|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-715 |
0e+00 |
|
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: 664.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 1 MAIKFIRQYDEKDCGPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKADsFDDLKQAQLPV 80
Cdd:COG2274 2 RKVPFVLQMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLD-LEELAELPLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 81 MVHIINQqgydHYIIIEKIKNNTLYIVDPAKGKYKLSSTEFGKYWTNIAVLIDKTDDFTTDNESPSYLNIFIDIFKNNYG 160
Cdd:COG2274 81 ILHWDGN----HFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVALLLEPTPEFDKRGEKPFGLRWFLRLLRRYRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 161 KLLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYF 240
Cdd:COG2274 157 LLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 241 YHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLR 320
Cdd:COG2274 237 RHLLRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 321 KPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVI 400
Cdd:COG2274 317 PRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVAL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 401 LWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRIAEITDLETETELYTSKQPY-TFKNNIRI 479
Cdd:COG2274 397 LWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLpRLKGDIEL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 480 ENVNFQYGFRSV-VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQ 558
Cdd:COG2274 477 ENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 559 NTFLFADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIF 638
Cdd:COG2274 557 DVFLFSGTIRENITLG-DPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILIL 635
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 639 DEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLWQLQM 715
Cdd:COG2274 636 DEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
8-710 |
4.72e-167 |
|
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: 496.95 E-value: 4.72e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 8 QYDEKDCGPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKAD-SFDDLKQAQLPVMVHIIN 86
Cdd:TIGR01193 1 QVDEKDCGIAALSMILKKYGTEYSLAKLRQLAKTDLEGTTVLGLVKAAEYLNFEAKAIQADmSLFEDKNLPLPFIAHVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 87 QQGYDHYIIIEKIKNNTLYIVDPAK--GKYKLSSTEFGKYWTNIAVLIDKTDDFTTDNESPSYLNIFIDIFKNNYGKLLF 164
Cdd:TIGR01193 81 NGKLPHYYVVYGVTKNHLIIADPDPtvGITKISKEDFYEEWTGIAIFISPTPEYKPIKEKENSLLKFIPLITRQKKLIVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 165 IAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVL 244
Cdd:TIGR01193 161 IVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 245 HLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRKPFE 324
Cdd:TIGR01193 241 ELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 325 KYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVILWLG 404
Cdd:TIGR01193 321 KLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 405 SYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRIAEITDLETEtelYTSKQPYTFKNN----IRIE 480
Cdd:TIGR01193 401 AYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSE---FINKKKRTELNNlngdIVIN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 481 NVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNT 560
Cdd:TIGR01193 478 DVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 561 FLFADTIKNNLLHGSNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDE 640
Cdd:TIGR01193 558 YIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 641 ATSALDSLTENKIMEhiDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNL 710
Cdd:TIGR01193 638 STSNLDTITEKKIVN--NLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
143-716 |
6.33e-159 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 471.57 E-value: 6.33e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 143 ESPSYLNIFIDIFKNNYGKLLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQ 222
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 223 LILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLL 301
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTnDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 302 LLITIIFIPCFIICSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFyigtTKFNGIIENL----LK 377
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREEREL----ERFREANEELrranLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 378 LGRFSNIQLTVNNFLKLTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRIAEITD 457
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 458 LETETELYTSKQPYT-FKNNIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMI 536
Cdd:COG1132 320 EPPEIPDPPGAVPLPpVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 537 DNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLLHGSNKYkSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLS 616
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDA-TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 617 GGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGT 696
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570 580
....*....|....*....|
gi 488434717 697 HDELIHLNGIYKNLWQLQMK 716
Cdd:COG1132 558 HEELLARGGLYARLYRLQFG 577
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
15-714 |
2.93e-117 |
|
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: 367.92 E-value: 2.93e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 15 GPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKAdSFDDLKQAQLPVmvhIINQQGyDHYI 94
Cdd:TIGR01846 1 GLEALSLLAQVHNIAVTPSQLRHMLGHAGASLDDLEILLAAKQLGLKAKAVKV-SIGRLNKLPLPA---LIDGEG-GWFV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 95 IIeKIKNNTLYIVDPAKGK-YKLSSTEFGKYWTNIAVLIdkTDDFTTDNESPSYLNIFIDIFKNNYGKLLFIAFISLFIN 173
Cdd:TIGR01846 76 LG-KLTANGVTIYDPPGDApEVLSREVLEALWSGTVILL--ATRSVAGKALKFGFSWFIPAIIRYRKQFREVLLISLALQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 174 IVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVLHLPMNFFDT 253
Cdd:TIGR01846 153 LFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 254 RKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRKPFEKYNQKVAEK 333
Cdd:TIGR01846 233 RRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 334 DAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVILWLGSYLVMTDSM 413
Cdd:TIGR01846 313 SAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGAL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 414 TLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRIAEITDLETETELYTSKQPYTFKNNIRIENVNFQYGFRS-VV 492
Cdd:TIGR01846 393 SPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRYAPDSpEV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLL 572
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 573 HGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENK 652
Cdd:TIGR01846 553 LC-NPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEAL 631
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 653 IMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLWQLQ 714
Cdd:TIGR01846 632 IMRNMREICR-GRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
159-452 |
9.40e-100 |
|
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: 308.61 E-value: 9.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 159 YGKLLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKD 238
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 239 YFYHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYT 318
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 319 LRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISL 398
Cdd:cd18570 161 FNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488434717 399 VILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18570 241 LILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
159-716 |
5.17e-93 |
|
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: 300.48 E-value: 5.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 159 YGKLLFIAFISLFINIV--GIVGALyFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLM 236
Cdd:TIGR02203 12 YKAGLVLAGVAMILVAAteSTLAAL-LKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 237 KDYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTfMIIIGAI--LLYMQSPLLLLITIIFIPCFI 313
Cdd:TIGR02203 91 VRMFEKLLGLPVSFFDRQPTGTLLSRITfDSEQVASAATDAFIVLVRET-LTVIGLFivLLYYSWQLTLIVVVMLPVLSI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 314 ICSYtLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKLGRFSNIQLTVNN-FL 392
Cdd:TIGR02203 170 LMRR-VSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYE----TRRFDAVSNRNRRLAMKMTSAGSISSpIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 393 KLTISL---VILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRIAEITDLETETELYTsKQ 469
Cdd:TIGR02203 245 QLIASLalaVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGT-RA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 470 PYTFKNNIRIENVNFQYGFRSV-VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD 548
Cdd:TIGR02203 324 IERARGDVEFRNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 549 LRKNIGYVSQNTFLFADTIKNNLLHGSNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLART 628
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 629 FLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYK 708
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYA 562
|
....*...
gi 488434717 709 NLWQLQMK 716
Cdd:TIGR02203 563 QLHNMQFR 570
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
477-714 |
1.43e-88 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 277.19 E-value: 1.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIY 636
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 637 IFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLWQLQ 714
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
477-711 |
5.99e-85 |
|
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: 267.94 E-value: 5.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSV-VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGY 555
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLW 711
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
163-714 |
8.86e-84 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 276.51 E-value: 8.86e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 163 LFIAFISLFINIVGIVGALYF--KLLTDHI--IPSNVLKnlhIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKD 238
Cdd:PRK11176 27 LIVAGVALILNAASDTFMLSLlkPLLDDGFgkADRSVLK---WMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 239 YFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSY 317
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 318 TLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSY---QSEDDRFyigTTKFNGIIENLLKLGRFSNIQltvNNFLKL 394
Cdd:PRK11176 184 VVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFggqEVETKRF---DKVSNRMRQQGMKMVSASSIS---DPIIQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 395 TISL---VILWLGSYLVMTDSMTLGSL-LAFNALtIYYLDPIERLINIQPTLQSSFVAARRIAEITDLETETELYTsKQP 470
Cdd:PRK11176 258 IASLalaFVLYAASFPSVMDTLTAGTItVVFSSM-IALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGK-RVI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 471 YTFKNNIRIENVNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL 549
Cdd:PRK11176 336 ERAKGDIEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFADTIKNNLLHGSNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTF 629
Cdd:PRK11176 416 RNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARAL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 630 LKDPDIYIFDEATSALDSLTENKIMEHIDLLtQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKN 709
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
....*
gi 488434717 710 LWQLQ 714
Cdd:PRK11176 575 LHKMQ 579
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
161-705 |
2.62e-83 |
|
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: 274.71 E-value: 2.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 161 KLLFIAFISLFINIVGIVGALYF------KLLTDHIIPSNVLKNLhiisFGILLLYIINALINYLRFQLILHLSLKIDVN 234
Cdd:COG4988 17 RWLALAVLLGLLSGLLIIAQAWLlasllaGLIIGGAPLSALLPLL----GLLLAVLLLRALLAWLRERAAFRAAARVKRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 235 LMKDYFYHVLHLPMNFFDTRKSGEILQRFMDT--------SKIREALSSS---TVTLLVDTFMI--IIGAILL------- 294
Cdd:COG4988 93 LRRRLLEKLLALGPAWLRGKSTGELATLLTEGvealdgyfARYLPQLFLAalvPLLILVAVFPLdwLSGLILLvtaplip 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 295 -YMqspllllitiifipcfiicsYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSED---DRFYIGTTKFNG 370
Cdd:COG4988 173 lFM--------------------ILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKaeaERIAEASEDFRK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 371 IIENLLKlgrfsnIQL---TVNNFLK-LTISLVILWLGSYLVmTDSMTLgsllaFNALTI------YYLdPIERLiniqp 440
Cdd:COG4988 233 RTMKVLR------VAFlssAVLEFFAsLSIALVAVYIGFRLL-GGSLTL-----FAALFVlllapeFFL-PLRDL----- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 441 tlqSSFV--------AARRIAEITDLETETELY-TSKQPYTFKNNIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGE 511
Cdd:COG4988 295 ---GSFYharangiaAAEKIFALLDAPEPAAPAgTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 512 SGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLLHGSNKYkSDEDIVKACQLA 591
Cdd:COG4988 372 SGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDA-SDEELEAALEAA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 592 ESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIIS 671
Cdd:COG4988 451 GLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILIT 529
|
570 580 590
....*....|....*....|....*....|....
gi 488434717 672 HKLSTIKNADNIYVLNEGQIAENGTHDELIHLNG 705
Cdd:COG4988 530 HRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
477-714 |
2.55e-82 |
|
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: 260.93 E-value: 2.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS--VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIG 554
Cdd:cd03249 1 IEFKNVSFRYPSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFADTIKNNLLHGSNkYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPD 634
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 635 IYIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLWQLQ 714
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
328-713 |
1.09e-79 |
|
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: 265.09 E-value: 1.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 328 QKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLL----KLGRFSNIQLTVNNFLKLTISLVILWL 403
Cdd:COG4987 185 RRLAAARAALRARLTDLLQGAAELAAYGALDRA----LARLDAAEARLAaaqrRLARLSALAQALLQLAAGLAVVAVLWL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 404 GSYLVMTDSM--------TLGSLLAFNALTiyyldPIERLINiqpTLQSSFVAARRIAEITDLETETELYTSKQPYTFKN 475
Cdd:COG4987 261 AAPLVAAGALsgpllallVLAALALFEALA-----PLPAAAQ---HLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIG 554
Cdd:COG4987 333 SLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPD 634
Cdd:COG4987 413 VVPQRPHLFDTTLRENLRLA-RPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAP 491
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 635 IYIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLWQL 713
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
382-714 |
2.87e-79 |
|
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: 265.15 E-value: 2.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 382 SNIQLTVNNF---LKLTISLV-ILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERL-----------INIQptlqSSF 446
Cdd:COG5265 258 SQTSLALLNFgqaLIIALGLTaMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLgfvyreirqalADME----RMF 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 447 VAARRIAEITDLETETELyTSKQPytfknNIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRY 526
Cdd:COG5265 334 DLLDQPPEVADAPDAPPL-VVGGG-----EVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 527 YTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNT 606
Cdd:COG5265 408 YDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG-RPDASEEEVEAAARAAQIHDFIESLPDGYDT 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 607 MLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVL 686
Cdd:COG5265 487 RVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVDADEILVL 565
|
330 340
....*....|....*....|....*...
gi 488434717 687 NEGQIAENGTHDELIHLNGIYKNLWQLQ 714
Cdd:COG5265 566 EAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
476-705 |
3.83e-77 |
|
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: 247.14 E-value: 3.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGY 555
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIKNNLLHGSNkYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRP-NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLtQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNG 705
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
161-710 |
1.40e-76 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 260.42 E-value: 1.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 161 KLLFIAFISLFINIVGIVGALYFK-LLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDY 239
Cdd:TIGR00958 161 PWLISAFVFLTLSSLGEMFIPFYTgRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 240 FYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSyt 318
Cdd:TIGR00958 241 FRSLLRQDLGFFDENKTGELTSRLSsDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAE-- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 319 lrKPFEKYNQKVAEKD----AELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKLGR---FSNI-QLTVNN 390
Cdd:TIGR00958 319 --KVFGKRYQLLSEELqeavAKANQVAEEALSGMRTVRSFAAEEGE----ASRFKEALEETLQLNKrkaLAYAgYLWTTS 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 391 FLKLTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRIAEITDLETETELYTSKQP 470
Cdd:TIGR00958 393 VLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAP 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 471 YTFKNNIRIENVNFQYGFRS--VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD 548
Cdd:TIGR00958 473 LNLEGLIEFQDVSFSYPNRPdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 549 LRKNIGYVSQNTFLFADTIKNNLLHGSNkYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLART 628
Cdd:TIGR00958 553 LHRQVALVGQEPVLFSGSVRENIAYGLT-DTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 629 FLKDPDIYIFDEATSALDSLTENKIMEhidLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYK 708
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
..
gi 488434717 709 NL 710
Cdd:TIGR00958 709 HL 710
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
154-715 |
5.54e-75 |
|
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: 255.65 E-value: 5.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 154 IFKNNYGKLLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDV 233
Cdd:TIGR03797 130 ALRGARRDLLAILAMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 234 NLMKDYFYHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPL----LLLITIIFI 309
Cdd:TIGR03797 210 SLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKlalvAVALALVAI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 310 PCFIICSYTLRKpfekYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVN 389
Cdd:TIGR03797 290 AVTLVLGLLQVR----KERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFN 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 390 NFLKLTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRIAEItdLETETELYTSK- 468
Cdd:TIGR03797 366 AVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPI--LEALPEVDEAKt 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 469 QPYTFKNNIRIENVNFQYGFRS-VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLS 547
Cdd:TIGR03797 444 DPGKLSGAIEVDRVTFRYRPDGpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQ 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 548 DLRKNIGYVSQNTFLFADTIKNNLLhGSNKYkSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLAR 627
Cdd:TIGR03797 524 AVRRQLGVVLQNGRLMSGSIFENIA-GGAPL-TLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIAR 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLtqhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIY 707
Cdd:TIGR03797 602 ALVRKPRILLFDEATSALDNRTQAIVSESLERL---KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLF 678
|
....*...
gi 488434717 708 KNLWQLQM 715
Cdd:TIGR03797 679 AQLARRQL 686
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
235-705 |
6.38e-69 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 236.78 E-value: 6.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 235 LMKDYFYHVLHLPMNFFDTRKSGEILQ---RFMDT------SKIREALSS--STVTLLVDTF-------MIIIGAILLYm 296
Cdd:PRK13657 91 VLTEYFERIIQLPLAWHSQRGSGRALHtllRGTDAlfglwlEFMREHLATlvALVVLLPLALfmnwrlsLVLVVLGIVY- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 297 qspllllitiifipcFIICSYTLRKPF------EKYNQKVAEK--DAELSSYLIESFdgsNTIksyQSEddrfyigTTKF 368
Cdd:PRK13657 170 ---------------TLITTLVMRKTKdgqaavEEHYHDLFAHvsDAIGNVSVVQSY---NRI---EAE-------TQAL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 369 NGIIENLLKLgrfsniQLTVNNFLKL---------TIS-LVILWLGSYLVMTDSMTLGSLLAFNA---LTIYYLDPIERL 435
Cdd:PRK13657 222 RDIADNLLAA------QMPVLSWWALasvlnraasTITmLAILVLGAALVQKGQLRVGEVVAFVGfatLLIGRLDQVVAF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 436 INiqptlqSSFVAARRIAEITDLETET----ELYTSKQPYTFKNNIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGE 511
Cdd:PRK13657 296 IN------QVFMAAPKLEEFFEVEDAVpdvrDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 512 SGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLLHGSNKyKSDEDIVKACQLA 591
Cdd:PRK13657 370 TGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD-ATDEEMRAAAERA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 592 ESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTqHGKTVIIIS 671
Cdd:PRK13657 449 QAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIA 527
|
490 500 510
....*....|....*....|....*....|....
