv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 -----YNIAFPRP-EATEEEVEKAAHLAGIHEFVI---GLKdgydtQVGERGIR-LSGGQKQRVALARAVLADRPILILD 501
Cdd:PRK13409 163 vhkpqYVDLIPKVfKGKVRELLKKVDERGKLDEVVerlGLE-----NILDRDISeLSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 818754182 502 EATSSVDaITEKeiqTNM----RAILTGKTAIIIAHRLSTIWGLADKIVVM 548
Cdd:PRK13409 238 EPTSYLD-IRQR---LNVarliRELAEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
471-562 |
1.17e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 471 GERGIRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL-TGKTAIIIAHRLSTIWGLADKIVVMD 549
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQLAHELTVID 218
|
90
....*....|...
gi 818754182 550 QGKKVEEGTHEEL 562
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
362-548 |
1.95e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.29 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 362 EPGQIVALVGQSGAGKTTIRKVIT-RLAPcQMGTITvagiDINDWN-------GSQLLEQFSYVPQGD-DVYIfdeSIRY 432
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgKLKP-NLGKFD----DPPDWDeildefrGSELQNYFTKLLEGDvKVIV---KPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 433 NIAFPRP-EATEEEVEKAAHLAGIHEFVIGLKDgyDTQVGERGI-RLSGGQKQRVALARAVLADRPILILDEATSSVD-- 508
Cdd:cd03236 96 VDLIPKAvKGKVGELLKKKDERGKLDELVDQLE--LRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLDik 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 818754182 509 -----AITEKEIQTNMRAIltgktaIIIAHRLSTIWGLADKIVVM 548
Cdd:cd03236 174 qrlnaARLIRELAEDDNYV------LVVEHDLAVLDYLSDYIHCL 212
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
87-309 |
2.15e-06 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 49.47 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 87 FRHLklsaitkfLKMNIPWHHQHNSGTLVGKVGDGVWKTLDIIDVMSWEFVPTVVQTVISLIPLFIISPWVALVAIITFV 166
Cdd:cd07346 79 FRHL--------QRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 167 LFAWLTLKGNREKQPFRSKRQDYYEEEWNKSIASVQSVETNLMFGQQPRLLNDQAVIHNGIISEALKEHRLGIFKYNRWR 246
Cdd:cd07346 151 LYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818754182 247 IrVLTIARRIILVVWILQLIQGSLTIAGLIFVSVLVERLFNSCWRFARLLDRAAENSEGAERL 309
Cdd:cd07346 231 L-LTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
356-539 |
3.90e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.75 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVagidinDWNGSQLleqfsYVPQGDdvYIFDESIRYNIA 435
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK------PAKGKLF-----YVPQRP--YMTLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 436 FP-RPEATEEEVEKAAHLAGIHEfVIGLKDGYDTQVGERGIR-----LSGGQKQRVALARAVLADRPILILDEATSSVDA 509
Cdd:TIGR00954 537 YPdSSEDMKRRGLSDKDLEQILD-NVQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180 190
....*....|....*....|....*....|
gi 818754182 510 ITEKEIQTNMRAIltGKTAIIIAHRlSTIW 539
Cdd:TIGR00954 616 DVEGYMYRLCREF--GITLFSVSHR-KSLW 642
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
354-515 |
7.29e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVIT-RLAPcQMGTITVA-GIDINDWNGSQLleqfsyvpqgdDVYIFDESIR 431
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAgELAP-VSGEIGLAkGIKLGYFAQHQL-----------EFLRADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 YNIAFPRPEATEEEVEKaaHLAGIhefviGLKDgydTQVGERGIRLSGGQKQRVALARAVLADRPILILDEATSSVD--- 508
Cdd:PRK10636 396 QHLARLAPQELEQKLRD--YLGGF-----GFQG---DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldm 465
|
....*....
gi 818754182 509 --AITEKEI 515
Cdd:PRK10636 466 rqALTEALI 474
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
354-563 |
8.02e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIrkvITRLAPCQMGTITVAGiDINdWNGSQLLEqfsYVPQGDDVYIFDESI--- 430
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTL---LLALAGKLDPSLKVSG-EIT-YNGYRLNE---FVPRKTSAYISQNDVhvg 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 -------------------RYNI----------AFPRPEATEEEVEKAAHLAGIHEFVI--------GLKDGYDTQVGER 473
Cdd:PLN03140 253 vmtvketldfsarcqgvgtRYDLlselarrekdAGIFPEAEVDLFMKATAMEGVKSSLItdytlkilGLDICKDTIVGDE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 474 GIR-LSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAILTGKTAIIIAHRLS---TIWGLADKIVVMD 549
Cdd:PLN03140 333 MIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapETFDLFDDIILLS 412
|
250
....*....|....
