|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
158-734 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 616.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 158 RKLLGLAYPERRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQ 237
Cdd:COG1132 10 RRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA---LLLLLLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 238 TSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATF 317
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 318 VLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAG 397
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 398 FFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPF 477
Cdd:COG1132 247 FFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 478 NEGVIlNEKSFQGALEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHD 557
Cdd:COG1132 327 PPGAV-PLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 558 IRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGG 637
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 638 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEE 717
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEE 560
|
570
....*....|....*..
gi 171184400 718 LLSKpNGIYRKLMNKQS 734
Cdd:COG1132 561 LLAR-GGLYARLYRLQF 576
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
158-729 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 555.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 158 RKLLGLAYPERRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVD-YSDNLTRLCLGLSAVFLCGAAANAIRVYLM 236
Cdd:TIGR00958 150 FRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPaLASAIFFMCLLSIASSVSAGLRGGSFNYTM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 237 QtsgqRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLAT 316
Cdd:TIGR00958 230 A----RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTM 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 317 FVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARA 396
Cdd:TIGR00958 306 VTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 397 GFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLP 476
Cdd:TIGR00958 386 GYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 477 FNegVILNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH 556
Cdd:TIGR00958 466 LT--GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 557 DIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSG 636
Cdd:TIGR00958 544 PLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD---TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSG 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEalDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHE 716
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
570
....*....|...
gi 171184400 717 ELLSKPnGIYRKL 729
Cdd:TIGR00958 699 QLMEDQ-GCYKHL 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
146-733 |
3.14e-169 |
|
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: 498.84 E-value: 3.14e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 146 RLRPAAAGLPEARkllglayPERRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCG 225
Cdd:TIGR02204 2 RLRPLAALWPFVR-------PYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSK---DSSGLLNRYFAFLLVVALVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 226 AAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGIS 305
Cdd:TIGR02204 72 ALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 306 MMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVM 385
Cdd:TIGR02204 152 MMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 386 QLARKEAFARAGffgatgLSGNLIVLS------VLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGL 459
Cdd:TIGR02204 232 EAARQRIRTRAL------LTAIVIVLVfgaivgVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 460 GAGGRLWELLEREPKLPFNEGVILNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSL 539
Cdd:TIGR02204 306 GAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 540 LLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNF 619
Cdd:TIGR02204 386 LLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPD---ATDEEVEAAARAAHAHEFISAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 620 PQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNAN 699
Cdd:TIGR02204 463 PEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKAD 542
|
570 580 590
....*....|....*....|....*....|....
gi 171184400 700 MVAVLDQGKITEYGKHEELLSKpNGIYRKLMNKQ 733
Cdd:TIGR02204 543 RIVVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
174-465 |
2.19e-157 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 457.36 E-value: 2.19e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 174 AVGFLTMSSVISMSAPFFLGKIIDVIYTN--PTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSL 251
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKEsgDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 252 FSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVI 331
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 332 YGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVL 411
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 171184400 412 SVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
158-733 |
3.88e-157 |
|
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: 472.40 E-value: 3.88e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 158 RKLLGLAYPERRRLAAAVGFLTMSSVISMSAPFFLGKIID-VIytnPTVDYsDNLTRLCLGLSAVFLCGAAANAIRVYLM 236
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDrVL---PNQDL-STLWVLAIGLLLALLFEGLLRLLRSYLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 237 QTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSsDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLAT 316
Cdd:COG2274 221 LRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLAL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 317 FVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARA 396
Cdd:COG2274 300 VVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 397 GFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLP 476
Cdd:COG2274 380 LLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPERE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 477 FNEGVILNEKsFQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH 556
Cdd:COG2274 460 EGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 557 DIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSG 636
Cdd:COG2274 538 DLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD---ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSG 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHE 716
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHE 694
|
570
....*....|....*..
gi 171184400 717 ELLSKpNGIYRKLMNKQ 733
Cdd:COG2274 695 ELLAR-KGLYAELVQQQ 710
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
493-733 |
2.92e-143 |
|
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: 419.25 E-value: 2.92e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 572
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 573 VSQEPILFSCSIAENIAYGADDPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNP 652
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDA---TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 653 KILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNK 732
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKA 237
|
.
gi 171184400 733 Q 733
Cdd:cd03249 238 Q 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
158-733 |
1.16e-133 |
|
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: 407.18 E-value: 1.16e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 158 RKLLGLAYPERRRL-AAAVGFLtmssVISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLM 236
Cdd:TIGR02203 3 RRLWSYVRPYKAGLvLAGVAMI----LVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 237 QTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLAT 316
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 317 FVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARA 396
Cdd:TIGR02203 159 IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 397 GFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLp 476
Cdd:TIGR02203 239 ISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 477 fNEGVILNEKSfQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH 556
Cdd:TIGR02203 318 -DTGTRAIERA-RGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 557 DIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAddPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSG 636
Cdd:TIGR02203 395 DLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR--TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHE 716
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHN 552
|
570
....*....|....*..
gi 171184400 717 ELLSKpNGIYRKLMNKQ 733
Cdd:TIGR02203 553 ELLAR-NGLYAQLHNMQ 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
239-733 |
6.87e-117 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 363.96 E-value: 6.87e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 239 SGqRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFV 318
Cdd:PRK11176 93 SG-KVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLIL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 319 LSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGF 398
Cdd:PRK11176 172 IVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSIS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 399 FGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLpfN 478
Cdd:PRK11176 252 DPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEK--D 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 479 EGVILNEKSfQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI 558
Cdd:PRK11176 330 EGKRVIERA-KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 559 RQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQ 638
Cdd:PRK11176 408 RDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYS--REQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 639 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEEL 718
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
490
....*....|....*
gi 171184400 719 LSKpNGIYRKLMNKQ 733
Cdd:PRK11176 566 LAQ-NGVYAQLHKMQ 579
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
174-465 |
4.61e-116 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 351.09 E-value: 4.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 174 AVGFLTMSSVISMSAPFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFS 253
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKG---GDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 254 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYG 333
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 334 RYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSV 413
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 171184400 414 LYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd18557 238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
492-729 |
2.75e-115 |
|
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: 346.91 E-value: 2.75e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKN 651
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPG---ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 652 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKL 729
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
492-733 |
1.00e-107 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 327.65 E-value: 1.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKN 651
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD---ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 652 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMN 731
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWK 234
|
..
gi 171184400 732 KQ 733
Cdd:cd03253 235 AQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
137-734 |
1.54e-105 |
|
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: 334.87 E-value: 1.54e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 137 PAAPPGDKGRLRPAAAGLPEARKLLGLAYPERRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIytnpTVDYSDNLTRLCL 216
Cdd:COG5265 1 APSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAI----DALLSGAAALLVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 217 GLSAVF------LCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGEL---INRlssdtallGRSVT 287
Cdd:COG5265 77 PVGLLLaygllrLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIER--------GTKGI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 288 ENLsdglragaqasvgISMMFF-VSPNLATFVLSVVppvsIIAVIYG--------------------------RYLRKLT 340
Cdd:COG5265 149 EFL-------------LRFLLFnILPTLLEIALVAG----ILLVKYDwwfalitlvtvvlyiaftvvvtewrtKFRREMN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 341 KvtQDSlaQATQLAEERIGNVRTVRAFGKEMTEIEKYASkvdhvmQLARKEAFARAGFfgaTGLSGNLIVLSVLYKGGL- 419
Cdd:COG5265 212 E--ADS--EANTRAVDSLLNYETVKYFGNEAREARRYDE------ALARYERAAVKSQ---TSLALLNFGQALIIALGLt 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 420 -LMGSA-------HMTVGEL---SSFLMYAFwvgISIGGLSSFYSELMKGLGAGGRLWELLEREPK---------LPFNe 479
Cdd:COG5265 279 aMMLMAaqgvvagTMTVGDFvlvNAYLIQLY---IPLNFLGFVYREIRQALADMERMFDLLDQPPEvadapdappLVVG- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 480 gvilneksfQGALEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR 559
Cdd:COG5265 355 ---------GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 560 QLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQK 639
Cdd:COG5265 424 DVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD---ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEK 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 640 QRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELL 719
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELL 580
|
650
....*....|....*
gi 171184400 720 SKpNGIYRKLMNKQS 734
Cdd:COG5265 581 AQ-GGLYAQMWARQQ 594
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
158-721 |
4.66e-104 |
|
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: 329.80 E-value: 4.66e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 158 RKLLGLAYPERRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVdySDNLTRLCLGLSAVFLCGAAANAIRVYLMQ 237
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAP--LSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 238 TSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELInrlssdtALLGRSVtENLsDGLRAG----AQASVGISMM-----F 308
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELA-------TLLTEGV-EAL-DGYFARylpqLFLAALVPLLilvavF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 309 FVSPNLATFVLSVVP--PVSIIAViyGRYLRKLTkvtQDSLAQATQLAE---ERIGNVRTVRAFGKEmteiEKYASKVDH 383
Cdd:COG4988 155 PLDWLSGLILLVTAPliPLFMILV--GKGAAKAS---RRQWRALARLSGhflDRLRGLTTLKLFGRA----KAEAERIAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 384 VMQLARKE-------AFARAG---FFGAtgLSgnlIVLSVLYkGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYS 453
Cdd:COG4988 226 ASEDFRKRtmkvlrvAFLSSAvleFFAS--LS---IALVAVY-IGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYH 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 454 ELMKGLGAGGRLWELLEREPKLPFNEGVILNEKSfQGALEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGK 533
Cdd:COG4988 300 ARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 534 STVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAV 613
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD---ASDEELEAALEAAGLD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 614 AFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLS 693
Cdd:COG4988 454 EFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLA 533
|
570 580
....*....|....*....|....*...
gi 171184400 694 TIKNANMVAVLDQGKITEYGKHEELLSK 721
Cdd:COG4988 534 LLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
177-464 |
6.45e-104 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 319.97 E-value: 6.45e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 177 FLTMSSVISMSAPFFLGKIIDVIYTNPTVDYSD---NLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFS 253
Cdd:cd18780 4 ALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEalrALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 254 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYG 333
Cdd:cd18780 84 AIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 334 RYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSV 413
Cdd:cd18780 164 KYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLV 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 171184400 414 LYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 464
Cdd:cd18780 244 LWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVR 294
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
490-721 |
1.19e-102 |
|
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: 314.16 E-value: 1.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 490 GALEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 569
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFSCSIAENIAYGADDPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALL 649
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNA---TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 650 KNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 721
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
183-734 |
3.06e-98 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 318.61 E-value: 3.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 183 VISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAF 262
Cdd:TIGR01846 153 LFALVTPLLFQVVIDKVLVHRGLS---TLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGY 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 263 FDKTRTGELINRLSSdtallgrsvTENLSDGLRAGAQAS--------VGISMMFFVSPNLATFVLSVVPPVSIIAVIYGR 334
Cdd:TIGR01846 230 FESRRVGDTVARVRE---------LEQIRNFLTGSALTVvldllfvvVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGP 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 335 YLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVdhVMQLARKEAFARAGFFG--ATGLSGNLIVLS 412
Cdd:TIGR01846 301 ILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQL--AAYVAASFRVTNLGNIAgqAIELIQKLTFAI 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 413 VLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLErEPKLPFNEGVILNEKsFQGAL 492
Cdd:TIGR01846 379 LLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALPE-LRGAI 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:TIGR01846 457 TFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFSCSIAENIAYGadDPSsVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKN 651
Cdd:TIGR01846 535 VVLQENVLFSRSIRDNIALC--NPG-APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGN 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 652 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMN 731
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL-QGLYARLWQ 690
|
...
gi 171184400 732 KQS 734
Cdd:TIGR01846 691 QQS 693
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
242-731 |
1.05e-95 |
|
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: 307.85 E-value: 1.05e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 242 RIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLA-TFVLS 320
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALAlVLALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 321 VVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFG 400
Cdd:COG4987 165 LLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 401 ATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFNEG 480
Cdd:COG4987 245 LLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 481 VILNEKsfQGALEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQ 560
Cdd:COG4987 325 PAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 561 LNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQ 640
Cdd:COG4987 402 LDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD---ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 641 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 720
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
490
....*....|.
gi 171184400 721 KpNGIYRKLMN 731
Cdd:COG4987 559 Q-NGRYRQLYQ 568
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
492-708 |
7.56e-89 |
|
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: 275.80 E-value: 7.56e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFSCSIAENIaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLKN 651
Cdd:cd03228 80 YVPQDPFLFSGTIRENI---------------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 652 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGK 708
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
161-736 |
4.14e-87 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 286.09 E-value: 4.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 161 LGLAYPERRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVdysdnltrlcLGLSAVFLCGAAANAIRVYLMQTSG 240
Cdd:PRK13657 11 LQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDI----------FPLLAAWAGFGLFNIIAGVLVARHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 241 QRIVNRLR----TSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLAT 316
Cdd:PRK13657 81 DRLAHRRRlavlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 317 fVLSVvppVSIIAVIYGRYLRKLTKVTQDSL-AQATQLAE---ERIGNVRTVRAFGKEMTEIEKYASKVDHVM--QLARK 390
Cdd:PRK13657 161 -VLVV---LGIVYTLITTLVMRKTKDGQAAVeEHYHDLFAhvsDAIGNVSVVQSYNRIEAETQALRDIADNLLaaQMPVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 391 EAFARAGffGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAfwvGISIGGL---SSFYSELMKglgAGGRLWE 467
Cdd:PRK13657 237 SWWALAS--VLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFA---TLLIGRLdqvVAFINQVFM---AAPKLEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 468 LLEREPKLPFNE---GVIlNEKSFQGALEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLY 544
Cdd:PRK13657 309 FFEVEDAVPDVRdppGAI-DLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 545 DPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFN 624
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD---ATDEEMRAAAERAQAHDFIERKPDGYD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 625 TVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVL 704
Cdd:PRK13657 463 TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVF 542
|
570 580 590
....*....|....*....|....*....|..
gi 171184400 705 DQGKITEYGKHEELLSKpNGIYRKLMNKQSFI 736
Cdd:PRK13657 543 DNGRVVESGSFDELVAR-GGRFAALLRAQGML 573
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
483-709 |
2.39e-86 |
|
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: 271.65 E-value: 2.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 483 LNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN 562
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 563 PVWLRSKIGTVSQEPILFSCSIAENIAYGAddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRI 642
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGL---QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 643 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKI 709
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
492-733 |
4.98e-85 |
|
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: 268.59 E-value: 4.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI 570
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILFSCSIAENIAYGADDPSsvtAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLK 650
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMS---MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 651 NPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLM 730
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLY 234
|
...
gi 171184400 731 NKQ 733
Cdd:cd03252 235 QLQ 237
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
174-462 |
1.21e-79 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 256.32 E-value: 1.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 174 AVGFLTMSSVISMSAPFFLGKIIDVIYTNPTvdySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFS 253
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGS---REAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 254 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYG 333
Cdd:cd18572 78 SLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 334 RYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSV 413
Cdd:cd18572 158 RYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 171184400 414 LYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAG 462
Cdd:cd18572 238 LFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAA 286
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
232-733 |
1.62e-78 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 262.73 E-value: 1.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 232 RVYLMQTSGQRIVnRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALL----GRSVTeNLSDGLRAGAqaSVGISMM 307
Cdd:PRK10789 57 RVLLFGASYQLAV-ELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaaGEGVL-TLVDSLVMGC--AVLIVMS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 308 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHV--- 384
Cdd:PRK10789 133 TQISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTgkk 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 385 -MQLARKEAFARAGFFGATGLSgNLIVLSvlykGGLLM---GSahMTVGELSSFLMYafwVGISIG---GLSSFYSELMK 457
Cdd:PRK10789 213 nMRVARIDARFDPTIYIAIGMA-NLLAIG----GGSWMvvnGS--LTLGQLTSFVMY---LGLMIWpmlALAWMFNIVER 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 458 GLGAGGRLWELLEREPKLPFNEGVILNEKsfqGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVL 537
Cdd:PRK10789 283 GSAAYSRIRAMLAEAPVVKDGSEPVPEGR---GELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 538 SLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIR 617
Cdd:PRK10789 359 SLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD---ATQQEIEHVARLASVHDDIL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 618 NFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN 697
Cdd:PRK10789 436 RLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTE 515
|
490 500 510
....*....|....*....|....*....|....*.
gi 171184400 698 ANMVAVLDQGKITEYGKHEELLSKPnGIYRKLMNKQ 733
Cdd:PRK10789 516 ASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQ 550
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
177-731 |
1.06e-76 |
|
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: 261.21 E-value: 1.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 177 FLTMssVISMSAPFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSIL 256
Cdd:TIGR01193 166 IIVT--LISIAGSYYLQKIIDTYIPH---KMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLF 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 257 RQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGIsmmFFVSPNLATFVLSVVP-PVSIIAVIYgrY 335
Cdd:TIGR01193 241 ELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGL---FLVRQNMLLFLLSLLSiPVYAVIIIL--F 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 336 LRKLTKVTQDSLAQATQLAE---ERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFfGATGLSGNLIV-L 411
Cdd:TIGR01193 316 KRTFNKLNHDAMQANAVLNSsiiEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQ-QAIKAVTKLILnV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 412 SVLYKGGLLMGSAHMTVGELSSF-LMYAFWVGiSIGGLSSFYSELMKGLGAGGRLWE--LLEREpklpFNEGVILNEKS- 487
Cdd:TIGR01193 395 VILWTGAYLVMRGKLTLGQLITFnALLSYFLT-PLENIINLQPKLQAARVANNRLNEvyLVDSE----FINKKKRTELNn 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 488 FQGALEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLR 567
Cdd:TIGR01193 470 LNGDIVINDVSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPILFSCSIAENIAYGADDpsSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 647
Cdd:TIGR01193 548 QFINYLPQEPYIFSGSILENLLLGAKE--NVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDgRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLsKPNGIYR 727
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYA 703
|
....
gi 171184400 728 KLMN 731
Cdd:TIGR01193 704 SLIH 707
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
155-721 |
2.39e-76 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 257.34 E-value: 2.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 155 PEARKLLGLAYPERRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDysdnlTRLCLGLSAVF----LCGAAANA 230
Cdd:PRK10790 9 PTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLP-----LGLVAGLAAAYvglqLLAAGLHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 231 IRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFV 310
Cdd:PRK10790 84 AQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 311 SPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNV------RTVRAFGKEMTEiekyASKvDHV 384
Cdd:PRK10790 164 DWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMsviqqfRQQARFGERMGE----ASR-SHY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 385 MqlARKEAFARAGFFgatgLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFwvgISIGG--------LSSFYSELM 456
Cdd:PRK10790 239 M--ARMQTLRLDGFL----LRPLLSLFSALILCGLLMLFGFSASGTIEVGVLYAF---ISYLGrlneplieLTTQQSMLQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 457 KGLGAGGRLWELLERePKLPFNEGVILNEksfQGALEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTV 536
Cdd:PRK10790 310 QAVVAGERVFELMDG-PRQQYGNDDRPLQ---SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 537 LSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADdpssVTAEEIQRVAEVANAVAFI 616
Cdd:PRK10790 384 ASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD----ISEEQVWQALETVQLAELA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 617 RNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIK 696
Cdd:PRK10790 460 RSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIV 539
|
570 580
....*....|....*....|....*
gi 171184400 697 NANMVAVLDQGKITEYGKHEELLSK 721
Cdd:PRK10790 540 EADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
174-465 |
2.64e-76 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 247.40 E-value: 2.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 174 AVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFS 253
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTA---SLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 254 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYG 333
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 334 RYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSV 413
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 171184400 414 LYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd18576 238 LWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
490-709 |
8.73e-73 |
|
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: 235.56 E-value: 8.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 490 GALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 569
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFSCSIAENIAYGAddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALL 649
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA---PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 650 KNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKI 709
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
148-733 |
4.25e-71 |
|
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: 245.64 E-value: 4.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 148 RPAAAGLPEARKLLGLAYPERRRLAAAVGFLTM-SSVISMSAPFFLGKIID-VIytnPTVDySDNLTRLCLGLSAVFLCG 225
Cdd:TIGR03797 114 RPLPDKALGLRDLLRFALRGARRDLLAILAMGLlGTLLGMLVPIATGILIGtAI---PDAD-RSLLVQIALALLAAAVGA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 226 AA---ANAIRVYLMQTsgqRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTA----LLGRSVTENLSdglraGA 298
Cdd:TIGR03797 190 AAfqlAQSLAVLRLET---RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQirriLSGSTLTTLLS-----GI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 299 QASVGISMMFFVSPNLATF-VLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAE--ERIGNVRT----VRAFGKEM 371
Cdd:TIGR03797 262 FALLNLGLMFYYSWKLALVaVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQliNGISKLRVagaeNRAFARWA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 372 teiEKYASKVDHVMqlarkeAFARAGFFGATGLSGNLIVLSVL--YKGGLLMGSAHMTVGELSSFlMYAFwvGISIGGLS 449
Cdd:TIGR03797 342 ---KLFSRQRKLEL------SAQRIENLLTVFNAVLPVLTSAAlfAAAISLLGGAGLSLGSFLAF-NTAF--GSFSGAVT 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 450 SFYSELMKGLGAGgRLWE----LLEREPKlpfNEGVILNEKSFQGALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTA 524
Cdd:TIGR03797 410 QLSNTLISILAVI-PLWErakpILEALPE---VDEAKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 525 LVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAddpsSVTAEEIQ 604
Cdd:TIGR03797 484 IVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA----PLTLDEAW 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 605 RVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRT 684
Cdd:TIGR03797 560 EAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVT 637
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 171184400 685 VLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPnGIYRKLMNKQ 733
Cdd:TIGR03797 638 RIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE-GLFAQLARRQ 685
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
211-729 |
3.49e-70 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 243.31 E-value: 3.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 211 LTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSsdtalLGRSVTENL 290
Cdd:TIGR03796 193 LRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQ-----LNDQVAEFL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 291 SDGLRAGAQASVGI----SMMFFVSPNLATFVLSVVPpVSIIAVIYGRYLRKLT--KVTQDSlAQATQLAEERIGNVRTV 364
Cdd:TIGR03796 268 SGQLATTALDAVMLvfyaLLMLLYDPVLTLIGIAFAA-INVLALQLVSRRRVDAnrRLQQDA-GKLTGVAISGLQSIETL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 365 RAFGKEMTEIEK----YASKVDHVMQLARKEAFARAGFFGATGLSgNLIVLSVlykGGLLMGSAHMTVGELSSFLmyafw 440
Cdd:TIGR03796 346 KASGLESDFFSRwagyQAKLLNAQQELGVLTQILGVLPTLLTSLN-SALILVV---GGLRVMEGQLTIGMLVAFQ----- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 441 vgiSIggLSSFYSELMKGLGAGGRLWEL---LER---------EPKLPFNEGVILNEKS---FQGALEFKNVHFAYpARP 505
Cdd:TIGR03796 417 ---SL--MSSFLEPVNNLVGFGGTLQELegdLNRlddvlrnpvDPLLEEPEGSAATSEPprrLSGYVELRNITFGY-SPL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 506 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIA 585
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVR 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 586 ENIAYGadDPSsVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALD 665
Cdd:TIGR03796 571 DNLTLW--DPT-IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171184400 666 AENEYLVQEALDRlmDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPnGIYRKL 729
Cdd:TIGR03796 648 PETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVG-GAYARL 708
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
170-704 |
1.78e-68 |
|
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: 234.49 E-value: 1.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 170 RLAAAVGFLTMSSVISMSapFFLGKIID-VIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLR 248
Cdd:TIGR02857 6 ALLALLGVLGALLIIAQA--WLLARVVDgLISAGEPLA---ELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 249 TSLFSSILRQEVAFFDKTRTGELinrlssdTALLGRSVtENLsDGLRAGAQASVGISMM---------FFVSPNLATFVL 319
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGEL-------ATLALEGV-EAL-DGYFARYLPQLVLAVIvplailaavFPQDWISGLILL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 320 SVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEI-------EKYASKVDHVMQLARKEA 392
Cdd:TIGR02857 152 LTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAaairrssEEYRERTMRVLRIAFLSS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 393 FARAgFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVgelssfLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLERE 472
Cdd:TIGR02857 232 AVLE-LFATLSVALVAVYIGFRLLAGDLDLATGLFV------LLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 473 PkLPFNEGVILNEKSFQgALEFKNVHFAYPARPEVPifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIS 552
Cdd:TIGR02857 305 P-RPLAGKAPVTAAPAS-SLEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 553 LDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGV 632
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPD---ASDAEIREALERAGLDEFVAALPQGLDTPIGEGGA 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 633 LLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVL 704
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
490-713 |
3.36e-67 |
|
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: 220.83 E-value: 3.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 490 GALEFKNVHFAYpaRPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 568
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 647
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL-----DPfGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG 713
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
157-730 |
2.62e-66 |
|
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: 230.16 E-value: 2.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 157 ARKLLGLAYPERRRLAAAVGFLTMSsVISMSAPFFLGKIIDVIytnptVDYSDNLTRLclglsAVFLCGAAANAIRVYLM 236
Cdd:TIGR01192 8 VRALSYLNVHKNRVLLIVIANITLA-AITIAEPILFGRIIDAI-----SSKSDVLPTL-----ALWAGFGVFNTIAYVLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 237 QTSGQRIVNRLRTSL----FSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSP 312
Cdd:TIGR01192 77 AREADRLAHGRRATLlteaFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 313 NLaTFVLSVVppvSIIAVIYGRYLRKLTKVTQDSLAQATQL----AEERIGNVRTVRAFGK---EMTEIEKYASKVDHVm 385
Cdd:TIGR01192 157 RL-SIVLMVL---GILYILIAKLVMQRTKNGQAAVEHHYHNvfkhVSDSISNVSVVHSYNRieaETSALKQFTNNLLSA- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 386 QLARKEAFARAGffGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAfwvGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:TIGR01192 232 QYPVLDWWALAS--GLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFA---NLLIGRLDQMSGFITQIFEARAKL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 466 WELLEREPKL-----PFNEGVILNEKsfqGALEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL 540
Cdd:TIGR01192 307 EDFFDLEDSVfqreePADAPELPNVK---GAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 541 LRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFP 620
Cdd:TIGR01192 382 QRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREG---ATDEEVYEAAKAAAAHDFILKRS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 621 QGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANM 700
Cdd:TIGR01192 459 NGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADL 538
|
570 580 590
....*....|....*....|....*....|
gi 171184400 701 VAVLDQGKITEYGKHEELLSKpNGIYRKLM 730
Cdd:TIGR01192 539 VLFLDQGRLIEKGSFQELIQK-DGRFYKLL 567
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
172-464 |
7.48e-65 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 217.41 E-value: 7.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 172 AAAVGfltmSSVISMSAPFFLGKIIDVI--YTNPTV-DYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLR 248
Cdd:cd18574 3 LSALA----AALVNIQIPLLLGDLVNVIsrSLKETNgDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 249 TSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSII 328
Cdd:cd18574 79 NDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 329 AVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNL 408
Cdd:cd18574 159 GTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 409 IVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 464
Cdd:cd18574 239 IVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGAR 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
228-728 |
5.88e-63 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 229.15 E-value: 5.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 228 ANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRT--GELINRLSSDTALLGRSVTENLSdglragaqASVGIS 305
Cdd:PTZ00265 882 SETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNIV--------IFTHFI 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 306 MMFFVSPNLATFVLSVVppVSIIAVIYGRYLR------KLTK--------VTQDSLAQA-----------TQLAEERIGN 360
Cdd:PTZ00265 954 VLFLVSMVMSFYFCPIV--AAVLTGTYFIFMRvfairaRLTAnkdvekkeINQPGTVFAynsddeifkdpSFLIQEAFYN 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 361 VRTVRAFGKE---MTEIEKyasKVDHVMQLARKEAFARAGFFGATGlSGNLIVLSVLYK-GGLLMGSAHMTVGELSSFLM 436
Cdd:PTZ00265 1032 MNTVIIYGLEdyfCNLIEK---AIDYSNKGQKRKTLVNSMLWGFSQ-SAQLFINSFAYWfGSFLIRRGTILVDDFMKSLF 1107
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 437 YAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPF--NEGV-ILNEKSFQGALEFKNVHFAYPARPEVPIFQDF 513
Cdd:PTZ00265 1108 TFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVrdNGGIrIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDL 1187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD------------------------------------------------ 545
Cdd:PTZ00265 1188 TFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsg 1267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 546 ------PASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNF 619
Cdd:PTZ00265 1268 edstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED---ATREDVKRACKFAAIDEFIESL 1344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 620 PQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN 697
Cdd:PTZ00265 1345 PNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKR 1424
|
570 580 590
....*....|....*....|....*....|....*.