gi 488434717 672 HKLSTIKNADNIYVLNEGQIAENGTHDELIHLNG 705
Cdd:PRK13657 528 HRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
477-714 |
2.67e-68 |
|
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: 224.29 E-value: 2.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS-VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGY 555
Cdd:cd03252 1 ITFEHVRFRYKPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03252 81 VLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLWQLQ 714
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
477-690 |
4.08e-67 |
|
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: 218.41 E-value: 4.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSV-VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGY 555
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIKNNLlhgsnkyksdedivkacqlaesldfiqkfpdqfntmlekeganLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQ 690
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
162-699 |
1.11e-56 |
|
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: 202.67 E-value: 1.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:COG4618 22 FLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNffdtRKSGEILQRFMDTSKIREALSSSTVTLLVDT----------FMI--------IIGAILL----YMQSp 299
Cdd:COG4618 102 AAFRAALR----GGGGAAAQALRDLDTLRQFLTGPGLFALFDLpwapiflavlFLFhpllgllaLVGALVLvalaLLNE- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 300 llllitiifipcfiicsYTLRKPFEKYNQKVAEKDAELSSYL-----IESFD-GSNTIKSYQSEDDRF---YIGTTKFNG 370
Cdd:COG4618 177 -----------------RLTRKPLKEANEAAIRANAFAEAALrnaevIEAMGmLPALRRRWQRANARAlalQARASDRAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 371 IIENLLKlgrfsniqltvnnFLKLTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAAR 450
Cdd:COG4618 240 GFSALSK-------------FLRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 451 RIAEI-TDLETETElyTSKQPyTFKNNIRIENVNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYT 528
Cdd:COG4618 307 RLNELlAAVPAEPE--RMPLP-RPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 529 ASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNL--LHGSNkyksDEDIVKACQLAESLDFIQKFPDQFNT 606
Cdd:COG4618 384 PTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIarFGDAD----PEKVVAAAKLAGVHEMILRLPDGYDT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 607 MLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVL 686
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVL 539
|
570
....*....|...
gi 488434717 687 NEGQIAENGTHDE 699
Cdd:COG4618 540 RDGRVQAFGPRDE 552
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
162-452 |
4.85e-56 |
|
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: 193.11 E-value: 4.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18555 4 LISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRK 321
Cdd:cd18555 84 HLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 322 PFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVIL 401
Cdd:cd18555 164 KIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLIL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488434717 402 WLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18555 244 WIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
476-695 |
1.13e-55 |
|
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: 189.72 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIG 554
Cdd:cd03245 2 RIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPD 634
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 635 IYIFDEATSALDSLTENKIMEHIDLLTQHgKTVIIISHKLSTIKNADNIYVLNEGQIAENG 695
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
162-452 |
5.33e-54 |
|
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: 187.77 E-value: 5.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18568 4 LAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRK 321
Cdd:cd18568 84 HLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 322 PFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVIL 401
Cdd:cd18568 164 KLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488434717 402 WLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18568 244 WYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
158-715 |
4.56e-53 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 193.40 E-value: 4.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 158 NYGKLLFIAFISLFIN-IVGIVGALYFKLLTDHIIPSNVLKnLHIIS---FGILLLYIINALINYLRFQLILHLSLKIDV 233
Cdd:PRK10790 20 PWRKPLGLAVLMLWVAaAAEVSGPLLISYFIDNMVAKGNLP-LGLVAglaAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 234 NLMKDYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDtfMIIIGAILLYMQS-------------P 299
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQPVGQLISRVTnDTEVIRDLYVTVVATVLRS--AALIGAMLVAMFSldwrmalvaimifP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 300 LLLLITIIfipcfiicsytlrkpFEKYNQKVAEKdaeLSSYLIESFDGSNTIksyqseddrfyigttkFNG--IIENLLK 377
Cdd:PRK10790 177 AVLVVMVI---------------YQRYSTPIVRR---VRAYLADINDGFNEV----------------INGmsVIQQFRQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 378 LGRFSNIQLTVN--------NFLKLTISLV--ILWLGSYLVM-----------TDSMTLGSLLAFnaltIYYL----DPI 432
Cdd:PRK10790 223 QARFGERMGEASrshymarmQTLRLDGFLLrpLLSLFSALILcgllmlfgfsaSGTIEVGVLYAF----ISYLgrlnEPL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 433 ERLINIQPTLQSSFVAARRIAEITDLETETelY-TSKQPYTfKNNIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGE 511
Cdd:PRK10790 299 IELTTQQSMLQQAVVAGERVFELMDGPRQQ--YgNDDRPLQ-SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGH 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 512 SGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLLHGSNkykSDEDIV----KA 587
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD---ISEEQVwqalET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 588 CQLAEsldFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHgKTV 667
Cdd:PRK10790 453 VQLAE---LARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTL 528
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 488434717 668 IIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLWQLQM 715
Cdd:PRK10790 529 VVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQL 576
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
394-712 |
7.72e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 192.35 E-value: 7.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 394 LTISLvILWLGSYLVMTDSMTlGSLLAFNALTIyyLDPIERLINIQPTLQ---SSFVAARRIAEITDLETETELYTSKQP 470
Cdd:PRK11160 257 LTVVL-MLWLAAGGVGGNAQP-GALIALFVFAA--LAAFEALMPVAGAFQhlgQVIASARRINEITEQKPEVTFPTTSTA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 471 YTFKNNIRIENVNFQYGFRSV-VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL 549
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFADTIKNNLLHGSNKyKSDEDIVKACQ------LAESldfiqkfPDQFNTMLEKEGANLSGGQGQRL 623
Cdd:PRK11160 413 RQAISVVSQRVHLFSATLRDNLLLAAPN-ASDEALIEVLQqvglekLLED-------DKGLNAWLGEGGRQLSGGEQRRL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 624 SLARTFLKDPDIYIFDEATSALDSLTENKIMEhidLLTQH--GKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILE---LLAEHaqNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
330
....*....|.
gi 488434717 702 HLNGIYKNLWQ 712
Cdd:PRK11160 562 AQQGRYYQLKQ 572
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
162-452 |
4.51e-51 |
|
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: 179.67 E-value: 4.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLR 320
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTsDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 321 KPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSED---DRFyigTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTIS 397
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEreiERF---REANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 398 LVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd07346 238 ALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
476-696 |
3.24e-50 |
|
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: 174.60 E-value: 3.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQYGFRS-VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIG 554
Cdd:cd03244 2 DIEFKNVSLRYRPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFADTIKNNLlhGSNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPD 634
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL--DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 635 IYIFDEATSALDSLTENKIMEHIDllTQ-HGKTVIIISHKLSTIKNADNIYVLNEGQIAENGT 696
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIR--EAfKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
477-686 |
9.86e-50 |
|
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: 182.49 E-value: 9.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFADTIKNNLLHGSnKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIY 636
Cdd:TIGR02857 402 PQHPFLFAGTIAENIRLAR-PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488434717 637 IFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVL 686
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
404-714 |
1.04e-47 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 177.60 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 404 GSYLVMTDSMTLGSLLAFN---ALTIYYLDPIERLINIQPTLQSSFVAARRIAEITDLETETELYTSKQPYTFKNNIRie 480
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVmylGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIR-- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 481 nvNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQN 559
Cdd:PRK10789 320 --QFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 560 TFLFADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFD 639
Cdd:PRK10789 398 PFLFSDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 640 EATSALDSLTENKIMEHidlLTQ--HGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLWQLQ 714
Cdd:PRK10789 477 DALSAVDGRTEHQILHN---LRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
477-690 |
1.65e-46 |
|
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: 163.79 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG----FRSVVLKDINLNIKKGQKVAIVGESGSGKST-----IGKLlnryyTASEGNIMidnyiiddidls 547
Cdd:cd03250 1 ISVEDASFTWDsgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSllsalLGEL-----EKLSGSVS------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 548 dLRKNIGYVSQNTFLFADTIKNNLLHGSnKYKSD--EDIVKACQLaeSLDfIQKFPDQFNTML-EKeGANLSGGQGQRLS 624
Cdd:cd03250 64 -VPGSIAYVSQEPWIQNGTIRENILFGK-PFDEEryEKVIKACAL--EPD-LEILPDGDLTEIgEK-GINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 625 LARTFLKDPDIYIFDEATSALDSLTENKIMEH-IDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQ 690
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| Peptidase_C39B |
cd02418 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
4-137 |
2.40e-46 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239099 [Multi-domain] Cd Length: 136 Bit Score: 161.22 E-value: 2.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 4 KFIRQYDEKDCGPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKAD-SFDDLKQAQLPVMV 82
Cdd:cd02418 2 PYVLQVDEMDCGAACLAMIAKYYGKNYSLAKLRELAGTDREGTSLLGLVKAAEKLGFETRAVKADmDLFELKDIPLPFIA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 83 HIINQQGYDHYIIIEKIKNNTLYIVDPAKGKYKLSSTEFGKYWTNIAVLIDKTDD 137
Cdd:cd02418 82 HVIKEWKLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVALFLEPTPN 136
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
158-707 |
1.22e-45 |
|
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: 176.29 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 158 NYGKL--LFIAFISLFINIVGIVGAL----YFKLLTDHIIPSNVLKNLHI---------ISFGIL-LLYIINALINYLRF 221
Cdd:TIGR00957 957 DYMKAigLFITFLSIFLFVCNHVSALasnyWLSLWTDDPMVNGTQNNTSLrlsvygalgILQGFAvFGYSMAVSIGGIQA 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 222 QLILHLSLkidvnlmkdyFYHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLL 301
Cdd:TIGR00957 1037 SRVLHQDL----------LHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPI 1106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 302 LLITIIFIPCFiicsYTLRKPFEKYNQKVAEKDAELS-----SYLIESFDGSNTIKSYQSEDDRFYIGTTKFNgiiENll 376
Cdd:TIGR00957 1107 AAVIIPPLGLL----YFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAFEEQERFIHQSDLKVD---EN-- 1177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 377 klGRFSNIQLTVNNFLKLTISLV----ILWLGSYLVMTDSM----TLGSLLAFNALTIYYLDpieRLINIQPTLQSSFVA 448
Cdd:TIGR00957 1178 --QKAYYPSIVANRWLAVRLECVgnciVLFAALFAVISRHSlsagLVGLSVSYSLQVTFYLN---WLVRMSSEMETNIVA 1252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 449 ARRIAEITDLETET--ELYTSKQPYTFKNNIRIENVNFQYGFR---SVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLL 523
Cdd:TIGR00957 1253 VERLKEYSETEKEApwQIQETAPPSGWPPRGRVEFRNYCLRYRedlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGL 1332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 524 NRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLLHGSNkyKSDEDIVKACQLAESLDFIQKFPDQ 603
Cdd:TIGR00957 1333 FRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ--YSDEEVWWALELAHLKTFVSALPDK 1410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 604 FNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDllTQHGK-TVIIISHKLSTIKNADN 682
Cdd:TIGR00957 1411 LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDcTVLTIAHRLNTIMDYTR 1488
|
570 580
....*....|....*....|....*
gi 488434717 683 IYVLNEGQIAENGTHDELIHLNGIY 707
Cdd:TIGR00957 1489 VIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
470-691 |
7.89e-45 |
|
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: 160.33 E-value: 7.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 470 PYTFKNNIRIENVNFQYGFR--SVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLS 547
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 548 DLRKNIGYVSQNTFLFADTIKNNLLHGSNKyKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLAR 627
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQS-CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIME-HIDLLTQHgkTVIIISHKLSTIKNADNIYVLNEGQI 691
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQaLYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
165-452 |
5.70e-44 |
|
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: 159.97 E-value: 5.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 165 IAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVL 244
Cdd:cd18588 7 VLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 245 HLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRKPFE 324
Cdd:cd18588 87 RLPLSYFESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 325 KYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEddrfyigtTKFNGIIENLL--------KLGRFSNIQLTVNNFLKLTI 396
Cdd:cd18588 167 RRLEEKFQRGAENQSFLVETVTGIETVKSLAVE--------PQFQRRWEELLaryvkasfKTANLSNLASQIVQLIQKLT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 397 SLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18588 239 TLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
477-691 |
1.19e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.13 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFADTIKNNLLHGSNKYKSDEDIVKACQLAESLDfiqkFPDQFntmLEKEGANLSGGQGQRLSLARTFLKDPDIY 636
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKFDRERALELLERLG----LPPDI---LDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 637 IFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI 691
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLrEYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
477-702 |
5.71e-43 |
|
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: 155.18 E-value: 5.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQN--TFLFADTIKNNLLHG-SNKYKSDEDIVKacQLAESLDF--IQKFpdqfntmLEKEGANLSGGQGQRLSLARTFLK 631
Cdd:COG1122 81 FQNpdDQLFAPTVEEDVAFGpENLGLPREEIRE--RVEEALELvgLEHL-------ADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 632 DPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDELIH 702
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
477-702 |
1.99e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 161.22 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS----VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDL 549
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTF--LFA-DTIKNNL-----LHGSNKYKSDEDIV----KACQLAEslDFIQKFPDQFntmlekeganlSG 617
Cdd:COG1123 341 RRRVQMVFQDPYssLNPrMTVGDIIaeplrLHGLLSRAERRERVaellERVGLPP--DLADRYPHEL-----------SG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 618 GQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENG 695
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLrDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*..
gi 488434717 696 THDELIH 702
Cdd:COG1123 488 PTEEVFA 494
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
490-710 |
2.41e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 162.32 E-value: 2.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 490 SVVLKDINLNIKKGQKVAIVGESGSGKSTigkLLN------RYytasEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLF 563
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTS---LLNallgflPY----QGSLKINGIELRELDPESWRKHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 564 ADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATS 643
Cdd:PRK11174 436 HGTLRDNVLLG-NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 644 ALDSLTENKIMEHIDLLTQHgKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNL 710
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRR-QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
478-690 |
5.93e-42 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 151.47 E-value: 5.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 478 RIENVNFQYG-FRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:cd03225 1 ELKNLSFSYPdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQN--TFLFADTIK-------NNLlhGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSLAR 627
Cdd:cd03225 81 FQNpdDQFFGPTVEeevafglENL--GLPEEEIEERVEEALELVGLEGLRDRSPFT-----------LSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQ 690
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
477-695 |
1.58e-41 |
|
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: 151.12 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQY---GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLR 550
Cdd:cd03257 2 LEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 551 KNIGYVSQNTF-----------LFADTIKnnlLHGSNKYKSDEDIVKA---CQLAESLDFIQKFPDQfntmlekeganLS 616
Cdd:cd03257 82 KEIQMVFQDPMsslnprmtigeQIAEPLR---IHGKLSKKEARKEAVLlllVGVGLPEEVLNRYPHE-----------LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 617 GGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAEN 694
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLkKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
.
gi 488434717 695 G 695
Cdd:cd03257 228 G 228
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
162-437 |
1.89e-40 |
|
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: 150.30 E-value: 1.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18567 4 LLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRK 321
Cdd:cd18567 84 HLLRLPLSYFEKRHLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 322 PFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVIL 401
Cdd:cd18567 164 PLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVI 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 488434717 402 WLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLIN 437
Cdd:cd18567 244 YLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLID 279
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
165-425 |
1.71e-39 |
|
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: 147.28 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 165 IAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVL 244
Cdd:cd18783 7 VAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 245 HLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRKPFE 324
Cdd:cd18783 87 SLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 325 KYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVILWLG 404
Cdd:cd18783 167 RRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVG 246
|
250 260
....*....|....*....|.
gi 488434717 405 SYLVMTDSMTLGSLLAFNALT 425
Cdd:cd18783 247 AYLVFAGSLTVGALIAFNMLA 267
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
160-452 |
2.63e-39 |
|
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: 146.92 E-value: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 160 GKLLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDY 239
Cdd:cd18779 2 GLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 240 FYHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTL 319
Cdd:cd18779 82 LEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 320 RKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSED---DRFyigTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTI 396
Cdd:cd18779 162 RRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDralDRW---SNLFVDQLNASLRRGRLDALVDALLATLRLAA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 397 SLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18779 239 PLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| Peptidase_C39 |
pfam03412 |
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
3-137 |
3.13e-39 |
|
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family.