gi 818754182 550 QGKKVEEGTHEELI 563
Cdd:PLN03140 413 EGQIVYQGPRDHIL 426
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
354-509 |
9.14e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVItrlapcqmgtitvAGIDiNDWNGSQLLEQ---FSYVPQ----------- 419
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVD-KDFNGEARPQPgikVGYLPQepqldptktvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 420 -------GDDVYIFDESIRYNIAFPRPEATEEEV-EKAAHLagihEFVIGLKDGY--DTQVgERGI-------------R 476
Cdd:TIGR03719 87 enveegvAEIKDALDRFNEISAKYAEPDADFDKLaAEQAEL----QEIIDAADAWdlDSQL-EIAMdalrcppwdadvtK 161
|
170 180 190
....*....|....*....|....*....|...
gi 818754182 477 LSGGQKQRVALARAVLADRPILILDEATSSVDA 509
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
362-548 |
1.12e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 362 EPGQIVALVGQSGAGKTTIRKVIT-RLAPcQMGTITVAGidinDWN-------GSQLLEQF----------SYVPQgddv 423
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSgELKP-NLGDYDEEP----SWDevlkrfrGTELQDYFkklangeikvAHKPQ---- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 424 YIfdesirYNIafprPEA----TEEEVEKAAHLAGIHEFV--IGLKDGYDTQVGErgirLSGGQKQRVALARAVLADRPI 497
Cdd:COG1245 168 YV------DLI----PKVfkgtVRELLEKVDERGKLDELAekLGLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 818754182 498 LILDEATSSVDaITEKeiqTNM-RAI--LT--GKTAIIIAHRLSTIWGLADKIVVM 548
Cdd:COG1245 234 YFFDEPSSYLD-IYQR---LNVaRLIreLAeeGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
354-521 |
3.59e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.94 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAGIDInDWNGSQLLEQFSYVPQ--GDDVYI-FDESI 430
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHrsGINPYLtLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 431 RYNIAFPRPEATEEEVEKAAHLAGIHEFVIGLkdgydtqvgergirLSGGQKQRVALARAVLADRPILILDEATSSVDAI 510
Cdd:PRK13540 96 LYDIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170
....*....|.
gi 818754182 511 TEKEIQTNMRA 521
Cdd:PRK13540 162 SLLTIITKIQE 172
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
349-508 |
4.77e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 349 EADG---------ALHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVAG--IDINDWN-----G--SQl 410
Cdd:NF033858 268 EARGltmrfgdftAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIAtrrrvGymSQ- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 411 leQFSyvpqgddvyIFDE-SIRYNIA-----FPRPEA-TEEEVEKAahlagIHEFviGLKDGYDTQVGergiRLSGGQKQ 483
Cdd:NF033858 347 --AFS---------LYGElTVRQNLElharlFHLPAAeIAARVAEM-----LERF--DLADVADALPD----SLPLGIRQ 404
|
170 180
....*....|....*....|....*
gi 818754182 484 RVALARAVLADRPILILDEATSSVD 508
Cdd:NF033858 405 RLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
87-174 |
7.88e-05 |
|
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: 44.91 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 87 FRHLKLSAITKFLKMNIPWHHQHNSGTLVGKVGDGVWKTLDIIDVMSWEFVPTVVQ-TVISLIPLFIISPWVALVAIITF 165
Cdd:cd18560 70 YRELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLElIVVSVVFAFHFGAWLALIVFLSV 149
|
....*....