gi 171184400 698 ANMVAVLDQGK-----ITEYGKHEELLSKPNGIYRK 728
Cdd:PTZ00265 1425 SDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKK 1460
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
307-721 |
9.52e-63 |
|
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: 219.62 E-value: 9.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 307 MFFVSPNLATFVL--SVVppVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGkeMTE--IEKYASKVD 382
Cdd:COG4618 150 LFLFHPLLGLLALvgALV--LVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMG--MLPalRRRWQRANA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 383 HVMQLARKeAFARAGFFGATGLSGNLIVLS-VLYKGGLLMGSAHMTVGEL--SSFLMyafwvG-------ISIGGLSSFy 452
Cdd:COG4618 226 RALALQAR-ASDRAGGFSALSKFLRLLLQSaVLGLGAYLVIQGEITPGAMiaASILM-----GralapieQAIGGWKQF- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 453 selMKGLGAGGRLWELLEREPKLPfnEGVILNEksFQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSG 532
Cdd:COG4618 299 ---VSARQAYRRLNELLAAVPAEP--ERMPLPR--PKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSG 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 533 KSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIA-YGADDPssvtaEEIQRVAEVAN 611
Cdd:COG4618 371 KSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIArFGDADP-----EKVVAAAKLAG 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 612 AVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAH 690
Cdd:COG4618 446 VHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITH 525
|
410 420 430
....*....|....*....|....*....|.
gi 171184400 691 RLSTIKNANMVAVLDQGKITEYGKHEELLSK 721
Cdd:COG4618 526 RPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
155-737 |
1.85e-62 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 227.60 E-value: 1.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 155 PEARKLLGLAYperrrlaaavgfltMSSVISM-SAPFFLgKIIDVIYTNptVDYSDNLTRLCLGLSAVFLCGAAANAIRV 233
Cdd:PTZ00265 56 ASHRKLLGVSF--------------VCATISGgTLPFFV-SVFGVIMKN--MNLGENVNDIIFSLVLIGIFQFILSFISS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 234 YLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTgeliNRLSSDTALLGRSVTENLSDG---LRAGAQASVGISMM-FF 309
Cdd:PTZ00265 119 FCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIGTKfitIFTYASAFLGLYIWsLF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 310 VSPNLATFVLSVVPPVSIIAVIYGRYLrKLTKVTQDSLAQAT-QLAEERIGNVRTVRAFGKEMTEIEKYaskvdHVMQLA 388
Cdd:PTZ00265 195 KNARLTLCITCVFPLIYICGVICNKKV-KINKKTSLLYNNNTmSIIEEALVGIRTVVSYCGEKTILKKF-----NLSEKL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 389 RKEAFARAGFFGA--TGLSGNLIVLSvlYKGGLLMGSaHMTVGELSSF-----LMYAFWVGISIGGLSSFY--------- 452
Cdd:PTZ00265 269 YSKYILKANFMESlhIGMINGFILAS--YAFGFWYGT-RIIISDLSNQqpnndFHGGSVISILLGVLISMFmltiilpni 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 453 SELMKGLGAGGRLWELLEREPKLPFN-EGVILNEKSfqgALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGS 531
Cdd:PTZ00265 346 TEYMKSLEATNSLYEIINRKPLVENNdDGKKLKDIK---KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGC 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 532 GKSTVLSLLLRLYDPASGTISL-DGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAY-------------------- 590
Cdd:PTZ00265 423 GKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgn 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 591 ----GADDPSSVTAE---------------------------EIQRVAEVANAVA---FIRNFPQGFNTVVGEKGVLLSG 636
Cdd:PTZ00265 503 dsqeNKNKRNSCRAKcagdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVLihdFVSALPDKYETLVGSNASKLSG 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVL---------- 704
Cdd:PTZ00265 583 GQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvd 662
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 705 --------------------DQGK-----------------ITEYGKHEELLSKPNGIYRKLMNKQSFIS 737
Cdd:PTZ00265 663 vdiigedptkdnkennnknnKDDNnnnnnnnnnkinnagsyIIEQGTHDALMKNKNGIYYTMINNQKVSS 732
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
174-465 |
1.45e-61 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 208.11 E-value: 1.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 174 AVGFLTMSSVISMSAPFFLGKIIDVIYTNPTvdySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFS 253
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGN---TALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 254 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYG 333
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 334 RYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSV 413
Cdd:cd18575 158 RRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 171184400 414 LYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd18575 238 LWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
183-721 |
3.30e-59 |
|
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: 209.51 E-value: 3.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 183 VISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVFlcgAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAF 262
Cdd:TIGR01842 20 ILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFL---GLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 263 FDKtRTGELINrlssDTALLGRSVTenlSDGLRAGAQAS-----VGISMMFFVSPNLATFVLSVVPPVsiIAVIYGRYLR 337
Cdd:TIGR01842 97 GSG-DGLQALR----DLDQLRQFLT---GPGLFAFFDAPwmpiyLLVCFLLHPWIGILALGGAVVLVG--LALLNNRATK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 338 KLTKVTQDSLAQATQLAEERIGNVRTVRAFG-------KEMTEIEKYASkvdhvmqlARKEAFARAGFFGATGLSGNLIV 410
Cdd:TIGR01842 167 KPLKEATEASIRANNLADSALRNAEVIEAMGmmgnltkRWGRFHSKYLS--------AQSAASDRAGMLSNLSKYFRIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 411 LS-VLYKGGLLMGSAHMTVGEL--SSFLMYAFWVGI--SIGGLSSFyselMKGLGAGGRLWELLEREP------KLPFNE 479
Cdd:TIGR01842 239 QSlVLGLGAYLAIDGEITPGMMiaGSILVGRALAPIdgAIGGWKQF----SGARQAYKRLNELLANYPsrdpamPLPEPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 480 GVILNEksfqgalefkNVHFAyPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR 559
Cdd:TIGR01842 315 GHLSVE----------NVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 560 QLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQK 639
Cdd:TIGR01842 384 QWDRETFGKHIGYLPQDVELFPGTVAENIARFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 640 QRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEEL 718
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEV 540
|
...
gi 171184400 719 LSK 721
Cdd:TIGR01842 541 LAK 543
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
464-733 |
4.44e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 209.68 E-value: 4.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 464 RLWELLEREPKLPFNEGVilNEKSFQGALEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL 543
Cdd:PRK11160 313 RINEITEQKPEVTFPTTS--TAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 544 YDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtaeeiQRVAEVANAV--AFIRNFPQ 621
Cdd:PRK11160 390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASD------EALIEVLQQVglEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 622 GFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMV 701
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260 270
....*....|....*....|....*....|..
gi 171184400 702 AVLDQGKITEYGKHEELLSKpNGIYRKLMNKQ 733
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQ-QGRYYQLKQRL 574
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
177-465 |
4.69e-59 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 201.39 E-value: 4.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 177 FLTMSSVISMSAPFFLGKIIDVIytnpTVDYS-DNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSI 255
Cdd:cd18784 4 FLLAAAVGEIFIPYYTGQVIDGI----VIEKSqDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 256 LRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRY 335
Cdd:cd18784 80 VSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 336 LRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLY 415
Cdd:cd18784 160 YKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 171184400 416 KGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd18784 240 YGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
171-438 |
3.19e-58 |
|
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: 198.64 E-value: 3.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIytNPTVDYSDN-LTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRT 249
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL--LPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 250 SLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIA 329
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 330 VIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLI 409
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260
....*....|....*....|....*....
gi 171184400 410 VLSVLYKGGLLMGSAHMTVGELSSFLMYA 438
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
171-465 |
1.02e-55 |
|
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: 192.38 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL---LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAV 330
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 331 IYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIV 410
Cdd:cd07346 158 YFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 411 LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd07346 238 ALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
171-465 |
3.49e-55 |
|
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: 191.11 E-value: 3.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNptvdysDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAG------GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAV 330
Cdd:cd18551 75 LWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 331 IYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIV 410
Cdd:cd18551 155 PLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 411 LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd18551 235 LVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
492-709 |
4.71e-53 |
|
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: 180.88 E-value: 4.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFSCSIAENIaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLKN 651
Cdd:cd03246 80 YLPQDDELFSGSIAENI---------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 652 PKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNANMVAVLDQGKI 709
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
492-722 |
1.21e-52 |
|
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: 181.76 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPI--LFSCSIAENIAYGaddP--SSVTAEEI-QRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRIA 643
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFG---PenLGLPREEIrERVEEALELVgleHLADRPPH-----------ELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 644 IARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSK 721
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224
|
.
gi 171184400 722 P 722
Cdd:COG1122 225 Y 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
492-728 |
3.19e-52 |
|
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: 189.34 E-value: 3.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARP--EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV---WL 566
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 567 RSKIGTVSQEPilFSC-----SIAENIAYGADDPSSVTAEEI-QRVAEVANAV----AFIRNFPQGFntvvgekgvllSG 636
Cdd:COG1123 341 RRRVQMVFQDP--YSSlnprmTVGDIIAEPLRLHGLLSRAERrERVAELLERVglppDLADRYPHEL-----------SG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALDaeneYLVQEA-LDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 709
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNLLRDlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250
....*....|....*....
gi 171184400 710 TEYGKHEELLSKPNGIYRK 728
Cdd:COG1123 484 VEDGPTEEVFANPQHPYTR 502
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
158-692 |
3.28e-52 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 189.88 E-value: 3.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 158 RKLLGLAYPERRRLAAAV--GFLTMSSVISMSapFFLGKIIDVIYTNPTVDYsdnltrLCLGLSAVFLCGAAANAIRvYL 235
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVllGALALGSAVALL--GVSAWLISRAAEMPPVLY------LSVAAVAVRAFGIGRAVFR-YL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 236 MQTSGQ----RIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVS 311
Cdd:TIGR02868 73 ERLVGHdaalRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 312 PN-----LATFVLS--VVPPVSIIAV-IYGRYLRKL-TKVTQDSLAQATQLAEERIGN-----VRTVRAFGKEMTEIEKY 377
Cdd:TIGR02868 153 VPaalilAAGLLLAgfVAPLVSLRAArAAEQALARLrGELAAQLTDALDGAAELVASGalpaaLAQVEEADRELTRAERR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 378 ASKVDHVMQlarkeafaragffGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMK 457
Cdd:TIGR02868 233 AAAATALGA-------------ALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 458 GLGAGGRLWELLE-----REPKLPFNEGVILNEKSfqgaLEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSG 532
Cdd:TIGR02868 300 VRAAAERIVEVLDaagpvAEGSAPAAGAVGLGKPT----LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 533 KSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANA 612
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPD---ATDEELWAALERVGL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 613 VAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRL 692
Cdd:TIGR02868 451 ADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
171-465 |
2.72e-51 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 180.31 E-value: 2.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEA---LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAV 330
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 331 IYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAG------FFGATGL 404
Cdd:cd18552 158 RIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALssplmeLLGAIAI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 405 SGnlivlsVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd18552 238 AL------VLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
172-726 |
7.09e-51 |
|
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: 192.85 E-value: 7.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 172 AAAVG-FLTMSSVIsmsapFFLGKIIDVIYTN---------PTVDYSDNLTRLCLGLSAVF--LCGAAanaIRVYLMQTS 239
Cdd:TIGR00957 959 MKAIGlFITFLSIF-----LFVCNHVSALASNywlslwtddPMVNGTQNNTSLRLSVYGALgiLQGFA---VFGYSMAVS 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 240 --GQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsVGISMMFFVSPNLATF 317
Cdd:TIGR00957 1031 igGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNV-IGALIVILLATPIAAV 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 318 VlsvVPPVSIIAVIYGRYL----RKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAF 393
Cdd:TIGR00957 1110 I---IPPLGLLYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIV 1186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 394 ARAGFFGATGLSGNLIVL-SVLYKgglLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLERE 472
Cdd:TIGR00957 1187 ANRWLAVRLECVGNCIVLfAALFA---VISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETE 1263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 473 PKLPF--NEGVILNEKSFQGALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG 549
Cdd:TIGR00957 1264 KEAPWqiQETAPPSGWPPRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEG 1341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 550 TISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVG 628
Cdd:TIGR00957 1342 EIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL-----DPfSQYSDEEVWWALELAHLKTFVSALPDKLDHECA 1416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 629 EKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGK 708
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 1496
|
570
....*....|....*...
gi 171184400 709 ITEYGKHEELLSKpNGIY 726
Cdd:TIGR00957 1497 VAEFGAPSNLLQQ-RGIF 1513
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
492-690 |
8.71e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 176.16 E-value: 8.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFSCSIAENIAYgaddPSSVTAEEIQRvaevANAVAFIRNFpqGFNTVVGEKGV-LLSGGQKQRIAIARALLK 650
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPF----PFQLRERKFDR----ERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 171184400 651 NPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAH 690
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
514-733 |
1.14e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 186.59 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRlYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAd 593
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 594 dpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQ 673
Cdd:PRK11174 448 --PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 674 EALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQ 733
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
492-722 |
2.64e-49 |
|
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: 172.77 E-value: 2.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 567
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPILFSC-SIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIA 643
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVgleDKADAYPAQ-----------LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 644 IARALLKNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEE 717
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPET---TQSILALLRDinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
....*
gi 171184400 718 LLSKP 722
Cdd:cd03258 228 VFANP 232
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
190-465 |
4.53e-49 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 174.58 E-value: 4.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 190 FFLGKIIDVI--YTNPTVDYS---DNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFD 264
Cdd:cd18577 20 IVFGDLFDAFtdFGSGESSPDeflDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 265 KTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQ 344
Cdd:cd18577 100 KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 345 DSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSA 424
Cdd:cd18577 180 EAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDG 259
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 171184400 425 HMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd18577 260 EISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
177-464 |
5.19e-49 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 174.06 E-value: 5.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 177 FLTMSSVISMSAPFFLGKIIDVIYTnptvDYSDNLTRLCLGLSAVFLCGAAANA-IRVYLMQTSGQRIVNRLRTSLFSSI 255
Cdd:cd18590 4 FLTLAVICETFIPYYTGRVIDILGG----EYQHNAFTSAIGLMCLFSLGSSLSAgLRGGLFMCTLSRLNLRLRHQLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 256 LRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRY 335
Cdd:cd18590 80 VQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 336 LRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLY 415
Cdd:cd18590 160 HQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 171184400 416 KGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 464
Cdd:cd18590 240 CGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAK 288
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
492-713 |
1.22e-48 |
|
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: 170.76 E-value: 1.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 567
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPilFSC-----SIAENIA--YGADDPSSVTAEEIQRVAEVANAV----AFIRNFPQGfntvvgekgvlLSG 636
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVglpeEVLNRYPHE-----------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 713
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
171-441 |
1.35e-48 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 173.00 E-value: 1.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGG---GLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAV 330
Cdd:cd18542 78 LYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 331 IYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIV 410
Cdd:cd18542 158 VFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQI 237
|
250 260 270
....*....|....*....|....*....|.
gi 171184400 411 LSVLYKGGLLMGSAHMTVGELSSFLMYAFWV 441
Cdd:cd18542 238 VLVLWVGGYLVINGEITLGELVAFISYLWML 268
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
492-718 |
2.26e-48 |
|
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: 170.05 E-value: 2.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDIRQL--NPV 564
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 565 WLRSKIGTVSQEPILFSCSIAENIAYGADDPSSVTAEEI-QRVAEVANAVAFIRNfpqgfntvVGEK--GVLLSGGQKQR 641
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDE--------VKDRlhALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 642 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 718
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
492-722 |
2.89e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 173.73 E-value: 2.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 567
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPILF-SCSIAENIAYgaddP---SSVTAEEI-QRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQ 638
Cdd:COG1135 82 RKIGMIFQHFNLLsSRTVAENVAL----PleiAGVPKAEIrKRVAELLELVglsDKADAYPsQ------------LSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 639 KQRIAIARALLKNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEY 712
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPET---TRSILDLLKDinrelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
250
....*....|
gi 171184400 713 GKHEELLSKP 722
Cdd:COG1135 223 GPVLDVFANP 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
492-708 |
6.34e-48 |
|
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: 168.03 E-value: 6.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEV--PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrsK 569
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFSCSIAENIAYGAD-DPssvtaeeiQRVAEVANAVAF---IRNFPQGFNTVVGEKGVLLSGGQKQRIAIA 645
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfDE--------ERYEKVIKACALepdLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 646 RALLKNPKILLLDEATSALDAE-NEYLVQEAL-DRLMDGRTVLVIAHRLSTIKNANMVAVLDQGK 708
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
491-723 |
2.99e-46 |
|
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: 165.22 E-value: 2.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI 570
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPIL-FSCSIAENIAYG----ADDPSSVTAEEIQRVAEV---ANAVAFI-RNFPQgfntvvgekgvlLSGGQKQR 641
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphLGLFGRPSAEDREAVEEAlerTGLEHLAdRPVDE------------LSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 642 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEEL 718
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
....*
gi 171184400 719 LSKPN 723
Cdd:COG1120 226 LTPEL 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
492-713 |
4.41e-46 |
|
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: 162.10 E-value: 4.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIG 571
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFSCSIAENIaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekGVLLSGGQKQRIAIARALLKN 651
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL------------------------------------------GRRFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 652 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG 713
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
161-474 |
7.24e-46 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 166.09 E-value: 7.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 161 LGLAYPERRRLAaaVGFLtmSSVISMSAP----FFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLM 236
Cdd:cd18578 1 LKLNKPEWPLLL--LGLI--GAIIAGAVFpvfaILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 237 QTSGQRIVNRLRTSLFSSILRQEVAFFDKTR--TGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNL 314
Cdd:cd18578 77 GIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 315 ATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFA 394
Cdd:cd18578 157 ALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 395 RAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPK 474
Cdd:cd18578 237 SGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
493-708 |
1.35e-45 |
|
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: 160.10 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 572
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 573 VSQepilfscsiaeniaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLKNP 652
Cdd:cd00267 78 VPQ----------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 653 KILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNA-NMVAVLDQGK 708
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
492-721 |
1.91e-45 |
|
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: 162.72 E-value: 1.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 571
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFS-CSIAENIAYGA---DDPSSVTAEEIQRVAEVANAVAFIrnfpqgfNTVVGEkgvlLSGGQKQRIAIARA 647
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYFAelyGLFDEELKKRIEELIELLGLEEFL-------DRRVGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 721
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
493-708 |
3.33e-45 |
|
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: 160.71 E-value: 3.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 572
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 573 VSQEP--ILFSCSIAENIAYGAdDPSSVTAEEI-QRVAEVANAvafirnfpqgfntvVGEKGVL------LSGGQKQRIA 643
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGL-ENLGLPEEEIeERVEEALEL--------------VGLEGLRdrspftLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 644 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGK 708
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
492-721 |
4.88e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.38 E-value: 4.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 571
Cdd:COG1131 1 IEVRGLTKRYGDKTAL---DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILF-SCSIAENIAYGAD---DPSSVTAEEIQRVAEVANAVAFIrnfpqgfNTVVGEkgvlLSGGQKQRIAIARA 647
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRFFARlygLPRKEARERIDELLELFGLTDAA-------DRKVGT----LSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSK 721
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
490-713 |
1.15e-44 |
|
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: 159.11 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 490 GALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 568
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVAnavafirnfpqgfntvvgEKGVLLSGGQKQRIAIARA 647
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL-----DPfDEYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG 713
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
492-722 |
1.42e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 160.16 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI----RQLNPvwLR 567
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINK--LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPILFS-CSIAENIAYGaddPSSV------TAEEI-----QRV--AEVANAvafirnFP-Qgfntvvgekgv 632
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVTLA---PIKVkkmskaEAEERamellERVglADKADA------YPaQ----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 633 lLSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDrLM-----DGRTVLVIAHRLSTIKN-ANMVAVLDQ 706
Cdd:COG1126 137 -LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMrdlakEGMTMVVVTHEMGFAREvADRVVFMDG 211
|
250
....*....|....*.
gi 171184400 707 GKITEYGKHEELLSKP 722
Cdd:COG1126 212 GRIVEEGPPEEFFENP 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
491-722 |
1.51e-44 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 160.59 E-value: 1.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD--P---ASGTISLDGHDI--RQLNP 563
Cdd:COG1117 11 KIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 564 VWLRSKIGTVSQEPILFSCSIAENIAYGA---DDPSSVTAEEI-----QRVA---EVANavafirnfpqgfntVVGEKGV 632
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhGIKSKSELDEIveeslRKAAlwdEVKD--------------RLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 633 LLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAH------RLStiknaNMVAVLDQ 706
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYL 228
|
250
....*....|....*.
gi 171184400 707 GKITEYGKHEELLSKP 722
Cdd:COG1117 229 GELVEFGPTEQIFTNP 244
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
492-722 |
4.42e-44 |
|
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: 159.00 E-value: 4.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFS-CSIAENIAYgadDPSSVTAEEIQRVAEVANAVAFIRNFPQGF-NTVVGEkgvlLSGGQKQRIAIARALL 649
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIAL---VPKLLKWPKEKIRERADELLALVGLDPAEFaDRYPHE----LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 650 KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRL-STIKNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
491-711 |
5.33e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.90 E-value: 5.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPA-RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP----VW 565
Cdd:COG1136 4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelaRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 566 LRSKIGTVSQEPILFSC-SIAENIAYGADdPSSVTAEEI-QRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQ 640
Cdd:COG1136 84 RRRHIGFVFQFFNLLPElTALENVALPLL-LAGVSRKERrERARELLERVglgDRLDHRP-------SQ----LSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 641 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITE 711
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
491-723 |
1.07e-43 |
|
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: 157.83 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLR 567
Cdd:COG1127 5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPILF-SCSIAENIAYGADDPSSVTAEEI-QRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRI 642
Cdd:COG1127 82 RRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIrELVLEKLELVglpGAADKMP-------SE----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 643 AIARALLKNPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEE 717
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
....*.
gi 171184400 718 LLSKPN 723
Cdd:COG1127 229 LLASDD 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
491-731 |
1.71e-43 |
|
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: 157.27 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 569
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPilfscsiaeniaYGADDPSSvTAEEI--------------QRVAEVANAV----AFIRNFP-Qgfntvvgek 630
Cdd:COG1124 81 VQMVFQDP------------YASLHPRH-TVDRIlaeplrihglpdreERIAELLEQVglppSFLDRYPhQ--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 631 gvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIknANM---V 701
Cdd:COG1124 139 ---LSGGQRQRVAIARALILEPELLLLDEPTSALDV----SVQaEILNLLKDlreerGLTYLFVSHDLAVV--AHLcdrV 209
|
250 260 270
....*....|....*....|....*....|.
gi 171184400 702 AVLDQGKITEYGKHEELLSKPNGIY-RKLMN 731
Cdd:COG1124 210 AVMQNGRIVEELTVADLLAGPKHPYtRELLA 240
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
510-662 |
2.75e-43 |
|
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: 153.19 E-value: 2.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFS-CSIAENI 588
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171184400 589 AYGADDPSSVTAEEIQRVAEVANAVAfIRNFPqgfNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 662
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLA---DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
491-722 |
3.47e-43 |
|
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: 163.92 E-value: 3.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA---SGTISLDGHDIRQLNPVWLR 567
Cdd:COG1123 4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPI--LFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRI 642
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVgleRRLDRYPH-----------QLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 643 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 719
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
...
gi 171184400 720 SKP 722
Cdd:COG1123 232 AAP 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
492-721 |
5.87e-43 |
|
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: 156.44 E-value: 5.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW-LRSKI 570
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEP-ILFSCSIAEN-IAYGaddPSS--VTAEEI-QRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRI 642
Cdd:TIGR04520 80 GMVFQNPdNQFVGATVEDdVAFG---LENlgVPREEMrKRVDEALKLVgmeDFRDREPH-----------LLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 643 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 720
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
.
gi 171184400 721 K 721
Cdd:TIGR04520 226 Q 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
492-708 |
6.15e-43 |
|
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: 153.50 E-value: 6.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN--PVWLRSK 569
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFS-CSIAENIAYGaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARAL 648
Cdd:cd03229 78 IGMVFQDFALFPhLTVLENIALG------------------------------------------LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 649 LKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGK 708
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
171-464 |
1.82e-42 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 156.02 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNP----TVDYsDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNR 246
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLggggGVDF-SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 247 LRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVS 326
Cdd:cd18547 80 LRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 327 IIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVmqlarKEAFARAGFFG-----A 401
Cdd:cd18547 160 LVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEEL-----YKASFKAQFYSgllmpI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 402 TGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 464
Cdd:cd18547 235 MNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
492-690 |
1.96e-42 |
|
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: 153.40 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlrsKI 570
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIAR 646
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELVglsGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 171184400 647 ALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAH 690
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTH 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
492-723 |
4.10e-42 |
|
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: 153.04 E-value: 4.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---RS 568
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEPILF-SCSIAENIAYGADDPSSVTAEEI-QRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRIA 643
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIrEIVLEKLEAVglrGAEDLYP-------AE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 644 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLS 720
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
...
gi 171184400 721 KPN 723
Cdd:cd03261 227 SDD 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
492-713 |
7.94e-42 |
|
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: 151.52 E-value: 7.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRsKIG 571
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-PPERR-NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILF-SCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIARA 647
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVgleGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYG 713
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
491-723 |
1.39e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.78 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnpvwlRSKI 570
Cdd:COG1121 6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQepilfscsiaeNIAYGADDPSSV------------------TAEEIQRVAEVANAV---AFIrnfpqgfNTVVGE 629
Cdd:COG1121 78 GYVPQ-----------RAEVDWDFPITVrdvvlmgrygrrglfrrpSRADREAVDEALERVgleDLA-------DRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 630 kgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTI-KNANMVAVLDQG 707
Cdd:COG1121 140 ----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLLNRG 215
|
250
....*....|....*.
gi 171184400 708 KITeYGKHEELLSKPN 723
Cdd:COG1121 216 LVA-HGPPEEVLTPEN 230
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
171-437 |
2.34e-41 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 152.93 E-value: 2.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYSdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQ-GLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTAllgrSVTENLSDGLRAGAQAS---VGI-SMMFFVSPNLATFVLSVVPPVS 326
Cdd:cd18544 80 LFSHIQRLPLSFFDRTPVGRLVTRVTNDTE----ALNELFTSGLVTLIGDLlllIGIlIAMFLLNWRLALISLLVLPLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 327 IIAVIYGRYLRKLTKVTQDSLAQA-TQLAeERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLS 405
Cdd:cd18544 156 LATYLFRKKSRKAYREVREKLSRLnAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELL 234
|
250 260 270
....*....|....*....|....*....|..