Pssm-ID: 367483 [Multi-domain] Cd Length: 133 Bit Score: 141.21 E-value: 3.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 3 IKFIRQYDEKDCGPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKADsFDDLKQAQLPVMV 82
Cdd:pfam03412 2 YKIVLQVDENDCGLACLAMILKYYGSNVSLEELRELAGTPAEGTSLLGLKKAAEKLGFKAKAIKAD-LSELKELPLPFIA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 83 HiiNQQGYDHYIIIEKIKNNTLYIVDPAKGKYKLSSTEFGKYWTNIAVLIDKTDD 137
Cdd:pfam03412 81 H--WDGNGGHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVALLVAPKPS 133
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
477-695 |
8.24e-39 |
|
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: 141.68 E-value: 8.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS-VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSdLRKNIGY 555
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIKNNLlhgsnkyksdedivkacqlaesldfiqkfpdqfntmlekeGANLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 636 YIFDEATSALDSLTENKIMEhidLLTQH--GKTVIIISHKLSTIKNADNIYVLNEGQIAENG 695
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLS---LIFEVlkDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
477-701 |
3.54e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 142.05 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNN--LLHGSNKYKSDEDIVKACQLAESLD-----FIQKFPDQfntmlekeganLSGGQGQRLSLART 628
Cdd:cd03295 81 IQQIGLFPHmTVEENiaLVPKLLKWPKEKIRERADELLALVGldpaeFADRYPHE-----------LSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 629 FLKDPDIYIFDEATSALDSLTENKIM-EHIDLLTQHGKTVIIISHKL-STIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQeEFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
401-674 |
3.54e-38 |
|
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: 149.43 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 401 LWLGSYLVMTDSMT--------LGSLLAFNALTIyyldpierLINIQPTLQSSFVAARRIAEITDLETETELYTSKQPYT 472
Cdd:TIGR02868 256 LWAGGPAVADGRLApvtlavlvLLPLAAFEAFAA--------LPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 473 F---KNNIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL 549
Cdd:TIGR02868 328 VglgKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFADTIKNNLLHGsNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTF 629
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARAL 486
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488434717 630 LKDPDIYIFDEATSALDSLTENKIMEhiDLL-TQHGKTVIIISHKL 674
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLE--DLLaALSGRTVVLITHHL 530
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
477-691 |
1.65e-37 |
|
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: 137.73 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGY 555
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIKNNLlhgsnkyksdedivkacqlaesldfiqkfpdqfntmlekeganLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQI 691
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
478-690 |
3.13e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.61 E-value: 3.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 478 RIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVS 557
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 QntflfadtiknnllhgsnkyksdedivkacqlaesldfiqkfpdqfntmlekeganLSGGQGQRLSLARTFLKDPDIYI 637
Cdd:cd00267 80 Q--------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488434717 638 FDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNA-DNIYVLNEGQ 690
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
477-710 |
4.43e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.66 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDlSDLRKNIGYV 556
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNL-----LHGSNKYKSDEDI---VKACQLAESLDfiqkfpdqfntmleKEGANLSGGQGQRLSLAR 627
Cdd:COG1131 79 PQEPALYPDlTVRENLrffarLYGLPRKEARERIdelLELFGLTDAAD--------------RKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDELI--HLN 704
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKarLLE 224
|
....*.
gi 488434717 705 GIYKNL 710
Cdd:COG1131 225 DVFLEL 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
477-696 |
9.89e-37 |
|
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: 136.77 E-value: 9.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFR-SVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGY 555
Cdd:cd03369 7 IEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIKNNlLHGSNKYkSDEDIVKACQLAESldfiqkfpdqfntmlekeGANLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03369 87 IPQDPTLFSGTIRSN-LDPFDEY-SDEEIYGALRVSEG------------------GLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGT 696
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
477-702 |
2.98e-36 |
|
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: 143.51 E-value: 2.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSV-VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTAS---EGNIMIDNYIIDDIDLSDLRKN 552
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 IGYVSQN--TFLFADTIKNNL-----LHGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSL 625
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIaealeNLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 626 ARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQ-HGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELIH 702
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
477-700 |
5.18e-36 |
|
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: 136.79 E-value: 5.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSV-VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMID-NYIIDDIDLSDLRKNIG 554
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgLDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQN--TFLFADTIKNNLLHG-SNKYKSDEDIVKacQLAESLDF--IQKFpdqfntmLEKEGANLSGGQGQRLSLARTF 629
Cdd:TIGR04520 81 MVFQNpdNQFVGATVEDDVAFGlENLGVPREEMRK--RVDEALKLvgMEDF-------RDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 630 LKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIrKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
163-432 |
7.99e-36 |
|
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: 136.62 E-value: 7.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 163 LFIAFISLFINIVG-IVGALYFKLLTDHIIPSN--VLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDY 239
Cdd:pfam00664 1 LILAILLAILSGAIsPAFPLVLGRILDVLLPDGdpETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 240 FYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYT 318
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTnDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 319 LRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKLGR----FSNIQLTVNNFLKL 394
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYE----LEKYDKALEEALKAGIkkavANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 488434717 395 TISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPI 432
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
477-700 |
1.32e-35 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 134.23 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNR-----YYTASEGNIMI--DNYIIDDIDLSDL 549
Cdd:cd03260 1 IELRDLNVYYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdgKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFADTIKNNL-----LHGSNKYKSDEDIVKacqlaESLDFIQkFPDQFNTMLEkeGANLSGGQGQRLS 624
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVayglrLHGIKLKEELDERVE-----EALRKAA-LWDEVKDRLH--ALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 625 LARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLtQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
477-700 |
6.13e-35 |
|
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: 133.00 E-value: 6.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGF---RSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNI 553
Cdd:COG1124 2 LEVRNLSVSYGQggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD---TIKNNL---LHGSNKYKSDEDIVKACQLAE-SLDFIQKFPDQfntmlekeganLSGGQGQRLSLA 626
Cdd:COG1124 82 QMVFQDPYASLHprhTVDRILaepLRIHGLPDREERIAELLEQVGlPPSFLDRYPHQ-----------LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 627 RTFLKDPDIYIFDEATSALDSLTENKIMehiDLLT----QHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEIL---NLLKdlreERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
477-702 |
1.51e-34 |
|
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: 131.47 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMID---NYIIDDIDLSDLRKNI 553
Cdd:cd03261 1 IELRGLTKSFGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgedISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD-TIKNNLL-----HGSNKYKSDEDIVKAC-QLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSLA 626
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAfplreHTRLSEEEIREIVLEKlEAVGLRGAEDLYPAE-----------LSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 627 RTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQ-HGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDELIH 702
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
477-694 |
2.65e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 130.55 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG---FRSVVLKDINLNIKKGQKVAIVGESGSGKSTigkLLN-----------RYY-------TASEGNim 535
Cdd:COG1136 5 LELRNLTKSYGtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKST---LLNilggldrptsgEVLidgqdisSLSERE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 536 idnyiiddidLSDLR-KNIGYVSQNTFLFAD-TIKNN-----LLHGSNKyksDEDIVKACQLAESL---DFIQKFPDQfn 605
Cdd:COG1136 80 ----------LARLRrRHIGFVFQFFNLLPElTALENvalplLLAGVSR---KERRERARELLERVglgDRLDHRPSQ-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 606 tmlekeganLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKNADNIY 684
Cdd:COG1136 145 ---------LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLrELNRELGTTIVMVTHDPELAARADRVI 215
|
250
....*....|
gi 488434717 685 VLNEGQIAEN 694
Cdd:COG1136 216 RLRDGRIVSD 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
477-707 |
5.57e-34 |
|
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: 130.00 E-value: 5.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGN---IMIDNYIIDDIDLSDLRKNI 553
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvliDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD-TIKNNLLHGSNKYKS----------DEDIVKACQLAESLDFIQKFpdqfntmlEKEGANLSGGQGQR 622
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRRStwrslfglfpKEEKQRALAALERVGLLDKA--------YQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 623 LSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIK-NADNIYVLNEGQIAENGTHDEL 700
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
|
....*....
gi 488434717 701 I--HLNGIY 707
Cdd:cd03256 233 TdeVLDEIY 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
200-718 |
6.55e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 139.73 E-value: 6.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 200 HIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVT 279
Cdd:PLN03232 341 YVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 280 LLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDD 359
Cdd:PLN03232 421 LWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKS 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 360 RfyigTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVI--LWLGSYLVMTDSMTLGSllAFNALTIYYL--DPIERL 435
Cdd:PLN03232 501 F----ESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVtlVSFGVFVLLGGDLTPAR--AFTSLSLFAVlrSPLNML 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 436 INIQPTLQSSFVAARRIAEItdLETETELYTSKQPYT-FKNNIRIENVNFQYGFRSV--VLKDINLNIKKGQKVAIVGES 512
Cdd:PLN03232 575 PNLLSQVVNANVSLQRIEEL--LLSEERILAQNPPLQpGAPAISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGT 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 513 GSGK-STIGKLLNRYYTASEGNImidnyiiddidlsDLRKNIGYVSQNTFLFADTIKNNLLHGSnKYKSDE--DIVKACQ 589
Cdd:PLN03232 653 GEGKtSLISAMLGELSHAETSSV-------------VIRGSVAYVPQVSWIFNATVRENILFGS-DFESERywRAIDVTA 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 590 LAESLDFiqkFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVII 669
Cdd:PLN03232 719 LQHDLDL---LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVL 795
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 488434717 670 ISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNLWQLQMKID 718
Cdd:PLN03232 796 VTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMD 844
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
165-452 |
7.10e-34 |
|
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: 131.55 E-value: 7.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 165 IAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVL 244
Cdd:cd18566 7 VLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 245 HLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVD--------TFMIIIGAILLYMqsplLLLITIIFIPCFIICS 316
Cdd:cd18566 87 SLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDlpfvliflGLIWYLGGKLVLV----PLVLLGLFVLVAILLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 317 YTLRKPFEKYNqkvaEKDAELSSYLIESFDGSNTIKSYQSED------DRFYIGTtkfngiIENLLKLGRFSNI-QLTVN 389
Cdd:cd18566 163 PILRRALKERS----RADERRQNFLIETLTGIHTIKAMAMEPqmlrryERLQANA------AYAGFKVAKINAVaQTLGQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 390 NFLKLTISLViLWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18566 233 LFSQVSMVAV-VAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
474-704 |
8.15e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.91 E-value: 8.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 474 KNNIRIENVNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKN 552
Cdd:PRK13635 3 EEIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 IGYVSQ---NTFLFAdTIKNNLLHG-SNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekEGANLSGGQGQRLSLART 628
Cdd:PRK13635 83 VGMVFQnpdNQFVGA-TVQDDVAFGlENIGVPREEMVERVDQALRQVGMEDFLNR-------EPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 629 FLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLN 704
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
492-700 |
8.25e-34 |
|
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: 131.13 E-value: 8.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDnyiiddidlsdlrKNIGYVSQNTFLFADTIKNNL 571
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS-------------GRISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 572 LHGSN----KYKSdedIVKACQLAESldfIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDS 647
Cdd:cd03291 119 IFGVSydeyRYKS---VVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488434717 648 LTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
477-691 |
1.01e-33 |
|
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: 128.76 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG---FRSVVLKDINLNIKKGQKVAIVGESGSGKST----IGKLLnryyTASEGNIMIDNYIIDDIDLSDL 549
Cdd:cd03255 1 IELKNLSKTYGgggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTllniLGGLD----RPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 ----RKNIGYVSQNTFLFAD-TIKNN-----LLHGSnkyKSDEDIVKACQLAESL---DFIQKFPDQfntmlekeganLS 616
Cdd:cd03255 77 aafrRRHIGFVFQSFNLLPDlTALENvelplLLAGV---PKKERRERAEELLERVglgDRLNHYPSE-----------LS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 617 GGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQI 691
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
477-700 |
1.04e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.50 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS-VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGY 555
Cdd:PRK13632 8 IKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQN---TFLFAdTIKNNLLHG--SNKYKSDE--DIVKacQLAESLDfIQKFpdqfntmLEKEGANLSGGQGQRLSLART 628
Cdd:PRK13632 88 IFQNpdnQFIGA-TVEDDIAFGleNKKVPPKKmkDIID--DLAKKVG-MEDY-------LDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 629 FLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHG-KTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
477-700 |
1.06e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.44 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidLSDLRKNIGYV 556
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFL---F----ADTI------KNNLLHGSNKykSDEDIVkacqlAESLDF--IQKFPD-QFNTmlekeganLSGGQG 620
Cdd:COG1121 81 PQRAEVdwdFpitvRDVVlmgrygRRGLFRRPSR--ADREAV-----DEALERvgLEDLADrPIGE--------LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 621 QRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDE 699
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVrEYFDRVLLLNRGLVAHGPPEEV 225
|
.
gi 488434717 700 L 700
Cdd:COG1121 226 L 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
477-690 |
4.27e-33 |
|
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: 125.38 E-value: 4.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMI--DNYIIDDIDLSDLRKNIG 554
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgEDLTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFAD-TIKNNLLHGsnkyksdedivkacqlaesldfiqkfpdqfntmlekeganLSGGQGQRLSLARTFLKDP 633
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 634 DIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQ 690
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLkSLQAQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
161-452 |
6.21e-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: 128.74 E-value: 6.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 161 KLLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYF 240
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 241 YHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMII-IGAILLYMqSPLLLLITIIFIPCFIICSYT 318
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVInDVNSLSDLLSNGLINLIPDLLTLVgIVIIMFSL-NVRLALVTLAVLPLLVLVVFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 319 LRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIgttkFNGIIENLLKlgrfSNIQLT-VNNFLKLTIS 397
Cdd:cd18545 160 LRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEI----FDELNRENRK----ANMRAVrLNALFWPLVE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 398 L-------VILWLGSYLVMTDSMTLGSLLAFnaltIYYL----DPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18545 232 LisalgtaLVYWYGGKLVLGGAITVGVLVAF----IGYVgrfwQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
163-452 |
8.44e-33 |
|
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: 128.31 E-value: 8.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 163 LFIAFISLFIniVGIVGALYFKL---LTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDY 239
Cdd:cd18552 1 LALAILGMIL--VAATTAALAWLlkpLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 240 FYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYT 318
Cdd:cd18552 79 FDKLLRLPLSFFDRNSSGDLISRITnDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 319 LRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDdrfYIgTTKFNGIIENL----LKLGRFSNIQLTVNNFLKL 394
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAED---YE-IKRFRKANERLrrlsMKIARARALSSPLMELLGA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 395 TISLVILWLGSYLVMTDSMTLGSLLAFnaLTIYYL--DPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18552 235 IAIALVLWYGGYQVISGELTPGEFISF--ITALLLlyQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
162-435 |
1.03e-32 |
|
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: 128.09 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18782 4 LIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRK 321
Cdd:cd18782 84 HLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 322 PFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVIL 401
Cdd:cd18782 164 ILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVL 243
|
250 260 270
....*....|....*....|....*....|....