gi 818754182 166 VLFAWLTLK 174
Cdd:cd18560 150 LLYGVFTIK 158
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
475-547 |
8.07e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.71 E-value: 8.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 475 IRLSGGQKQRVALARAVLADRPILILDEATSSVDAITEKEIQTNMRAIL--TGKTAIIIAHRLSTIWGLADKIVV 547
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
306-385 |
8.79e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 306 AERLANLLLePEPIETGSIQSVPAGPIGVSLSDVCFAYeGDYSeadgALHDFSLEIEPGQIVALVGQSGAGKTTIRKVIT 385
Cdd:PRK10938 234 SEQLEGVQL-PEPDEPSARHALPANEPRIVLNNGVVSY-NDRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT 307
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
354-560 |
9.16e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQM--GTITVAGIDINDwngsqlLEQFSYVPQGddvyIFdESIR 431
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIleGDILFKGESILD------LEPEERAHLG----IF-LAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 432 YNIAFP---------------RPEATEEEVEKAAHLAGIHEF--VIGLKDGYDTQVGERGirLSGGQKQRVALARAVLAD 494
Cdd:CHL00131 92 YPIEIPgvsnadflrlaynskRKFQGLPELDPLEFLEIINEKlkLVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 495 RPILILDEATSSVDAITEKEIQTNMRAILTGKTAII-IAH--RLSTiWGLADKIVVMDQGKKVEEGTHE 560
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLD-YIKPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
369-533 |
1.26e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 369 LVGQSGAGKTTIRKVITR-LAPCQmGTITvagIDINDWNGSQLLEQFSYvpqgDDVYIFDESI------------RYNIa 435
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGdLEPSA-GNVS---LDPNERLGKLRQDQFAF----EEFTVLDTVImghtelwevkqeRDRI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 436 FPRPEATEEEVEKAAHLagihEFVIGLKDGY--DTQVGE----RGIRL----------SGGQKQRVALARAVLADRPILI 499
Cdd:PRK15064 103 YALPEMSEEDGMKVADL----EVKFAEMDGYtaEARAGElllgVGIPEeqhyglmsevAPGWKLRVLLAQALFSNPDILL 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 818754182 500 LDEATSSVDAITEKEIQTnmraILTGK--TAIIIAH 533
Cdd:PRK15064 179 LDEPTNNLDINTIRWLED----VLNERnsTMIIISH 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
430-563 |
3.40e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 430 IRY---NIAfprpEATEEEVEKAAH----LAGIHEFVIGLKD---GYdTQVGERGIRLSGGQKQRVALARAVLAD---RP 496
Cdd:TIGR00630 778 VKYkgkNIA----DVLDMTVEEAYEffeaVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRT 852
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818754182 497 ILILDEATSSV--DAItEKEIQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVMDQ------GKKVEEGTHEELI 563
Cdd:TIGR00630 853 LYILDEPTTGLhfDDI-KKLLEVLQRLVDKGNTVVVIEHNLDVI-KTADYIIDLGPeggdggGTVVASGTPEEVA 925
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
20-173 |
3.56e-04 |
|
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: 42.81 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 20 ILLAFLYETVQLGASYVISLVVTLFGTGVAPWIWVVLILGLLIFDEfnmrLDNAFDWHIISKQSHPIFRHLKLSAITKFL 99
Cdd:cd18551 5 LLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQA----VLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818754182 100 KMNIPWHHQHNSGTLVGKVGDGVWKTLDIIDVMSWEFVPTVVQTVISLIPLFIISPWVALVAIITFVLFAWLTL 173
Cdd:cd18551 81 RLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIIL 154
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
356-508 |
5.41e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 356 DFSLEIEPGQIVALVGQSGAGKTTIRKVITRLAPCQMGTITVagidindwnGSQLleQFSYVPQGddvyifdesiRYNIA 435
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI---------GETV--KLAYVDQS----------RDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 436 fprPEAT--EE-------------EVEKAAHLAGiheFviGLKdGYDTQ--VGErgirLSGGQKQRVALARAVLADRPIL 498
Cdd:PRK11819 401 ---PNKTvwEEisggldiikvgnrEIPSRAYVGR---F--NFK-GGDQQkkVGV----LSGGERNRLHLAKTLKQGGNVL 467
|
170
....*....|
gi 818754182 499 ILDEATSSVD 508
Cdd:PRK11819 468 LLDEPTNDLD 477
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
354-509 |
1.63e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 354 LHDFSLEIEPGQIVALVGQSGAGKTTIRKVItrlapcqmgtitvAGIDiNDWNG-SQLLEQFS--YVPQ----------- 419
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVD-KEFEGeARPAPGIKvgYLPQepqldpektvr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 420 -------GDDVYIFDesiRYN---IAFPRPEA-TEEEVEKAAHLagihEFVIGLKDGY--DTQVgERGI----------- 475
Cdd:PRK11819 89 enveegvAEVKAALD---RFNeiyAAYAEPDAdFDALAAEQGEL----QEIIDAADAWdlDSQL-EIAMdalrcppwdak 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 818754182 476 --RLSGGQKQRVALARAVLADRPILILDEATSSVDA 509
Cdd:PRK11819 161 vtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
77-186 |
1.66e-03 |
|
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: 40.56 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 77 HIISKQSHPIFRHLklsaitkfLKMNIPWHHQHNSGTLVGKVGDGVWKTLDIIDVMSWEFVPTVVQTVISLIPLFII-SP 155
Cdd:cd18582 68 RAVRRLALRVFRHL--------HSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLyGW 139
|
90 100 110
....*....|....*....|....*....|.