gi 171184400 406 GNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 437
Cdd:cd18544 235 SSLALALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
234-731 |
4.39e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 162.45 E-value: 4.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 234 YLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSpn 313
Cdd:PLN03232 972 FWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS-- 1049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 314 laTFVLSVVPPVSII---AVIY----GRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKeMTEIEKYASKVDHVMQ 386
Cdd:PLN03232 1050 --TISLWAIMPLLILfyaAYLYyqstSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDR-MAKINGKSMDNNIRFT 1126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 387 LARKEAfARAGFFGATGLSGNLIVLSVLYkGGLLMGSAHMTVGELSS---FLMYAFWVGISIGGLSSFYSELMKGLGAGG 463
Cdd:PLN03232 1127 LANTSS-NRWLTIRLETLGGVMIWLTATF-AVLRNGNAENQAGFASTmglLLSYTLNITTLLSGVLRQASKAENSLNSVE 1204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 464 RLWELLEREPKLPfneGVILNEKS-----FQGALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVL 537
Cdd:PLN03232 1205 RVGNYIDLPSEAT---AIIENNRPvsgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSML 1279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 538 SLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFI 616
Cdd:PLN03232 1280 NALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-----DPfSEHNDADLWEALERAHIKDVI 1354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 617 RNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIK 696
Cdd:PLN03232 1355 DRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTII 1434
|
490 500 510
....*....|....*....|....*....|....*
gi 171184400 697 NANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMN 731
Cdd:PLN03232 1435 DCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
492-709 |
5.28e-41 |
|
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: 149.18 E-value: 5.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---- 566
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 567 RSKIGTVSQE----PILfscSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirNFPQGFNTVVGEkgvlLSGGQKQRI 642
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEELLERV----GLGDRLNHYPSE----LSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 643 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIKNANMVAVLDQGKI 709
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
493-713 |
5.47e-41 |
|
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: 147.97 E-value: 5.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 572
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 573 VSQepilfscsiaeniaygaddpssvtaeeiqrVAEVANAVAFIRnfpQGFNTvvgekgvlLSGGQKQRIAIARALLKNP 652
Cdd:cd03214 78 VPQ------------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171184400 653 KILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYG 713
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
491-690 |
6.66e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 150.63 E-value: 6.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlrsK 569
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRIAIA 645
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELLELVglaGFEDAYP-------HQ----LSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 171184400 646 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH 690
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
234-729 |
1.29e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 161.06 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 234 YLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVtenlsdglragaqaSVGISM-MFFVSP 312
Cdd:PLN03130 975 YWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNV--------------AVFVNMfLGQIFQ 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 313 NLATFVL-SVVPPVSIIAVI------YGRYL------RKLTKVtqDSLAQATQLAE--ERIGNVRTVRAFG--KEMTEIE 375
Cdd:PLN03130 1041 LLSTFVLiGIVSTISLWAIMpllvlfYGAYLyyqstaREVKRL--DSITRSPVYAQfgEALNGLSTIRAYKayDRMAEIN 1118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 376 kyASKVDHVMQlarkeafaragfFGATGLSGN---LIVLSVLykGGLL---------MGSAHM--------TVGELssfL 435
Cdd:PLN03130 1119 --GRSMDNNIR------------FTLVNMSSNrwlAIRLETL--GGLMiwltasfavMQNGRAenqaafasTMGLL---L 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 436 MYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFnegVILNEKS-----FQGALEFKNVHFAYpaRPEVP-I 509
Cdd:PLN03130 1180 SYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPL---VIENNRPppgwpSSGSIKFEDVVLRY--RPELPpV 1254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIa 589
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL- 1333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 590 ygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN 668
Cdd:PLN03130 1334 ----DPfNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 669 EYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKL 729
Cdd:PLN03130 1410 DALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
492-711 |
1.32e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 148.28 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLRS 568
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQE-PILFSCSIAENIAY-----GADDpssvtaEEIQ-RVAEVANAV---AFIRNFPQgfntvvgEkgvlLSGGQ 638
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR------KEIRrRVREVLDLVglsDKAKALPH-------E----LSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 639 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNANM-VAVLDQGKITE 711
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
492-709 |
2.00e-40 |
|
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: 146.00 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 571
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFScsiaeniaygaddpsSVTAEEIqrvaevanavafirnfpqgfntvvgekgVLLSGGQKQRIAIARALLKN 651
Cdd:cd03230 77 YLPEEPSLYE---------------NLTVREN----------------------------LKLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 652 PKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 709
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
491-723 |
5.12e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 150.63 E-value: 5.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRsKI 570
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKR-NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILFS-CSIAENIAYGADDpSSVTAEEI-QRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRIAIA 645
Cdd:COG3842 80 GMVFQDYALFPhLTVAENVAFGLRM-RGVPKAEIrARVAELLELVgleGLADRYPH-----------QLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 646 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS---TIknANMVAVLDQGKITEYGKHEELLS 720
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIYE 225
|
...
gi 171184400 721 KPN 723
Cdd:COG3842 226 RPA 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
492-723 |
6.05e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 146.82 E-value: 6.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 571
Cdd:COG3840 2 LRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIARA 647
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVglaGLLDRLPGQ-----------LSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 648 LLKNPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
.
gi 171184400 723 N 723
Cdd:COG3840 222 P 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
489-719 |
1.26e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.44 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 489 QGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 568
Cdd:PRK13632 5 SVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEP--ILFSCSIAENIAYGADD---PSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIA 643
Cdd:PRK13632 84 KIGIIFQNPdnQFIGATVEDDIAFGLENkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 644 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELL 719
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
171-437 |
1.60e-39 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 147.56 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIyTNPTVDYSDnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDAL-TAGTLTASQ-LLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTAllgrSVTENLSDGLRAGAQASVG----ISMMFFVSPNLATFVLSVVPPVS 326
Cdd:cd18541 79 LFAHLLTLSPSFYQKNRTGDLMARATNDLN----AVRMALGPGILYLVDALFLgvlvLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 327 IIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSG 406
Cdd:cd18541 155 LLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLI 234
|
250 260 270
....*....|....*....|....*....|.
gi 171184400 407 NLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 437
Cdd:cd18541 235 GLSFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
176-461 |
1.65e-39 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 147.62 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 176 GFLTMSSVISMSAPFFLGKIIDVIYTNPTVD-YSDNLTRLCL--GLSAV--FLCgaaaNAIRVYLMQtsgqRIVNRLRTS 250
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEaFTAAITVMSLltIASAVseFVC----DLIYNITMS----RIHSRLQGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAV 330
Cdd:cd18589 75 VFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 331 IYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIV 410
Cdd:cd18589 155 FVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 171184400 411 LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGA 461
Cdd:cd18589 235 VGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGS 285
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
512-723 |
5.32e-39 |
|
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: 144.40 E-value: 5.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTVSQEPILF-SCSIAENIAY 590
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 591 GADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY 670
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 671 LVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:cd03299 167 KLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
171-434 |
1.06e-38 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 145.32 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGL---LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAV 330
Cdd:cd18550 78 LYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 331 IYGRYLRKLTKVTQDSLAQATQLAEER--IGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNL 408
Cdd:cd18550 158 RVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAI 237
|
250 260
....*....|....*....|....*.
gi 171184400 409 IVLSVLYKGGLLMGSAHMTVGELSSF 434
Cdd:cd18550 238 GPALVYWVGGLLVIGGGLTIGTLVAF 263
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
492-718 |
4.90e-38 |
|
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: 141.94 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPArpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---RS 568
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEPILFS-CSIAENIAYGADD--------PSSVTAEEIQRVAEVANAV-----AFIRnfpqgfntvVGEkgvlL 634
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVglldkAYQR---------ADQ----L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 635 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIK-NANMVAVLDQGKITE 711
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVF 225
|
....*..
gi 171184400 712 YGKHEEL 718
Cdd:cd03256 226 DGPPAEL 232
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
173-438 |
1.42e-37 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 142.26 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 173 AAVGFLTM--SSVISMSAPFFLGKIID--VIYTNPTVDYSDnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLR 248
Cdd:cd18563 1 LILGFLLMllGTALGLVPPYLTKILIDdvLIQLGPGGNTSL-LLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 249 TSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsVGIS-MMFFVSPNLATFVLSVVPPVSI 327
Cdd:cd18563 80 RDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMI-IGIGvVLFSLNWKLALLVLIPVPLVVW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 328 IAVIYGRYLRKL-TKVTQDSLAQATQLAEErIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSG 406
Cdd:cd18563 159 GSYFFWKKIRRLfHRQWRRWSRLNSVLNDT-LPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLT 237
|
250 260 270
....*....|....*....|....*....|..
gi 171184400 407 NLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 438
Cdd:cd18563 238 SLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYL 269
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
492-709 |
1.97e-37 |
|
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: 139.20 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI----RQLNPvwLR 567
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINE--LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPILFS-CSIAENIAYGaddPSSV----------TAEEI-QRV--AEVANAvafirnFPQGfntvvgekgvl 633
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLA---PIKVkgmskaeaeeRALELlEKVglADKADA------YPAQ----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 634 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGK 708
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVMKDlaeeGMTMVVVTHEMGFAREvADRVIFMDDGR 212
|
.
gi 171184400 709 I 709
Cdd:cd03262 213 I 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
493-709 |
3.37e-37 |
|
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: 138.44 E-value: 3.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnpvwlRSKIGT 572
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 573 VSQEPIL---FSCSIAENIAYGADDPSS----VTAEEIQRVAEVANAV---AFI-RNFpqgfntvvGEkgvlLSGGQKQR 641
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGlfrrLSKADKAKVDEALERVglsELAdRQI--------GE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 642 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTI-KNANMVAVLDQGKI 709
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
493-722 |
6.23e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 141.86 E-value: 6.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS--- 568
Cdd:PRK11153 3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQE-PILFSCSIAENIAYgaddP---SSVTAEEI-QRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQK 639
Cdd:PRK11153 83 QIGMIFQHfNLLSSRTVFDNVAL----PlelAGTPKAEIkARVTELLELVglsDKADRYPaQ------------LSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 640 QRIAIARALLKNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 713
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPAT---TRSILELLKDinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
....*....
gi 171184400 714 KHEELLSKP 722
Cdd:PRK11153 224 TVSEVFSHP 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
491-709 |
3.17e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 136.73 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 567
Cdd:COG3638 2 MLELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPILFS-CSIAENIAYG--ADDP------SSVTAEEIQRVAEVANAV-----AFIRnfpqgfntvVGEkgvl 633
Cdd:COG3638 80 RRIGMIFQQFNLVPrLSVLTNVLAGrlGRTStwrsllGLFPPEDRERALEALERVgladkAYQR---------ADQ---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 634 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EYLVQEALDrlmDGRTVLVIAHRLSTIKN-ANMVAVLDQG 707
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTarqvmDLLRRIARE---DGITVVVNLHQVDLARRyADRIIGLRDG 223
|
..
gi 171184400 708 KI 709
Cdd:COG3638 224 RV 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
492-722 |
4.14e-36 |
|
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: 138.65 E-value: 4.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDP---ASGTISLDGHDIRQLNPVWLR 567
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 S----KIGTVSQEPilFSC---------SIAENIAYGADDPSsvtAEEIQRVAEVANAV------AFIRNFP-Qgfntvv 627
Cdd:COG0444 82 KirgrEIQMIFQDP--MTSlnpvmtvgdQIAEPLRIHGGLSK---AEARERAIELLERVglpdpeRRLDRYPhE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 628 gekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANM 700
Cdd:COG0444 151 ------LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNLLKDlqrelGLAILFITHDLGVVAEiADR 220
|
250 260
....*....|....*....|..
gi 171184400 701 VAVLDQGKITEYGKHEELLSKP 722
Cdd:COG0444 221 VAVMYAGRIVEEGPVEELFENP 242
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
508-730 |
6.21e-36 |
|
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: 136.19 E-value: 6.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 508 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAEN 587
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 588 IaygaDDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 667
Cdd:cd03288 115 L----DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 668 NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLM 730
Cdd:cd03288 191 TENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
495-710 |
8.17e-36 |
|
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: 134.31 E-value: 8.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 495 KNVHFAYPARPEvpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdiRQLNPVWLRSKIGTVS 574
Cdd:cd03226 3 ENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 575 QEP--ILFSCSIAENIAYGADDPSSVtAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNP 652
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAG-NEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 653 KILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKIT 710
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
491-722 |
1.47e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 136.08 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL--LRLYDPASGT-ISLDGHDIRQLNpVW-L 566
Cdd:PRK13640 5 IVEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLIngLLLPDDNPNSkITVDGITLTAKT-VWdI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 567 RSKIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVA---FIRNFPQGfntvvgekgvlLSGGQKQR 641
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGmldYIDSEPAN-----------LSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 642 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELL 719
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
...
gi 171184400 720 SKP 722
Cdd:PRK13640 232 SKV 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
511-722 |
7.09e-35 |
|
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: 133.54 E-value: 7.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS----KIGTVSQEPILF-SCSIA 585
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 586 ENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATS 662
Cdd:cd03294 121 ENVAFGLEVQGVPRAEREERAAEALELVgleGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 663 ALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
492-722 |
7.18e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 132.96 E-value: 7.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIrqlnPVWL---RS 568
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLpprER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEPILF-SCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQKQRIA 643
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEELLELVqleGLADRYPsQ------------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 644 IARALLKNPKILLLDEATSALDA----ENEYLVQEALDRLmdGRTVLVIAH------RLstiknANMVAVLDQGKITEYG 713
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVG 216
|
....*....
gi 171184400 714 KHEELLSKP 722
Cdd:COG1118 217 TPDEVYDRP 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
514-722 |
9.98e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 132.16 E-value: 9.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLRSKIGTVSQEPilFSC-----SIA 585
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDP--YASlnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 586 ENIAYGADDPSSVTAEEIQ-RVAEVANAV----AFIRNFPQGFntvvgekgvllSGGQKQRIAIARALLKNPKILLLDEA 660
Cdd:COG4608 116 DIIAEPLRIHGLASKAERReRVAELLELVglrpEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 661 TSALDAEneylVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:COG4608 185 VSALDVS----IQaQVLNLLEDlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
492-720 |
1.02e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.52 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdiRQLNP--VW-LRS 568
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEetVWdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIA 643
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVgmeDFLNREPHR-----------LSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 644 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 720
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
492-723 |
1.02e-33 |
|
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: 129.28 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 571
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIARA 647
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGLRLKKLPKAEIKERVAEALDLVqleGYANRKPSQ-----------LSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
492-713 |
1.84e-33 |
|
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: 127.69 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGsVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 571
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILF-SCSIAENIAYGA---DDPSSvtaEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARA 647
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYIAwlkGIPSK---EVKARVDEVLELV--------NLGDRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 713
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
170-455 |
2.87e-33 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 129.90 E-value: 2.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 170 RLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRT 249
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSG---LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 250 SLFSSILRQEVAFFDKTRTGELINRLSSDTallgrsvtENLSDGLRAGAQASVG--------ISMMFFVSPNLATFVLSV 321
Cdd:cd18545 78 DLFSHLQKLSFSFFDSRPVGKILSRVINDV--------NSLSDLLSNGLINLIPdlltlvgiVIIMFSLNVRLALVTLAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 322 VPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGA 401
Cdd:cd18545 150 LPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 402 TGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA--FWVGISigGLSSFYSEL 455
Cdd:cd18545 230 VELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVgrFWQPIR--NLSNFYNQL 283
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
490-723 |
5.85e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.58 E-value: 5.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 490 GALEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSK 569
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILF-SCSIAENIAYG---ADdpssVTAEEI-QRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQR 641
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklRK----VPKAEIdRRVREAAELLgleDLLDRKPKQ-----------LSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 642 IAIARALLKNPKILLLDEATSALDAEneyLVQEA---LDRLMDGR---TVLV---------IAHRlstiknanmVAVLDQ 706
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAK---LRVEMraeIKRLHRRLgttTIYVthdqveamtLADR---------IAVMND 209
|
250
....*....|....*..
gi 171184400 707 GKITEYGKHEELLSKPN 723
Cdd:COG3839 210 GRIQQVGTPEELYDRPA 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
492-709 |
2.23e-32 |
|
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: 124.83 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN----PvWLR 567
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiP-YLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQE-PILFSCSIAENIAYgADDPSSVTAEEIQ-RVAEVANAVAF---IRNFPQGfntvvgekgvlLSGGQKQRI 642
Cdd:cd03292 78 RKIGVVFQDfRLLPDRNVYENVAF-ALEVTGVPPREIRkRVPAALELVGLshkHRALPAE-----------LSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 643 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 709
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
491-723 |
4.05e-32 |
|
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: 124.76 E-value: 4.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwLRSKI 570
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL---DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV--QERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILFS-CSIAENIAYG------ADDPSSvtAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQ 640
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGlrvkprSERPPE--AEIRAKVHELLKLVqldWLADRYPAQ-----------LSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 641 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDG---RTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEE 717
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
....*.
gi 171184400 718 LLSKPN 723
Cdd:cd03296 224 VYDHPA 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
492-722 |
6.52e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.43 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNV--HFAyparpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR--QLNPVWLR 567
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEPILFSCSIA-ENIAYGaddP------SSVTAEEIQR-------VAEVANavafirNFPqgfntvvGEkgvl 633
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFG---PlrvrgaSKEEAEKQARellakvgLAERAH------HYP-------SE---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 634 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALdRLM-----DGRTVLVIAHRLS-TIKNANMVAVLDQG 707
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE---LRHEVL-KVMqdlaeEGMTMVIVTHEIGfAEKVASRLIFIDKG 212
|
250
....*....|....*
gi 171184400 708 KITEYGKHEELLSKP 722
Cdd:PRK09493 213 RIAEDGDPQVLIKNP 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
491-723 |
1.40e-31 |
|
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: 123.66 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG-TISLDGHDIRQLNPVWLRSK 569
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVS---QEPILFSCSIAENIAYGADD----PSSVTAEEIQRVAEVANAVAFI----RNFPQgfntvvgekgvlLSGGQ 638
Cdd:COG1119 80 IGLVSpalQLRFPRDETVLDVVLSGFFDsiglYREPTDEQRERARELLELLGLAhladRPFGT------------LSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 639 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNA-NMVAVLDQGKITEYGKH 715
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPK 227
|
....*...
gi 171184400 716 EELLSKPN 723
Cdd:COG1119 228 EEVLTSEN 235
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
171-437 |
1.91e-31 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 124.93 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIID-VIYTNPTVDYSDN-----------LTRLCLGLSAVFLCGAAANAIRVYLMQT 238
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDdVLGDKPLPGLLGLapllgpdplalLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 239 SGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFV 318
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 319 LSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGF 398
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 171184400 399 FGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 437
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
492-730 |
2.25e-31 |
|
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: 129.42 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPAR--------PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLyDPASGTISLDGHDI----- 558
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLdglsr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 559 RQLNPvwLRSKIGTVSQEPilFSC-----SIAENIAYG--ADDPSSVTAEEIQRVAEVANAV----AFIRNFPQGFntvv 627
Cdd:COG4172 355 RALRP--LRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrVHGPGLSAAERRARVAEALEEVgldpAARHRYPHEF---- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 628 gekgvllSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANM 700
Cdd:COG4172 427 -------SGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQaQILDLLRDlqrehGLAYLFISHDLAVVRAlAHR 495
|
250 260 270
....*....|....*....|....*....|.
gi 171184400 701 VAVLDQGKITEYGKHEELLSKPNGIY-RKLM 730
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDAPQHPYtRALL 526
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
242-730 |
4.75e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 130.87 E-value: 4.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 242 RIVNRLRTSLFSSILRQEVAFFDKTR----TGELINRLSSDTALLgRSVTENLSdGLRAgAQASVGISMMFF-----VSP 312
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDANAL-QQIAEQLH-GLWS-APFRIIVSMVLLyqqlgVAS 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 313 NLATFVLSVVPPVSIIAViygRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEA 392
Cdd:PLN03232 444 LFGSLILFLLIPLQTLIV---RKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQ 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 393 FARAgfFGATGLSGNLIVLSVLYKGG-LLMGSAHMTVGELSSFLMYAFwVGISIGGLSSFYSELMKGLGAGGRLWELLER 471
Cdd:PLN03232 521 LLSA--FNSFILNSIPVVVTLVSFGVfVLLGGDLTPARAFTSLSLFAV-LRSPLNMLPNLLSQVVNANVSLQRIEELLLS 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 472 EPKL-----PFNEGVilneksfqGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDP 546
Cdd:PLN03232 598 EERIlaqnpPLQPGA--------PAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 547 ASGTisldghdirqlnPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtaeeiqRVAEVANAVAFIRN---FPQGF 623
Cdd:PLN03232 670 AETS------------SVVIRGSVAYVPQVSWIFNATVRENILFGSDFESE-------RYWRAIDVTALQHDldlLPGRD 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 624 NTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLV-QEALDRLMDGRTVLVIAHRLSTIKNANMVA 702
Cdd:PLN03232 731 LTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRII 810
|
490 500
....*....|....*....|....*...
gi 171184400 703 VLDQGKITEYGKHEElLSKPNGIYRKLM 730
Cdd:PLN03232 811 LVSEGMIKEEGTFAE-LSKSGSLFKKLM 837
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-722 |
8.48e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 121.69 E-value: 8.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 509 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH------DIRQLNPVWLRSKIGTVSQEPILFS- 581
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 582 CSIAENIAYGADDPSSVTAEEIQRVAEVA-NAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 660
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEEClRKVGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 661 TSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
492-720 |
9.27e-31 |
|
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: 120.23 E-value: 9.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKI 570
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILF-SCSIAENIAYGADD-PSSVTAEEIQRVAEVanavafirnFPqgfntVVGE----KGVLLSGGQKQRIAI 644
Cdd:cd03224 78 GYVPEGRRIFpELTVEENLLLGAYArRRAKRKARLERVYEL---------FP-----RLKErrkqLAGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 645 ARALLKNPKILLLDEATSALdAENeyLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 719
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGL-APK--IVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
.
gi 171184400 720 S 720
Cdd:cd03224 221 A 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
485-726 |
9.73e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.56 E-value: 9.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 485 EKSFQGALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPv 564
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 565 wLRSKIGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFntvVGEKGVLLSGGQKQRIA 643
Cdd:PRK11607 89 -YQRPINMMFQSYALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-----QEF---AKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 644 IARALLKNPKILLLDEATSALDAE----NEYLVQEALDRLmdGRTVLVIAH-RLSTIKNANMVAVLDQGKITEYGKHEEL 718
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
....*...
gi 171184400 719 LSKPNGIY 726
Cdd:PRK11607 238 YEHPTTRY 245
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
492-725 |
3.07e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.24 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPArPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPI-LFSCSIAE-NIAYGADDpSSVTAEEIQR-VAEVANAVAFI--RNF-PQGfntvvgekgvlLSGGQKQRIAIA 645
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLEN-HAVPYDEMHRrVSEALKQVDMLerADYePNA-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 646 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
..
gi 171184400 724 GI 725
Cdd:PRK13648 235 EL 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
491-723 |
3.66e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.23 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI 570
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIA 645
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVrmwDFRDKPPYH-----------LSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 646 RALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKhEELLSKPN 723
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDED 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
492-723 |
4.36e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.22 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpVW-LRSKI 570
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN-VWdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFNTvvgEKGVLLSGGQKQRIAIARAL 648
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM-----QDFKE---REPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 649 LKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
512-713 |
4.75e-30 |
|
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: 117.98 E-value: 4.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTVSQEPILFS-CSIAENIAY 590
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 591 GADDPSSVTAEEIQRVAEVANAVAFirnfpQGFNTVVGEKgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAEney 670
Cdd:cd03298 94 GLSPGLKLTAEDRQAIEVALARVGL-----AGLEKRLPGE---LSGGERQRVALARVLVRDKPVLLLDEPFAALDPA--- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 171184400 671 LVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 713
Cdd:cd03298 163 LRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
514-722 |
1.22e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.95 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDI--RQLNPVWLRSKIGTVSQEPILFSCSIAE 586
Cdd:PRK14239 25 SLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 587 NIAYGADDPSSVTAEEIQRVAEVANAVAFIrnfpqgFNTV---VGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 663
Cdd:PRK14239 105 NVVYGLRLKGIKDKQVLDEAVEKSLKGASI------WDEVkdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 664 LDAENEYLVQEALDRLMDGRTVLVIAHRL---STIknANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
512-722 |
1.54e-29 |
|
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: 120.59 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKSTVLSL---LLRlydPASGTISLDGH-----DIRQLNPVWLRSkIGTVSQEPILFS-C 582
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdsARGIFLPPHRRR-IGYVFQEARLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENIAYGADD-PSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEAT 661
Cdd:COG4148 93 SVRGNLLYGRKRaPRAERRISFDEVVELLGIGHLLDRRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 662 SALDAENEYLVQEALDRLMD--GRTVLVIAH------RLstiknANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:COG4148 162 AALDLARKAEILPYLERLRDelDIPILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
492-704 |
1.79e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 116.74 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFSCSIAENIAYgaddPSSVTAEEIQRVAEVANAVAFirNFPQgfNTVvgEKGV-LLSGGQKQRIAIARALLK 650
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIF----PWQIRNQQPDPAIFLDDLERF--ALPD--TIL--TKNIaELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 651 NPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVL 704
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
171-452 |
2.04e-29 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 118.79 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIyTNPTVDySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLV-TIGSKS-LGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsVGIS-MMFFVSPNLATFVLSVVPPVSIIA 329
Cdd:cd18778 79 LYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTL-VGVAiILFSINPKLALLTLIPIPFLALGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 330 VIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLI 409
Cdd:cd18778 158 WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 171184400 410 VLSVLYKGGLLMGSAHMTVGELSSFLMYafwvgisiggLSSFY 452
Cdd:cd18778 238 TVLVLGFGGRLVLAGELTIGDLVAFLLY----------LGLFY 270
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
171-445 |
2.09e-29 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 118.66 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSY---ILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAV 330
Cdd:cd18548 78 LFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 331 IYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIV 410
Cdd:cd18548 158 LIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAI 237
|
250 260 270
....*....|....*....|....*....|....*
gi 171184400 411 LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISI 445
Cdd:cd18548 238 VAILWFGGHLINAGSLQVGDLVAFINYLMQILMSL 272
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
491-730 |
2.25e-29 |
|
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: 125.83 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYpARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDpasgtiSLDGHdirqlnpVWLRSKI 570
Cdd:TIGR00957 636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD------KVEGH-------VHMKGSV 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILFSCSIAENIAYGaddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLK 650
Cdd:TIGR00957 702 AYVPQQAWIQNDSLRENILFG----KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 651 NPKILLLDEATSALDAE-NEYLVQEAL--DRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYR 727
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR-DGAFA 856
|
...
gi 171184400 728 KLM 730
Cdd:TIGR00957 857 EFL 859
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
171-437 |
2.72e-29 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 118.36 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIID--VIYTNPTVdysdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLR 248
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDsgVRAGDLGV-----LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 249 TSLFSSILRQEVAFFDKTRTGELINRLSSDTAllgrSVTENLSDGLRAGAQAS---VGIS-MMFFVSPNLATFVLSVVPP 324
Cdd:cd18546 76 LRVFAHLQRLSLDFHERETSGRIMTRMTSDID----ALSELLQTGLVQLVVSLltlVGIAvVLLVLDPRLALVALAALPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 325 VSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGL 404
Cdd:cd18546 152 LALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVEL 231
|
250 260 270
....*....|....*....|....*....|...
gi 171184400 405 SGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 437
Cdd:cd18546 232 LGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
492-722 |
2.74e-29 |
|
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: 116.62 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK-- 569
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHRIARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILF-SCSIAENI---AYGADDPSSVtAEEIQRVAEVanavafirnFPqgfntVVGE----KGVLLSGGQKQR 641
Cdd:COG0410 80 IGYVPEGRRIFpSLTVEENLllgAYARRDRAEV-RADLERVYEL---------FP-----RLKErrrqRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 642 IAIARALLKNPKILLLDEATSALdAENeyLVQE---ALDRLMD-GRTVLV----------IAHRlstiknanmVAVLDQG 707
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGL-APL--IVEEifeIIRRLNReGVTILLveqnarfaleIADR---------AYVLERG 212
|
250
....*....|....*
gi 171184400 708 KITEYGKHEELLSKP 722
Cdd:COG0410 213 RIVLEGTAAELLADP 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
506-722 |
3.45e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 506 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL---YDPA--SGTISLDGHDIRQLNPVWLRSKIGTVSQEP-IL 579
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 580 FSCSIAENIAYGADDPSSVT--AEEIQRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLL 657
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKskKELQERVRWALEKAQLWDEVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 658 DEATSALDAENEYLVQEALDRLMDGRTVLVIAH------RLStiknaNMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
171-437 |
3.85e-29 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 117.94 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVgfltMSSVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18549 8 LFCAV----LIAALDLVFPLIVRYIIDDLLPSKNLR---LILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTallgRSVTEnLS-----DGLRAGAQASVGISMMFFVSPNLATFVLSVVPPV 325
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDL----FDISE-LAhhgpeDLFISIITIIGSFIILLTINVPLTLIVFALLPLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 326 SIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVmQLARKEAF-ARAGFFGATGL 404
Cdd:cd18549 156 IIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRF-LESKKKAYkAMAYFFSGMNF 234
|
250 260 270
....*....|....*....|....*....|...