gi 488434717 402 WLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERL 435
Cdd:cd18782 244 WVGAYLVLRGELTLGQLIAFRILSGYVTGPILRL 277
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
477-701 |
1.88e-32 |
|
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: 125.39 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG---FRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLR 550
Cdd:cd03258 2 IELKNVSKVFGdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 551 KNIGYVSQNTFLFAD-TIKNNL-----LHGSNKYKSDEDIVKACQLAESLDFIQKFPdqfntmlekegANLSGGQGQRLS 624
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENValpleIAGVPKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 625 LARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELI 701
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLrDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
339-701 |
2.92e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 134.77 E-value: 2.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 339 SYLIESFDGSNTIKSYQSED---DRFYIGTTKFNGIIenlLKLGRFSNIQLTVNNFLKLTISLVILWLGSYLVMTD---- 411
Cdd:PTZ00265 237 SIIEEALVGIRTVVSYCGEKtilKKFNLSEKLYSKYI---LKANFMESLHIGMINGFILASYAFGFWYGTRIIISDlsnq 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 412 ------------SMTLGSLLAFNALTIYyldpierLINIQPTLQSsFVAARRIAEITDLETETELYTSKQPYTFKNNIRI 479
Cdd:PTZ00265 314 qpnndfhggsviSILLGVLISMFMLTII-------LPNITEYMKS-LEATNSLYEIINRKPLVENNDDGKKLKDIKKIQF 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 480 ENVNFQYGFRSVV--LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMID-NYIIDDIDLSDLRKNIGYV 556
Cdd:PTZ00265 386 KNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVV 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFADTIKNN------------------------------------------------------LLHGSNKYKS-- 580
Cdd:PTZ00265 466 SQDPLLFSNSIKNNikyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneLIEMRKNYQTik 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 581 DEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DL 659
Cdd:PTZ00265 546 DSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInNL 625
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 488434717 660 LTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PTZ00265 626 KGNENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIG 667
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
477-691 |
4.82e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 122.12 E-value: 4.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLsDLRKNIGYV 556
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLlhgsnkyksdedivkacqlaesldfiqkfpdqfntmlekegaNLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03230 79 PEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI 691
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
477-691 |
5.57e-32 |
|
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: 123.41 E-value: 5.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMI--DNYIIDDIDLSDLRKNIG 554
Cdd:cd03262 1 IEIKNLHKSFGDF-HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdgLKLTDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFAD-TIKNNL------LHGSNKyksDEDIVKACQLAES---LDFIQKFPDQfntmlekeganLSGGQGQRLS 624
Cdd:cd03262 80 MVFQQFNLFPHlTVLENItlapikVKGMSK---AEAEERALELLEKvglADKADAYPAQ-----------LSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 625 LARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI 691
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
477-702 |
8.95e-32 |
|
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: 123.94 E-value: 8.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLRKNI 553
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgQDITGLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD-TIKNNLL-----HGSNKYKSDEDIVKAC-QLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSLA 626
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAfplreHTDLSEAEIRELVLEKlELVGLPGAADKMPSE-----------LSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 627 RTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELIH 702
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIrELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
478-691 |
1.30e-31 |
|
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: 122.37 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 478 RIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGnimIDNYIIDDIDLSDLRKNIGYVS 557
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSG---SILLNGKPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 QNT--FLFADTIKNNLLHGSNKYksDEDIVKACQLAESLDFiqkfpdqfNTMLEKEGANLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKEL--DAGNEQAETVLKDLDL--------YALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI 691
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
477-693 |
1.31e-31 |
|
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: 122.58 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS---VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidLSDLRKNI 553
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFA-DTIKNN-----LLHGSNKYKSDE---DIVKACQLAeslDFIQKFPDQfntmlekeganLSGGQGQRLS 624
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvalglELQGVPKAEAREraeELLELVGLS---GFENAYPHQ-----------LSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 625 LARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLS-TIKNADNIYVLNE--GQIAE 693
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELlDIWRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
493-643 |
2.21e-31 |
|
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: 119.67 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFAD-TIKNNL 571
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 572 LHGSN--KYKSDEDIVKACQLAESLDfiqkFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATS 643
Cdd:pfam00005 81 RLGLLlkGLSKREKDARAEEALEKLG----LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
474-713 |
1.15e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 129.76 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 474 KNNIRIENVNFQYGFRSVV--LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYT----------------------- 528
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 529 -------------------------------ASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLLHGSNK 577
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 578 yKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI 657
Cdd:PTZ00265 1323 -ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 658 -DLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQ-----IAENGTHDELIHL-NGIYKNLWQL 713
Cdd:PTZ00265 1402 vDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVqDGVYKKYVKL 1464
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
478-692 |
2.36e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 118.79 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 478 RIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidLSDLRKNIGYVS 557
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 QNT---FLFADTIKNNLLHGSNKY--------KSDEDIVKacqlaESLDFIQkfpdqfntMLEKEGAN---LSGGQGQRL 623
Cdd:cd03235 75 QRRsidRDFPISVRDVVLMGLYGHkglfrrlsKADKAKVD-----EALERVG--------LSELADRQigeLSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 624 SLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIA 692
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVlEYFDRVLLLNRTVVA 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
477-701 |
3.96e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 118.94 E-value: 3.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMI--DNYIIDDIDLSDLRKNIG 554
Cdd:COG1126 2 IEIENLHKSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdgEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFAD-TIKNNL------LHGSNKyksDEdivkACQLAESL-------DFIQKFPDQfntmlekeganLSGGQG 620
Cdd:COG1126 81 MVFQQFNLFPHlTVLENVtlapikVKKMSK---AE----AEERAMELlervglaDKADAYPAQ-----------LSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 621 QRLSLARTFLKDPDIYIFDEATSALDSltEN-----KIMEHidlLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAEN 694
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDP--ELvgevlDVMRD---LAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEE 217
|
....*..
gi 488434717 695 GTHDELI 701
Cdd:COG1126 218 GPPEEFF 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
478-695 |
5.45e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 116.77 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 478 RIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVS 557
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 QntflfadtiknnllhgsnkyksdedivkACQLAESLDFIQKFpdqFNTmlekeganLSGGQGQRLSLARTFLKDPDIYI 637
Cdd:cd03214 80 Q----------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 638 FDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENG 695
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLrRLARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
477-695 |
5.96e-30 |
|
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: 117.62 E-value: 5.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGnimidNYIIDDIDLSDL---RKNI 553
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSG-----EILIDGRDVTGVppeRRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD-TIKNNLLHG-SNKYKSDEDIVKACQLAESL----DFIQKFPDQfntmlekeganLSGGQGQRLSLAR 627
Cdd:cd03259 75 GMVFQDYALFPHlTVAENIAFGlKLRGVPKAEIRARVRELLELvgleGLLNRYPHE-----------LSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLS---TIknADNIYVLNEGQIAENG 695
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELkELQRELGITTIYVTHDQEealAL--ADRIAVMNEGRIVQVG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
162-701 |
7.96e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 127.01 E-value: 7.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFisLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLL-YIINALINylRFQLI---LHLSLKIDVNLMK 237
Cdd:PLN03232 916 ILLVCY--LTTEVLRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFgQVAVTFTN--SFWLIsssLHAAKRLHDAMLN 991
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 238 DyfyhVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTL------LVDTFMII--IGAILLYMQSPLLLLItiif 308
Cdd:PLN03232 992 S----ILRAPMLFFHTNPTGRVINRFSkDIGDIDRNVANLMNMFmnqlwqLLSTFALIgtVSTISLWAIMPLLILF---- 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 309 ipcfiicsYTLRKPFEKYNQKVAEKDAELSSYLI----ESFDGSNTIKSYQSEDDRFYI-GTTKFNGIienllklgRFSN 383
Cdd:PLN03232 1064 --------YAAYLYYQSTSREVRRLDSVTRSPIYaqfgEALNGLSSIRAYKAYDRMAKInGKSMDNNI--------RFTL 1127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 384 IQLTVNNFLKL---TISLVILWL-GSYLVMTD---------SMTLGSLLAFnalTIYYLDPIERLINIQPTLQSSFVAAR 450
Cdd:PLN03232 1128 ANTSSNRWLTIrleTLGGVMIWLtATFAVLRNgnaenqagfASTMGLLLSY---TLNITTLLSGVLRQASKAENSLNSVE 1204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 451 RIAEITDLETE-TELYTSKQP---YTFKNNIRIENVNFQY--GFRSVvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLN 524
Cdd:PLN03232 1205 RVGNYIDLPSEaTAIIENNRPvsgWPSRGSIKFEDVHLRYrpGLPPV-LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF 1283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 525 RYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLLHGSNkyKSDEDIVKACQLAESLDFIQKFPDQF 604
Cdd:PLN03232 1284 RIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSE--HNDADLWEALERAHIKDVIDRNPFGL 1361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 605 NTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSAL----DSLTENKIMEHIdlltqHGKTVIIISHKLSTIKNA 680
Cdd:PLN03232 1362 DAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVdvrtDSLIQRTIREEF-----KSCTMLVIAHRLNTIIDC 1436
|
570 580
....*....|....*....|.
gi 488434717 681 DNIYVLNEGQIAENGTHDELI 701
Cdd:PLN03232 1437 DKILVLSSGQVLEYDSPQELL 1457
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
201-701 |
8.87e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 126.78 E-value: 8.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 201 IISFGILLLYIINAlinylrFQLILHlSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIRE--ALSSS- 276
Cdd:PLN03130 961 LLSFGQVLVTLLNS------YWLIMS-SLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAkDLGDIDRnvAVFVNm 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 277 ---TVTLLVDTFMII--IGAILLYMQSPLLLLItiifipcfiicsYTLRKPFEKYNQKVAEKDAELSSYLI----ESFDG 347
Cdd:PLN03130 1034 flgQIFQLLSTFVLIgiVSTISLWAIMPLLVLF------------YGAYLYYQSTAREVKRLDSITRSPVYaqfgEALNG 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 348 SNTIKSYQSEDDRFYI-GTTKFNGIienllklgRFSNIQLTVNNFlkLTISLVIL-----WL-GSYLVMTDSM------- 413
Cdd:PLN03130 1102 LSTIRAYKAYDRMAEInGRSMDNNI--------RFTLVNMSSNRW--LAIRLETLgglmiWLtASFAVMQNGRaenqaaf 1171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 414 --TLGSLLAFnALTIY-YLDPIERLINIQptlQSSFVAARRIAEITDLETETELYT-SKQP---YTFKNNIRIENVNFQY 486
Cdd:PLN03130 1172 asTMGLLLSY-ALNITsLLTAVLRLASLA---ENSLNAVERVGTYIDLPSEAPLVIeNNRPppgWPSSGSIKFEDVVLRY 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 487 gfRS---VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLF 563
Cdd:PLN03130 1248 --RPelpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLF 1325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 564 ADTIKNNlLHGSNKYkSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATS 643
Cdd:PLN03130 1326 SGTVRFN-LDPFNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 644 ALDSLTENKIMEHIdllTQHGK--TVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PLN03130 1404 AVDVRTDALIQKTI---REEFKscTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
367-710 |
1.35e-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: 126.21 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 367 KFNGIIENLLKLGRFSNIQLTVNNFL----KLTISLVILWLgsYLVMTDSMTLGSLLAFNALTIYyldPIERL-INIQPT 441
Cdd:TIGR00957 521 KVEGIRQEELKVLKKSAYLHAVGTFTwvctPFLVALITFAV--YVTVDENNILDAEKAFVSLALF---NILRFpLNILPM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 442 LQSSFVAA----RRIAEITDLETETELYTSKQPYT--FKNNIRIENVNFQYGfRSV--VLKDINLNIKKGQKVAIVGESG 513
Cdd:TIGR00957 596 VISSIVQAsvslKRLRIFLSHEELEPDSIERRTIKpgEGNSITVHNATFTWA-RDLppTLNGITFSIPEGALVAVVGQVG 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 514 SGKSTIGKLLNRYYTASEGNIMidnyiiddidlsdLRKNIGYVSQNTFLFADTIKNNLLHG----SNKYKSdedIVKACQ 589
Cdd:TIGR00957 675 CGKSSLLSALLAEMDKVEGHVH-------------MKGSVAYVPQQAWIQNDSLRENILFGkalnEKYYQQ---VLEACA 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 590 LAESLDFIqkfPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI----DLLTqhGK 665
Cdd:TIGR00957 739 LLPDLEIL---PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpeGVLK--NK 813
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488434717 666 TVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKNL 710
Cdd:TIGR00957 814 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
477-710 |
2.24e-29 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 117.32 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGY 555
Cdd:cd03288 20 IKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIKNNLlhGSNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03288 100 ILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 636 YIFDEATSALDSLTENkIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELI-HLNGIYKNL 710
Cdd:cd03288 178 LIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
492-700 |
2.70e-29 |
|
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: 125.41 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDnyiiddidlsdlrKNIGYVSQNTFLFADTIKNNL 571
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS-------------GRISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 572 LHGSN----KYKSdedIVKACQLAESldfIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDS 647
Cdd:TIGR01271 508 IFGLSydeyRYTS---VIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488434717 648 LTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:TIGR01271 582 VTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
490-701 |
1.22e-28 |
|
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: 115.82 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 490 SVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL----RKNIGYVSQNTFLFAD 565
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 566 -TIKNNL-----LHGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSLARTFLKDPDIYIFD 639
Cdd:cd03294 117 rTVLENVafgleVQGVPRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 640 EATSALDSLTENKIMEH-IDLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:cd03294 186 EAFSALDPLIRREMQDElLRLQAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
476-702 |
1.01e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.03 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEG------NIMIDNYIIDDIDLSDL 549
Cdd:COG4161 2 SIQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGqlniagHQFDFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFAD-TIKNNLLH------GSNKyksDEDIVKACQLAESL---DFIQKFPdqfntmlekegANLSGGQ 619
Cdd:COG4161 81 RQKVGMVFQQYNLWPHlTVMENLIEapckvlGLSK---EQAREKAMKLLARLrltDKADRFP-----------LHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 620 GQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHD 698
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDAS 226
|
....
gi 488434717 699 ELIH 702
Cdd:COG4161 227 HFTQ 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
477-693 |
1.13e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 111.30 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLRKNI 553
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngQDLSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD-TIKNNL-----LHGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSLAR 627
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENValplrVTGKSRKEIRRRVREVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADN-IYVLNEGQIAE 693
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
477-698 |
1.67e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEG------NIMIDNYIIDDIDLSDLR 550
Cdd:PRK11124 3 IQLNGINCFYG-AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlniagNHFDFSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 551 KNIGYVSQNTFLFAD-TIKNNLLH------GSNKyksDEDIVKACQLAESL---DFIQKFPDQfntmlekeganLSGGQG 620
Cdd:PRK11124 82 RNVGMVFQQYNLWPHlTVQQNLIEapcrvlGLSK---DQALARAEKLLERLrlkPYADRFPLH-----------LSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 621 QRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHD 698
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
477-701 |
1.97e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.39 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMID-NYIIDDIDLSDLRKNIGY 555
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQN--TFLFADTIKNNLLHG-SNKYKSDEDIVKACQLAESLDFIQKFPdqfntmlEKEGANLSGGQGQRLSLARTFLKD 632
Cdd:PRK13644 82 VFQNpeTQFVGRTVEEDLAFGpENLCLPPIEIRKRVDRALAEIGLEKYR-------HRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 633 PDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
475-700 |
2.62e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.77 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 475 NNIRIENVNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNI 553
Cdd:PRK13648 6 SIIVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQN--TFLFADTIKNNLLHG----SNKYKSDEDIVKacQLAESLDFIQKFPDqfntmlekEGANLSGGQGQRLSLAR 627
Cdd:PRK13648 86 GIVFQNpdNQFVGSIVKYDVAFGlenhAVPYDEMHRRVS--EALKQVDMLERADY--------EPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQ-HGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
477-693 |
4.74e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.95 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS---VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidLSDLRKNI 553
Cdd:COG1116 8 LELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFA-DTIKNNLLHG--SNKYKSDEDIVKACQLAESL---DFIQKFPDQfntmlekeganLSGGQGQRLSLAR 627
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGleLRGVPKAERRERARELLELVglaGFEDAYPHQ-----------LSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISH------KLstiknADNIYVLNE--GQIAE 693
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELlRLWQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
477-701 |
4.95e-27 |
|
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: 110.56 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDN-YIIDDIDLSDLRKNIGY 555
Cdd:COG1119 4 LELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFgERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VS---QNTFLFADTIKNNLL---HGS----NKYkSDEDIVKACQLAESLDfIQKFPDQ-FNTmlekeganLSGGQGQRLS 624
Cdd:COG1119 83 VSpalQLRFPRDETVLDVVLsgfFDSiglyREP-TDEQRERARELLELLG-LAHLADRpFGT--------LSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 625 LARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVII-ISHKLSTIKNA-DNIYVLNEGQIAENGTHDELI 701
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
162-452 |
1.50e-26 |
|
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: 110.29 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKN----LHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMK 237
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGntslLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 238 DYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMII-IGAILLYMqSPLLLLITIIFIPCFIIC 315
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTsDTDRLQDFLSDGLPDFLTNILMIIgIGVVLFSL-NWKLALLVLIPVPLVVWG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 316 SYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFyigtTKFNGIIENLLKLG-RFSNIQLTVNNFLKL 394
Cdd:cd18563 160 SYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREI----KRFDEANQELLDANiRAEKLWATFFPLLTF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 395 TIS---LVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18563 236 LTSlgtLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
477-699 |
3.49e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.98 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG----FRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMI--DNYIIDDIDLSDLR 550
Cdd:PRK13637 3 IKIENLTHIYMegtpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 551 KNIGYVSQ--NTFLFADTIKNNLLHG-SNKYKSDEDI---VKACQLAESLDfiqkfpdqFNTMLEKEGANLSGGQGQRLS 624
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpINLGLSEEEIenrVKRAMNIVGLD--------YEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 625 LARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDE 699
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIkELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
162-443 |
1.17e-25 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 107.56 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNV---LKNLhIISFGILLLyiINALINYLRFQLILHLSLKIDVNLMKD 238
Cdd:cd18569 4 LLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLpdwLRPL-LLGMALTAL--LQGLLTWLQQYYLLRLETKLALSSSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 239 YFYHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPC-FIICSY 317
Cdd:cd18569 81 FFWHVLRLPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLnLLVLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 318 TLRKPFEKyNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFyigtTKFNGIIENLL----KLGRFSNIQLTVNNFLK 393
Cdd:cd18569 161 VSRKRVDL-NRRLLQDSGKLTGTTMSGLQMIETLKASGAESDFF----SRWAGYQAKVLnaqqELGRTNQLLGALPTLLS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488434717 394 LTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQ 443
Cdd:cd18569 236 ALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQ 285
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
163-452 |
1.42e-25 |
|
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: 107.52 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 163 LFIAFISLFINIV-GIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18542 1 YLLAILALLLATAlNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLR 320
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTsDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 321 KPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDdrFYIGttKFNGIIENLLKLgrfsNIQLT--------VNNFL 392
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFARED--YEIE--KFDKENEEYRDL----NIKLAkllakywpLMDFL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 393 KLTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIE---RLINIqptLQSSFVAARRI 452
Cdd:cd18542 233 SGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRqlgRLIND---MSRASASAERI 292
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
162-452 |
2.39e-25 |
|
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: 106.72 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNV------LKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNL 235
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGggggvdFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 236 MKDYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFII 314
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTnDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 315 CSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKLGR----FSNIQLTVNN 390
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEA----IEEFDEINEELYKASFkaqfYSGLLMPIMN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 391 FLKLTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18547 237 FINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
477-700 |
5.42e-25 |
|
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: 103.86 E-value: 5.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimIDNYIIDDIDLSDLRKNIGYV 556
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGE--ILLDGKDITNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLLHGSNKYKSDEDIVKAcQLAESLDFIQ------KFPDQfntmlekeganLSGGQGQRLSLARTF 629
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGLRLKKLPKAEIKE-RVAEALDLVQlegyanRKPSQ-----------LSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 630 LKDPDIYIFDEATSALD-SLTENKIMEHIDLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:cd03300 146 VNEPKVLLLDEPLGALDlKLRKDMQLELKRLQKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
474-700 |
7.12e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.81 E-value: 7.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 474 KNNIRIENVNFQY--GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRK 551
Cdd:PRK13650 2 SNIIEVKNLTFKYkeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 552 NIGYVSQ---NTFLFAdTIKNNLLHG-SNKYKSDEDIVKACQLAESLDFIQKFPDqfntmleKEGANLSGGQGQRLSLAR 627
Cdd:PRK13650 82 KIGMVFQnpdNQFVGA-TVEDDVAFGlENKGIPHEEMKERVNEALELVGMQDFKE-------REPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIkGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
162-452 |
1.09e-24 |
|
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: 104.78 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNV--LKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDY 239
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQgdLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 240 FYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMII-IGAILLYMqSPLLLLITIIFIPCFIICSY 317
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTnDTEALNELFTSGLVTLIGDLLLLIgILIAMFLL-NWRLALISLLVLPLLLLATY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 318 TLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFyigtTKFNGIIENLLKLGRFSN----IQLTVNNFLK 393
Cdd:cd18544 160 LFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREF----EEFDEINQEYRKANLKSIklfaLFRPLVELLS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 394 LTISLVILWLGSYLVMTDSMTLGSLLAFnaltIYYL----DPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18544 236 SLALALVLWYGGGQVLSGAVTLGVLYAF----IQYIqrffRPIRDLAEKFNILQSAMASAERI 294
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
477-702 |
1.09e-24 |
|
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: 105.52 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLK---DINLNIKKGQKVAIVGESGSGKSTIGKLLNRYY------------------TASEgnim 535
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppgitsgeilfdgedllKLSE---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 536 idnyiiddIDLSDLR-KNIGYVSQNTF-----------LFADTIKnnlLHGSNKYKSDEDIV----KACQLAESLDFIQK 599
Cdd:COG0444 78 --------KELRKIRgREIQMIFQDPMtslnpvmtvgdQIAEPLR---IHGGLSKAEARERAiellERVGLPDPERRLDR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 600 FPDQFntmlekeganlSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIK 678
Cdd:COG0444 147 YPHEL-----------SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLkDLQRELGLAILFITHDLGVVA 215
|
250 260
....*....|....*....|....*
gi 488434717 679 N-ADNIYVLNEGQIAENGTHDELIH 702
Cdd:COG0444 216 EiADRVAVMYAGRIVEEGPVEELFE 240
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
167-452 |
2.07e-24 |
|
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: 103.67 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 167 FISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGIL-LLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVLH 245
Cdd:cd18551 2 ILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLvALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 246 LPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRKPFE 324
Cdd:cd18551 82 LPVSFFDRRRSGDLVSRVTnDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 325 KYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVILWLG 404
Cdd:cd18551 162 KASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 488434717 405 SYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18551 242 GARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
477-710 |
3.26e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.06 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS--VVLKDINLNIKKGQKVAIVGESGSGK-STIGKLLNRYYTASEGNIMidnyiiddidlsdLRKNI 553
Cdd:PLN03130 615 ISIKNGYFSWDSKAerPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVV-------------IRGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFADTIKNNLLHGS----NKYksdEDIVKACQLAESLDFIqkfPDQFNTMLEKEGANLSGGQGQRLSLARTF 629
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSpfdpERY---ERAIDVTALQHDLDLL---PGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 630 LKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHLNGIYKN 709
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQK 835
|
.