gi 818754182 156 WVALVAIITFVLFAWLTLKGNREKQPFRSKR 186
Cdd:cd18582 140 SYALITLVTVALYVAFTIKVTEWRTKFRREM 170
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
16-174 |
2.63e-03 |
|
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: 40.16 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 16 FYVFILLAFLYETVQLGASYVISLVV---TLFGT--GVAPWIWVVLILGLLIFdefnmrldnAFDW---HIISKQSHPIF 87
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdgpIAHGDrsALWPLVLLLLALGVAEA---------VLSFlrrYLAGRLSLGVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 88 RHLKLSAITKFLKMNIPWHHQHNSGTLVGKVgdgvwkTLDIIDVMSW-EFVP----TVVQTVISLIPLFIISPWVALVAI 162
Cdd:cd18543 72 HDLRTDLFAHLQRLDGAFHDRWQSGQLLSRA------TSDLSLVQRFlAFGPfllgNLLTLVVGLVVMLVLSPPLALVAL 145
|
170
....*....|..
gi 818754182 163 ITFVLFAWLTLK 174
Cdd:cd18543 146 ASLPPLVLVARR 157
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
477-557 |
4.19e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.46 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 477 LSGGQKQRVALARAVLADRP--ILILDEATSSVD-AITEKEIQTNMRAILTGKTAIIIAHRLSTIwGLADKIVVM----- 548
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHqQDINQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFgpgsg 166
|
90
....*....|
gi 818754182 549 -DQGKKVEEG 557
Cdd:cd03238 167 kSGGKVVFSG 176
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
106-309 |
5.24e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 39.03 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 106 HHQHNSGTLVGKVgdgvwkTLDII---DVMSWEFVPTVVQTVI---SLIPLFIISPWVALVAIITFVLFAWLTLK-GNRE 178
Cdd:cd18564 105 HDRRRTGDLLSRL------TGDVGaiqDLLVSGVLPLLTNLLTlvgMLGVMFWLDWQLALIALAVAPLLLLAARRfSRRI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 179 KQPFRSKRQDYYE-----EEWNKSIASVQSvetnlmFGQQPRLLNDQAVIHNGIISEALKEHRLgifKYNRWRIRVLTIA 253
Cdd:cd18564 179 KEASREQRRREGAlasvaQESLSAIRVVQA------FGREEHEERRFARENRKSLRAGLRAARL---QALLSPVVDVLVA 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818754182 254 RRIILVVWI--LQLIQGSLTIAGL-IFVSVLvERLFNSCWRFARLLDRAAENSEGAERL 309
Cdd:cd18564 250 VGTALVLWFgaWLVLAGRLTPGDLlVFLAYL-KNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
385-565 |
5.35e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 385 TRLAPcQMGTITVAGIDINDwngsqlleqFSYVPQgDDVYIFDESIRYNiafPRPEATEEEVekaahLAGIHEFVIGLKD 464
Cdd:TIGR00630 414 TRLKP-EALAVTVGGKSIAD---------VSELSI-REAHEFFNQLTLT---PEEKKIAEEV-----LKEIRERLGFLID 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818754182 465 -GYDTQVGERGIR-LSGGQKQRVALARAVLADRP--ILILDEATSSV---DaiTEKEIQTNMRAILTGKTAIIIAHRLST 537
Cdd:TIGR00630 475 vGLDYLSLSRAAGtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhqrD--NRRLINTLKRLRDLGNTLIVVEHDEDT 552
|
170 180 190
....*....|....*....|....*....|....
gi 818754182 538 IwGLADKIVVMDQ------GKKVEEGTHEELIKS 565
Cdd:TIGR00630 553 I-RAADYVIDIGPgagehgGEVVASGTPEEILAN 585
|
|
| |