gi 171184400 405 SGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 437
Cdd:cd18549 235 FTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
492-690 |
4.58e-29 |
|
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: 114.88 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAypaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 571
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILF-SCSIAENIAYGAD-DPSSVTAEEIQRVAEVANAVAFIRNFPQgfntvvgekgvLLSGGQKQRIAIARALL 649
Cdd:COG4133 79 YLGHADGLKpELTVRENLRFWAAlYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 171184400 650 KNPKILLLDEATSALDAENEYLVQEALDR-LMDGRTVLVIAH 690
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
511-722 |
6.32e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 116.42 E-value: 6.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDI--RQLNPVWLRSKIGTVSQEPILFSCS 583
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 IAENIAYGAD------DPSSVTAEEIQRVA---EVANAVAfirnfpqgfntvvgEKGVLLSGGQKQRIAIARALLKNPKI 654
Cdd:PRK14243 107 IYDNIAYGARingykgDMDELVERSLRQAAlwdEVKDKLK--------------QSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 655 LLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRL-STIKNANMVAVLD---------QGKITEYGKHEELLSKP 722
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSP 250
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
512-713 |
6.76e-29 |
|
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: 114.70 E-value: 6.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIP---SGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDG---HDIRQ---LNPVwlRSKIGTVSQEPILFS- 581
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkinLPPQ--QRKIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 582 CSIAENIAYGADDPSSvtAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEAT 661
Cdd:cd03297 90 LNVRENLAFGLKRKRN--REDRISVDELLDLL--------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 662 SALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYG 713
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
512-723 |
1.09e-28 |
|
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: 117.91 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDG---HDIRQ---LNPVwlRSKIGTVSQEPILFS-CSI 584
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPE--KRRIGYVFQEARLFPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 585 AENIAYG---ADDPSSVTAEEiqRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEAT 661
Cdd:TIGR02142 93 RGNLRYGmkrARPSERRISFE--RVIELLGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 662 SALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
492-713 |
1.24e-28 |
|
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: 113.89 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 571
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILF-SCSIAENIAYG---ADDPSSVTAEEIQRVAEVAnavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARA 647
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklRKVPKDEIDERVREVAELL-----------QIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH-RLSTIKNANMVAVLDQGKITEYG 713
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
512-726 |
1.79e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.51 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnpvwlRS----KIGTVSQEPILFS-CSIAE 586
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSiqqrDICMVFQSYALFPhMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 587 NIAYGAdDPSSVTAEEI-QRVAEVANAVAFIrnfpqGFntvvGEKGV-LLSGGQKQRIAIARALLKNPKILLLDEATSAL 664
Cdd:PRK11432 98 NVGYGL-KMLGVPKEERkQRVKEALELVDLA-----GF----EDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 665 DAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPNGIY 726
Cdd:PRK11432 168 DANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
491-723 |
2.41e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.48 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvWLRSKI 570
Cdd:PRK13548 2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 -GTVSQEPIL-FSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFI----RNFPQgfntvvgekgvlLSGGQKQRIAI 644
Cdd:PRK13548 78 rAVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAhlagRDYPQ------------LSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 645 ARALL------KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLstikN-----ANMVAVLDQGKITE 711
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHDL----NlaaryADRIVLLHQGRLVA 221
|
250
....*....|..
gi 171184400 712 YGKHEELLSKPN 723
Cdd:PRK13548 222 DGTPAEVLTPET 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
492-665 |
2.99e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 117.36 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 571
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFS-CSIAENIAYGADdPSSVTAEEIQ-RVAEvanAVAFIR--NFPQgfntvvgEKGVLLSGGQKQRIAIARA 647
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGLR-MQKTPAAEITpRVME---ALRMVQleEFAQ-------RKPHQLSGGQQQRVAIARA 158
|
170
....*....|....*...
gi 171184400 648 LLKNPKILLLDEATSALD 665
Cdd:PRK09452 159 VVNKPKVLLLDESLSALD 176
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
171-454 |
3.96e-28 |
|
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: 114.89 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTvdySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGD---RSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSvtenLSDGLRA---GAQASVGISMMFFVSPNLATFVLSVVPPVSI 327
Cdd:cd18543 78 LFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF----LAFGPFLlgnLLTLVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 328 IAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGN 407
Cdd:cd18543 154 VARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 171184400 408 LIVLSVLYKGGLLMGSAHMTVGELSSFLMYAF---WVGISIGGLSSFYSE 454
Cdd:cd18543 234 LGLAAVLALGGWLVANGSLTLGTLVAFSAYLTmlvWPVRMLGWLLAMAQR 283
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
511-709 |
5.01e-28 |
|
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: 112.92 E-value: 5.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIGTVS--QEPILF-SCSIAEN 587
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 588 IAYGA-------DDPSSVTAEEIQRVAEVANAVAFIRNFPQGfNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 660
Cdd:cd03219 96 VMVAAqartgsgLLLARARREEREARERAEELLERVGLADLA-DRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 171184400 661 TSALDAEneyLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 709
Cdd:cd03219 171 AAGLNPE---ETEELAELIRElrerGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
492-720 |
5.61e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:PRK11231 3 LRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQ-----EPIlfscSIAENIAYG------------ADDPSSVT-AEEIQRVAEVAnavafirnfpqgfntvvgEKGVL 633
Cdd:PRK11231 80 LLPQhhltpEGI----TVRELVAYGrspwlslwgrlsAEDNARVNqAMEQTRINHLA------------------DRRLT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 634 -LSGGQKQRIAIARALLKNPKILLLDEATSALDAENeylvQEALDRLM-----DGRTVLVIAHRLS-TIKNANMVAVLDQ 706
Cdd:PRK11231 138 dLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH----QVELMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLAN 213
|
250
....*....|....
gi 171184400 707 GKITEYGKHEELLS 720
Cdd:PRK11231 214 GHVMAQGTPEEVMT 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
511-709 |
6.17e-28 |
|
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: 111.93 E-value: 6.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWlrSKIGTVSQEPILF-SCSIAENIA 589
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYpNLTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 590 YGADDPsSVTAEEIQRVAEVAnavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 669
Cdd:cd03268 95 LLARLL-GIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 171184400 670 YLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKI 709
Cdd:cd03268 163 KELRELILSLRDqGITVLISSHLLSEIqKVADRIGIINKGKL 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
503-667 |
7.83e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.42 E-value: 7.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 503 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDP---ASGTISLDGHDIRQLNPvwLRSKIGTVSQEPIL 579
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 580 FS-CSIAENIAYGAddPSSVTAEeiQRVAEVANAVA------FIRNFPqgfNTvvgekgvlLSGGQKQRIAIARALLKNP 652
Cdd:COG4136 88 FPhLSVGENLAFAL--PPTIGRA--QRRARVEQALEeaglagFADRDP---AT--------LSGGQRARVALLRALLAEP 152
|
170
....*....|....*
gi 171184400 653 KILLLDEATSALDAE 667
Cdd:COG4136 153 RALLLDEPFSKLDAA 167
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
505-707 |
8.29e-28 |
|
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: 111.65 E-value: 8.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 505 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI----SLDGHDIRQLNPVWLRSKIGTVSQEPILF 580
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 581 SCSIAENIAYGaddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA 660
Cdd:cd03290 92 NATVEENITFG----SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 171184400 661 TSALDAE-NEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVLDQG 707
Cdd:cd03290 168 FSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
492-709 |
1.22e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.49 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVH--FaYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRS 568
Cdd:COG1101 2 LELKNLSktF-NPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 K-IGTVSQEPILFSC---SIAEN--IAYGADDP----SSVTAEEIQRVAEvanavaFIRNFPQGF----NTVVGekgvLL 634
Cdd:COG1101 80 KyIGRVFQDPMMGTApsmTIEENlaLAYRRGKRrglrRGLTKKRRELFRE------LLATLGLGLenrlDTKVG----LL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 635 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKI 709
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
492-713 |
1.41e-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: 110.33 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARP---EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL--LRLYDPASGTISLDGHDIRqlnPVWL 566
Cdd:cd03213 4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 567 RSKIGTVSQEPILFSC-SIAENIAYGAddpssvtaeEIQRvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIA 645
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMFAA---------KLRG----------------------------LSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 646 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLST--IKNANMVAVLDQGKITEYG 713
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
492-710 |
1.59e-27 |
|
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: 109.06 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKI 570
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQepilfscsiaeniaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLK 650
Cdd:cd03216 78 AMVYQ----------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 651 NPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKIT 710
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
491-714 |
5.67e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPA-RP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI------RQLN 562
Cdd:PRK13649 2 GINLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 563 PVwlRSKIGTVSQ--EPILFSCSIAENIAYGADDpSSVTAEEIQRVA-EVANAVAFIRNFpqgFNTVVGEkgvlLSGGQK 639
Cdd:PRK13649 82 QI--RKKVGLVFQfpESQLFEETVLKDVAFGPQN-FGVSQEEAEALArEKLALVGISESL---FEKNPFE----LSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 640 QRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGK 714
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
464-691 |
5.79e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.06 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 464 RLWEL---LEREPKLPFNEGVIlnEKSFQGALEFKNVHFAYPArpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTvlslL 540
Cdd:COG4178 334 RLAGFeeaLEAADALPEAASRI--ETSEDGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST----L 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 541 LR----LYDPASGTISL-DGHDIrqlnpVWLrskigtvSQEPILFSCSIAENIAYgADDPSSVTAEEIQRVAEVANAVAF 615
Cdd:COG4178 406 LRaiagLWPYGSGRIARpAGARV-----LFL-------PQRPYLPLGTLREALLY-PATAEAFSDAELREALEAVGLGHL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 616 IRNFpqgfnTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHR 691
Cdd:COG4178 473 AERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
209-731 |
9.42e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.19 E-value: 9.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 209 DNLTRLCLGLSAVFLcGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTE 288
Cdd:PTZ00243 996 SAATYLYVYLGIVLL-GTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPM 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 289 NLSDGLRAGAQASVGISMMFFVSPnlatFVLSVVPPVSI----IAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTV 364
Cdd:PTZ00243 1075 SYLYLLQCLFSICSSILVTSASQP----FVLVALVPCGYlyyrLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATI 1150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 365 RAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKG--GLLMGSAHMTVGELSSFLMYAF--- 439
Cdd:PTZ00243 1151 TAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGviGTMLRATSQEIGLVSLSLTMAMqtt 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 440 ----W----VGISIGGLSS-----FYS-----ELMKGLGAggrLWELLEREPKLPFN-EGVILNEKSF----------QG 490
Cdd:PTZ00243 1231 atlnWlvrqVATVEADMNSverllYYTdevphEDMPELDE---EVDALERRTGMAADvTGTVVIEPASptsaaphpvqAG 1307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 569
Cdd:PTZ00243 1308 SLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARAL 648
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNV-----DPfLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 649 LK-NPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYR 727
Cdd:PTZ00243 1461 LKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
....
gi 171184400 728 KLMN 731
Cdd:PTZ00243 1541 SMVE 1544
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
511-709 |
1.11e-26 |
|
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: 109.74 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvWLRSKIGtVS---QEPILF-SCSIAE 586
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLG-IArtfQNPRLFpELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 587 NIAYGAD------------DPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKI 654
Cdd:COG0411 99 NVLVAAHarlgrgllaallRLPRARREEREARERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 655 LLLDEATSALDAEneyLVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 709
Cdd:COG0411 174 LLLDEPAAGLNPE---ETEELAELIRRlrderGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
491-716 |
1.29e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.95 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI---RQLNP---V 564
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEkaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 565 WLRSKIGTVSQE----PILfscSIAENIAygaDDPSSV---TAEEIQRVAEVANAVAFIRNFPQGFNtvvgekgVLLSGG 637
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLI---EAPCKVlglSKEQAREKAMKLLARLRLTDKADRFP-------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 638 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKH 715
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDA 225
|
.
gi 171184400 716 E 716
Cdd:COG4161 226 S 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
503-731 |
2.12e-26 |
|
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: 109.12 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 503 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW---LRSKIGTVSQEpil 579
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQD--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 580 fscsiaeniAYGADDPSSvTAEEI-----------------QRVAEVANAVAF----IRNFPQGFntvvgekgvllSGGQ 638
Cdd:TIGR02769 97 ---------SPSAVNPRM-TVRQIigeplrhltsldeseqkARIAELLDMVGLrsedADKLPRQL-----------SGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 639 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKH 715
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDV 235
|
250
....*....|....*.
gi 171184400 716 EELLSKPNGIYRKLMN 731
Cdd:TIGR02769 236 AQLLSFKHPAGRNLQS 251
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
492-723 |
2.85e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYpaRPEVPiFQ-----DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI------RQ 560
Cdd:PRK13634 3 ITFQKVEHRY--QYKTP-FErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 561 LNPvwLRSKIGTVSQ--EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVL-LSGG 637
Cdd:PRK13634 80 LKP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELV--------GLPEELLARSPFeLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 638 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGK 714
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*....
gi 171184400 715 HEELLSKPN 723
Cdd:PRK13634 230 PREIFADPD 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
509-722 |
3.06e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.94 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 509 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlRS-KIGTVSQEPILFS-CSIAE 586
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDrKVGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 587 NIAYGA------DDPSSvtAEEIQRVAEVANAVAFIR---NFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLL 657
Cdd:PRK10851 94 NIAFGLtvlprrERPNA--AAIKAKVTQLLEMVQLAHladRYPAQ-----------LSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171184400 658 DEATSALDAEneylVQEALDRLMdgR---------TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK10851 161 DEPFGALDAQ----VRKELRRWL--RqlheelkftSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
494-712 |
3.59e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.24 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 494 FKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhDIRqlnpvwlrskIGTV 573
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 574 SQEPILFS-CSIAENIAYGADDPSSVTAE-------------------EIQ-------------RVAEVANAVafirNFP 620
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaELQeefealggweaeaRAEEILSGL----GFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 621 QG-FNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EYLVQEaldrlmDGrTVLVIAH-R-- 691
Cdd:COG0488 143 EEdLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY------PG-TVLVVSHdRyf 211
|
250 260
....*....|....*....|.
gi 171184400 692 LSTIknANMVAVLDQGKITEY 712
Cdd:COG0488 212 LDRV--ATRILELDRGKLTLY 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
509-721 |
4.95e-26 |
|
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: 108.40 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 509 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDpASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENI 588
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 589 aygadDPSSV-TAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 667
Cdd:cd03289 98 -----DPYGKwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 171184400 668 NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 721
Cdd:cd03289 173 TYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
492-720 |
5.00e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.26 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpVW-LRSKI 570
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN-VWnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTvvgEKGVLLSGGQKQRIAIARAL 648
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-----DFKT---REPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171184400 649 LKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 720
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
491-690 |
6.97e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.64 E-value: 6.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPA-RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnPVWLRsk 569
Cdd:COG4525 3 MLTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 iGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFntvvGEKGVL-LSGGQKQRIAIARA 647
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEELLALVGL-----ADF----ARRRIWqLSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH 690
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH 193
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
492-709 |
8.13e-26 |
|
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: 106.05 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 571
Cdd:cd03263 1 LQIRNLTKTYK-KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFS-CSIAENIAYGAddpsSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLK 650
Cdd:cd03263 79 YCPQFDALFDeLTVREHLRFYA----RLKGLPKSEIKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 651 NPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKI 709
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
492-721 |
8.86e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.87 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPE---VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW-LR 567
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQ-RVAEVANAVA---FIRNFPQgfntvvgekgvLLSGGQKQR 641
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPEN-LGIPPEEIReRVDESLKKVGmyeYRRHAPH-----------LLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 642 IAIARALLKNPKILLLDEATSALDAENEylvQEALDRLMD-----GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHE 716
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGR---REVVNTIKElnkkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 171184400 717 ELLSK 721
Cdd:PRK13633 230 EIFKE 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
491-718 |
1.02e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSK 569
Cdd:COG1129 4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFSC-SIAENIAYGADDPSSVT---AEEIQRVAEVANAVafirnfpqGFN----TVVGEkgvlLSGGQKQR 641
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIFLGREPRRGGLidwRAMRRRARELLARL--------GLDidpdTPVGD----LSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 642 IAIARALLKNPKILLLDEATSAL-DAENEYLVqEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 718
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLtEREVERLF-RIIRRLKAqGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
509-722 |
1.09e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.98 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 509 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR-------QLNPV------WLRSKIGTVSQ 575
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVAdknqlrLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 576 EPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgEKGVLLSGGQKQRIAIARALLKNPKI 654
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171184400 655 LLLDEATSALDAEneyLVQEALdRLM-----DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK10619 174 LLFDEPTSALDPE---LVGEVL-RIMqqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
159-718 |
1.34e-25 |
|
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: 111.81 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 159 KLLGLAYPERRRLAAAVGFLtmSSVISMsapFFLGKIIDVIyTNPTVDYSDNLTRLCLGLSAVFLCGAAANairvYLMQT 238
Cdd:COG4615 5 RLLLRESRWLLLLALLLGLL--SGLANA---GLIALINQAL-NATGAALARLLLLFAGLLVLLLLSRLASQ----LLLTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 239 SGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVtENLSDGLRAGAQASVGISMMFFVSPNLATFV 318
Cdd:COG4615 75 LGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCLAYLAWLSPPLFLLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 319 LSVVppvSIIAVIYGRYLRKLTKvtqdSLAQATQLAEERIGNVRTV----------RAFGKEMTEiEKYASKVDHVMQLa 388
Cdd:COG4615 154 LVLL---GLGVAGYRLLVRRARR----HLRRAREAEDRLFKHFRALlegfkelklnRRRRRAFFD-EDLQPTAERYRDL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 389 RKEAFAragFFGATGLSGNLIVLSVLykGGLLMGSAHMTVGELSSFLMYA----FWVGiSIGGLSSFYSELMKGLGAGGR 464
Cdd:COG4615 225 RIRADT---IFALANNWGNLLFFALI--GLILFLLPALGWADPAVLSGFVlvllFLRG-PLSQLVGALPTLSRANVALRK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 465 LWEL---LEREPKLPFNEGVILNEKSFQgALEFKNVHFAYPARPEVPIFQ--DFSLSIPSGSVTALVGPSGSGKSTVLSL 539
Cdd:COG4615 299 IEELelaLAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 540 LLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFscsiaENIaYGADDPssVTAEEIQ---RVAEVANAVAFi 616
Cdd:COG4615 378 LTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRL-LGLDGE--ADPARARellERLELDHKVSV- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 617 rnfpqgfntvvgEKGVL----LSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-EYLVQEALDRLMD-GRTVLVIAH 690
Cdd:COG4615 449 ------------EDGRFsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFrRVFYTELLPELKArGKTVIAISH 516
|
570 580 590
....*....|....*....|....*....|....*..
gi 171184400 691 ---------RLstIKnanmvavLDQGKITEYGKHEEL 718
Cdd:COG4615 517 ddryfdladRV--LK-------MDYGKLVELTGPAAL 544
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
491-711 |
1.60e-25 |
|
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: 105.59 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN----PVW 565
Cdd:COG4181 8 IIELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 566 LRSKIGTVSQ-EPILFSCSIAENIAY-----GADDPSSVTAEEIQRV--AEVANAvafirnFPQGfntvvgekgvlLSGG 637
Cdd:COG4181 88 RARHVGFVFQsFQLLPTLTALENVMLplelaGRRDARARARALLERVglGHRLDH------YPAQ-----------LSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 638 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITE 711
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
246-721 |
1.75e-25 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 113.47 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 246 RLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLR-----AGAQASVGIsmmffvspnLATFVLS 320
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQltlivLGAIFVVSV---------LQPYIFI 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 321 VVPPVSIIAVIYGRY-LRKLTKVTQDSLAQATQLAEERIGNVR---TVRAFGKE---------------------MTEIE 375
Cdd:TIGR01271 1030 AAIPVAVIFIMLRAYfLRTSQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQsyfetlfhkalnlhtanwflyLSTLR 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 376 KYASKVDHVMQLarkeafaragFFGAtglsgnLIVLSVLYKG------GLLMGSAHMtvgeLSSFLMYAFWVGISIGGLS 449
Cdd:TIGR01271 1110 WFQMRIDIIFVF----------FFIA------VTFIAIGTNQdgegevGIILTLAMN----ILSTLQWAVNSSIDVDGLM 1169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 450 SFYSELMKGLGAGGRLWELLEREPKLPFNEGVILNEKSFQ------GALEFKNVHFAYPARPEVpIFQDFSLSIPSGSVT 523
Cdd:TIGR01271 1170 RSVSRVFKFIDLPQEEPRPSGGGGKYQLSTVLVIENPHAQkcwpsgGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRV 1248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 524 ALVGPSGSGKSTVLSLLLRLYDpASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIaygadDP-SSVTAEE 602
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL-----DPyEQWSDEE 1322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 603 IQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDG 682
Cdd:TIGR01271 1323 IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN 1402
|
490 500 510
....*....|....*....|....*....|....*....
gi 171184400 683 RTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 721
Cdd:TIGR01271 1403 CTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
515-722 |
2.19e-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: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 515 LSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV--------WLRSKIGTVSQEPILFSC-SIA 585
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirQLRQHVGFVFQNFNLFPHrTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 586 ENIAYGaddPSSVTAEEiqRVAEVANAVAFIRNfpqgfntvVGEKGV------LLSGGQKQRIAIARALLKNPKILLLDE 659
Cdd:PRK11264 104 ENIIEG---PVIVKGEP--KEEATARARELLAK--------VGLAGKetsyprRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 660 ATSALDAEneyLVQEALDRLM----DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK11264 171 PTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
177-735 |
2.46e-25 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 112.70 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 177 FLTMSSVISMSAPFFLGKIIDVIytNPTVDYSDNLT-RLCLGLSAVFLcgaaanaIRVYLMQTSG---QRIVNRLRTSLF 252
Cdd:TIGR01271 88 LLYFGEATKAVQPLLLGRIIASY--DPFNAPEREIAyYLALGLCLLFI-------VRTLLLHPAIfglHHLGMQMRIALF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 253 SSI----LRQEVAFFDKTRTGELINRLSSDTALLGRSVtenlsdglraGAQASVGIS------MMFFVSPNLATFVLSVV 322
Cdd:TIGR01271 159 SLIykktLKLSSRVLDKISTGQLVSLLSNNLNKFDEGL----------ALAHFVWIAplqvilLMGLIWELLEVNGFCGL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 323 PPVSIIAVIYGRYLRKLTKVTQDSLAQATQ---LAEERIGNVRTVRAFGKE--MTEIEKYASKVDhvMQLARKEAFARAG 397
Cdd:TIGR01271 229 GFLILLALFQACLGQKMMPYRDKRAGKISErlaITSEIIENIQSVKAYCWEeaMEKIIKNIRQDE--LKLTRKIAYLRYF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 398 FFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYafwVGISI-----GGLSSFYSELmkglGAGGRLWELLER- 471
Cdd:TIGR01271 307 YSSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYCIV---LRMTVtrqfpGAIQTWYDSL----GAITKIQDFLCKe 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 472 -----EPKLPFNEGVILN-------------EKSFQGALEFK------NVHFAYPARPEVPIFQDFSLSIPSGSVTALVG 527
Cdd:TIGR01271 380 eyktlEYNLTTTEVEMVNvtaswdegigelfEKIKQNNKARKqpngddGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 528 PSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrsKIGTVSQEPILFSCSIAENIAYGaddpssVTAEEIqRVA 607
Cdd:TIGR01271 460 STGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFG------LSYDEY-RYT 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 608 EVANAVAF---IRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEA-LDRLMDGR 683
Cdd:TIGR01271 520 SVIKACQLeedIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNK 599
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 171184400 684 TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQSF 735
Cdd:TIGR01271 600 TRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAF 651
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
511-710 |
2.83e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.12 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKIGTVSQEPILF-SCSIAENI 588
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIALGIGMVHQHFMLVpNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 589 AYGADDPSSV---TAEEIQRVAEVANAVafirnfpqGF----NTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEAT 661
Cdd:COG3845 102 VLGLEPTKGGrldRKAARARIRELSERY--------GLdvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 662 SALDAeneylvQEAlDRLMD--------GRTVLVIAHRLSTIK-NANMVAVLDQGKIT 710
Cdd:COG3845 170 AVLTP------QEA-DELFEilrrlaaeGKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-722 |
3.40e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 105.95 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 509 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG-----TISLDGHDIRQLNPVW-LRSKIGTVSQEPILFSC 582
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 662
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWD---AVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 663 ALDAENEYLVQEALDRLMDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
513-720 |
4.79e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.28 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 513 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTVSQEPILFS-CSIAENIAYG 591
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 592 ADDPSSVTAEEIQRVAEVANAVaFIRNFpqgFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDA--ENE 669
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIARQM-GIEDL---LARLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPalRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 171184400 670 YLvqEALDRLMDGR--TVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLS 720
Cdd:PRK10771 168 ML--TLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
511-726 |
6.05e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.81 E-value: 6.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS----KIGTVSQEPILFS-CSIA 585
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 586 ENIAYGAdDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALD 665
Cdd:PRK10070 125 DNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171184400 666 AENEYLVQEALDRLM--DGRTVLVIAHRL-STIKNANMVAVLDQGKITEYGKHEELLSKPNGIY 726
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
492-721 |
6.20e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 6.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH--DIRQLNPVWLRSK 569
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQRVAEVA---NAVAFIRNFPQGFntvvgekgvlLSGGQKQRIAI 644
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVN-LKLPEDEVRKRVDNAlkrTGIEHLKDKPTHC----------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 645 ARALLKNPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIK-NANMVAVLDQGKITEYGKHEELL 719
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
..
gi 171184400 720 SK 721
Cdd:PRK13636 231 AE 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
495-717 |
7.42e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.13 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 495 KNVHFAY-PARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI--RQLNPVWLRSKI 570
Cdd:PRK13637 6 ENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEP--ILFSCSIAENIAYGaddPSS--VTAEEIQ-RVAEVANAVAFirnfpqGFNTVVGEKGVLLSGGQKQRIAIA 645
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAFG---PINlgLSEEEIEnRVKRAMNIVGL------DYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 646 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEE 717
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
491-723 |
7.48e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.30 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYParPEVPI----FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR----QLN 562
Cdd:PRK13641 2 SIKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 563 PVWLRSKIGTVSQ--EPILFSCSIAENIAYGaddPSSVTAEEiQRVAEvaNAVAFIRNFpqGFNTVVGEKGVL-LSGGQK 639
Cdd:PRK13641 80 LKKLRKKVSLVFQfpEAQLFENTVLKDVEFG---PKNFGFSE-DEAKE--KALKWLKKV--GLSEDLISKSPFeLSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 640 QRIAIARALLKNPKILLLDEATSALDAEN-EYLVQEALDRLMDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEE 717
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKE 231
|
....*.
gi 171184400 718 LLSKPN 723
Cdd:PRK13641 232 IFSDKE 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
491-716 |
7.86e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.94 E-value: 7.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH-----------DIR 559
Cdd:PRK11124 2 SIQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 560 QLnpvwlRSKIGTVSQE----PILfscSIAENI------AYGADDPSSVT-AEEI---QRVAEVANAvafirnFPQGfnt 625
Cdd:PRK11124 79 EL-----RRNVGMVFQQynlwPHL---TVQQNLieapcrVLGLSKDQALArAEKLlerLRLKPYADR------FPLH--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 626 vvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAV 703
Cdd:PRK11124 142 --------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVArKTASRVVY 213
|
250
....*....|...