gi 488434717 710 L 710
Cdd:PLN03130 836 L 836
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
477-696 |
4.02e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.00 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVN--FQYGFRSVV-LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLR 550
Cdd:COG1135 2 IELENLSktFPTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 551 KNIGYVSQNtFlfadtiknNLLHGSNKY-----------KSDEDIVKacQLAESLDFI------QKFPDQfntmlekega 613
Cdd:COG1135 82 RKIGMIFQH-F--------NLLSSRTVAenvalpleiagVPKAEIRK--RVAELLELVglsdkaDAYPSQ---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 614 nLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKImehIDLL----TQHGKTVIIISHKLSTIKN-ADNIYVLNE 688
Cdd:COG1135 141 -LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSI---LDLLkdinRELGLTIVLITHEMDVVRRiCDRVAVLEN 216
|
....*...
gi 488434717 689 GQIAENGT 696
Cdd:COG1135 217 GRIVEQGP 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
475-700 |
6.04e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.19 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 475 NNIRIENVNFQY-GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDN---YIIDDIDLSDLR 550
Cdd:PRK13640 4 NIVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITvdgITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 551 KNIGYVSQN---TFLFAdTIKNNLLHG-SNKYKSDEDIVKACQLAES----LDFIQKFPdqfntmlekegANLSGGQGQR 622
Cdd:PRK13640 84 EKVGIVFQNpdnQFVGA-TVGDDVAFGlENRAVPRPEMIKIVRDVLAdvgmLDYIDSEP-----------ANLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 623 LSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIrKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
477-672 |
6.39e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 101.65 E-value: 6.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYY-----TASEGNIMIDNY--IIDDIDLSDL 549
Cdd:COG1117 12 IEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEdiYDPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFADTIKNNL-----LHGsNKYKSD-EDIVKACQLAESLdfiqkfPDQFNTMLEKEGANLSGGQGQRL 623
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVayglrLHG-IKSKSElDEIVEESLRKAAL------WDEVKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488434717 624 SLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHgKTVIIISH 672
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTH 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
477-700 |
7.64e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.17 E-value: 7.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG----FRSVVLKDINLNIKKGQKVAIVGESGSGKST----IGKLLNRYYTASEGNIMIDNYIIDDIDLSD 548
Cdd:PRK13646 3 IRFDNVSYTYQkgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTliqnINALLKPTTGTVTVDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 549 LRKNIGYVSQ--NTFLFADTIKNNLLHGSNKYKSDEDIVKA------CQLAESLDFIQKFPDQfntmlekeganLSGGQG 620
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNyahrllMDLGFSRDVMSQSPFQ-----------MSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 621 QRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHD 698
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLkSLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPK 231
|
..
gi 488434717 699 EL 700
Cdd:PRK13646 232 EL 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
477-700 |
7.92e-24 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 100.20 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGY 555
Cdd:cd03224 1 LEVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFAD-TIKNNLLHGSnkYKSDEDIVKAcQLAESLDFiqkFPDqFNTMLEKEGANLSGGQGQRLSLARTFLKDPD 634
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGA--YARRRAKRKA-RLERVYEL---FPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 635 IYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
477-689 |
8.62e-24 |
|
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: 100.10 E-value: 8.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIG-KLLNRYYTASEG---NIMIDNYIIDDIDLSDLRKN 552
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKvhwSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 IGYVSQNTFLFADTIKNNLLHGS----NKYKSdedIVKACQLAESLDFIqKFPDQfnTMLEKEGANLSGGQGQRLSLART 628
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSpfnkQRYKA---VTDACSLQPDIDLL-PFGDQ--TEIGERGINLSGGQRQRICVARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 629 FLKDPDIYIFDEATSALDSLTENKIMEH--IDLLTQHGKTVIIISHKLSTIKNADNIYVLNEG 689
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
477-692 |
1.10e-23 |
|
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: 97.88 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGY 555
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQntflfadtiknnllhgsnkyksdedivkacqlaesldfiqkfpdqfntmlekeganLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03216 80 VYQ--------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIA 692
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
474-700 |
1.19e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.32 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 474 KNNIRIENVNFQY-----GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNY-IIDDIDLS 547
Cdd:PRK13633 2 NEMIKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 548 DLRKNIGYVSQN--TFLFADTIKNNLLHGSNKYKSDEDIVKAcQLAESLDFIQkfpdqfntMLE-KEGAN--LSGGQGQR 622
Cdd:PRK13633 82 DIRNKAGMVFQNpdNQIVATIVEEDVAFGPENLGIPPEEIRE-RVDESLKKVG--------MYEyRRHAPhlLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 623 LSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIkELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
477-696 |
1.29e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.36 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG----FRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEG----NIMIDNYIIDDIDLSD 548
Cdd:PRK13649 3 INLQNVSYTYQagtpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvDDTLITSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 549 LRKNIGYVSQ--NTFLFADTIKNNLLHGSNKYKSDEDivKACQLA-ESLDFIQKFPDQFntmlEKEGANLSGGQGQRLSL 625
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQE--EAEALArEKLALVGISESLF----EKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 626 ARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGT 696
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| Peptidase_C39F |
cd02425 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
3-132 |
1.35e-23 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239105 [Multi-domain] Cd Length: 126 Bit Score: 96.56 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 3 IKFIRQYDEKDCGPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKADSFDDLKQAQLPVMV 82
Cdd:cd02425 1 VKPILQNNQTECGLACYAMILNYFGYKVSLNELREKYELGRDGLSLSYLKQLLEEYGFKCKVYKISFKKNLYPLKLPVII 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488434717 83 HIINQqgydHYIIIEKIKNNTLYIVDPAKGKYKLSSTEFGKYWTNIAVLI 132
Cdd:cd02425 81 FWNNN----HFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYILTF 126
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
477-702 |
1.39e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.35 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG----FRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNI----MIDNYIIDDIDLSD 548
Cdd:PRK13643 2 IKFEKVNYTYQpnspFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 549 LRKNIGYVSQ--NTFLFADTIKNNLLHGSNKYK-SDEDIVKACqlAESLDFIqKFPDQFntmLEKEGANLSGGQGQRLSL 625
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGiPKEKAEKIA--AEKLEMV-GLADEF---WEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 626 ARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELIH 702
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
224-649 |
1.60e-23 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 106.92 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 224 ILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLY--MQSPLL 301
Cdd:TIGR01271 949 LVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVsvLQPYIF 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 302 LLITIIFIPCFIICSYTLRKPfEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEddrfyigtTKFNGIIENLLKLGrf 381
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTS-QQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQ--------SYFETLFHKALNLH-- 1097
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 382 sniqlTVNNFLKLT----------ISLVILWLGSYL--VMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAA 449
Cdd:TIGR01271 1098 -----TANWFLYLStlrwfqmridIIFVFFFIAVTFiaIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSV 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 450 RRIAEITDLETE-TELYTSKQPYTFKNNIRIEN-------------------VNFQYGFRSVvLKDINLNIKKGQKVAIV 509
Cdd:TIGR01271 1173 SRVFKFIDLPQEePRPSGGGGKYQLSTVLVIENphaqkcwpsggqmdvqgltAKYTEAGRAV-LQDLSFSVEGGQRVGLL 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 510 GESGSGKSTIGKLLNRYyTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNNLlhgsNKYK--SDEDIVKA 587
Cdd:TIGR01271 1252 GRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL----DPYEqwSDEEIWKV 1326
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 588 CQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLT 649
Cdd:TIGR01271 1327 AEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
477-700 |
4.10e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 100.09 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG----FRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM----IDNYIIDDIDLSD 548
Cdd:PRK13634 3 ITFQKVEHRYQyktpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigerVITAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 549 LRKNIGYVSQntF----LFADTIKNNLLHG-SNKYKSDEDivkACQLA-ESLDFIQKFPDqfntMLEKEGANLSGGQGQR 622
Cdd:PRK13634 83 LRKKVGIVFQ--FpehqLFEETVEKDICFGpMNFGVSEED---AKQKArEMIELVGLPEE----LLARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 623 LSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFyKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
477-700 |
4.71e-23 |
|
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: 97.96 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS-VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNiMIDNYIIDDIDLSDLRKNIGY 555
Cdd:cd03263 1 LQIRNLTKTYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT-AYINGYSIRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFAD-TIKNNL-----LHGSNKYKSDEDIVkacQLAESLDFIQKfpdqfntmLEKEGANLSGGQGQRLSLARTF 629
Cdd:cd03263 80 CPQFDALFDElTVREHLrfyarLKGLPKSEIKEEVE---LLLRVLGLTDK--------ANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 630 LKDPDIYIFDEATSALDSLTENKIMEHIdLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLI-LEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
477-701 |
5.55e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMI--DNYIIDDIDLSDLRKNIG 554
Cdd:PRK09493 2 IEFKNVSKHFG-PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdgLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFAD-TIKNNLLHGSNKYK--SDEDivkACQLAESLdfiqkfpdqfntmLEKEG---------ANLSGGQGQR 622
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFGPLRVRgaSKEE---AEKQAREL-------------LAKVGlaerahhypSELSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 623 LSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
163-452 |
5.65e-23 |
|
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: 99.92 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 163 LFIAFISLFI-NIVGIVGALYFKLLTDHI-IPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYF 240
Cdd:cd18778 1 LILTLLCALLsTLLGLVPPWLIRELVDLVtIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 241 YHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMII-IGAILLYMQS----------PLLLLITIIf 308
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVInDVANVERLIADGIPQGITNVLTLVgVAIILFSINPklalltlipiPFLALGAWL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 309 ipcfiicsYTLR-KPFEKYNQKVAekdAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENL----LKLGRFSN 383
Cdd:cd18778 160 --------YSKKvRPRYRKVREAL---GELNALLQDNLSGIREIQAFGREEEE----AKRFEALSRRYrkaqLRAMKLWA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 384 IQLTVNNFLKLTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18778 225 IFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
491-710 |
7.41e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 104.86 E-value: 7.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIdnyiiddidlsdlRKNIGYVSQNTFLFADTIKNN 570
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LLHGSNKYKSD-EDIVKACQLAESLdfiQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLT 649
Cdd:PTZ00243 741 ILFFDEEDAARlADAVRVSQLEADL---AQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 650 ENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELIHlNGIYKNL 710
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-TSLYATL 877
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
491-700 |
7.58e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.28 E-value: 7.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNI--------MIDNYIIDDIDLSDLRKNIGYVSQNTFL 562
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidTARSLSQQKGLIRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 563 FAD-TIKNNLLHGS---NKYKSDEDIVKACQLAESLDFIQK---FPDQfntmlekeganLSGGQGQRLSLARTFLKDPDI 635
Cdd:PRK11264 97 FPHrTVLENIIEGPvivKGEPKEEATARARELLAKVGLAGKetsYPRR-----------LSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
477-674 |
7.98e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.70 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-------L 549
Cdd:PRK14243 11 LRTENLNVYYG-SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYApdvdpveV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFADTIKNNLLHGS--NKYKSDEDIVKACQLAESLDFiqkfpDQFNTMLEKEGANLSGGQGQRLSLAR 627
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAYGAriNGYKGDMDELVERSLRQAALW-----DEVKDKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHgKTVIIISHKL 674
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNM 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
493-695 |
1.05e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 96.98 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIK---KGQKVAIVGESGSGKSTIGKLLNRYYTASEG----NIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFAD 565
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 566 -TIKNNLLHGSNKYKSDEDIVKACQLAESLDfIQKfpdqfntMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSA 644
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDRISVDELLDLLG-LDH-------LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488434717 645 LDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENG 695
Cdd:cd03297 162 LDRALRLQLLPELkQIKKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
161-438 |
1.41e-22 |
|
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: 98.68 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 161 KLLFIA--FISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRfQLILH-LSLKIDVNLMK 237
Cdd:cd18549 1 KKLFFLdlFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFV-TYWGHvMGARIETDMRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 238 DYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICS 316
Cdd:cd18549 80 DLFEHLQKLSFSFFDNNKTGQLMSRITnDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 317 YTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSED---DRFYIGTTKFNGIIENLLK-LGRFSniqlTVNNFL 392
Cdd:cd18549 160 IYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEyeiEKFDEGNDRFLESKKKAYKaMAYFF----SGMNFF 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488434717 393 KLTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINI 438
Cdd:cd18549 236 TNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNF 281
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
477-695 |
2.47e-22 |
|
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: 95.78 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDlrKNIGYV 556
Cdd:cd03301 1 VELENVTKRFGNV-TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLLHG--SNKYKSDEDIVKACQLAESLdfiqkfpdQFNTMLEKEGANLSGGQGQRLSLARTFLKDP 633
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGlkLRKVPKDEIDERVREVAELL--------QIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 634 DIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISH-KLSTIKNADNIYVLNEGQIAENG 695
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELkRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
476-701 |
5.81e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.21 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQYGfrsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDlRKnigy 555
Cdd:COG3840 1 MLRLDDLTYRYG---DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VS---QNTFLFAD-TIKNNL---LHGSNKYkSDEDIVKACQLAESL---DFIQKFPDQfntmlekeganLSGGQGQRLSL 625
Cdd:COG3840 73 VSmlfQENNLFPHlTVAQNIglgLRPGLKL-TAEQRAQVEQALERVglaGLLDRLPGQ-----------LSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 626 ARTFLKDPDIYIFDEATSALD-SLTEnkimEHIDLLTQ----HGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDE 699
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpALRQ----EMLDLVDElcreRGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
..