gi 171184400 704 LDQGKITEYGKHE 716
Cdd:PRK11124 214 MENGHIVEQGDAS 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
492-709 |
9.95e-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: 102.83 E-value: 9.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAY-PARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKI 570
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALL 649
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYFAGLYGLKGDELTARLEELADRL--------GMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 650 KNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 709
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
508-735 |
1.01e-24 |
|
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: 104.55 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 508 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrsKIGTVSQEPILFSCSIAEN 587
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 588 IAYGaddpssVTAEEIqRVAEVANAVAF---IRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 664
Cdd:cd03291 118 IIFG------VSYDEY-RYKSVVKACQLeedITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 665 DAENEYLVQEA-LDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQSF 735
Cdd:cd03291 191 DVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTF 262
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
501-729 |
1.21e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 110.64 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 501 YPARPEVpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTisldghdirqlnpVWLRSKIGTVSQEPILF 580
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-------------VWAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 581 SCSIAENIAYGADDpssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA 660
Cdd:PTZ00243 734 NATVRGNILFFDEE----DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 661 TSALDAE-NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPngIYRKL 729
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATL 877
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
492-718 |
1.38e-24 |
|
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: 102.99 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL-RSKI 570
Cdd:TIGR03410 1 LEVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVanavafirnFPQGFnTVVGEKGVLLSGGQKQRIAIARALL 649
Cdd:TIGR03410 78 AYVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYEL---------FPVLK-EMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 650 KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 718
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
492-725 |
1.78e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.62 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL--RSK 569
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEP--ILFSCSIAENIAYGaddPSSV--TAEEIQ-RVAEVANAVAFirnfpQGFNTVVGEKgvlLSGGQKQRIAI 644
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFG---PLNLglSKEEVEkRVKEALKAVGM-----EGFENKPPHH---LSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 645 ARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
...
gi 171184400 723 NGI 725
Cdd:PRK13639 229 ETI 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
464-732 |
2.61e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.44 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 464 RLWELLERE-----PKLPFNEGvilneksfQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLS 538
Cdd:PLN03130 590 RLEELLLAEervllPNPPLEPG--------LPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 539 LLLRLYDPASGTIsldghdirqlnpVWLRSKIGTVSQEPILFSCSIAENIAYGADdpssVTAEEIQRVAEVANAVAFIRN 618
Cdd:PLN03130 662 AMLGELPPRSDAS------------VVIRGTVAYVPQVSWIFNATVRDNILFGSP----FDPERYERAIDVTALQHDLDL 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 619 FPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneYLVQEALDRL----MDGRTVLVIAHRLST 694
Cdd:PLN03130 726 LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA---HVGRQVFDKCikdeLRGKTRVLVTNQLHF 802
|
250 260 270
....*....|....*....|....*....|....*....
gi 171184400 695 IKNANMVAVLDQGKITEYGKHEELLSkpNG-IYRKLMNK 732
Cdd:PLN03130 803 LSQVDRIILVHEGMIKEEGTYEELSN--NGpLFQKLMEN 839
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
491-722 |
2.97e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 102.61 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYpARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDI--RQLNP 563
Cdd:PRK14267 4 AIETVNLRVYY-GSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 564 VWLRSKIGTVSQEPILFS-CSIAENIAYGADDPSSVTA-EEIQRVAEVA-NAVAFIRNFPQGFNTVVGEkgvlLSGGQKQ 640
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPhLTIYDNVAIGVKLNGLVKSkKELDERVEWAlKKAALWDEVKDRLNDYPSN----LSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 641 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHR-LSTIKNANMVAVLDQGKITEYGKHEELL 719
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
...
gi 171184400 720 SKP 722
Cdd:PRK14267 237 ENP 239
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
492-713 |
3.12e-24 |
|
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: 101.06 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAypaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL--YDPASGTISLDGHDIRQLnPVWLRSK 569
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDL-PPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IG-TVS-QEPIlfscsiaeniaygaddpssvtaeeiqRVAEVANAvAFIRNFPQGFntvvgekgvllSGGQKQRIAIARA 647
Cdd:cd03217 77 LGiFLAfQYPP--------------------------EIPGVKNA-DFLRYVNEGF-----------SGGEKKRNEILQL 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH--RLSTIKNANMVAVLDQGKITEYG 713
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
470-712 |
1.62e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.15 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 470 EREPKLPFNEGVILNEKsfqgALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG 549
Cdd:COG0488 298 DKTVEIRFPPPERLGKK----VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 550 TISLdGHDIrqlnpvwlrsKIGTVSQEPILFSC--SIAENIAYGADDpssvtAEEIQrvaevanavafIRNFPQGFN--- 624
Cdd:COG0488 371 TVKL-GETV----------KIGYFDQHQEELDPdkTVLDELRDGAPG-----GTEQE-----------VRGYLGRFLfsg 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 625 ----TVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmDGrTVLVIAH-R--LSTIkn 697
Cdd:COG0488 424 ddafKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV-- 495
|
250
....*....|....*
gi 171184400 698 ANMVAVLDQGKITEY 712
Cdd:COG0488 496 ATRILEFEDGGVREY 510
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
491-722 |
2.34e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.11 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS-----GTISLDGHDI--RQLNP 563
Cdd:PRK14258 7 AIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 564 VWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAfirNFPQGFNTVVGEKGVLLSGGQKQRIA 643
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDA---DLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 644 IARALLKNPKILLLDEATSALDA----ENEYLVQEAldRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQ-----GKITEYG 713
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFG 238
|
....*....
gi 171184400 714 KHEELLSKP 722
Cdd:PRK14258 239 LTKKIFNSP 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
492-731 |
2.51e-23 |
|
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: 104.38 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKN--VHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKS-TVLSLLlRLYDP----ASGTISLDGHDIRQLNPV 564
Cdd:COG4172 7 LSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 565 WLR----SKIGTVSQEPI-----LFSCS--IAENIA--YGADDpssvtAEEIQRVAEVANAVAfIRN-------FP-Qgf 623
Cdd:COG4172 85 ELRrirgNRIAMIFQEPMtslnpLHTIGkqIAEVLRlhRGLSG-----AAARARALELLERVG-IPDperrldaYPhQ-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 624 ntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIKN 697
Cdd:COG4172 157 ----------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDLLKDlqrelGMALLLITHDLGVVRR 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 171184400 698 -ANMVAVLDQGKITEYGKHEELLSKPNGIY-RKLMN 731
Cdd:COG4172 223 fADRVAVMRQGEIVEQGPTAELFAAPQHPYtRKLLA 258
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
182-465 |
2.63e-23 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 100.98 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 182 SVISMSAPFFLGKIIDVIYtnPTVDYsDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVA 261
Cdd:cd18570 15 TLLGIAGSFFFQILIDDII--PSGDI-NLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 262 FFDKTRTGELINRLsSDT----ALLGRSVTENLSDGLragaQASVGISMMFFVSPNLATFVLSVVPpvsIIAVIYGRYLR 337
Cdd:cd18570 92 FFETRKTGEIISRF-NDAnkirEAISSTTISLFLDLL----MVIISGIILFFYNWKLFLITLLIIP---LYILIILLFNK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 338 KLTKVTQDSLAQATQLAE---ERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVL 414
Cdd:cd18570 164 PFKKKNREVMESNAELNSyliESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLIL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 171184400 415 YKGGLLMGSAHMTVGELSSFL-MYAFWVGiSIGGLSSFYSELMKGLGAGGRL 465
Cdd:cd18570 244 WIGSYLVIKGQLSLGQLIAFNaLLGYFLG-PIENLINLQPKIQEAKVAADRL 294
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
514-722 |
3.16e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 101.19 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI-----------RQ------------LNPvwlRSKI 570
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaqkllRQkiqivfqnpygsLNP---RKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILFscsiaeNIAYGAddpssvtAEEIQRVAEVANAVA----FIRNFPQGFntvvgekgvllSGGQKQRIAIAR 646
Cdd:PRK11308 112 GQILEEPLLI------NTSLSA-------AERREKALAMMAKVGlrpeHYDRYPHMF-----------SGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 647 ALLKNPKILLLDEATSALDAEneylVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 719
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVS----VQaQVLNLMMDlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 243
|
...
gi 171184400 720 SKP 722
Cdd:PRK11308 244 NNP 246
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
503-690 |
4.68e-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: 98.11 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 503 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL---LRLYDPASGTISLDGhdiRQLNPVWLRSKIGTVSQEPIL 579
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 580 FSC-SIAENIAYGADDPSSVTAEEIQRVAEVA----NAVAfirnfpqgfNTVVGEKGVL-LSGGQKQRIAIARALLKNPK 653
Cdd:cd03234 93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVEdvllRDLA---------LTRIGGNLVKgISGGERRRVSIAVQLLWDPK 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 171184400 654 ILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAH 690
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIH 201
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
506-690 |
9.52e-23 |
|
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: 97.50 E-value: 9.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 506 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH----DIRQLNPVWL----RSKIGTVSQep 577
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREIlalrRRTIGYVSQ-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 578 ilFSCSIaeniaygaddPSsVTAEEIqrVAE------VANAVAFIR--------NFPQGF-----NTvvgekgvlLSGGQ 638
Cdd:COG4778 101 --FLRVI----------PR-VSALDV--VAEpllergVDREEARARarellarlNLPERLwdlppAT--------FSGGE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 639 KQRIAIARALLKNPKILLLDEATSALDAENE----YLVQEALDRlmdGRTVLVIAH 690
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKAR---GTAIIGIFH 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
512-718 |
1.05e-22 |
|
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: 97.06 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIGTVSQEPILFSCSIA-ENIAY 590
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 591 GADDPSSVTAEEIQRVAEVANAVAF-------IRNFpqgfntvvgekgvllSGGQKQRIAIARALLKNPKILLLDEATSA 663
Cdd:cd03265 97 HARLYGVPGAERRERIDELLDFVGLleaadrlVKTY---------------SGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 664 LDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL 718
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
492-733 |
1.48e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 97.99 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAY------PARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH--------- 556
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdyky 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 557 ---DIR---Q-----LNPvwlRSKIGTVSQEPILFScsiaeniaygaddpSSVTAEE-IQRVAEVANAVAFIRN----FP 620
Cdd:COG4167 85 rckHIRmifQdpntsLNP---RLNIGQILEEPLRLN--------------TDLTAEErEERIFATLRLVGLLPEhanfYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 621 QgfntvvgekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE------NEYL-VQEALdrlmdGRTVLVIAHRLS 693
Cdd:COG4167 148 H-----------MLSSGQKQRVALARALILQPKIIIADEALAALDMSvrsqiiNLMLeLQEKL-----GISYIYVSQHLG 211
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 171184400 694 TIKN-ANMVAVLDQGKITEYGKHEELLSKP-NGIYRKLMNKQ 733
Cdd:COG4167 212 IVKHiSDKVLVMHQGEVVEYGKTAEVFANPqHEVTKRLIESH 253
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
492-708 |
1.87e-22 |
|
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: 94.05 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrskig 571
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 tvsqepilfscsiAENIAYgaddpssvtaeeiqrvaevanavafirnFPQgfntvvgekgvlLSGGQKQRIAIARALLKN 651
Cdd:cd03221 62 -------------TVKIGY----------------------------FEQ------------LSGGEKMRLALAKLLLEN 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 652 PKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH-R--LSTIknANMVAVLDQGK 708
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
494-722 |
2.06e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 99.72 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 494 FKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTV 573
Cdd:PRK11000 6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 574 SQEPILFS-CSIAENIAYGADDPSSVTAEEIQRV---AEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALL 649
Cdd:PRK11000 81 FQSYALYPhLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 650 KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH-RLSTIKNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
492-721 |
2.60e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYpaRPEVPIFQ----DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDghDI--------R 559
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstskqK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 560 QLNPVwlRSKIGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQRV-AEVANAVAFIRNFpqgfntvvGEKGVL-LS 635
Cdd:PRK13643 78 EIKPV--RKKVGVVFQFPesQLFEETVLKDVAFGPQN-FGIPKEKAEKIaAEKLEMVGLADEF--------WEKSPFeLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 636 GGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 713
Cdd:PRK13643 147 GGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
....*...
gi 171184400 714 KHEELLSK 721
Cdd:PRK13643 227 TPSDVFQE 234
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
220-461 |
4.90e-22 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 97.35 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 220 AVFLCGAAANAIRVYLMQTS-----GQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGL 294
Cdd:cd18558 62 AYYYLIIGAIVLITAYIQGSfwglaAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 295 RAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEI 374
Cdd:cd18558 142 QNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 375 EKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSE 454
Cdd:cd18558 222 TRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA 301
|
....*..
gi 171184400 455 LMKGLGA 461
Cdd:cd18558 302 FANARGA 308
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
503-711 |
4.91e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 96.29 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 503 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQL--------------------- 561
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraqrkafrrdiqmvfqdsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 562 --NPvwlRSKIGTVSQEPILFSCSIAEniaygaddpssvtAEEIQRVAEVANAV----AFIRNFPQGfntvvgekgvlLS 635
Cdd:PRK10419 101 avNP---RKTVREIIREPLRHLLSLDK-------------AERLARASEMLRAVdlddSVLDKRPPQ-----------LS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 636 GGQKQRIAIARALLKNPKILLLDEATSALDAeneYLVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 709
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDL---VLQAGVIRLLKKlqqqfGTACLFITHDLRLVERfCQRVMVMDNGQI 230
|
..
gi 171184400 710 TE 711
Cdd:PRK10419 231 VE 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
492-723 |
5.42e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.59 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI---SLDGHDIRQLNPVwlRS 568
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGI--RK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEP--ILFSCSIAENIAYGaddPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIAR 646
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFG---PENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 647 ALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
515-722 |
6.69e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.02 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 515 LSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH---DIRQlnPVWL---RSKIGTVSQEPILFS-CSIAEN 587
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLppeKRRIGYVFQDARLFPhYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 588 IAYGAddpSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 667
Cdd:PRK11144 97 LRYGM---AKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 668 NEYLVQEALDRLmdGRTV----LVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK11144 163 RKRELLPYLERL--AREInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
493-723 |
6.78e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.54 E-value: 6.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 572
Cdd:COG4604 3 EIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 573 VSQEPILfscsiaeniaygaddPSSVTAEEIqrvaevanaVAFIRnFP--QGFNTVVGEKGV--------L--------- 633
Cdd:COG4604 80 LRQENHI---------------NSRLTVREL---------VAFGR-FPysKGRLTAEDREIIdeaiayldLedladryld 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 634 -LSGGQKQRIAIARALLKNPKILLLDEATSALDAenEYLVQ--EALDRLMD--GRTVLVIAHRLstiknaNMVAV----- 703
Cdd:COG4604 135 eLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM--KHSVQmmKLLRRLADelGKTVVIVLHDI------NFASCyadhi 206
|
250 260
....*....|....*....|..
gi 171184400 704 --LDQGKITEYGKHEELLSKPN 723
Cdd:COG4604 207 vaMKDGRVVAQGTPEEIITPEV 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
492-730 |
9.51e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 9.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARP--------EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPASGTISLDGHDIRQLNP 563
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 564 ---VWLRSKIGTVSQEPilFSC-----SIAENIAYG--ADDPSSVTAEEIQRVAEVANAV----AFIRNFPQGFntvvge 629
Cdd:PRK15134 355 rqlLPVRHRIQVVFQDP--NSSlnprlNVLQIIEEGlrVHQPTLSAAQREQQVIAVMEEVgldpETRHRYPAEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 630 kgvllSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTV--LVIAHRLSTIKN-ANMVAVLDQ 706
Cdd:PRK15134 427 -----SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQ 501
|
250 260
....*....|....*....|....*
gi 171184400 707 GKITEYGKHEELLSKPNGIY-RKLM 730
Cdd:PRK15134 502 GEVVEQGDCERVFAAPQQEYtRQLL 526
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
466-733 |
9.60e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.84 E-value: 9.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 466 WELLEREPKLPFNEGVILNEKSFQGALEFKNVHfayparpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD 545
Cdd:PRK13631 5 FMKKKLKVPNPLSDDIILRVKNLYCVFDEKQEN-------ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 546 PASGTISLD----GHDIRQLNPVW------------LRSKIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVA 607
Cdd:PRK13631 78 SKYGTIQVGdiyiGDKKNNHELITnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 608 EVANAVA----FIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY-LVQEALDRLMDG 682
Cdd:PRK13631 158 FYLNKMGlddsYLERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 683 RTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL-----------------------LSKPNGIYRKLMNKQ 733
Cdd:PRK13631 227 KTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIftdqhiinstsiqvprviqvindLIKKDPKYKKLYQKQ 301
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
171-438 |
1.44e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 96.10 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTN------------PTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQT 238
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGeasflplvpaslGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 239 SGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFV 318
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 319 LSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGF 398
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAF 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 171184400 399 FGATGLSGNLIVLSVLYKGGLL------MGSAHMTVGELSSFLMYA 438
Cdd:cd18565 241 FPVIRLVAGAGFVATFVVGGYWvldgppLFTGTLTVGTLVTFLFYT 286
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
506-722 |
1.55e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.60 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 506 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPIL-FSCSI 584
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 585 AENIAYG---------ADDPSSVTAeeIQRVAEVANAVAFIrnfPQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKIL 655
Cdd:PRK09536 95 RQVVEMGrtphrsrfdTWTETDRAA--VERAMERTGVAQFA---DRPVTS--------LSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 656 LLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
486-713 |
2.53e-21 |
|
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: 93.37 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 486 KSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlNPVW 565
Cdd:cd03220 14 KGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 566 LrskIG-TVSQEP-------ILFSCSIaeniaYGaddpssVTAEEIQRVaevanaVAFIRNF---PQGFNTVVGEkgvlL 634
Cdd:cd03220 88 L---LGlGGGFNPeltgrenIYLNGRL-----LG------LSRKEIDEK------IDEIIEFselGDFIDLPVKT----Y 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 635 SGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDRLM----DGRTVLVIAHRLSTIKN-ANMVAVLDQGKI 709
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAA---FQEKCQRRLRellkQGKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
....
gi 171184400 710 TEYG 713
Cdd:cd03220 221 RFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
491-734 |
2.74e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.61 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYP-------------------ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI 551
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 552 SLDGhdirqlNPVWL-------------RskigtvsqEPILFSCSIaeniaYGaddpssVTAEEI-QRVAEVanaVAF-- 615
Cdd:COG1134 84 EVNG------RVSALlelgagfhpeltgR--------ENIYLNGRL-----LG------LSRKEIdEKFDEI---VEFae 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 616 IRNFpqgFNTVVGekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDRLMD----GRTVLVIAHR 691
Cdd:COG1134 136 LGDF---IDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA---FQKKCLARIRElresGRTVIFVSHS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 171184400 692 LSTIKN-ANMVAVLDQGKITEYGKHEELLSKpngiYRKLMNKQS 734
Cdd:COG1134 206 MGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA----YEALLAGRE 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
500-704 |
2.94e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 500 AYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHdiRQLNPVWLRSKIgtvsqePIL 579
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAYVPQRSEV------PDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 580 FSCSIAENIAYGADDPSS----VTAEEIQRVAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKIL 655
Cdd:NF040873 70 LPLTVRDLVAMGRWARRGlwrrLTRDDRAAVDDALERVGLADLAGRQLGE--------LSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 171184400 656 LLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKNANMVAVL 704
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
492-713 |
3.33e-21 |
|
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: 92.34 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpvwlRSKIG 571
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILF-SCSIAENIAYGADdPSSVTAEEIQRVAEvanavAFIRNFPQG--FNTVVGEkgvlLSGGQKQRIAIARAL 648
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYLAQ-LKGLKKEEARRRID-----EWLERLELSeyANKRVEE----LSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 649 LKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 713
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
508-722 |
4.47e-21 |
|
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: 92.61 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 508 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK--IGTVSQEPILF-SCSI 584
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARlgIGYLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 585 AENIaYGADDPSSVTAEEIQRVAEvanavAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 664
Cdd:cd03218 93 EENI-LAVLEIRGLSKKEREEKLE-----ELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 665 D----AENEYLVQEALDRlmdGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:cd03218 165 DpiavQDIQKIIKILKDR---GIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
509-720 |
6.76e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.13 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 509 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEpilfscsiaeni 588
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 589 aygADDPSSVTAEEIQRVAEVANAVAFIRNFPQ------------GFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILL 656
Cdd:PRK10253 90 ---ATTPGDITVQELVARGRYPHQPLFTRWRKEdeeavtkamqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 657 LDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLS 720
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
492-716 |
8.49e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.05 E-value: 8.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHfaypARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTvLSLLL---RLYDPASGTISLDGHDIRQLnPVWLR 567
Cdd:COG0396 1 LEIKNLH----VSVEgKEILKGVNLTIKPGEVHAIMGPNGSGKST-LAKVLmghPKYEVTSGSILLDGEDILEL-SPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SK--IGTVSQEPILFS-CSIAE--NIAYGADDPSSVTAEE-IQRVAEVANAVafirNFPQGF-----NtvVGekgvlLSG 636
Cdd:COG0396 75 ARagIFLAFQYPVEIPgVSVSNflRTALNARRGEELSAREfLKLLKEKMKEL----GLDEDFldryvN--EG-----FSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH--RLSTIKNANMVAVLDQGKITEYG 713
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
...
gi 171184400 714 KHE 716
Cdd:COG0396 224 GKE 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
492-690 |
1.05e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.10 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---- 566
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 567 RSKIGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRvaevanAVAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIA 645
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEVPAVYAGLERKQRLLR------AQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 171184400 646 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH 690
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTH 202
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
492-659 |
1.11e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK-- 569
Cdd:COG1137 4 LEAENLVKSYGKRTVV---KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKRARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILF-SCSIAENIaYGADDPSSVTAEEIQRVAEvanavAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARAL 648
Cdd:COG1137 80 IGYLPQEASIFrKLTVEDNI-LAVLELRKLSKKEREERLE-----ELLEEF--GITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|.
gi 171184400 649 LKNPKILLLDE 659
Cdd:COG1137 152 ATNPKFILLDE 162
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
491-690 |
1.56e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.68 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdIRQLNPVWLRski 570
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQ-EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFntvvGEKGVL-LSGGQKQRIAIARAL 648
Cdd:PRK11248 73 GVVFQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-----EGA----EKRYIWqLSGGQRQRVGIARAL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 171184400 649 LKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAH 690
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWqeTGKQVLLITH 187
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
512-718 |
1.69e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.48 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpvwlRSKIGTVSQEPILF-SCSIAENIAY 590
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKVGEQLVY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 591 -----GaddpssVTAEEIQR----------VAEVANAvafirnfpqgfntVVGEkgvlLSGGQKQRIAIARALLKNPKIL 655
Cdd:COG4152 95 larlkG------LSKAEAKRradewlerlgLGDRANK-------------KVEE----LSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 656 LLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL 718
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
492-730 |
3.11e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.46 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKN--VHF------AYPARPEVPI--FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQL 561
Cdd:PRK15079 9 LEVADlkVHFdikdgkQWFWQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 562 NPV-WL--RSKIGTVSQEPiLFSC----SIAENIAygadDP-----SSVTAEEI-QRVAEVANAVAFIRN----FPQGFn 624
Cdd:PRK15079 89 KDDeWRavRSDIQMIFQDP-LASLnprmTIGEIIA----EPlrtyhPKLSRQEVkDRVKAMMLKVGLLPNlinrYPHEF- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 625 tvvgekgvllSGGQKQRIAIARALLKNPKILLLDEATSALD----AENEYLVQEaLDRLMdGRTVLVIAHRLSTIKN-AN 699
Cdd:PRK15079 163 ----------SGGQCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSD 230
|
250 260 270
....*....|....*....|....*....|..
gi 171184400 700 MVAVLDQGKITEYGKHEELLSKPNGIYRK-LM 730
Cdd:PRK15079 231 RVLVMYLGHAVELGTYDEVYHNPLHPYTKaLM 262
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
487-732 |
3.49e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.61 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 487 SFQGALEFKNVHFAYPARP--EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG-TISLD---GHDIRQ 560
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDyaiPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 561 LNPVW-LRSKIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFpqgfntvVGEKGVLLSGG 637
Cdd:PRK13645 82 IKEVKrLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDY-------VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 638 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYG- 713
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGs 234
|
250 260
....*....|....*....|....*...
gi 171184400 714 -----KHEELLSK----PNGIYrKLMNK 732
Cdd:PRK13645 235 pfeifSNQELLTKieidPPKLY-QLMYK 261
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
492-720 |
8.07e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.18 E-value: 8.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK-- 569
Cdd:PRK10895 4 LTAKNLAKAYKGRRVV---EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARARrg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQ-RVAEVANA--VAFIRNfpqgfntvvgEKGVLLSGGQKQRIAIA 645
Cdd:PRK10895 80 IGYLPQEASIFRrLSVYDNLMAVLQIRDDLSAEQREdRANELMEEfhIEHLRD----------SMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 646 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL-STIKNANMVAVLDQGKITEYGKHEELLS 720
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
491-719 |
1.40e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.25 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKI 570
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVV---DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQ----EPilfSCSIAENIA-----YGaddpssVTAEEIQrvAEVANAVAFIRnFPQGFNTVVGEkgvlLSGGQKQR 641
Cdd:PRK13537 83 GVVPQfdnlDP---DFTVRENLLvfgryFG------LSAAAAR--ALVPPLLEFAK-LENKADAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 642 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 719
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
511-690 |
1.97e-19 |
|
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: 87.91 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLrskigTVSQEPILFS-CSIAENIA 589
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 590 YgADDPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 669
Cdd:TIGR01184 77 L-AVDRVLPDLSKSERRAIVEEHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|...
gi 171184400 670 YLVQEALDRLMD--GRTVLVIAH 690
Cdd:TIGR01184 151 GNLQEELMQIWEehRVTVLMVTH 173
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
183-438 |
2.18e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 89.44 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 183 VISMSAPFFLGKIID-VIytnPTVDYsDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVA 261
Cdd:cd18567 16 LFALASPLYLQLVIDeVI---VSGDR-DLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 262 FFDKTRTGELINRLSS-DT--ALLGRSVTENLSDGLragaQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRK 338
Cdd:cd18567 92 YFEKRHLGDIVSRFGSlDEiqQTLTTGFVEALLDGL----MAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 339 LTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGG 418
Cdd:cd18567 168 ATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGA 247
|
250 260
....*....|....*....|
gi 171184400 419 LLMGSAHMTVGELSSFLMYA 438
Cdd:cd18567 248 LLVLDGEFTVGMLFAFLAYK 267
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
492-723 |
2.90e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAY-PARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI------RQLNP 563
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 564 VwlRSKIGTVSQ--EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNfpqgfntVVGEKGVLLSGGQKQR 641
Cdd:PRK13646 83 V--RKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRD-------VMSQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 642 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL 718
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
....*
gi 171184400 719 LSKPN 723
Cdd:PRK13646 234 FKDKK 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
492-723 |
2.92e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.71 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 571
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALL 649
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML--------GLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 650 KNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQG---VKELIDFLNDlpetyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
510-709 |
4.43e-19 |
|
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: 85.56 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKIGTVSQEP----ILFSCSI 584
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 585 AENIAYGaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 664
Cdd:cd03215 96 AENIALS----------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 171184400 665 DAENEYLVQEALDRLMD-GRTVLVIahrlST-----IKNANMVAVLDQGKI 709
Cdd:cd03215 136 DVGAKAEIYRLIRELADaGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
506-730 |
4.58e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 506 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI-----RQLNPvwLRSKIGTVSQEPILf 580
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQA--LRRDIQFIFQDPYA- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 581 SCSIAENIAYGADDPSSVTA-----EEIQRVAEVANAVAFIRN----FPQGFntvvgekgvllSGGQKQRIAIARALLKN 651
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGllpgkAAAARVAWLLERVGLLPEhawrYPHEF-----------SGGQRQRICIARALALN 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 652 PKILLLDEATSALDAE-NEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGIY-R 727
Cdd:PRK10261 482 PKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYtR 561
|
...