gi 488434717 700 LI 701
Cdd:COG3840 217 LL 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
479-691 |
6.01e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.90 E-value: 6.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 479 IENVNFQYGFRSVvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidLSDLRKNIGYVSQ 558
Cdd:PRK11247 15 LNAVSKRYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP-----LAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 559 NTFL--FADTIKNNLLHGSNKYKSD-EDIVKACQLAeslDFIQKFPdqfntmlekegANLSGGQGQRLSLARTFLKDPDI 635
Cdd:PRK11247 89 DARLlpWKKVIDNVGLGLKGQWRDAaLQALAAVGLA---DRANEWP-----------AALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 636 YIFDEATSALDSLTENKIMEHID-LLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQI 691
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIEsLWQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
475-695 |
7.09e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.96 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 475 NNIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIG 554
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQ--NTFLFADTIKNNLLHGSNKYKSDEDIVKAcQLAESLDFI--QKFPDqfntmleKEGANLSGGQGQRLSLARTFL 630
Cdd:PRK13647 83 LVFQdpDDQVFSSTVWDDVAFGPVNMGLDKDEVER-RVEEALKAVrmWDFRD-------KPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 631 KDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQ-IAENG 695
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRvLAEGD 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
476-695 |
1.06e-21 |
|
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: 93.38 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTigkLLN-----RYYTASEGnimIDNYIIDDIDLSDLR 550
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKST---LLNalagrRTGLGVSG---EVLINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 551 KNIGYVSQNTFLFAD-TIKnnllhgsnkyksdedivkacqlaESLDFIQKFpdqfntmlekegANLSGGQGQRLSLARTF 629
Cdd:cd03213 82 KIIGYVPQDDILHPTlTVR-----------------------ETLMFAAKL------------RGLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 630 LKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLST--IKNADNIYVLNEGQIAENG 695
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
477-700 |
1.66e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.16 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVV--LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIG 554
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQ---NTFLFAdTIKNNLLHG-SNKYKSDEDIVKacQLAESLDFIQKFpdQFNTmleKEGANLSGGQGQRLSLARTFL 630
Cdd:PRK13642 85 MVFQnpdNQFVGA-TVEDDVAFGmENQGIPREEMIK--RVDEALLAVNML--DFKT---REPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 631 KDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIhEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
477-701 |
1.81e-21 |
|
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: 93.94 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfrSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDidLSDLRKNIGYV 556
Cdd:cd03299 1 LKVENLSKDWK--EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLLHGSNKYKSD--EDIVKACQLAESLDFiqkfpdqfNTMLEKEGANLSGGQGQRLSLARTFLKDP 633
Cdd:cd03299 77 PQNYALFPHmTVYKNIAYGLKKRKVDkkEIERKVLEIAEMLGI--------DHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 634 DIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELI 701
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELkKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
477-696 |
1.82e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.41 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVN--FQYGFRSVV-LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLR 550
Cdd:PRK11153 2 IELKNISkvFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 551 KNIGYVSQNtflFadtiknNLLHGSNKY-----------KSDEDIVKacQLAESLDFI------QKFPdqfntmlekegA 613
Cdd:PRK11153 82 RQIGMIFQH---F------NLLSSRTVFdnvalplelagTPKAEIKA--RVTELLELVglsdkaDRYP-----------A 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 614 NLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMehiDLLTQ----HGKTVIIISHKLSTIKN-ADNIYVLNE 688
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL---ELLKDinreLGLTIVLITHEMDVVKRiCDRVAVIDA 216
|
....*...
gi 488434717 689 GQIAENGT 696
Cdd:PRK11153 217 GRLVEQGT 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
477-695 |
2.26e-21 |
|
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: 93.20 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG---FRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLsDLRKNI 553
Cdd:cd03266 2 ITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD-TIKNNL-----LHGsnkYKSDEDIVKACQLAESLDFiqkfpdqfNTMLEKEGANLSGGQGQRLSLAR 627
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLeyfagLYG---LKGDELTARLEELADRLGM--------EELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENG 695
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
477-700 |
3.93e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.99 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMI--DNYIIDDIDLSDLRKNIG 554
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgEPIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNT--FLFADTIKNNLLHGSNKYKSDEDIVKAcQLAESL------DFIQKFPDqfntmlekegaNLSGGQGQRLSLA 626
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEK-RVKEALkavgmeGFENKPPH-----------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 627 RTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
162-452 |
4.13e-21 |
|
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: 94.21 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18586 4 FVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNffdTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICS----Y 317
Cdd:cd18586 84 AVLELPLE---SRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAwlnhR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 318 TLRKPFEKYNQKVAEKDAelssYLIESFDGSNTIKSYQSED---DRFYigtTKFNGIIENLLKLGRFSNIQLTVNNFLKL 394
Cdd:cd18586 161 ATRKPLGEANEAQAARDA----LAAETLRNAETIKALGMLGnlrRRWE---ARHAETLELQIRASDLAGAISAIGKTLRM 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 395 TISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18586 234 ALQSLILGVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYERL 291
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
477-690 |
5.48e-21 |
|
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: 92.11 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENV--NF----QYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLS--- 547
Cdd:COG4778 5 LEVENLskTFtlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 548 ----DLRKN-IGYVSQntFLFA-------DTIKNNLLH-GSNKyksDEDIVKACQLAESLDFIQK----FPdqfntmlek 610
Cdd:COG4778 85 reilALRRRtIGYVSQ--FLRViprvsalDVVAEPLLErGVDR---EEARARARELLARLNLPERlwdlPP--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 611 egANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEG 689
Cdd:COG4778 151 --ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
.
gi 488434717 690 Q 690
Cdd:COG4778 229 S 229
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
162-452 |
5.91e-21 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 93.70 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLfiniVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18576 2 LILLLLSSA----IGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLR 320
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSnDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 321 KPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSY---QSEDDRFyigTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTIS 397
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFtreDYEIERY---RKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 398 LVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18576 235 VAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
477-672 |
7.18e-21 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 91.39 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKST----IGKLLnryyTASEGNIMIDNYIIDDIDlSDLRKN 552
Cdd:COG4133 3 LEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLL----PPSAGEVLWNGEPIRDAR-EDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 IGYVSQNTFLFAD-TIKNNL-----LHGSNKykSDEDIVKACQ---LAESLDfiqkfpdqfntmleKEGANLSGGQGQRL 623
Cdd:COG4133 77 LAYLGHADGLKPElTVRENLrfwaaLYGLRA--DREAIDEALEavgLAGLAD--------------LPVRQLSAGQKRRV 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488434717 624 SLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISH 672
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| C39G |
COG3271 |
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ... |
6-132 |
1.06e-20 |
|
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442502 [Multi-domain] Cd Length: 179 Bit Score: 90.05 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 6 IRQYDEKDCGPTCLA-MISQFYGKRVS----IPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKADsFDDLKQAQLPV 80
Cdd:COG3271 46 VRQQYDYSCGAAALAtLLNYHYGRPVSeaevLEGMLTHGDQRRRGFSLLDMKRYLEALGLRADGYRLT-LDDLAQLGIPA 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488434717 81 MVHIiNQQGYDHYIIIEKIKNNTLYIVDPAKGKYKLSSTEFGKYWTNIAVLI 132
Cdd:COG3271 125 IVLI-NLGGYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVLFV 175
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
477-700 |
1.66e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.67 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG-FRsvVLKDINLNIKKGQKVAIVGESGSGKSTI------------GK-LLN--RYYTAsegnimidnyi 540
Cdd:COG1118 3 IEVRNISKRFGsFT--LLDDVSLEIASGELVALLGPSGSGKTTLlriiagletpdsGRiVLNgrDLFTN----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 541 iddidLSDLRKNIGYVSQNTFLFAD-TIKNNLLHGSNKYKSDEDIVKAcQLAESLDFIQ------KFPDQfntmlekega 613
Cdd:COG1118 70 -----LPPRERRVGFVFQHYALFPHmTVAENIAFGLRVRPPSKAEIRA-RVEELLELVQlegladRYPSQ---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 614 nLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEH-IDLLTQHGKTVIIISHklstikN-------ADNIYV 685
Cdd:COG1118 134 -LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWlRRLHDELGGTTVFVTH------DqeealelADRVVV 206
|
250
....*....|....*
gi 488434717 686 LNEGQIAENGTHDEL 700
Cdd:COG1118 207 MNQGRIEQVGTPDEV 221
|
|
| Peptidase_C39G |
cd02423 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
6-132 |
1.83e-20 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature.
Pssm-ID: 239103 [Multi-domain] Cd Length: 129 Bit Score: 87.71 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 6 IRQYDEKDCGPTCLA-MISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKADsFDDLKQAQLPVMVhI 84
Cdd:cd02423 4 VRQSYDFSCGPAALAtLLRYYGGINITEQEVLKLMLIRSEGFSMLDLKRYAEALGLKANGYRLN-LDKLNALQIPVIV-L 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488434717 85 INQQGYDHYIIIEKIKNNTLYIVDPAKGKYKLSSTEFGKYWTNIAVLI 132
Cdd:cd02423 82 VNNGGYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNALFV 129
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
161-420 |
1.90e-20 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 92.51 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 161 KLLFIAFISLFInivGIVGALYFKLLT----DHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLM 236
Cdd:cd18571 2 KLILQLLLGLLL---GSLLQLIFPFLTqsivDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 237 KDYFYHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIII-GAILLYMQSPLLLLITIIFIPCFIIC 315
Cdd:cd18571 79 SDFLIKLMRLPISFFDTKMTGDILQRINDHSRIESFLTSSSLSILFSLLNLIVfSIVLAYYNLTIFLIFLIGSVLYILWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 316 SYTLRKPfEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYigttKFNGIIENLLKLG----RFSNIQLTVNNF 391
Cdd:cd18571 159 LLFLKKR-KKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRW----EWERIQAKLFKINikslKLDQYQQIGALF 233
|
250 260
....*....|....*....|....*....
gi 488434717 392 LKLTISLVILWLGSYLVMTDSMTLGSLLA 420
Cdd:cd18571 234 INQLKNILITFLAAKLVIDGEITLGMMLA 262
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
477-700 |
2.75e-20 |
|
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: 90.48 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDlrKNIGYV 556
Cdd:cd03296 3 IEVRNVSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLLHG----SNKYKSDEDIVKAcQLAESLDFIQ------KFPDQfntmlekeganLSGGQGQRLSL 625
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGlrvkPRSERPPEAEIRA-KVHELLKLVQldwladRYPAQ-----------LSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 626 ARTFLKDPDIYIFDEATSALDSltenKIMEHI-----DLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDE 699
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDA----KVRKELrrwlrRLHDELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDE 223
|
.
gi 488434717 700 L 700
Cdd:cd03296 224 V 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
477-700 |
3.82e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.44 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEG---------Nimidnyiiddidls 547
Cdd:COG3839 4 LELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGeiliggrdvT-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 548 DL---RKNIGYVSQNTFLFAD-TIKNNLLHG--SNKYKSDE------DIVKACQLAESLDfiqKFPDQfntmlekeganL 615
Cdd:COG3839 69 DLppkDRNIAMVFQSYALYPHmTVYENIAFPlkLRKVPKAEidrrvrEAAELLGLEDLLD---RKPKQ-----------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 616 SGGQGQRLSLARTFLKDPDIYIFDEATSALD-SLTENKIMEHIDLLTQHGKTVIIISHKLS---TIknADNIYVLNEGQI 691
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDaKLRVEMRAEIKRLHRRLGTTTIYVTHDQVeamTL--ADRIAVMNDGRI 212
|
....*....
gi 488434717 692 AENGTHDEL 700
Cdd:COG3839 213 QQVGTPEEL 221
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
163-452 |
5.32e-20 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 90.93 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 163 LFIAFISLFI-NIVGIVGALYFKLLTDHIIPSNV-LKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYF 240
Cdd:cd18541 1 YLLGILFLILvDLLQLLIPRIIGRAIDALTAGTLtASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 241 YHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLlVDTFMIIIgAILLYM--QSPLLLLITIIFIPCFIICSY 317
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATnDLNAVRMALGPGILYL-VDALFLGV-LVLVMMftISPKLTLIALLPLPLLALLVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 318 TLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKlgrfSNIQLT-VNNFLKLTI 396
Cdd:cd18541 159 RLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAE----IERFDKLNEEYVE----KNLRLArVDALFFPLI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 397 SL-------VILWLGSYLVMTDSMTLGSLLAFNAltiyYLD----PIE---RLINIqptLQSSFVAARRI 452
Cdd:cd18541 231 GLliglsflIVLWYGGRLVIRGTITLGDLVAFNS----YLGmliwPMMalgWVINL---IQRGAASLKRI 293
|
|
| Peptidase_C39E |
cd02424 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
3-130 |
5.93e-20 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family, which contains Colicin V perocessing peptidase.
Pssm-ID: 239104 [Multi-domain] Cd Length: 129 Bit Score: 86.24 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 3 IKFIRQYDEKDCGPTCLAMI-SQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKADSFDDLKQAQlpVM 81
Cdd:cd02424 1 MKIIKQTDLNDCGIAVIQMLyNHYYKKKYDLNELKIKANLKKNGLSIYDLENLAKKFGLETESYQGSFLEFLELKN--KF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488434717 82 VHIINQQGYDHYIIIEKIKNNTLYIVDPAKGKYKLSSTEFGKYWTNIAV 130
Cdd:cd02424 79 IILLKSNGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNIII 127
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
477-700 |
6.21e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.08 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGnimidNYIIDDIDLSDL---RKNI 553
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSG-----RILLDGRDVTGLppeKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD-TIKNNL---LHGSNKYKSD-----EDIVKACQLAeslDFIQKFPDQfntmlekeganLSGGQGQRLS 624
Cdd:COG3842 80 GMVFQDYALFPHlTVAENVafgLRMRGVPKAEirarvAELLELVGLE---GLADRYPHQ-----------LSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 625 LARTFLKDPDIYIFDEATSALDslteNKIMEHI-----DLLTQHGKTVIIISHKLS---TIknADNIYVLNEGQIAENGT 696
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALD----AKLREEMreelrRLQRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
....
gi 488434717 697 HDEL 700
Cdd:COG3842 220 PEEI 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
490-702 |
7.69e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.40 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 490 SVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL----RKNIGYVSQNTFLFAD 565
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 566 -TIKNNL-----LHGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSLARTFLKDPDIYIFD 639
Cdd:PRK10070 121 mTVLDNTafgmeLAGINAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 640 EATSALDSLTENKIM-EHIDLLTQHGKTVIIISHKL-STIKNADNIYVLNEGQIAENGTHDELIH 702
Cdd:PRK10070 190 EAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
166-452 |
7.88e-20 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 90.31 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 166 AFISLFINIVG-IVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVL 244
Cdd:cd18557 1 GLLFLLISSAAqLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 245 HLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRKPF 323
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSsDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 324 EKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDdrfyIGTTKFNGIIENLLKLGRFSNIQLT----VNNFLKLTISLV 399
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEE----KEIRRYSEALDRSYRLARKKALANAlfqgITSLLIYLSLLL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488434717 400 ILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18557 237 VLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
474-700 |
1.19e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.26 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 474 KNNIRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD----- 548
Cdd:PRK10619 3 ENKLNVIDLHKRYG-EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 549 --------LRKNIGYVSQNTFLFAD-TIKNNLLH------GSNKYKSDEDIVKACQLAESLDFIQ-KFPdqfntmlekeg 612
Cdd:PRK10619 82 adknqlrlLRTRLTMVFQHFNLWSHmTVLENVMEapiqvlGLSKQEARERAVKYLAKVGIDERAQgKYP----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 613 ANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADN-IYVLNEGQI 691
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQGKI 230
|
....*....