gi 171184400 728 KLM 730
Cdd:PRK10261 562 KLM 564
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
168-455 |
4.94e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 88.31 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 168 RRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLclglSAVFLCGAAANAIRVYLMQTSGQRI---V 244
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLD---GLTGF----ILLYLGLILIQALSVFLFIRLAGKIemgV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 245 NR-LRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVP 323
Cdd:cd18540 74 SYdLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 324 PVSIIAVIYGRYL----RKLTKVTqdslAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFF 399
Cdd:cd18540 154 VLAVVSIYFQKKIlkayRKVRKIN----SRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 400 GATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA---FWvgiSIGGLSSFYSEL 455
Cdd:cd18540 230 PIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYAtqfFE---PIQQLARVLAEL 285
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
491-716 |
5.27e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.12 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlNPV-----W 565
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVV---NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG------VPVpararL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 566 LRSKIGTVSQEPIL-FSCSIAEN-IAYGAddPSSVTAEEIQRVaeVANAVAFIRnFPQGFNTVVGEkgvlLSGGQKQRIA 643
Cdd:PRK13536 112 ARARIGVVPQFDNLdLEFTVRENlLVFGR--YFGMSTREIEAV--IPSLLEFAR-LESKADARVSD----LSGGMKRRLT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 644 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQG-KITEYGKHE 716
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHA 258
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
509-693 |
5.69e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.79 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 509 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQL---NPVWLRS-KIGTVSQ-EPILFSCS 583
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 IAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 663
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|..
gi 171184400 664 LDAENEYLVQEALDRL--MDGRTVLVIAHRLS 693
Cdd:PRK11629 176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
492-717 |
6.47e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.08 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEVPIFQDFSLSipSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV---WLRS 568
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMR--PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEP-ILFSCSIAENIAYgaddP---SSVTAEEIQR-VAEVANAVAFI---RNFPqgfntvvgekgVLLSGGQKQ 640
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVAI----PliiAGASGDDIRRrVSAALDKVGLLdkaKNFP-----------IQLSGGEQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 641 RIAIARALLKNPKILLLDEATSALDAEneylVQEALDRLMD-----GRTVLVIAHRLSTIKNANM-VAVLDQGKITEyGK 714
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLDDA----LSEGILRLFEefnrvGVTVLMATHDIGLISRRSYrMLTLSDGHLHG-GV 219
|
...
gi 171184400 715 HEE 717
Cdd:PRK10908 220 GGE 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
492-705 |
7.67e-19 |
|
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: 84.13 E-value: 7.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPArpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHdirqlnpvwlrSKIG 571
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQEPILFSCSIAENIAYGADDpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvLLSGGQKQRIAIARALLKN 651
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDD--------------------------------------VLSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 652 PKILLLDEATSALDAENE-YLVQEALDRLMdgrTVLVIAHRLSTIKNANMVAVLD 705
Cdd:cd03223 110 PKFVFLDEATSALDEESEdRLYQLLKELGI---TVISVGHRPSLWKFHDRVLDLD 161
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
503-690 |
1.14e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 503 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTvsQEPILFSC 582
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGH--RNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENIA-----YGADDPSsvtaeeiqrVAEVANAVAF--IRNFPQGFntvvgekgvlLSGGQKQRIAIARALLKNPKIL 655
Cdd:PRK13539 89 TVAENLEfwaafLGGEELD---------IAAALEAVGLapLAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 171184400 656 LLDEATSALDAENEYLVQEAL-DRLMDGRTVLVIAH 690
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
508-727 |
1.40e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 508 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH--DIRQLNPVWLRSKIGTVSQEP--ILFSCS 583
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 IAENIAYGADDPSSVTAEEIQRVAEVANAVAfirnfPQGFNTvvgEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 663
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVD-----AQHFRH---QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 664 LDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGIYR 727
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAMEQ 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
506-691 |
1.53e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.01 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 506 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLY--DPASGTISLDGHDIrqlnpvwlrskigtvSQEpilfsCS 583
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 IAENIaygADDPSSVTAEEIQRVAEVANAVAFIRNFPQgfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSA 663
Cdd:COG2401 102 LIDAI---GRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|
gi 171184400 664 LDAENEYLVQEALDRLMD--GRTVLVIAHR 691
Cdd:COG2401 167 LDRQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
515-709 |
1.86e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.83 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 515 LSIPSGSVTALVGPSGSGKSTVLSLLLRLY--DPASGT-ISLDGH----------DIRQLnpvwlRSKIGTVSQEPILFS 581
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRtvqregrlarDIRKS-----RANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 582 -CSIAENIAYGA--DDP------SSVTAEEIQRVAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLKNP 652
Cdd:PRK09984 100 rLSVLENVLIGAlgSTPfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 653 KILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKI 709
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
168-456 |
2.79e-18 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 86.11 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 168 RRRLAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRL 247
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLA---TLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 248 RTSLFSSILRQEVAFFDKTRTGELINRLSS-DTA---LLGRSVTENLSdglraGAQASVGISMMFFVSPNLATFVLSVVP 323
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRISElDTIrgfLTGTALTTLLD-----VLFSVIYIAVLFSYSPLLTLVVLATVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 324 PVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATG 403
Cdd:cd18782 153 LQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 171184400 404 LSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELM 456
Cdd:cd18782 233 FLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQ 285
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
492-720 |
3.95e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARP--EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISL---DGHDIRQLNPVW- 565
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 566 --------------------LRSKIGTVSQ--EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQG- 622
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRs 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 623 -FNtvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL-STIKNAN 699
Cdd:PRK13651 163 pFE---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEWTK 233
|
250 260
....*....|....*....|.
gi 171184400 700 MVAVLDQGKITEYGKHEELLS 720
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
505-696 |
5.24e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 505 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKIGTVSQE-PILFSC 582
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHkLAAQLGIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENIAYGADDPSSVTAEEI---QRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDE 659
Cdd:PRK09700 96 TVLENLYIGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 171184400 660 ATSAL-DAENEYLVQeALDRLM-DGRTVLVIAHRLSTIK 696
Cdd:PRK09700 172 PTSSLtNKEVDYLFL-IMNQLRkEGTAIVYISHKLAEIR 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
495-719 |
6.71e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.45 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 495 KNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVS 574
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 575 QE-PILFSCSIAENIAYGA----DDPSSVTAEEIQRVAEvanAVAFIRNFPQGFNTVVGekgvlLSGGQKQRIAIARALL 649
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGRypwhGALGRFGAADREKVEE---AISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 650 KNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAhrlsTIKNANMVA-------VLDQGKITEYGKHEELL 719
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA----VLHDINMAArycdylvALRGGEMIAQGTPAELM 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
509-709 |
8.02e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.96 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 509 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIsLDG----HDIRQlnpvwlrsKIGTVSQEPILFSC-S 583
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGtaplAEARE--------DTRLMFQDARLLPWkK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 IAENIAYGaddpssVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 663
Cdd:PRK11247 98 VIDNVGLG------LKGQWRDAALQALAAV--------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 171184400 664 LDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKI 709
Cdd:PRK11247 164 LDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
184-438 |
1.18e-17 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 84.39 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 184 ISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANA----IRVYLMQTSGQRIVNRLRTSLFSSILRQE 259
Cdd:cd18554 14 IPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFLILRPpveyYRQYFAQWIANKILYDIRKDLFDHLQKLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 260 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLaTFVLSVVPPVSIIAV--IYGRyLR 337
Cdd:cd18554 94 LRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKL-TFVSLVIFPFYILAVkyFFGR-LR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 338 KLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKG 417
Cdd:cd18554 172 KLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFA 251
|
250 260
....*....|....*....|.
gi 171184400 418 GLLMGSAHMTVGELSSFLMYA 438
Cdd:cd18554 252 AYLVIEGNLTVGTLVAFVGYM 272
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
491-666 |
1.29e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.89 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKNVHFAYPARpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSkI 570
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRD-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 571 GTVSQEPILFS-CSIAENIAYGADDpSSVTAEEI-QRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIA 645
Cdd:PRK11650 79 AMVFQNYALYPhMSVRENMAYGLKI-RGMPKAEIeERVAEAARILelePLLDRKPRE-----------LSGGQRQRVAMG 146
|
170 180
....*....|....*....|.
gi 171184400 646 RALLKNPKILLLDEATSALDA 666
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDA 167
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
513-723 |
3.74e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 513 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPASGTISLDGHDIRQLNPVWLRSKIGTVSQE-PILFSCSIAENIAYG 591
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 592 AdDPSSVTAEEIQRVAEVANAVAFI----RNFPQgfntvvgekgvlLSGGQKQRIAIARALLK-----NP--KILLLDEA 660
Cdd:COG4138 94 Q-PAGASSEAVEQLLAQLAEALGLEdklsRPLTQ------------LSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 661 TSALD-AEneylvQEALDRLMD-----GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:COG4138 161 MNSLDvAQ-----QAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
498-710 |
5.04e-17 |
|
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: 80.84 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 498 HFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHD--IRQLNpvwLRSKIGTV-- 573
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRKK---FLRRIGVVfg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 574 SQEPILFSCSIAENIA-----YGADDpssvtAEEIQRVAEVANAVafirNFPQGFNTVVGEkgvlLSGGQKQRIAIARAL 648
Cdd:cd03267 102 QKTQLWWDLPVIDSFYllaaiYDLPP-----ARFKKRLDELSELL----DLEELLDTPVRQ----LSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 649 LKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTI-KNANMVAVLDQGKIT 710
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLL 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
492-718 |
5.45e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIG 571
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 T--VSQEPILF-SCSIAENIAYGADDPSSVTAEEIQRVAEVanavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARAL 648
Cdd:PRK15439 88 IylVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQLLAAL------------GCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 649 LKNPKILLLDEATSALD-AENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 718
Cdd:PRK15439 156 MRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
504-720 |
7.35e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.71 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 504 RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLrLYDPA----SGTISLDGHDIrqlNPVWLRSKIGTVSQEPIL 579
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 580 F-SCSIAENIAYGAD--DPSSVTAEE-IQRVAEVANAVAFIRnfpqGFNTVVGEKGVL--LSGGQKQRIAIARALLKNPK 653
Cdd:TIGR00955 111 IpTLTVREHLMFQAHlrMPRRVTKKEkRERVDEVLQALGLRK----CANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 654 ILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLST--IKNANMVAVLDQGKITEYGKHEELLS 720
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
512-731 |
1.26e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKS-TVLSLLLRLYDPA----SGTISLDGHDIRQLNPVWLR----SKIGTVSQEPILfSC 582
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV-SL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENIAYGADDPSSV---------TAEEIQ---RVAeVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLK 650
Cdd:PRK15134 106 NPLHTLEKQLYEVLSLhrgmrreaaRGEILNcldRVG-IRQAAKRLTDYPHQ-----------LSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 651 NPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGI 725
Cdd:PRK15134 174 RPELLIADEPTTALDvsvqAQILQLLRELQQEL--NMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHP 251
|
....*..
gi 171184400 726 Y-RKLMN 731
Cdd:PRK15134 252 YtQKLLN 258
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
513-723 |
1.46e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 513 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPASGTISLDGHDIRQLNPVWLRSKIGTVSQE-PILFSCSIAENIA-Y 590
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 591 GADdpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLK-----NP--KILLLDEATSA 663
Cdd:PRK03695 94 QPD--KTRTEAVASALNEVAEALGLDDKLGRSVNQ--------LSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 664 LDAENeylvQEALDRLMD-----GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:PRK03695 164 LDVAQ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
489-695 |
3.34e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 489 QGALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLR 567
Cdd:PRK11288 2 SPYLSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQE----PILfscSIAENI-------AYGADDPSSVTAEEIQRVAEVANAVAfirnfPqgfNTVVGEkgvlLSG 636
Cdd:PRK11288 79 AGVAIIYQElhlvPEM---TVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDID-----P---DTPLKY----LSI 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALDA-ENEYLVQeALDRLMD-GRTVLVIAHRLSTI 695
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRAeGRVILYVSHRMEEI 203
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
492-712 |
3.70e-16 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 77.28 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA--SGTISLDGhdiRQLNPVWLRS 568
Cdd:cd03232 4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING---RPLDKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 kIGTVSQEPILFSCSiaeniaygaddpssvTAEEIQRVAevanavAFIRNfpqgfntvvgekgvlLSGGQKQRIAIARAL 648
Cdd:cd03232 81 -TGYVEQQDVHSPNL---------------TVREALRFS------ALLRG---------------LSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 649 LKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLS--TIKNANMVAVLDQGKITEY 712
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADsGQAILCTIHQPSasIFEKFDRLLLLKRGGKTVY 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
510-710 |
7.46e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.83 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKIGTVS----QEPILFSCSI 584
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 585 AENIAYGADDPSSvTAEEIQRVAEVANAVAFIRNF---PQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEAT 661
Cdd:COG1129 348 RENITLASLDRLS-RGGLLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 662 SALD--AENEylVQEALDRLMD-GRTVLVI----------AHRlstiknanmVAVLDQGKIT 710
Cdd:COG1129 423 RGIDvgAKAE--IYRLIRELAAeGKAVIVIsselpellglSDR---------ILVMREGRIV 473
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
508-734 |
1.36e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.60 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 508 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIrQLNPVWLRSKIGTVSQEPILFS-CSIAE 586
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 587 NIAYGADDPSSvTAEEIQRVAEvanavAFIRNfpQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDA 666
Cdd:TIGR01257 1023 HILFYAQLKGR-SWEEAQLEME-----AMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 667 ENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKIteYGKHEELLSKP---NGIY----RKLMNKQS 734
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRL--YCSGTPLFLKNcfgTGFYltlvRKMKNIQS 1168
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
505-722 |
1.41e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 505 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA----SGTISLDGhdiRQLNPVWLRSK-IGTVSQEP-- 577
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDG---KPVAPCALRGRkIATIMQNPrs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 578 ------ILFSCSIAENIAYGADDPSSVTAEEIQRVAeVANAVAFIRNFPqgFNtvvgekgvlLSGGQKQRIAIARALLKN 651
Cdd:PRK10418 91 afnplhTMHTHARETCLALGKPADDATLTAALEAVG-LENAARVLKLYP--FE---------MSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171184400 652 PKILLLDEATSALDAENEYLVQEALDRLMDGRT--VLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
503-667 |
1.63e-15 |
|
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: 75.47 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 503 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSC 582
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENIAYGADDPSSVtaeeiQRVAEVANAVAFIRNFPQgfnTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATS 662
Cdd:TIGR01189 89 SALENLHFWAAIHGGA-----QRTIEDALAAVGLTGFED---LPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
....*
gi 171184400 663 ALDAE 667
Cdd:TIGR01189 157 ALDKA 161
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
492-714 |
2.30e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnpvW-----L 566
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD----WqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 567 RSKIGTVSQEPILFS-CSIAENIAYG---ADdpSSVTAEEIQRVAEVanavafirnFPQGFNTVVGEKGVLlSGGQKQRI 642
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGgffAE--RDQFQERIKWVYEL---------FPRLHERRIQRAGTM-SGGEQQML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 643 AIARALLKNPKILLLDEATSALDAeneYLVQEALDRLM----DGRTVLVIAhrlstiKNANMVAVL-DQGKITEYGK 714
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAP---IIIQQIFDTIEqlreQGMTIFLVE------QNANQALKLaDRGYVLENGH 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
492-731 |
3.89e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.34 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAypaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---RS 568
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 KIGTVSQEPILFS-CSIAENIAYgaddPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 647
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAY----P---LREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHR----LSTIKNANMVAvlDQgKITEYGKHEELLSK 721
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVA--DK-KIVAHGSAQALQAN 234
|
250
....*....|
gi 171184400 722 PNGIYRKLMN 731
Cdd:PRK11831 235 PDPRVRQFLD 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
463-710 |
4.31e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 463 GRlwELLEREPKLPFNEGVILneksfqgaLEFKNVHfaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLR 542
Cdd:COG3845 239 GR--EVLLRVEKAPAEPGEVV--------LEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 543 LYDPASGTISLDGHDIRQLNPVWLR-SKIGTVSQEPILFSC----SIAENIAYGA-DDPSSVTAEEIQRVAEVANAVAFI 616
Cdd:COG3845 307 LRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRLGRGLvpdmSVAENLILGRyRRPPFSRGGFLDRKAIRAFAEELI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 617 RNF---PQGFNTVVGekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL 692
Cdd:COG3845 387 EEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDaGAAVLLISEDL 462
|
250
....*....|....*....
gi 171184400 693 STIKN-ANMVAVLDQGKIT 710
Cdd:COG3845 463 DEILAlSDRIAVMYEGRIV 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
520-720 |
5.21e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.77 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 520 GSVTALVGPSGSGKSTVLSLLL-RLYDPA-SGTISLDGhdiRQLNPVWLRsKIGTVSQEPILFS-CSIAENIAYGA--DD 594
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhLTVRETLVFCSllRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 595 PSSVTAEEIQRVAEvanAVAFIRNFPQGFNTVVGEKGVL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY-LV 672
Cdd:PLN03211 170 PKSLTKQEKILVAE---SVISELGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYrLV 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 171184400 673 QEALDRLMDGRTVLVIAHRLST--IKNANMVAVLDQGKITEYGKHEELLS 720
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
503-676 |
9.00e-15 |
|
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: 73.68 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 503 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSC 582
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENIAYGADDPSSVTAEEIqrVAEVanavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 662
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEA--LARV------------GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 171184400 663 ALDAENEYLVQEAL 676
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
183-456 |
1.27e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 75.29 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 183 VISMSAPFFLGKIID--VIYTNptvdySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 260
Cdd:cd18568 16 LLGLALPLFTQIILDrvLVHKN-----ISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 261 AFFDKTRTGELINRLSSD---TALLGRSVTENLSDGLragaQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLR 337
Cdd:cd18568 91 SFFASRKVGDIITRFQENqkiRRFLTRSALTTILDLL----MVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 338 KL-TKVTQDSLAQATQLAEErIGNVRTVRAFGKEMTEI----EKYASKVDHVMQLARKEAFARAgffgATGLSGNLIVLS 412
Cdd:cd18568 167 RNsREIFQANAEQQSFLVEA-LTGIATIKALAAERPIRwrweNKFAKALNTRFRGQKLSIVLQL----ISSLINHLGTIA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 171184400 413 VLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELM 456
Cdd:cd18568 242 VLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQ 285
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
171-383 |
1.28e-14 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 75.23 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 171 LAAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLsavFLCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALL---VLASVLLVLLRWLLFVLAGLRASRRLHDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPnlatFVLSVVPPVSIIAV 330
Cdd:cd18580 78 LLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYY 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 331 IYGRY-------LRKLtkvtqDSLAQA---TQLAEErIGNVRTVRAFGKEMTEIEKYASKVDH 383
Cdd:cd18580 154 LLQRYylrtsrqLRRL-----ESESRSplySHFSET-LSGLSTIRAFGWQERFIEENLRLLDA 210
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
188-438 |
1.44e-14 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 74.84 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 188 APFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTR 267
Cdd:cd18588 21 TPLFFQVIIDKVLVHRSLS---TLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 268 TGELINRL------------SSDTALLgrsvtenlsDGLRAGaqasVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRY 335
Cdd:cd18588 98 VGDTVARVrelesirqfltgSALTLVL---------DLVFSV----VFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 336 LRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASkvdhvmQLAR--KEAFARAGFFGATGLSGNLI---- 409
Cdd:cd18588 165 LRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEE------LLARyvKASFKTANLSNLASQIVQLIqklt 238
|
250 260
....*....|....*....|....*....
gi 171184400 410 VLSVLYKGGLLMGSAHMTVGELSSFLMYA 438
Cdd:cd18588 239 TLAILWFGAYLVMDGELTIGQLIAFNMLA 267
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
519-705 |
1.65e-14 |
|
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: 71.25 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 519 SGSVTALVGPSGSGKSTVLSLLLRLYDPASGT-ISLDGHDIRQLNPVWLRskigtvsqepilfscsiaeniaygaddpss 597
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 598 vtaeeiqrvaevanavafirnfpqgfNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALD 677
Cdd:smart00382 51 --------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
170 180 190
....*....|....*....|....*....|....*
gi 171184400 678 RLMD-------GRTVLVIAHRLSTIKNANMVAVLD 705
Cdd:smart00382 105 LRLLlllksekNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
492-713 |
1.87e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.91 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL--RLYDPASGTISLDGHDIRQLNPVwLRSK 569
Cdd:CHL00131 8 LEIKNLHASVN---ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPE-ERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGT------------VSQEPILFSCSIAENIAYGADDPSSVTAEEIqrVAEVANAV----AFI-RNFPQGFntvvgekgv 632
Cdd:CHL00131 84 LGIflafqypieipgVSNADFLRLAYNSKRKFQGLPELDPLEFLEI--INEKLKLVgmdpSFLsRNVNEGF--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 633 llSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH--RLSTIKNANMVAVLDQGKI 709
Cdd:CHL00131 153 --SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKI 230
|
....
gi 171184400 710 TEYG 713
Cdd:CHL00131 231 IKTG 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
510-723 |
4.12e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnpVWLRSKIGTVSQ-EPILFSCSI-AEN 587
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYVPQsEEVDWSFPVlVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 588 IA----YGADDPSSVTAEEIQRVAEVANAVAFIRNFPqgfNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSA 663
Cdd:PRK15056 100 VVmmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFR---HRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 664 LDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 723
Cdd:PRK15056 173 VDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAEN 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
504-722 |
5.62e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 504 RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILfSCS 583
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPST-SLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 IAENIAYGADDP----SSVTAEEI-QRVAEVANAVAFIRN----FPQgfntvvgekgvLLSGGQKQRIAIARALLKNPKI 654
Cdd:PRK15112 102 PRQRISQILDFPlrlnTDLEPEQReKQIIETLRQVGLLPDhasyYPH-----------MLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 655 LLLDEATSALDAEneylVQEALDRLM------DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 722
Cdd:PRK15112 171 IIADEALASLDMS----MRSQLINLMlelqekQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
505-711 |
7.32e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 505 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPA---SGTISLDG-----HDIRQLNpvwlRSKIGTVSQE 576
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRDSE----ALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 577 ----PILfscSIAENI-------AYGADDPSSVTAEEIQRVAEVAnavafIRNFPQgfnTVVGEKGVllsgGQKQRIAIA 645
Cdd:NF040905 87 laliPYL---SIAENIflgneraKRGVIDWNETNRRARELLAKVG-----LDESPD---TLVTDIGV----GKQQLVEIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 646 RALLKNPKILLLDEATSAL-DAENEYLvqeaLDRLMD----GRTVLVIAHRLSTI-KNANMVAVLDQGKITE 711
Cdd:NF040905 152 KALSKDVKLLILDEPTAALnEEDSAAL----LDLLLElkaqGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
510-730 |
7.66e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.27 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDiRQLNPVW----------LRSKIGTVSQEP-- 577
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDLYalseaerrrlLRTEWGFVHQHPrd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 578 -ILFSCSIAENI-----AYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGFntvvgekgvllSGGQKQRIAIARALLKN 651
Cdd:PRK11701 101 gLRMQVSAGGNIgerlmAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTF-----------SGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 652 PKILLLDEATSALDAEneylVQEaldRLMD---------GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 721
Cdd:PRK11701 170 PRLVFMDEPTGGLDVS----VQA---RLLDllrglvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDD 242
|
....*....
gi 171184400 722 PNGIYRKLM 730
Cdd:PRK11701 243 PQHPYTQLL 251
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
492-708 |
9.43e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPA---SGTISLDG-----HDIRQLNp 563
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGeelqaSNIRDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 564 vwlRSKIGTVSQEPILFS-CSIAENIAYGAD-------DPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEkgvlLS 635
Cdd:PRK13549 81 ---RAGIAIIHQELALVKeLSVLENIFLGNEitpggimDYDAMYLRAQKLLAQLKLDI--------NPATPVGN----LG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 636 GGQKQRIAIARALLKNPKILLLDEATSAL-DAENEYLvqeaLDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGK 708
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLtESETAVL----LDIIRDlkahGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
496-728 |
1.15e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 496 NVHFaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP--VWLRSK---- 569
Cdd:PRK10261 19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRqvIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 --------IGTVSQEPI-----LFScsIAENIAYGADDPSSVTAEEiqRVAEVANAVAFIRnFPQGfNTVVGEKGVLLSG 636
Cdd:PRK10261 98 mrhvrgadMAMIFQEPMtslnpVFT--VGEQIAESIRLHQGASREE--AMVEAKRMLDQVR-IPEA-QTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRT--VLVIAHRLSTIKN-ANMVAVLDQGKITEYG 713
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETG 251
|
250
....*....|....*
gi 171184400 714 KHEELLSKPNGIYRK 728
Cdd:PRK10261 252 SVEQIFHAPQHPYTR 266
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
489-695 |
1.16e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 489 QGALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlRS 568
Cdd:PRK10762 2 QALLQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP---KS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 569 K----IGTVSQE-PILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIA 643
Cdd:PRK10762 76 SqeagIGIIHQElNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 644 IARALLKNPKILLLDEATSAL-DAENEYL---VQEALDRlmdGRTVLVIAHRLSTI 695
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTETESLfrvIRELKSQ---GRGIVYISHRLKEI 204
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
513-722 |
1.37e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 513 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPaSGTIS-----LDGHDIRQLNPV----WLRSKIGTVSQEPIlfSCS 583
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTadrfrWNGIDLLKLSPRerrkIIGREIAMIFQEPS--SCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 iaeniaygadDPSSVTAEEIqrvAEVANAVAFIRNFPQGFNTV----------VG---EKGVL------LSGGQKQRIAI 644
Cdd:COG4170 103 ----------DPSAKIGDQL---IEAIPSWTFKGKWWQRFKWRkkraiellhrVGikdHKDIMnsypheLTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 645 ARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 721
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249
|
.
gi 171184400 722 P 722
Cdd:COG4170 250 P 250
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
512-732 |
2.34e-13 |
|
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: 70.51 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGS-----VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIrQLNPVWLRSKI-GTVSQepILFScsia 585
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYeGTVRD--LLSS---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 586 eniaygaDDPSSVTAEEIQrvAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALD 665
Cdd:cd03237 85 -------ITKDFYTHPYFK--TEIAKPLQIEQILDREVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 666 AENEYLVQEALDRLMDG--RTVLVIAHRLSTIKN-ANMVAVLDqGKITEYGkheeLLSKPNGIyRKLMNK 732
Cdd:cd03237 148 VEQRLMASKVIRRFAENneKTAFVVEHDIIMIDYlADRLIVFE-GEPSVNG----VANPPQSL-RSGMNR 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
492-691 |
2.41e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI--------RQLNP 563
Cdd:PRK13540 2 LDVIELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctyqKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 564 VWLRSKIgtvsqEPILfscSIAENIAYgaDDPSSVTAEEIQRVAEVANAVAFIrNFPQGfntvvgekgvLLSGGQKQRIA 643
Cdd:PRK13540 79 VGHRSGI-----NPYL---TLRENCLY--DIHFSPGAVGITELCRLFSLEHLI-DYPCG----------LLSSGQKRQVA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 171184400 644 IARALLKNPKILLLDEATSALDAEN-EYLVQEALDRLMDGRTVLVIAHR 691
Cdd:PRK13540 138 LLRLWMSKAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
514-725 |
2.48e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSKIGTVS--QEPILF-SCSIAEN--I 588
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVRtfQHVRLFrEMTVIENllV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 589 AYGADDPSSVTA-------------EEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKIL 655
Cdd:PRK11300 104 AQHQQLKTGLFSgllktpafrraesEALDRAATWLERV--------GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 656 LLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGI 725
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDVI 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
506-665 |
2.88e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 506 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLRSK-IGTVSQEPILFS 581
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 582 CSIA-ENIAYgaddPSSVTAEEIQRVAEvaNAVAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA 660
Cdd:PRK10584 102 TLNAlENVEL----PALLRGESSRQSRN--GAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
....*
gi 171184400 661 TSALD 665
Cdd:PRK10584 174 TGNLD 178
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
511-707 |
5.82e-13 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 69.57 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVL------SLLLRLYdpASGTISLDGHDIRQLNPVwlrSKIGTVSQEPI------ 578
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLH--LKKEQPGNHDRIEGLEHI---DKVIVIDQSPIgrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 579 --------------LFsCSIAE----------------NIAygadDPSSVTAEEiqrvaevanAVAFIRNFPQGFNTV-- 626
Cdd:cd03271 87 npatytgvfdeireLF-CEVCKgkrynretlevrykgkSIA----DVLDMTVEE---------ALEFFENIPKIARKLqt 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 627 ----------VGEKGVLLSGGQKQRIAIARALLK---NPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL 692
Cdd:cd03271 153 lcdvglgyikLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNL 232
|
250
....*....|....*
gi 171184400 693 STIKNANMvaVLDQG 707
Cdd:cd03271 233 DVIKCADW--IIDLG 245
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
492-721 |
1.11e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARP-EV-PIfqdfSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 569
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFSCSIaeNIAYGADDPSSVTA--EEIQ---RVAEVANAVAFIRnfpqgfntvvgekgvlLSGGQKQRIAI 644
Cdd:PRK10522 399 FSAVFTDFHLFDQLL--GPEGKPANPALVEKwlERLKmahKLELEDGRISNLK----------------LSKGQKKRLAL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 645 ARALLKNPKILLLDEATSALDAE-NEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKITE-YGKHEELLSK 721
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
494-666 |
1.19e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 67.29 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 494 FKNVHF-AYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL---LRLYDPASGTISLDGHDIRqlnpvwlrsK 569
Cdd:cd03233 6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYK---------E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQEPILFScsiaeniayGADD--PSSVTAEEIQRVAEVANAVAFIRnfpqgfntvvgekGVllSGGQKQRIAIARA 647
Cdd:cd03233 77 FAEKYPGEIIYV---------SEEDvhFPTLTVRETLDFALRCKGNEFVR-------------GI--SGGERKRVSIAEA 132
|
170
....*....|....*....
gi 171184400 648 LLKNPKILLLDEATSALDA 666
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDS 151
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
511-721 |
1.63e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRsKIGTV----SQ----EPILFSC 582
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQlwwdLPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENIaYGADDpssvtAEEIQRVAEvanavafirnfpqgFNTVVGEKGVL------LSGGQKQRIAIARALLKNPKILL 656
Cdd:COG4586 118 RLLKAI-YRIPD-----AEYKKRLDE--------------LVELLDLGELLdtpvrqLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 657 LDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 721
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
492-694 |
4.48e-12 |
|
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: 69.19 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLdGHDIrqlnpvwlrsKIG 571
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQ--EPILFSCSIAENIAYGADdpssvtaeeIQRVAEVA-NAVAFIRNFpqGFNTVVGEKGV-LLSGGQKQRIAIARA 647
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGLD---------IIKLGKREiPSRAYVGRF--NFKGSDQQKKVgQLSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH------RLST 694
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
492-721 |
5.21e-12 |
|
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: 69.06 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL--LRLYDPASGTISLDGHDIRQLNPVWLRSK 569
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVALCEKCGYVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTvsqepilfSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFP-QGFNTVV-------------GEKGVL-- 633
Cdd:TIGR03269 78 VGE--------PCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFAlYGDDTVLdnvlealeeigyeGKEAVGra 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 634 -------------------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRL 692
Cdd:TIGR03269 150 vdliemvqlshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWP 229
|
250 260 270
....*....|....*....|....*....|
gi 171184400 693 STIKNANMVAV-LDQGKITEYGKHEELLSK 721
Cdd:TIGR03269 230 EVIEDLSDKAIwLENGEIKEEGTPDEVVAV 259
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
505-714 |
7.94e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 505 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVL-SLLLRLYD---PASGTISLDGHDIRQLNPvWLRSKIGTVSQEPILF 580
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGfhiGVEGVITYDGITPEEIKK-HYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 581 -SCSIAENIAYGA------DDPSSVTAEEiqRVAEVANAVAFIRNFPQGFNTVVGE---KGVllSGGQKQRIAIARALLK 650
Cdd:TIGR00956 151 pHLTVGETLDFAArcktpqNRPDGVSREE--YAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLG 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 651 NPKILLLDEATSALDAENEYLVQEALD---RLMDGrTVLVIAHRLS--TIKNANMVAVLDQGKITEYGK 714
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKtsaNILDT-TPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGP 294
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
172-389 |
1.10e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 66.34 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 172 AAAVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVF-LCGAAANAIRVYLMQTSGQRIVNRLRTS 250
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIYALIsLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPnlaTFVLsvvpPVSIIAV 330
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSP---AFLL----PAVVLAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 331 IYGRYLRKLTKVTQD-----SLAQA---TQLAEERIGNVrTVRAFGKEMTEIEKYASKVDHVMQLAR 389
Cdd:cd18604 155 LYVYIGRLYLRASRElkrleSVARSpilSHFGETLAGLV-TIRAFGAEERFIEEMLRRIDRYSRAFR 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
504-667 |
1.21e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 504 RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS--KIGTVS------- 574
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllYLGHQPgiktelt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 575 -QEPILFSCSIAENiaygADDpssvtaeeiqrvAEVANAVAfirnfpqgfntVVGEKGVL------LSGGQKQRIAIARA 647
Cdd:PRK13538 91 aLENLRFYQRLHGP----GDD------------EALWEALA-----------QVGLAGFEdvpvrqLSAGQQRRVALARL 143
|
170 180
....*....|....*....|
gi 171184400 648 LLKNPKILLLDEATSALDAE 667
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQ 163
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
500-690 |
1.96e-11 |
|
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: 67.27 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 500 AYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTisldghdirqlnpVWLRS--KIGTVSQEP 577
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-------------ARPQPgiKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 578 IL-FSCSIAENIAYGADDpssvTAEEIQRVAEVANAVAfirNFPQGFNTVVGEKGVL----------------------- 633
Cdd:TIGR03719 78 QLdPTKTVRENVEEGVAE----IKDALDRFNEISAKYA---EPDADFDKLAAEQAELqeiidaadawdldsqleiamdal 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 634 -----------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmDGrTVLVIAH 690
Cdd:TIGR03719 151 rcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
512-726 |
1.99e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKS-TVLSL--LLRLYDPASGTISLDGHDI-----RQLNPvwLRS-KIGTVSQEPIlfsC 582
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREIlnlpeKELNK--LRAeQISMIFQDPM---T 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIaeniaygadDPSSVTAEEIQRV----AEVANAVAF------------------IRNFPQGFntvvgekgvllSGGQKQ 640
Cdd:PRK09473 109 SL---------NPYMRVGEQLMEVlmlhKGMSKAEAFeesvrmldavkmpearkrMKMYPHEF-----------SGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 641 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEE 717
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARD 248
|
....*....
gi 171184400 718 LLSKPNGIY 726
Cdd:PRK09473 249 VFYQPSHPY 257
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
460-705 |
2.33e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.08 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 460 GAGGRLWELLEREPKLPFNEGVIlneksfqgalEFKNVHFAYPARpEVPIfQDFSLSIPSGSVTALVGPSGSGKSTVLSL 539
Cdd:TIGR00954 430 REGGRNSNLVPGRGIVEYQDNGI----------KFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRI 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 540 LLRLYDPASGTISLDGhdirqlnpvwlRSKIGTVSQEPILFSCSIAENIAYgaddPSSV---------TAEEIQRVAEVA 610
Cdd:TIGR00954 498 LGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIY----PDSSedmkrrglsDKDLEQILDNVQ 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 611 NAVAFIRNfpQGFNTVVGEKGVLlSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH 690
Cdd:TIGR00954 563 LTHILERE--GGWSAVQDWMDVL-SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSH 637
|
250
....*....|....*
gi 171184400 691 RLSTIKNANMVAVLD 705
Cdd:TIGR00954 638 RKSLWKYHEYLLYMD 652
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
169-455 |
2.66e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 65.22 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 169 RRLAAAVGFLTM-SSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTrlcLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRL 247
Cdd:cd18555 1 KKLLISILLLSLlLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLG---IGILILFLLYGLFSFLRGYIIIKLQTKLDKSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 248 RTSLFSSILRQEVAFFDKTRTGELINRLSSDTA---LLGRSVTENLSDGLRAGaqasVGISMMFFVSPNLATFVLSVVPP 324
Cdd:cd18555 78 MSDFFEHLLKLPYSFFENRSSGDLLFRANSNVYirqILSNQVISLIIDLLLLV----IYLIYMLYYSPLLTLIVLLLGLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 325 VSIIAVIYGRYLRKLTK--VTQDSLAQATQLaeERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFaRAGFFG-- 400
Cdd:cd18555 154 IVLLLLLTRKKIKKLNQeeIVAQTKVQSYLT--ETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKER-LSNILNsi 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 401 ATGLS--GNLIVLSVlykGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSEL 455
Cdd:cd18555 231 SSSIQfiAPLLILWI---GAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQF 284
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
512-665 |
3.04e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKIGTVSQEP----ILFSCSIAE 586
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 587 NIAYGADDPSSVTAEEIQRVAEVANAVAFIRNF----PqGFNTVVGekgvLLSGGQKQRIAIARALLKNPKILLLDEATS 662
Cdd:PRK10762 350 NMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
...
gi 171184400 663 ALD 665
Cdd:PRK10762 425 GVD 427
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
520-695 |
3.41e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 520 GSVTALVGPSGSGKSTVLSLLLRLYDPA---SGTISLDGhdiRQLNPVWLRSkIGTVSQEPI-LFSCSIAENIAYGA--D 593
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNG---RPLDSSFQRS-IGYVQQQDLhLPTSTVRESLRFSAylR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 594 DPSSVTAEEIQRVAEvanAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILL-LDEATSALDAENEYLV 672
Cdd:TIGR00956 865 QPKSVSKSEKMEYVE---EVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSI 941
|
170 180
....*....|....*....|....
gi 171184400 673 QEALDRLMD-GRTVLVIAHRLSTI 695
Cdd:TIGR00956 942 CKLMRKLADhGQAILCTIHQPSAI 965
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
493-690 |
4.20e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIsldghdirqlnpvwlrsKIGT 572
Cdd:PRK11147 321 EMENVNYQIDGKQLV---KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------------HCGT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 573 vSQEPILFSC---------SIAENIAYGADDpssVTAEEIQRvaevaNAVAFIRNF---PQGFNTVVGEkgvlLSGGQKQ 640
Cdd:PRK11147 381 -KLEVAYFDQhraeldpekTVMDNLAEGKQE---VMVNGRPR-----HVLGYLQDFlfhPKRAMTPVKA----LSGGERN 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 171184400 641 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRlMDGrTVLVIAH 690
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS-YQG-TVLLVSH 495
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
514-720 |
4.27e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.98 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISL----DGHDIRQLNPVwLRSK----IGTVSQEPILFS-CSI 584
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRakryIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 585 AENI--AYGADDPSsvtaeeiqrvaEVANAVAFIRNFPQGFNTVVGEKgVL------LSGGQKQRIAIARALLKNPKILL 656
Cdd:TIGR03269 383 LDNLteAIGLELPD-----------ELARMKAVITLKMVGFDEEKAEE-ILdkypdeLSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 657 LDEATSALDAENEYLVQEAL--DRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLS 720
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
495-692 |
6.00e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 495 KNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlRSKIGTVS 574
Cdd:PRK09544 8 ENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 575 QEpILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAvAFIRNFPQgfntvvgEKgvlLSGGQKQRIAIARALLKNPKI 654
Cdd:PRK09544 74 QK-LYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQA-GHLIDAPM-------QK---LSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 171184400 655 LLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRL 692
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
492-715 |
8.55e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.89 E-value: 8.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL--RLYDPASGTISLDGHDIRQLNP------ 563
Cdd:PRK09580 2 LSIKDLHVSVE---DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 564 -VWLR----SKIGTVSQEpILFSCSIAENIAYGADDP------SSVTAEEIQRVAEVANAVAfiRNFPQGFntvvgekgv 632
Cdd:PRK09580 79 gIFMAfqypVEIPGVSNQ-FFLQTALNAVRSYRGQEPldrfdfQDLMEEKIALLKMPEDLLT--RSVNVGF--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 633 llSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDG-RTVLVIAHR---LSTIKnANMVAVLDQGK 708
Cdd:PRK09580 147 --SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHYqriLDYIK-PDYVHVLYQGR 223
|
....*..
gi 171184400 709 ITEYGKH 715
Cdd:PRK09580 224 IVKSGDF 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
496-713 |
1.02e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 496 NVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL-RLYDPA-------SGTISLDGHDIRQLNPVWLR 567
Cdd:PRK13547 3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 568 SKIGTVSQ--EPIlFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAvAFIRnfpQGFNTVVGEKGVLLSGGQKQRIAIA 645
Cdd:PRK13547 83 RLRAVLPQaaQPA-FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQ-ALAL---AGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 646 RALLK---------NPKILLLDEATSALDAENEYLVQEALDRLM-DGRT-VLVIAHRLS-TIKNANMVAVLDQGKITEYG 713
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
512-695 |
1.44e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGS-----VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDghdIR-QLNPVWLRSKI-GTVSQepilFSCSI 584
Cdd:PRK13409 352 DFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKiSYKPQYIKPDYdGTVED----LLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 585 AENIAygaddpSSVTAEEIQRvaevanavafirnfPQGFNTV----VGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 660
Cdd:PRK13409 425 TDDLG------SSYYKSEIIK--------------PLQLERLldknVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190
....*....|....*....|....*....|....*..
gi 171184400 661 TSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTI 695
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
500-667 |
2.17e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 500 AYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTisldghdirqlnpVWLRS--KIGTVSQEP 577
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-------------ARPAPgiKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 578 IL-FSCSIAENIAYGADDpssvTAEEIQRVAEVANAVAfirNFPQGFNTVVGEKGVL----------------------- 633
Cdd:PRK11819 80 QLdPEKTVRENVEEGVAE----VKAALDRFNEIYAAYA---EPDADFDALAAEQGELqeiidaadawdldsqleiamdal 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 171184400 634 -----------LSGGQKQRIAIARALLKNPKILLLDEATSALDAE 667
Cdd:PRK11819 153 rcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
183-436 |
2.65e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 62.22 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 183 VISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAF 262
Cdd:cd18566 16 ILALATPLFILQVYDRVIPNESIP---TLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 263 FDKTRTGELINRLSSdtallgrsvTENLSDGLrAGAQASVGISM---------MFFVSPNLATFVLSVVPPVSIIAVIYG 333
Cdd:cd18566 93 FEREPSGAHLERLNS---------LEQIREFL-TGQALLALLDLpfvliflglIWYLGGKLVLVPLVLLGLFVLVAILLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 334 RYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKY----ASKVDHVMQLARKEAFARAGFFGATGLSGnLI 409
Cdd:cd18566 163 PILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYerlqANAAYAGFKVAKINAVAQTLGQLFSQVSM-VA 241
|
250 260
....*....|....*....|....*..
gi 171184400 410 VLSVlykGGLLMGSAHMTVGELSSFLM 436
Cdd:cd18566 242 VVAF---GALLVINGDLTVGALIACTM 265
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
510-695 |
3.01e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIPSGS-----VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDghdirqLN----PVWLRSKI-GTVSQepIL 579
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKisykPQYISPDYdGTVEE--FL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 580 FScsiaeniAYGADDPSSVTAEEIQRvaevanavafirnfPQGFNTVVgEKGVL-LSGGQKQRIAIARALLKNPKILLLD 658
Cdd:COG1245 423 RS-------ANTDDFGSSYYKTEIIK--------------PLGLEKLL-DKNVKdLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190
....*....|....*....|....*....|....*....
gi 171184400 659 EATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTI 695
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI 519
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
496-718 |
6.18e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 496 NVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLlrlydpaSGTISLD------GHDIR----QLNPVw 565
Cdd:PRK11147 5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdgriiyEQDLIvarlQQDPP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 566 lRSKIGTVsqepilFScSIAENIAYGAD--------------DPSSVTAEEIQRVAEV---ANAvafiRNFPQGFNTVVG 628
Cdd:PRK11147 77 -RNVEGTV------YD-FVAEGIEEQAEylkryhdishlvetDPSEKNLNELAKLQEQldhHNL----WQLENRINEVLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 629 EKGV-------LLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-EYLvqEALdrLMDGRTVLV-IAHRLSTIKN-A 698
Cdd:PRK11147 145 QLGLdpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL--EGF--LKTFQGSIIfISHDRSFIRNmA 220
|
250 260
....*....|....*....|....*....
gi 171184400 699 NMVAVLDQGKITEY---------GKHEEL 718
Cdd:PRK11147 221 TRIVDLDRGKLVSYpgnydqyllEKEEAL 249
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
174-459 |
7.40e-10 |
|
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: 60.59 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 174 AVGFLTMSSVISMSAPFFLGKIIDVIyTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFS 253
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDAL-SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 254 SILRQEVAFFDKTRTGEL---INRLSsdtallgRSVTENLSdglragaqasvgiSMMFFVSPNLATFVLSVV-------P 323
Cdd:cd18582 80 HLHSLSLRFHLSRKTGALsraIERGT-------RGIEFLLR-------------FLLFNILPTILELLLVCGilwylygW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 324 PVSIIA----VIYGRYLRKLTK---------VTQDSlaQATQLAEERIGNVRTVRAFGKEMTEIEKYaskvDHVMQLARK 390
Cdd:cd18582 140 SYALITlvtvALYVAFTIKVTEwrtkfrremNEADN--EANAKAVDSLLNYETVKYFNNEEYEAERY----DKALAKYEK 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 391 EAFARAGFFGATGLSGNLIV----LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGL 459
Cdd:cd18582 214 AAVKSQTSLALLNIGQALIIslglTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
492-712 |
8.92e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.18 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEvpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI--------------SLDGHD 557
Cdd:PLN03073 509 ISFSDASFGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 558 IrqlnpvwlrskigtvSQEPILFscsiaeniaygaddpssvtaeeiqrvaevanavaFIRNFP----QGFNTVVGEKGV- 632
Cdd:PLN03073 587 L---------------SSNPLLY----------------------------------MMRCFPgvpeQKLRAHLGSFGVt 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 633 ---------LLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-EYLVQEALdrLMDGrTVLVIAHRLSTIKNA-NMV 701
Cdd:PLN03073 618 gnlalqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV--LFQG-GVLMVSHDEHLISGSvDEL 694
|
250
....*....|.
gi 171184400 702 AVLDQGKITEY 712
Cdd:PLN03073 695 WVVSEGKVTPF 705
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
514-715 |
1.45e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS--GTISLDGHDIRQLNPVWLRSK-IGTVSQEPILF-SCSIAENIA 589
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpELSVAENIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 590 YGAD--DPSSVT--AEEIQRVAEVANAVafirNFPQGFNT-VVGEKGvllsGGQKQRIAIARALLKNPKILLLDEATSAL 664
Cdd:TIGR02633 101 LGNEitLPGGRMayNAMYLRAKNLLREL----QLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 171184400 665 -DAENEYLVQEALDRLMDGRTVLVIAHRLSTIKnanmvAVLDQGKITEYGKH 715
Cdd:TIGR02633 173 tEKETEILLDIIRDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQH 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
511-698 |
2.31e-09 |
|
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: 57.33 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRlydpASGTISLDGhdirqLNPVWLRSKIGTVSQEPILfscsIAENIAY 590
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLIS-----FLPKFSRNKLIFIDQLQFL----IDVGLGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 591 gaddpssVTaeeiqrvaevanavafirnfpqgfntvVGEKGVLLSGGQKQRIAIARALLKNPK--ILLLDEATSALDAEN 668
Cdd:cd03238 79 -------LT---------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|.
gi 171184400 669 EYLVQEALDRLMD-GRTVLVIAHRLSTIKNA 698
Cdd:cd03238 125 INQLLEVIKGLIDlGNTVILIEHNLDVLSSA 155
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
510-705 |
2.34e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIPS-GSVTALVGPSGSGKSTVLSLLlrlydpaSGTI--SLDGHDIrqlNPVW---LRSKIGTVSQEpiLFSCS 583
Cdd:PRK13409 88 FKLYGLPIPKeGKVTGILGPNGIGKTTAVKIL-------SGELipNLGDYEE---EPSWdevLKRFRGTELQN--YFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 IAENIAygaddpssvTAEEIQRVAEVANAVafirnfpQGfnTV------VGEKGVL-------------------LSGGQ 638
Cdd:PRK13409 156 YNGEIK---------VVHKPQYVDLIPKVF-------KG--KVrellkkVDERGKLdevverlglenildrdiseLSGGE 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 639 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLstiknanmvAVLD 705
Cdd:PRK13409 218 LQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL---------AVLD 275
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
520-693 |
2.59e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 520 GSVTALVGPSGSGKSTVLSLLL--RLYDPASGTISLDGHDIRQLNpvwlRSKIGTVSQEPILFS--CSIAENIAYGA--D 593
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKKQET----FARISGYCEQNDIHSpqVTVRESLIYSAflR 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 594 DPSSVTAEEIQR-VAEVANAVAfIRNFPqgfNTVVGEKGVL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYL 671
Cdd:PLN03140 982 LPKEVSKEEKMMfVDEVMELVE-LDNLK---DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180
....*....|....*....|...
gi 171184400 672 VQEALDRLMD-GRTVLVIAHRLS 693
Cdd:PLN03140 1058 VMRTVRNTVDtGRTVVCTIHQPS 1080
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
514-726 |
2.89e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.43 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRL----YDPASGTISLDGHDIRQLNPVWLRSKIG-TVS---QEPIlfSCSia 585
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGhNVSmifQEPQ--SCL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 586 eniaygadDPS-SVTAEEIQ--------------------RVAEVANAVAF------IRNFPQGfntvvgekgvlLSGGQ 638
Cdd:PRK15093 103 --------DPSeRVGRQLMQnipgwtykgrwwqrfgwrkrRAIELLHRVGIkdhkdaMRSFPYE-----------LTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 639 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKH 715
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPS 243
|
250
....*....|.
gi 171184400 716 EELLSKPNGIY 726
Cdd:PRK15093 244 KELVTTPHHPY 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
492-709 |
3.00e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA-SGTISLDGHDIRQLNPV-WLRSK 569
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 570 IGTVSQE-------PILfscSIAENIAYGA----------DDPSSVTA--EEIQRVaEVANAVAFIrnfPQGfntvvgek 630
Cdd:TIGR02633 338 IAMVPEDrkrhgivPIL---GVGKNITLSVlksfcfkmriDAAAELQIigSAIQRL-KVKTASPFL---PIG-------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 631 gvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGK 708
Cdd:TIGR02633 403 --RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGK 480
|
.
gi 171184400 709 I 709
Cdd:TIGR02633 481 L 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
463-710 |
3.65e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 463 GRlwELLEREPKLPFNEGVILneksfqgaLEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLR 542
Cdd:PRK13549 241 GR--ELTALYPREPHTIGEVI--------LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 543 LYDPAS-GTISLDGHDIRQLNPV-WLRSKIGTVSQE-------PILfscSIAENIAYGA----------DDPSSVTA--E 601
Cdd:PRK13549 311 AYPGRWeGEIFIDGKPVKIRNPQqAIAQGIAMVPEDrkrdgivPVM---GVGKNITLAAldrftggsriDDAAELKTilE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 602 EIQRVaEVANAVAFIRnfpqgfntvVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY--------LVQ 673
Cdd:PRK13549 388 SIQRL-KVKTASPELA---------IAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYeiyklinqLVQ 453
|
250 260 270
....*....|....*....|....*....|....*...
gi 171184400 674 EaldrlmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKIT 710
Cdd:PRK13549 454 Q-------GVAIIVISSELPEVLGlSDRVLVMHEGKLK 484
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
514-726 |
4.10e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKStVLSL-LLRLYD-PA---SGTISLDGHDIRQLNPVWLRSKIGT----VSQEPILfSCSI 584
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKS-VSSLaIMGLIDyPGrvmAEKLEFNGQDLQRISEKERRNLVGAevamIFQDPMT-SLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 585 AENIAYGADDPSSV-----TAEEIQRVAEVANAVAF------IRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPK 653
Cdd:PRK11022 105 CYTVGFQIMEAIKVhqggnKKTRRQRAIDLLNQVGIpdpasrLDVYPHQ-----------LSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 654 ILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKPNGIY 726
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
493-697 |
6.93e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 493 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL-----------LRLYDPASG---TIsldgHDI 558
Cdd:PRK10938 262 VLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLFGRRRGsgeTI----WDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 559 RQlnpvwlrsKIGTVSQEPIL---FSCSIAENIAYGADDPSSVtaeeIQRVAEVANAVAfirnfPQ-----GFNTVVGEK 630
Cdd:PRK10938 335 KK--------HIGYVSSSLHLdyrVSTSVRNVILSGFFDSIGI----YQAVSDRQQKLA-----QQwldilGIDKRTADA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 631 GVL-LSGGQkQRIA-IARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLV------------IAHRLSTI 695
Cdd:PRK10938 398 PFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLfvshhaedapacITHRLEFV 476
|
..
gi 171184400 696 KN 697
Cdd:PRK10938 477 PD 478
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
510-705 |
7.21e-09 |
|
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: 59.03 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIP-SGSVTALVGPSGSGKSTVLSLLlrlydpaSGtisldghdirQLNPvwlrsKIGTVSQEP----IL--FSC 582
Cdd:COG1245 88 FRLYGLPVPkKGKVTGILGPNGIGKSTALKIL-------SG----------ELKP-----NLGDYDEEPswdeVLkrFRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENiaYgaddpssvtaeeIQRVAE----VANAVAFIRNFPQGFNTVVG-------EKGVL------------------ 633
Cdd:COG1245 146 TELQD--Y------------FKKLANgeikVAHKPQYVDLIPKVFKGTVRellekvdERGKLdelaeklglenildrdis 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 634 -LSGGQKQRIAIARALLKNPKILLLDEATSALD-------AEneyLVQEALDrlmDGRTVLVIAHRLstiknanmvAVLD 705
Cdd:COG1245 212 eLSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrlnvAR---LIRELAE---EGKYVLVVEHDL---------AILD 276
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
505-708 |
8.48e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 505 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR-QLNPVWLRSKIGTVSQE-PILFSC 582
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 583 SIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 662
Cdd:PRK10982 89 SVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 171184400 663 AL-DAENEYLVQeALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGK 708
Cdd:PRK10982 164 SLtEKEVNHLFT-IIRKLKErGCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
175-413 |
1.16e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 57.10 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 175 VGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTRL----CLGLSAVFLCGAAAnairvYLMQTSGQRIVNRLRTS 250
Cdd:cd18603 5 LLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRDYRLgvygALGLGQAIFVFLGS-----LALALGCVRASRNLHNK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 251 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsvgISMMFFVSPNLATFVLSVVPpvsiIAV 330
Cdd:cd18603 80 LLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQV---ISTLVVISISTPIFLVVIIP----LAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 331 IYG----------RYLRKLTKVT--------QDSLAQATqlaeerignvrTVRAFGKEMTEIEKYASKVDHvmqlarkea 392
Cdd:cd18603 153 LYFfiqrfyvatsRQLKRLESVSrspiyshfSETLQGAS-----------TIRAYGVQERFIRESDRRVDE--------- 212
|
250 260 270
....*....|....*....|....*....|
gi 171184400 393 FARAGFFGATG---LS------GNLIVLSV 413
Cdd:cd18603 213 NQRAYYPSIVSnrwLAvrleflGNLIVLFA 242
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
174-414 |
1.17e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 57.11 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 174 AVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTrLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFS 253
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYL-LALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 254 SILRQEVAFFDKTRTGELINRLSSDTALLGrSVTENLSDGLRAGAQASVGISMMFFVspnlatFVLSVVPPVSIIAVI-- 331
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIE-DFFLFLHYLWSAPLQIIVALYLLYRL------LGWAALAGLGVLLLLip 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 332 YGRYLRKLTKVTQDSLAQAT----QLAEERIGNVRTVRAFGKEmteiEKYASKVDHV----MQLARKEAFARAGFFGATG 403
Cdd:cd18579 154 LQAFLAKLISKLRKKLMKATdervKLTNEILSGIKVIKLYAWE----KPFLKRIEELrkkeLKALRKFGYLRALNSFLFF 229
|
250
....*....|.