gi 488434717 692 AENGTHDEL 700
Cdd:PRK10619 231 EEEGAPEQL 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
477-672 |
1.30e-19 |
|
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: 87.85 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLRKNI 553
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD-TIKNNLLHGSN-KYKSDEDIVKacQLAESLDFIqKFPDQFNTMlekeGANLSGGQGQRLSLARTFLK 631
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALEvTGVPPREIRK--RVPAALELV-GLSHKHRAL----PAELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488434717 632 DPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISH 672
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
492-691 |
1.85e-19 |
|
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: 89.14 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTI-GKLLNRYYTasEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFADTIKNN 570
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLNT--EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LlhGSNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTe 650
Cdd:cd03289 97 L--DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488434717 651 NKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQI 691
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
477-700 |
2.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 88.73 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG----FRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM----IDNYIIDDIDLSD 548
Cdd:PRK13641 3 IKFENVDYIYSpgtpMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 549 LRKNIGYVSQ--NTFLFADTIKNNLLHGSNKYKSDEDIVKacqlAESLDFIQK--FPDQfntMLEKEGANLSGGQGQRLS 624
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAK----EKALKWLKKvgLSED---LISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 625 LARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
477-690 |
2.89e-19 |
|
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: 84.81 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidlsdlrkNIGYV 556
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQntflfadtiknnllhgsnkyksdedivkacqlaesldfiqkfpdqfntmlekeganLSGGQGQRLSLARTFLKDPDIY 636
Cdd:cd03221 69 EQ--------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 637 IFDEATSALDSLTenkIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQ 690
Cdd:cd03221 93 LLDEPTNHLDLES---IEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
477-695 |
4.49e-19 |
|
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: 86.12 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGniMIDNYIIDDIDLSDLRKNIG-Y 555
Cdd:cd03268 1 LKTNDLTKTYGKKRV-LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG--EITFDGKSYQKNIEALRRIGaL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIKNNLLHGSNKYKSDEDIVKACQLAESLDFIQKfpdqfntmleKEGANLSGGQGQRLSLARTFLKDPDI 635
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAK----------KKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENG 695
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
488-702 |
4.72e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 91.28 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 488 FRSVV-----LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYyTASEGNIM---IDNYIIDDIDLSDLRKNIGYVSQN 559
Cdd:COG4172 292 FRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRfdgQDLDGLSRRALRPLRRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 560 TF-------LFADTIKNNL-LH--GSNKYKSDEDIVKAcqLAE---SLDFIQKFPDQFntmlekeganlSGGQGQRLSLA 626
Cdd:COG4172 371 PFgslsprmTVGQIIAEGLrVHgpGLSAAERRARVAEA--LEEvglDPAARHRYPHEF-----------SGGQRQRIAIA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 627 RTFLKDPDIYIFDEATSALDSLTENKImehIDLL----TQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELI 701
Cdd:COG4172 438 RALILEPKLLVLDEPTSALDVSVQAQI---LDLLrdlqREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
.
gi 488434717 702 H 702
Cdd:COG4172 515 D 515
|
|
| Peptidase_C39C |
cd02419 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
6-130 |
5.31e-19 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239100 [Multi-domain] Cd Length: 127 Bit Score: 83.46 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 6 IRQYDEKDCGPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKADsFDDLKQAQLPVMVHii 85
Cdd:cd02419 4 ILQTEAAECGLACLAMIASYHGHHVDLASLRQRFPVSLKGATLADLIDIAQQLGLSTRALRLD-LEELGQLKLPCILH-- 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488434717 86 nqQGYDHYIIIEKIKNNTLYIVDPAKGKYKLSSTEFGKYWTNIAV 130
Cdd:cd02419 81 --WDMNHFVVLKKVSRRRIVIHDPALGKRKLSLEEASRHFTGVAL 123
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
477-686 |
5.98e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 86.31 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:PRK10247 8 LQLQNVGYLAGDA-KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFADTIKNNLL--HGSNKYKSDEDIVkacqlaesLDFIQKF--PDqfnTMLEKEGANLSGGQGQRLSLARTFLKD 632
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIfpWQIRNQQPDPAIF--------LDDLERFalPD---TILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 633 PDIYIFDEATSALDSLTENKIMEHID-LLTQHGKTVIIISHKLSTIKNADNIYVL 686
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHrYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
479-672 |
9.48e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 9.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 479 IENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDnyiiddidlSDLRknIGYVSQ 558
Cdd:COG0488 1 LENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 559 NTFLFAD-TIKNNLLHGSNKYK---------------SDEDIVKACQLAESLDFIQ---------------KFPDqfnTM 607
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGDAELRaleaeleeleaklaePDEDLERLAELQEEFEALGgweaearaeeilsglGFPE---ED 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 608 LEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDsltenkiMEHI----DLLTQHGKTVIIISH 672
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIewleEFLKNYPGTVLVVSH 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
477-700 |
9.74e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNT--FLFADTIKNNLLHGSNKYKSDEDIVKAcQLAESLDFIqkfpdQFNTMLEKEGANLSGGQGQRLSLARTFLKDPD 634
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGPINLGLDEETVAH-RVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 635 IYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLnDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
471-700 |
1.00e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.37 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 471 YTFKNNIRIENVNFQYG----FRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASE-----GNIMIDNYII 541
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAkktpFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETgqtivGDYAIPANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 542 DDIDLSDLRKNIGYVSQ--NTFLFADTIKNNLLHGSNKYKSD-EDIVKacQLAESLDFIQkFPDQFntmLEKEGANLSGG 618
Cdd:PRK13645 81 KIKEVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENkQEAYK--KVPELLKLVQ-LPEDY---VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 619 QGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQ-HGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGT 696
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
....
gi 488434717 697 HDEL 700
Cdd:PRK13645 235 PFEI 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
477-700 |
1.52e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDN--YIIDDIDLSDLRKNIG 554
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQ--NTFLFADTIKNNLLHGSNKYKSDEDIVKacqlaESLDFIQKfPDQFNTMLEKEGANLSGGQGQRLSLARTFLKD 632
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGAVNLKLPEDEVR-----KRVDNALK-RTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 633 PDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIK-NADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
10-131 |
1.55e-18 |
|
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families.
Pssm-ID: 239073 [Multi-domain] Cd Length: 122 Bit Score: 82.05 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 10 DEKDCGPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKADSFdDLKQAQLPVMVHiinqQG 89
Cdd:cd02259 3 GPLDCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLA-ALSRLQLPALLL----WK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488434717 90 YDHYIIIEKIKNNTLYIVDP-AKGKYKLSSTEFGKYWTNIAVL 131
Cdd:cd02259 78 QGHFVILYGADKGQVLIADPlEEGPVTLSESELEERWTGHWVL 120
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
491-703 |
1.62e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.52 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimidnyiiddidlsdLRKNiGYVS------------- 557
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR---------------VEVN-GRVSallelgagfhpel 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 ---QNTFLFAdtiknnLLHGsnkyKSDEDIvkacqlAESLDFIQKF---PDQFNTMLEkegaNLSGGQGQRL--SLArTF 629
Cdd:COG1134 104 tgrENIYLNG------RLLG----LSRKEI------DEKFDEIVEFaelGDFIDQPVK----TYSSGMRARLafAVA-TA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 630 LkDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELIHL 703
Cdd:COG1134 163 V-DPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
476-700 |
1.94e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDlrKNIGY 555
Cdd:PRK10851 2 SIEIANIKKSFG-RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFAD-TIKNNLLHG----SNKYKSDEDIVKAcQLAESLDFIQ------KFPDQfntmlekeganLSGGQGQRLS 624
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlPRRERPNAAAIKA-KVTQLLEMVQlahladRYPAQ-----------LSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 625 LARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGK-TVIIISH-KLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
477-695 |
1.98e-18 |
|
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: 84.47 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVvlkDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDlrKNIGYV 556
Cdd:cd03298 1 VRLDKIRFSYGEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLLHGSNK----YKSDEDIVKACQLAESLD-FIQKFPDQfntmlekeganLSGGQGQRLSLARTFL 630
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGLSPglklTAEDRQAIEVALARVGLAgLEKRLPGE-----------LSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 631 KDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENG 695
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVlDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
491-714 |
2.37e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTI-----GKLLNRYYTASEGNIMIDNYIIDDIDLSD-----------LRKNIG 554
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLvthfnGLIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQ--NTFLFADTIKNNLLHGS-----NKYKSDEdivKACQLAESLDFIQKFpdqfntmLEKEGANLSGGQGQRLSLAR 627
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGPvalgvKKSEAKK---LAKFYLNKMGLDDSY-------LERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTH--------- 697
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPyeiftdqhi 269
|
250 260 270
....*....|....*....|....*....|..
gi 488434717 698 ---------------DELIHLNGIYKNLWQLQ 714
Cdd:PRK13631 270 instsiqvprviqviNDLIKKDPKYKKLYQKQ 301
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
183-452 |
2.67e-18 |
|
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: 86.41 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 183 FKLLTDHIIPSNVLKNLHIISF---------------GILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVLHLP 247
Cdd:cd18564 22 LKVVIDDVLGDKPLPGLLGLAPllgpdplallllaaaALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 248 MNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFmIIIG--AILLYMQ----------SPllllitiifipCFII 314
Cdd:cd18564 102 LSFHDRRRTGDLLSRLTgDVGAIQDLLVSGVLPLLTNLL-TLVGmlGVMFWLDwqlalialavAP-----------LLLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 315 CSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSY---QSEDDRFYIGTTKfngiieNL---LKLGRFS-NIQLT 387
Cdd:cd18564 170 AARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFgreEHEERRFARENRK------SLragLRAARLQaLLSPV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 388 VnNFLKLTISLVILWLGSYLVMTDSMTLGSLLAFnaltIYYL----DPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18564 244 V-DVLVAVGTALVLWFGAWLVLAGRLTPGDLLVF----LAYLknlyKPVRDLAKLTGRIAKASASAERV 307
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
477-700 |
3.80e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSV----VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEG-------------NIMIDNY 539
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 540 IIDDIDLS-----------DLRKNIGYVSQntF----LFADTIKNNLLHGSNKYKSDEDivKACQLAESLDFIQKFPDQF 604
Cdd:PRK13651 83 VLEKLVIQktrfkkikkikEIRRRVGVVFQ--FaeyqLFEQTIEKDIIFGPVSMGVSKE--EAKKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 605 ntmLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKL-STIKNADNI 683
Cdd:PRK13651 159 ---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRT 235
|
250
....*....|....*...
gi 488434717 684 YVLNEGQIAENG-THDEL 700
Cdd:PRK13651 236 IFFKDGKIIKDGdTYDIL 253
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
477-672 |
4.17e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 82.20 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNyiiddidlsdlRKNIGYV 556
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFADTIKNNLLhgsnkYKSDEdivkacqlaesldfiqkfpdqfntmlekegaNLSGGQGQRLSLARTFLKDPDIY 636
Cdd:cd03223 70 PQRPYLPLGTLREQLI-----YPWDD-------------------------------VLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*.
gi 488434717 637 IFDEATSALDSLTENKIMEhidLLTQHGKTVIIISH 672
Cdd:cd03223 114 FLDEATSALDEESEDRLYQ---LLKELGITVISVGH 146
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
162-421 |
4.96e-18 |
|
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: 85.23 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVgalyFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18575 2 LIALLIAAAATLALGQG----LRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLR 320
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTtDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 321 KPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKLGRFSNIQ---LTVnnflkLTIS 397
Cdd:cd18575 158 RRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAE----RQRFATAVEAAFAAALRRIRAralLTA-----LVIF 228
|
250 260 270
....*....|....*....|....*....|
gi 488434717 398 LV------ILWLGSYLVMTDSMTLGSLLAF 421
Cdd:cd18575 229 LVfgaivfVLWLGAHDVLAGRMSAGELSQF 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
477-699 |
5.27e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimidnyiiddidlsdlRK----- 551
Cdd:COG0488 316 LELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT----------------VKlgetv 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 552 NIGYVSQNTFLF--ADTIKNNLLHGSnkykSDEDIVKACQLAESLDFIqkfPDQfntmLEKEGANLSGGQGQRLSLARTF 629
Cdd:COG0488 379 KIGYFDQHQEELdpDKTVLDELRDGA----PGGTEQEVRGYLGRFLFS---GDD----AFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 630 LKDPDIYIFDEATSALD--SLTenkIMEhiDLLTQHGKTVIIISHK---LSTIknADNIYVLNEGQIAE-NGTHDE 699
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDieTLE---ALE--EALDDFPGTVLLVSHDryfLDRV--ATRILEFEDGGVREyPGGYDD 516
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
476-702 |
7.24e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDlrKNIGY 555
Cdd:PRK11000 3 SVTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLF-----ADTIKNNL-LHGSNKYKSDEdivKACQLAESLdfiqkfpdQFNTMLEKEGANLSGGQGQRLSLARTF 629
Cdd:PRK11000 80 VFQSYALYphlsvAENMSFGLkLAGAKKEEINQ---RVNQVAEVL--------QLAHLLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 630 LKDPDIYIFDEATSALDSLTENKIMEHIDLLTQH-GKTVIIISH-KLSTIKNADNIYVLNEGQIAENGTHDELIH 702
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
477-700 |
7.52e-18 |
|
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: 82.80 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG-FRSVvlKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDlSDLRKNIGY 555
Cdd:cd03265 1 IEVENLVKKYGdFEAV--RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNtfLFADTI----KNNLLHGS-NKYKSDEdivKACQLAESLDFIQ--KFPDqfntmleKEGANLSGGQGQRLSLART 628
Cdd:cd03265 78 VFQD--LSVDDEltgwENLYIHARlYGVPGAE---RRERIDELLDFVGllEAAD-------RLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 629 FLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDEL 700
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIeKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
165-425 |
1.61e-17 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB 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 LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 83.64 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 165 IAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVL 244
Cdd:cd18587 7 VLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSRLFERVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 245 HLPMNFfDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRKPFE 324
Cdd:cd18587 87 GLRLEA-RPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 325 KYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEdDRF------YIGTTKFNGiienlLKLGRFSNIQLTVNNFLKLTISL 398
Cdd:cd18587 166 RLVEESMRESAQKNALLVESLSGLETIKALGAE-GRMqrrweeAVAALARSS-----LKSRLLSSSATNFAQFVQQLVTV 239
|
250 260
....*....|....*....|....*..
gi 488434717 399 VILWLGSYLVMTDSMTLGSLLAFNALT 425
Cdd:cd18587 240 AIVIVGVYLISDGELTMGGLIACVILS 266
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
477-691 |
1.75e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 81.56 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDidlsDLRKNIGYV 556
Cdd:cd03269 1 LEVENVTKRFG-RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLLH-GSNKYKSDEDIvkacqLAESLDFIQKF--PDQFNTMLEKeganLSGGQGQRLSLARTFLKD 632
Cdd:cd03269 76 PEERGLYPKmKVIDQLVYlAQLKGLKKEEA-----RRRIDEWLERLelSEYANKRVEE----LSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 633 PDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI 691
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
367-690 |
1.95e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 367 KFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVILWLGSYLVMTDSMTLGSL----LAFNALT---IYYLDPIERLINIQ 439
Cdd:COG4178 250 RFDAVIANWRRLIRRQRNLTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLmqaaSAFGQVQgalSWFVDNYQSLAEWR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 440 PTLQ--SSFVAArrIAEITDLETETELYTSKQPytfkNNIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKS 517
Cdd:COG4178 330 ATVDrlAGFEEA--LEAADALPEAASRIETSED----GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKS 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 518 TIGKLLNRYYTASEGNIMIDNyiiddidlsdlRKNIGYVSQNTFLFADTIKNNLL--HGSNKYkSDEDIVKA---CQLae 592
Cdd:COG4178 404 TLLRAIAGLWPYGSGRIARPA-----------GARVLFLPQRPYLPLGTLREALLypATAEAF-SDAELREAleaVGL-- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 593 sldfiqkfpDQFNTMLEKE---GANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEhidLLTQH--GKTV 667
Cdd:COG4178 470 ---------GHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ---LLREElpGTTV 537
|
330 340
....*....|....*....|...