gi 171184400 404 LSGNLIVLSVL 414
Cdd:cd18579 230 STPVLVSLATF 240
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
473-690 |
1.34e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 473 PKLPFNEGvilnEKSFQGALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIS 552
Cdd:PRK15064 305 PFIRFEQD----KKLHRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 553 ldghdirqlnpvWlrskigtvsqepilfscsiAEN--IAYGADDPSSVTAEEIqrvaevaNAVAFIRNF--PQGFNTVVg 628
Cdd:PRK15064 378 ------------W-------------------SENanIGYYAQDHAYDFENDL-------TLFDWMSQWrqEGDDEQAV- 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171184400 629 eKGVL----------------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDrLMDGrTVLVIAH 690
Cdd:PRK15064 419 -RGTLgrllfsqddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFVSH 493
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
513-701 |
4.03e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.11 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 513 FSLSI---PSgSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLrSKIGtvSQEPILFSCSIAENIA 589
Cdd:PRK13541 17 FDLSItflPS-AITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 590 YGADDPSSVTAeeiqrvaeVANAVAFIRnfpqgFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 669
Cdd:PRK13541 93 FWSEIYNSAET--------LYAAIHYFK-----LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
170 180 190
....*....|....*....|....*....|...
gi 171184400 670 YLVQEALD-RLMDGRTVLVIAHRLSTIKNANMV 701
Cdd:PRK13541 160 DLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
511-701 |
4.21e-08 |
|
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: 56.95 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLL------RLYdpASGTISLDGHDIRQLNPVwlrSKIGTVSQEPI------ 578
Cdd:TIGR00630 625 KNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanRLN--GAKTVPGRYTSIEGLEHL---DKVIHIDQSPIgrtprs 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 579 --------------LFscsiAE----------------NIAYGA----------------DDPSSVTAE----------- 601
Cdd:TIGR00630 700 npatytgvfdeireLF----AEtpeakvrgytpgrfsfNVKGGRceacqgdgvikiemhfLPDVYVPCEvckgkrynret 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 602 -EIQ----RVAEVAN-----AVAFIRNFPQ-----------GFNTV-VGEKGVLLSGGQKQRIAIARALLK---NPKILL 656
Cdd:TIGR00630 776 lEVKykgkNIADVLDmtveeAYEFFEAVPSisrklqtlcdvGLGYIrLGQPATTLSGGEAQRIKLAKELSKrstGRTLYI 855
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 171184400 657 LDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMV 701
Cdd:TIGR00630 856 LDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYI 901
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
522-690 |
4.34e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 54.15 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 522 VTALVGPSGSGKSTVLSLLLrlydpasgtISLDGHDIRQLNPVWLRSKIgtvsqepilfsCSIAENIAYGADDPSSVTAE 601
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK---------YALTGELPPNSKGGAHDPKL-----------IREGEVRAQVKLAFENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 602 E--IQRVAEVANAVAFIRnfpQG-FNTVVGEKGVLLSGGQKQ------RIAIARALLKNPKILLLDEATSALDAENeylV 672
Cdd:cd03240 84 KytITRSLAILENVIFCH---QGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---I 157
|
170 180
....*....|....*....|....
gi 171184400 673 QEALDRLMD------GRTVLVIAH 690
Cdd:cd03240 158 EESLAEIIEerksqkNFQLIVITH 181
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
169-438 |
5.19e-08 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 55.22 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 169 RRLAAAVGFLTMS-SVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRL 247
Cdd:cd18783 1 KRLFRDVAIASLIlHVLALAPPIFFQIVIDKVLVHQSYS---TLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 248 RTSLFSSILRQEVAFFDKTRTGELINRLSSDTALlgRS-VTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVS 326
Cdd:cd18783 78 ALRTFDRLLSLPIDFFERTPAGVLTKHMQQIERI--RQfLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 327 IIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSG 406
Cdd:cd18783 156 LIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLE 235
|
250 260 270
....*....|....*....|....*....|..
gi 171184400 407 NLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 438
Cdd:cd18783 236 KLMTVGVIWVGAYLVFAGSLTVGALIAFNMLA 267
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
510-710 |
5.50e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIGTV-----SQEPILF-SCS 583
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 IAENIaygaddpSSVTAEE----IQRVAEVANAVAFIRNFPQGFNTVvgEKGV-LLSGGQKQRIAIARALLKNPKILLLD 658
Cdd:PRK15439 358 LAWNV-------CALTHNRrgfwIKPARENAVLERYRRALNIKFNHA--EQAArTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 659 EATSALD--AENE-YLVQEALDRlmDGRTVLVIAHRLSTI-KNANMVAVLDQGKIT 710
Cdd:PRK15439 429 EPTRGVDvsARNDiYQLIRSIAA--QNVAVLFISSDLEEIeQMADRVLVMHQGEIS 482
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
511-711 |
5.62e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKIGTVSQ---EPILFS-CSIA 585
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdAVKKGMAYITEsrrDNGFFPnFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 586 ENIA-------------YGADDPSsvtaeEIQRVAEVANAVAFIRNfpQGFNTVVGEkgvlLSGGQKQRIAIARALLKNP 652
Cdd:PRK09700 360 QNMAisrslkdggykgaMGLFHEV-----DEQRTAENQRELLALKC--HSVNQNITE----LSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 653 KILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNA-NMVAVLDQGKITE 711
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADdGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
632-729 |
6.02e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.96 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 632 VLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKI 709
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGEP 149
|
90 100
....*....|....*....|
gi 171184400 710 TEYGKHEELLSKPNGIYRKL 729
Cdd:cd03222 150 GVYGIASQPKGTREGINRFL 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
514-733 |
6.10e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVsqepilfscsiaENIAYGAD 593
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENIELKGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 594 dPSSVTAEEIQ----RVAEVANAVAFIRnfpQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDaenE 669
Cdd:PRK13545 112 -MMGLTKEKIKeiipEIIEFADIGKFIY---QPVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGD---Q 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 670 YLVQEALDRLMD----GRTVLVIAHRLSTIKNANMVAV-LDQGKITEYGKHEELLSKPNGIYRKL--MNKQ 733
Cdd:PRK13545 177 TFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDHYDEFLKKYnqMSVE 247
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
510-693 |
9.88e-08 |
|
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: 53.91 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 510 FQDFSLSIP-SGSVTALVGPSGSGKSTVLSLLlrlydpaSGTI--SLDGHDIrqlNPVW---LRSKIGTVSQEpilFSCS 583
Cdd:cd03236 15 FKLHRLPVPrEGQVLGLVGPNGIGKSTALKIL-------AGKLkpNLGKFDD---PPDWdeiLDEFRGSELQN---YFTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 584 IAENIAYGADDPSSV----------TAEEIQRVAEvanavafiRNFPQGFNTVVGEKGVL------LSGGQKQRIAIARA 647
Cdd:cd03236 82 LLEGDVKVIVKPQYVdlipkavkgkVGELLKKKDE--------RGKLDELVDQLELRHVLdrnidqLSGGELQRVAIAAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 171184400 648 LLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLS 693
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAeDDNYVLVVEHDLA 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
503-690 |
1.17e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 503 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpvwlRSK-IGTVSQEPILFS 581
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 582 -CSIAENIAYgaddPSSVTAEEIQRVAEVANAVAFIRNFPQgfnTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 660
Cdd:PRK13543 96 dLSTLENLHF----LCGLHGRRAKQMPGSALAIVGLAGYED---TLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 171184400 661 TSALDAENEYLVQEALD-RLMDGRTVLVIAH 690
Cdd:PRK13543 165 YANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
511-710 |
1.31e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHdirqlnPVWLRSKIGTVS-----------QEPIL 579
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK------PIDIRSPRDAIRagimlcpedrkAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 580 FSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNF----PQGfntvvGEKGVLLSGGQKQRIAIARALLKNPKIL 655
Cdd:PRK11288 344 PVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLniktPSR-----EQLIMNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 171184400 656 LLDEATSALD--AENE-YLVQEALDRlmDGRTVLVIAHRL-STIKNANMVAVLDQGKIT 710
Cdd:PRK11288 419 LLDEPTRGIDvgAKHEiYNVIYELAA--QGVAVLFVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
514-720 |
3.14e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTvLSLLLrlydpaSGTISL-DGHDIRQLNPVWLRS-----KIgtVSQEpilFSCSIAEN 587
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSA-LARAL------AGELPLlSGERQSQFSHITRLSfeqlqKL--VSDE---WQRNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 588 IAYGADDPSSVTAEEIQ-------RVAEVANAVA----FIRNFPQgfntvvgekgvlLSGGQKQRIAIARALLKNPKILL 656
Cdd:PRK10938 91 LSPGEDDTGRTTAEIIQdevkdpaRCEQLAQQFGitalLDRRFKY------------LSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 657 LDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLS 720
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
492-690 |
6.18e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 492 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLdGHDIrqlnpvwlrsKIG 571
Cdd:PRK11819 325 IEAENLSKSFGDRL---LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 572 TVSQ--EPILFSCSIAENIAYGADdpssvtaeeIQRVA--EVaNAVAFIRNFpqGFNTVVGEKGV-LLSGGQKQRIAIAR 646
Cdd:PRK11819 391 YVDQsrDALDPNKTVWEEISGGLD---------IIKVGnrEI-PSRAYVGRF--NFKGGDQQKKVgVLSGGERNRLHLAK 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 171184400 647 ALLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH 690
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVETLRALEEALLEF--PGCAVVISH 500
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
628-724 |
6.77e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 628 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLV-QEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLD 705
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|....*....
gi 171184400 706 QGKITEYGKHEELLSKPNG 724
Cdd:NF000106 219 RGRVIADGKVDELKTKVGG 237
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
221-383 |
7.95e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 51.38 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 221 VFLCGAAANAI----RVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRA 296
Cdd:cd18605 47 VYGFLAGLNSLftllRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 297 GAQASVGISMMFFVSPNLATFVLsvvppvsIIAVIYGRY----------LRKLTKVTQDSLaqATQLAEErIGNVRTVRA 366
Cdd:cd18605 127 LFGLLGYLVVICYQLPWLLLLLL-------PLAFIYYRIqryyratsreLKRLNSVNLSPL--YTHFSET-LKGLVTIRA 196
|
170
....*....|....*..
gi 171184400 367 FGKEMTEIEKYASKVDH 383
Cdd:cd18605 197 FRKQERFLKEYLEKLEN 213
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
511-731 |
9.57e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH-DIRQLNpVWLRSKIGTVsqEPILFSCSIaenIA 589
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAIS-AGLSGQLTGI--ENIEFKMLC---MG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 590 YGADDPSSVTAEEIqrvaEVANAVAFIRNFPQGFntvvgekgvllSGGQKQRIAIARALLKNPKILLLDEATSALDaenE 669
Cdd:PRK13546 115 FKRKEIKAMTPKII----EFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD---Q 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 670 YLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKpngiYRKLMN 731
Cdd:PRK13546 177 TFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK----YEAFLN 239
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
514-699 |
1.32e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 514 SLSIPSGSVTALVGPSGSGKSTVLSlllrlydpasgTISLdghdirqlnpvwlrskigtvsqepILFSCSIAENIAYGAD 593
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILD-----------AIGL------------------------ALGGAQSATRRRSGVK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 594 DPSSVTAEEIQrvaevanavaFIRNFPQgfntvvgekgvlLSGGQKQRIAIARAL---LKNPKIL-LLDEATSALDAENE 669
Cdd:cd03227 60 AGCIVAAVSAE----------LIFTRLQ------------LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|.
gi 171184400 670 YLVQEAL-DRLMDGRTVLVIAHRLSTIKNAN 699
Cdd:cd03227 118 QALAEAIlEHLVKGAQVIVITHLPELAELAD 148
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
216-382 |
2.72e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 49.91 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 216 LGLSAVFLCGAAanairVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLR 295
Cdd:cd18602 59 LSLGAVILSLVT-----NLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 296 AGAQASVGISMMFFVSPnlaTFVLSVVpPVSIIAVIYGRYLRKLTKVTQ--DSLAQATQLAE--ERIGNVRTVRAFGKEM 371
Cdd:cd18602 134 FLLLCLSAIIVNAIVTP---YFLIALI-PIIIVYYFLQKFYRASSRELQrlDNITKSPVFSHfsETLGGLTTIRAFRQQA 209
|
170
....*....|.
gi 171184400 372 TEIEKYASKVD 382
Cdd:cd18602 210 RFTQQMLELID 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
512-665 |
2.82e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 512 DFSLSIPSGSVTALVGPSGSGKSTVLSLLlrlydpA------SGTISLDGHDI------RQLNPvwlrsKIGTVSQ---- 575
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLI------AgarkiqQGRVEVLGGDMadarhrRAVCP-----RIAYMPQglgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 576 --EPILfscSIAENIA-----YGADdpssvTAEEIQRVAEVANAV---AFiRNFPQGfntvvgeKgvlLSGGQKQRIAIA 645
Cdd:NF033858 88 nlYPTL---SVFENLDffgrlFGQD-----AAERRRRIDELLRATglaPF-ADRPAG-------K---LSGGMKQKLGLC 148
|
170 180
....*....|....*....|
gi 171184400 646 RALLKNPKILLLDEATSALD 665
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVD 168
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
172-461 |
4.96e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 48.82 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 172 AAAVGFLTMSSVISMSapFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSL 251
Cdd:cd18561 1 SVLLGLLITALYIAQA--WLLARALARIFAG---GPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 252 FSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVI 331
Cdd:cd18561 76 FAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 332 YGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKE---AFARAGFFGATGLSGNL 408
Cdd:cd18561 156 WDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVlavSLLSSGIMGLATALGTA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 171184400 409 IVLSVLyKGGLLMGSAHMTVGELSSFLMYAFWvgISIGGLSSFYSELMKGLGA 461
Cdd:cd18561 236 LALGVG-ALRVLGGQLTLSSLLLILFLSREFF--RPLRDLGAYWHAGYQGISA 285
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
174-459 |
7.71e-06 |
|
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: 48.37 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 174 AVGFLTMSSVISMSAPFFLGKIIDVIYTNPTVDYSdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFS 253
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLE-SAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 254 SILRQEVAFFDKTRTGELINRLSSDTallgRSVTENLSdglragaqasvgiSMMFFVSPNLATFVLSVV-------PPVS 326
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRIMDRGT----ESANTLLS-------------YLVFYLVPTLLELIVVSVvfafhfgAWLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 327 IIA----VIYGRYLRKLTK---------VTQDSlaQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAF 393
Cdd:cd18560 143 LIVflsvLLYGVFTIKVTEwrtkfrraaNKKDN--EAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQA 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 394 AragfFGATGLSGNLIVLSVLYkGGLLMGS-----AHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGL 459
Cdd:cd18560 221 S----LSLLNVGQQLIIQLGLT-LGLLLAGyrvvdGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
634-698 |
2.10e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.10 E-value: 2.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184400 634 LSGGQKQRIAIARALLK--NPKIL-LLDEATSAL---DaeneylVQ---EALDRLMD-GRTVLVIAHRLSTIKNA 698
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLhfhD------IRkllEVLHRLVDkGNTVVVIEHNLDVIKTA 895
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
511-701 |
2.42e-05 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTV----------------LSLLLR-----LYDPA-------SGTISLDGHDIRQlN 562
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARqflgqMDKPDvdsieglSPAIAIDQKTTSR-N 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 563 PvwlRSKIGTVSQ----EPILFScsiaeniaygaddpssvtaeeiqRVAeVANAVAFIRNFPQGFNTVVGEKGVLlSGGQ 638
Cdd:cd03270 91 P---RSTVGTVTEiydyLRLLFA-----------------------RVG-IRERLGFLVDVGLGYLTLSRSAPTL-SGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171184400 639 KQRIAIARALLKNPK--ILLLDEATSAL-DAENEYLVqEALDRLMD-GRTVLVIAHRLSTIKNANMV 701
Cdd:cd03270 143 AQRIRLATQIGSGLTgvLYVLDEPSIGLhPRDNDRLI-ETLKRLRDlGNTVLVVEHDEDTIRAADHV 208
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
634-698 |
2.88e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.76 E-value: 2.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 634 LSGGQKQRIAIARALLKNP--KIL-LLDEATSALDAENeylVQ---EALDRLMD-GRTVLVIAHRLSTIKNA 698
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFED---IRkllEVLHRLVDkGNTVVVIEHNLDVIKTA 899
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
508-721 |
5.74e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.93 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 508 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIGTVSQEPILFSCSIAEN 587
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 588 IAYGADDPSSVTAEEIQRVAEVAnavafIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 667
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 171184400 668 NEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 721
Cdd:TIGR01257 2105 ARRMLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
217-335 |
5.90e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 45.77 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 217 GLSAVFLCGAAANAIRV-YLMQTSGQRIVNRLrtslFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLR 295
Cdd:cd18601 67 GLTAATFVFGFLRSLLFfHVAVSASKNLHNKM----FASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQ 142
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 171184400 296 AGAQASVGISMMFFVSPnlatFVLSVVPPVSIIAVIYGRY 335
Cdd:cd18601 143 LLLQVVGVVLLAVVVNP----WVLIPVIPLVILFLFLRRY 178
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
169-290 |
6.10e-05 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 45.71 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 169 RRLAAAVGFLTMSSVISMS-APFFLGKIIDVIytnpTVDYSDNLTRLCLgLSAVFLCGAAANAIRVYL---MQTSGQ-RI 243
Cdd:cd18556 1 KLLFFSILFISLLSSILISiSPVILAKITDLL----TSSSSDSYNYIVV-LAALYVITISATKLLGFLslyLQSSLRvEL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 171184400 244 VNRLRTSLFSSILRQEVAFFDKTRTGEL---INRLSSDTALLGRSVTENL 290
Cdd:cd18556 76 IISISSSYFRYLYEQPKTFFVKENSGDItqrLNQASNDLYTLVRNLSTNI 125
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
491-688 |
7.43e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 491 ALEFKN--VHfaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKsTVL--SLLLRLYDP-ASGTISLDGHDIRqlnpvw 565
Cdd:NF040905 257 VFEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELamSVFGRSYGRnISGTVFKDGKEVD------ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 566 lrskIGTVSQepilfscSIAENIAYGADD------------PSSVTAEEIQRVAE--VANAVAFIR---NFPQGFNT--- 625
Cdd:NF040905 328 ----VSTVSD-------AIDAGLAYVTEDrkgyglnliddiKRNITLANLGKVSRrgVIDENEEIKvaeEYRKKMNIktp 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171184400 626 VVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVI 688
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVI 460
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
508-665 |
1.10e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 508 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDirqlnpvwlrsKIGTVSQEPILF-SCSIAE 586
Cdd:PRK15064 15 PLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-----------RLGKLRQDQFAFeEFTVLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 587 NIAYGADDPSSV-------------TAEEIQRVAEVANAVAFIRNFpqgfnTVVGEKGVLLSG----------------- 636
Cdd:PRK15064 84 TVIMGHTELWEVkqerdriyalpemSEEDGMKVADLEVKFAEMDGY-----TAEARAGELLLGvgipeeqhyglmsevap 158
|
170 180
....*....|....*....|....*....
gi 171184400 637 GQKQRIAIARALLKNPKILLLDEATSALD 665
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
508-665 |
1.53e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 508 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-----------VWLRSKIGTVSQE 576
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneainhgfalvTEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 577 PILFSCSIAENIAY----GADDPSSVTAEeIQRVAEVANAVAfirnfpQGFNTVVGEkgvlLSGGQKQRIAIARALLKNP 652
Cdd:PRK10982 342 DIGFNSLISNIRNYknkvGLLDNSRMKSD-TQWVIDSMRVKT------PGHRTQIGS----LSGGNQQKVIIGRWLLTQP 410
|
170
....*....|...
gi 171184400 653 KILLLDEATSALD 665
Cdd:PRK10982 411 EILMLDEPTRGID 423
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
168-431 |
1.54e-04 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 44.52 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 168 RRRLAAAVGFLTMSSVISMSAPFFLGKIID-VIYTN--PTvdysdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIV 244
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDrVLPSGslST------LLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 245 NRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLragaQASVGISMMFFVSPNLATFVLSVVPP 324
Cdd:cd18586 75 VELGRRVFRAVLELPLESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLP----WAPLFLAVIFLIHPPLGWVALVGAPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 325 VSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGL 404
Cdd:cd18586 151 LVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKT 230
|
250 260
....*....|....*....|....*..
gi 171184400 405 SGNLIVLSVLYKGGLLMGSAHMTVGEL 431
Cdd:cd18586 231 LRMALQSLILGVGAYLVIDGELTIGAL 257
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
217-383 |
1.91e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 44.09 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 217 GLSAVFLCGAaaNAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRA 296
Cdd:cd18599 65 GGSILVILLL--SLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 297 GAQASVGISMMFFVSPnlatFVLSVVPPVSIIAVIYGRYLRKLTKVTQD----------SLAQATqlaeerIGNVRTVRA 366
Cdd:cd18599 143 VLLVVFSLIIIAIVFP----WFLIALIPLAIIFVFLSKIFRRAIRELKRlenisrsplfSHLTAT------IQGLSTIHA 212
|
170
....*....|....*..
gi 171184400 367 FGKEMTEIEKYASKVDH 383
Cdd:cd18599 213 FNKEKEFLSKFKKLLDQ 229
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
211-438 |
2.69e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 43.69 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 211 LTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALlgRSV-TEN 289
Cdd:cd18779 41 LGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNATI--RELlTSQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 290 LSDGLRAGAQASVGISMMFFVSPNLATFVLSV-VPPVSIIAVIYGRyLRKLTK--VTQDSLAQATQLaeERIGNVRTVRA 366
Cdd:cd18779 119 TLSALLDGTLVLGYLALLFAQSPLLGLVVLGLaALQVALLLATRRR-VRELMAreLAAQAEAQSYLV--EALSGIETLKA 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 367 FGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 438
Cdd:cd18779 196 SGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALA 267
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
634-701 |
2.75e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 634 LSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMV 701
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHqGHTVVIIEHNMHVVKVADYV 881
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
635-690 |
3.49e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 3.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184400 635 SGGQKQRIAIARALLKNPKILLLDEATSALDAE-----NEYLVQEAldrlmdgRTVLVIAH 690
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwlETYLLKWP-------KTFIVVSH 399
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
218-337 |
4.19e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 42.85 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 218 LSAVFLCGAAanairvYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTallgRSVTENLSDGLRag 297
Cdd:cd18606 47 LQAIFLFLFG------LLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDT----DVLDNELPDSLR-- 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 171184400 298 aQASVGISMMFfvspnlATFVLSVV---------PPVSIIAVIYGRYLR 337
Cdd:cd18606 115 -MFLYTLSSII------GTFILIIIylpwfaialPPLLVLYYFIANYYR 156
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
510-548 |
4.21e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.12 E-value: 4.21e-04
10 20 30
....*....|....*....|....*....|....*....
gi 171184400 510 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS 548
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
510-557 |
6.15e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.68 E-value: 6.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 171184400 510 FQDFSLSIPSGsVTALVGPSGSGKSTVLSLLLRLYDPaSGTISLDGHD 557
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGP-SSSRKFDEED 59
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
177-419 |
8.74e-04 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 41.85 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 177 FLTMSSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTrLCLGLSAVFLcgaaanaIRVYLMQT---SGQRIVNRLRTSLFS 253
Cdd:cd18594 5 LLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYL-YALGLSLCAF-------LRVLLHHPyffGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 254 SILRQEVAF----FDKTRTGELINRLSSDTALLGRSVTenlsdglragaqasvgISMMFFVSP--NLATFVL-------S 320
Cdd:cd18594 77 LIYKKTLKLsssaLSKITTGHIVNLLSNDVQKFDEVLV----------------YLHFLWIAPlqVIVLTGLlwreigpS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 321 VVPPVSIIAVI------YGRYLRKLTKvtqdslaQATQLAEER-------IGNVRTVRAFGKEmteiEKYASKVDHV--- 384
Cdd:cd18594 141 SLAGLGVLLLLlplqayLGKLFAKYRR-------KTAGLTDERvkimneiISGMRVIKMYTWE----ESFAKLIENIrkk 209
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 171184400 385 -MQLARKEAFARAGFFGATGLSGNLIVL-----SVLYKGGL 419
Cdd:cd18594 210 eLKLIRKAAYIRAFNMAFFFFSPTLVSFatfvpYVLTGNTL 250
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
520-561 |
1.12e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 39.81 E-value: 1.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 171184400 520 GSVTALVGPSGSGKSTVLSlllRLYDPASgTISLDghDIRQL 561
Cdd:COG4639 2 LSLVVLIGLPGSGKSTFAR---RLFAPTE-VVSSD--DIRAL 37
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
522-583 |
1.43e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.22 E-value: 1.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 522 VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI-GTVSQEPILFSCS 583
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLnGIDPKEPIEFEIS 63
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
633-701 |
1.59e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171184400 633 LLSGGQKQRIAIA--RALLK-NPK-ILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMV 701
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQKyKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKL 1149
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
511-726 |
1.89e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 511 QDFSLSIPSGSVTALVGPSGSGKSTVLS---------LLLRLYDPASGTISLDGHDIrqlnPVWLRSKIGT--------- 572
Cdd:PRK00635 1507 QNLNVSAPLHSLVAISGVSGSGKTSLLLegfykqacaLIEKGPSVFSEIIFLDSHPQ----ISSQRSDISTyfdiapslr 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 573 -----VSQEPIL------FS-------CSIAENIAYGADDPSSVTAEE----------IQRVA----------------- 607
Cdd:PRK00635 1583 nfyasLTQAKALnisasmFStntkqgqCSDCWGLGYQWIDRAFYALEKrpcptcsgfrIQPLAqevvyegkhfgqllqtp 1662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 608 --EVANAVAFIRNFPQGFNTVV---------GEKGVLLSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEYLVQ 673
Cdd:PRK00635 1663 ieEVAETFPFLKKIQKPLQALIdnglgylplGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALL 1742
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 171184400 674 EALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKiTEYGKHEELLSKPNGIY 726
Cdd:PRK00635 1743 VQLRTLVSlGHSVIYIDHDPALLKQADYLIEMGPGS-GKTGGKILFSGPPKDIS 1795
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
633-700 |
4.04e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.99 E-value: 4.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171184400 633 LLSGGQKQRIAIAR--ALLK-NPK-ILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANM 700
Cdd:cd03278 113 LLSGGEKALTALALlfAIFRvRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADR 184
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
176-279 |
4.83e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 39.46 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 176 GFLTMSSVISMSAPFFLGKIIDVIyTNPTVDYSDNLTrLCLGLSAVFLCGAAANAIRVYLMQtsgqRIVNRLRTSLFSSI 255
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFL-EDSSEPLSDGYL-YALGLVLSSLLGALLSSHYNFQMN----KVSLKVRAALVTAV 77
|
90 100
....*....|....*....|....*...
gi 171184400 256 ----LRQEVAFFDKTRTGELINRLSSDT 279
Cdd:cd18598 78 yrkaLRVRSSSLSKFSTGEIVNLMSTDA 105
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
621-700 |
5.39e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184400 621 QGFNTVVGEKGVL-----LSGGQKQ------RIAIARALLKNPKILLLDEATSALDAENEY----LVQEALDRLMDGRTV 685
Cdd:PRK01156 784 QDFNITVSRGGMVegidsLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTnlkdIIEYSLKDSSDIPQV 863
|
90
....*....|....*
gi 171184400 686 LVIAHRLSTIKNANM 700
Cdd:PRK01156 864 IMISHHRELLSVADV 878
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
525-563 |
7.13e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.50 E-value: 7.13e-03
10 20 30
....*....|....*....|....*....|....*....
gi 171184400 525 LVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP 563
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
525-546 |
8.62e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 37.13 E-value: 8.62e-03
|
| |