gi 488434717 668 IIISHKLSTIKNADNIYVLNEGQ 690
Cdd:COG4178 538 ISVGHRSTLAAFHDRVLELTGDG 560
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
495-700 |
2.24e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.01 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 495 DINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLRKNIGYVSQNTF--L-----FA 564
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgQDITGLSGRELRPLRRRMQMVFQDPYasLnprmtVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 565 DTIKNNLL-HGSNKYKSDEDIVkacqlAESLD-------FIQKFPDQFntmlekeganlSGGQGQRLSLARTFLKDPDIY 636
Cdd:COG4608 116 DIIAEPLRiHGLASKAERRERV-----AELLElvglrpeHADRYPHEF-----------SGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 637 IFDEATSALD--------SLTEnkimehiDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:COG4608 180 VCDEPVSALDvsiqaqvlNLLE-------DLQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
477-699 |
2.85e-17 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 81.71 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYG-FrsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGnimidNYIIDDIDLSDL------ 549
Cdd:cd03219 1 LEVRGLTKRFGgL--VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSG-----SVLFDGEDITGLppheia 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFAD-TIKNNLL-----------HGSNKYKSDEDIVKacQLAESLDF--IQKFPDQfntmlekEGANL 615
Cdd:cd03219 74 RLGIGRTFQIPRLFPElTVLENVMvaaqartgsglLLARARREEREARE--RAEELLERvgLADLADR-------PAGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 616 SGGQGQRLSLARTFLKDPDIYIFDEATSALdSLTE-NKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQ-IA 692
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGL-NPEEtEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRvIA 223
|
....*..
gi 488434717 693 EnGTHDE 699
Cdd:cd03219 224 E-GTPDE 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
477-700 |
3.60e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVlKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTAS-----EGNIM--IDNYIIDDIDLSDL 549
Cdd:PRK14258 8 IKVNNLSFYYDTQKIL-EGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEffNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFADTIKNNLLHGSN------KYKSDEDIVKACQLAESLDFIQKfpdqfntMLEKEGANLSGGQGQRL 623
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpKLEIDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 624 SLARTFLKDPDIYIFDEATSALDSLTENKImEHI--DLLTQHGKTVIIISHKLSTIKNADNIYVL---NE---GQIAENG 695
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLiqSLRLRSELTMVIVSHNLHQVSRLSDFTAFfkgNEnriGQLVEFG 238
|
....*
gi 488434717 696 THDEL 700
Cdd:PRK14258 239 LTKKI 243
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
477-701 |
4.57e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 81.70 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:COG4559 2 LEAENLSVRLGGRTL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNT-----FLFADTIKNNLLHGSNKYKSDEDIVKAC-QLAESLDFIQKFpdqFNTmlekeganLSGGQGQRLSLARTF- 629
Cdd:COG4559 81 PQHSslafpFTVEEVVALGRAPHGSSAAQDRQIVREAlALVGLAHLAGRS---YQT--------LSGGEQQRVQLARVLa 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 630 -LKDPDI----YIF-DEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLstikN-----ADNIYVLNEGQIAENGTHD 698
Cdd:COG4559 150 qLWEPVDggprWLFlDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDL----NlaaqyADRILLLHQGRLVAQGTPE 225
|
...
gi 488434717 699 ELI 701
Cdd:COG4559 226 EVL 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
394-700 |
7.70e-17 |
|
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: 84.08 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 394 LTISLVILWLGSYLvmtdSMTLGSLLAFnALTIYYL-DPIERLINIQPTLQSSFVAARRIAEI----TDLETETELYTSK 468
Cdd:COG4615 245 ALIGLILFLLPALG----WADPAVLSGF-VLVLLFLrGPLSQLVGALPTLSRANVALRKIEELelalAAAEPAAADAAAP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 469 QPYTFKNNIRIENVNFQY-------GFRsvvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYII 541
Cdd:COG4615 320 PAPADFQTLELRGVTYRYpgedgdeGFT---LGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 542 DDIDLSDLRKNIGYVSQNTFLFADtiknnlLHGSNKYKSDEDI---VKACQLAESLDFIQkfpDQFNTMlekegaNLSGG 618
Cdd:COG4615 397 TADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPARArelLERLELDHKVSVED---GRFSTT------DLSQG 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 619 QGQRLSLARTFLKDPDIYIFDEATSALDS----------LTEnkimehidlLTQHGKTVIIISHKLSTIKNADNIYVLNE 688
Cdd:COG4615 462 QRKRLALLVALLEDRPILVFDEWAADQDPefrrvfytelLPE---------LKARGKTVIAISHDDRYFDLADRVLKMDY 532
|
330
....*....|..
gi 488434717 689 GQIAENGTHDEL 700
Cdd:COG4615 533 GKLVELTGPAAL 544
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
477-695 |
1.30e-16 |
|
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: 79.16 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQkVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDlSDLRKNIGYV 556
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQnTFLFADTIKNN-------LLHGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSLARTF 629
Cdd:cd03264 78 PQ-EFGVYPNFTVRefldyiaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 630 LKDPDIYIFDEATSALDSLTENKIMEHIDLLTQhGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENG 695
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
492-693 |
2.01e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.05 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMID---NYIIDDIDLSDLR-KNIGYVSQNTFLFA--D 565
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVgqpLHQMDEEARAKLRaKHVGFVFQSFMLIPtlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 566 TIKN----NLLHGSNKYKSDEDivkACQLAESLDFIQKfpdqfntmLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEA 641
Cdd:PRK10584 105 ALENvelpALLRGESSRQSRNG---AKALLEQLGLGKR--------LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 642 TSALDSLTENKImehIDLL----TQHGKTVIIISHKLSTIKNADNIYVLNEGQIAE 693
Cdd:PRK10584 174 TGNLDRQTGDKI---ADLLfslnREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
207-701 |
2.18e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.06 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 207 LLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTF 285
Cdd:PTZ00243 1005 LGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSrDIDILDNTLPMSYLYLLQCLF 1084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 286 MIIIGAILLYMQSPLLLLITIIFipcfiicSYTLRKPFEKYNQKVAE-------KDAELSSYLIESFDGSNTIKSYQS-- 356
Cdd:PTZ00243 1085 SICSSILVTSASQPFVLVALVPC-------GYLYYRLMQFYNSANREirriksvAKSPVFTLLEEALQGSATITAYGKah 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 357 ---EDDRFYIGTTKFNGIIENL------LKLGRFSNIQLTVNNFLKLT----------ISLVILWLGsyLVMTDSMTLGS 417
Cdd:PTZ00243 1158 lvmQEALRRLDVVYSCSYLENVanrwlgVRVEFLSNIVVTVIALIGVIgtmlratsqeIGLVSLSLT--MAMQTTATLNW 1235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 418 LLAFNALT----------IYYLDPIERliNIQPTLQSSFVAARR----IAEIT-DLETETELYTSKQPYTFK-NNIRIEN 481
Cdd:PTZ00243 1236 LVRQVATVeadmnsverlLYYTDEVPH--EDMPELDEEVDALERrtgmAADVTgTVVIEPASPTSAAPHPVQaGSLVFEG 1313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 482 VNFQY--GFrSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQN 559
Cdd:PTZ00243 1314 VQMRYreGL-PLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQD 1392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 560 TFLFADTIKNNL---LHGSNkyksdEDIVKACQLAESLDFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIY 636
Cdd:PTZ00243 1393 PVLFDGTVRQNVdpfLEASS-----AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGF 1467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 637 IF-DEATS----ALDSLTENKIMEHIDlltqhGKTVIIISHKLSTIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PTZ00243 1468 ILmDEATAnidpALDRQIQATVMSAFS-----AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
161-452 |
2.48e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 80.22 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 161 KLLFIAFISLFInIVGIVGALY---FKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMK 237
Cdd:cd18540 1 KKLLILLIILML-LVALLDAVFpllTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 238 DYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICS 316
Cdd:cd18540 80 KAFEHLQTLSFSYFDKTPVGWIMARVTsDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 317 YTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFyigtTKFNGIIENL----LKLGRFSNIQLTVNNFL 392
Cdd:cd18540 160 IYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNL----REFKELTEEMrrasVRAARLSALFLPIVLFL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 393 -KLTISLViLWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18540 236 gSIATALV-LWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
493-700 |
2.73e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.78 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLRKNIGYVSQNTFlfadtikn 569
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgQDLLKADPEAQKLLRQKIQIVFQNPY-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 570 nllhGS-NKYKSDEDIvkacqLAESLdfiqkfpdQFNT-------------MLEKEGAN----------LSGGQGQRLSL 625
Cdd:PRK11308 103 ----GSlNPRKKVGQI-----LEEPL--------LINTslsaaerrekalaMMAKVGLRpehydryphmFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 626 ARTFLKDPDIYIFDEATSALD-SLTE---NKIMehiDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDvSVQAqvlNLMM---DLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
475-694 |
3.14e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.85 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 475 NNIRienVNFQYGFRSV-VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL---- 549
Cdd:PRK10535 8 KDIR---RSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFAD-TIKNN-----LLHGSNKYKSDEDIVKACQ---LAESLDFiqkFPDQfntmlekeganLSGGQG 620
Cdd:PRK10535 85 REHFGFIFQRYHLLSHlTAAQNvevpaVYAGLERKQRLLRAQELLQrlgLEDRVEY---QPSQ-----------LSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 621 QRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAEN 694
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
477-696 |
3.76e-16 |
|
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: 78.24 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRS---VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimidnYIIDDIDLSDL---- 549
Cdd:COG4181 9 IELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT-----VRLAGQDLFALdeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 -----RKNIGYVSQNTFLFAdtiknNL-----------LHG-SNKYKSDEDIVKACQLAESLDFiqkFPDQfntmlekeg 612
Cdd:COG4181 84 rarlrARHVGFVFQSFQLLP-----TLtalenvmlpleLAGrRDARARARALLERVGLGHRLDH---YPAQ--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 613 anLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKImehIDLL----TQHGKTVIIISHKLSTIKNADNIYVLNE 688
Cdd:COG4181 147 --LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQI---IDLLfelnRERGTTLVLVTHDPALAARCDRVLRLRA 221
|
....*...
gi 488434717 689 GQIAENGT 696
Cdd:COG4181 222 GRLVEDTA 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
474-700 |
3.79e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.80 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 474 KNNIRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNR----YYTAS-EGNIMIDNYIIDDIDLSD 548
Cdd:PRK14247 1 MNKIEIRDLKVSFG-QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 549 LRKNIGYVSQ------NTFLFADT---IKNNLLhGSNKYKSDEDIVKACQLAEsldfiqkFPDQFNTMLEKEGANLSGGQ 619
Cdd:PRK14247 80 LRRRVQMVFQipnpipNLSIFENValgLKLNRL-VKSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 620 GQRLSLARTFLKDPDIYIFDEATSALDSLTENKImEHIDLLTQHGKTVIIISH-KLSTIKNADNIYVLNEGQIAENGTHD 698
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTR 230
|
..
gi 488434717 699 EL 700
Cdd:PRK14247 231 EV 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
477-674 |
4.40e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.66 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRY-------YTASEGNIMIDNYIIDDIDLSDL 549
Cdd:PRK14239 6 LQVSDLSVYYN-KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpevTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RKNIGYVSQNTFLFADTIKNNLLHG------SNKYKSDEDIVKACQLAESLDFIQKfpdqfntMLEKEGANLSGGQGQRL 623
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488434717 624 SLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLtQHGKTVIIISHKL 674
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSM 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
477-696 |
5.18e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:PRK13548 3 LEARNLSVRLGGR-TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNT-----FLFADTIKNNLLHGSNKYKSDEDIV-KACQLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSLARTFL 630
Cdd:PRK13548 82 PQHSslsfpFTVEEVVAMGRAPHGLSRAEDDALVaAALAQVDLAHLAGRDYPQ-----------LSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 631 ------KDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLstikN-----ADNIYVLNEGQIAENGT 696
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLArQLAHERGLAVIVVLHDL----NlaaryADRIVLLHQGRLVADGT 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
491-703 |
8.27e-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: 8.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGYVSQNTFLFAD-TIK 568
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 569 NNLLHGSNKYKS-----DEDIVKACQLAESLDFiqkfpdQFNtmLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATS 643
Cdd:COG1129 98 ENIFLGREPRRGglidwRAMRRRARELLARLGL------DID--PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 644 ALDSlTE-NKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENG-----THDELIHL 703
Cdd:COG1129 170 SLTE-REvERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
492-695 |
1.69e-15 |
|
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: 76.16 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTI-----GKLLNRYYTASEgnimiDNYIIDDIDLSDLRKNIGYVSQN------- 559
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLldaisGRVEGGGTTSGQ-----ILFNGQPRKPDQFQKCVAYVRQDdillpgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 560 ----TFLFADTIKN-NLLHGSNKYKSDEDIV-KACQLAESLDFIQKfpdqfntmlekegaNLSGGQGQRLSLARTFLKDP 633
Cdd:cd03234 97 tvreTLTYTAILRLpRKSSDAIRKKRVEDVLlRDLALTRIGGNLVK--------------GISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 634 DIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHK-LSTIKNA-DNIYVLNEGQIAENG 695
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLfDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
167-452 |
1.85e-15 |
|
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: 77.52 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 167 FISLFINIVGIVGALYFKLLT----DHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYH 242
Cdd:cd18543 2 ILALLAALLATLAGLAIPLLTrraiDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 243 VLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSStVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRK 321
Cdd:cd18543 82 LQRLDGAFHDRWQSGQLLSRATsDLSLVQRFLAFG-PFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 322 PFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSED---DRFYIGTTKFNGiiENLLKLGRFSNIQLTVNNFLKLTISL 398
Cdd:cd18543 161 RYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERrelDRFEAAARRLRA--TRLRAARLRARFWPLLEALPELGLAA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488434717 399 ViLWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18543 239 V-LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-701 |
2.45e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVlKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSdLRKNIGYV 556
Cdd:PRK13536 42 IDLAGVSKSYGDKAVV-NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL-ARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLLHGSNKYKSDEDIVKACqLAESLDFIQkfpdqfntmLEKEG----ANLSGGQGQRLSLARTFLK 631
Cdd:PRK13536 120 PQFDNLDLEfTVRENLLVFGRYFGMSTREIEAV-IPSLLEFAR---------LESKAdarvSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 632 DPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEG-QIAENGTH---DELI 701
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHaliDEHI 264
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
477-700 |
2.60e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 76.38 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEG-------------NIMIDNYIIDD 543
Cdd:COG4598 9 LEVRDLHKSFGDLEV-LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGeirvggeeirlkpDRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 544 IDLSDLRKNIGYVSQNTFLFAD-TIKNNL----LH--GSNKyksDEDIVKACQLaesldfiqkfpdqfntmLEKEG---- 612
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHmTVLENVieapVHvlGRPK---AEAIERAEAL-----------------LAKVGladk 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 613 -----ANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVL 686
Cdd:COG4598 148 rdaypAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDvSSHVVFL 227
|
250
....*....|....
gi 488434717 687 NEGQIAENGTHDEL 700
Cdd:COG4598 228 HQGRIEEQGPPAEV 241
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
477-701 |
2.79e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVlKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:PRK11231 3 LRTENLTVGYGTKRIL-NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNtFLFADTIKNNLL--HGSNKYK------SDEDIVKACQLAESLdfiqkfpdQFNTMLEKEGANLSGGQGQRLSLART 628
Cdd:PRK11231 82 PQH-HLTPEGITVRELvaYGRSPWLslwgrlSAEDNARVNQAMEQT--------RINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 629 FLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
492-695 |
3.26e-15 |
|
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: 75.26 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLS-----DL--RKNIgyvsqntflfa 564
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGggfnpELtgRENI----------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 565 dtIKNNLLHGsnkyKSDEDIvkacqlAESLDFIQKF---PDQFNTMLEkegaNLSGGQGQRLSLARTFLKDPDIYIFDEA 641
Cdd:cd03220 106 --YLNGRLLG----LSRKEI------DEKIDEIIEFselGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 642 TSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENG 695
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
477-700 |
4.19e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 78.57 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIEN--VNF-QYGFRSVVLKDINLNIKKGQKVAIVGESGSGKS----TIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL 549
Cdd:COG4172 7 LSVEDlsVAFgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 RK----NIGYVSQN--TFLfadtiknNLLHgsnkyksdeDIVKacQLAESLDFIQK------------------------ 599
Cdd:COG4172 87 RRirgnRIAMIFQEpmTSL-------NPLH---------TIGK--QIAEVLRLHRGlsgaaararalellervgipdper 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 600 ----FPDQfntmlekeganLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKL 674
Cdd:COG4172 149 rldaYPHQ-----------LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLkDLQRELGMALLLITHDL 217
|
250 260
....*....|....*....|....*..
gi 488434717 675 STIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:COG4172 218 GVVRRfADRVAVMRQGEIVEQGPTAEL 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
474-700 |
7.08e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.68 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 474 KNNIRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSdlRKNI 553
Cdd:PRK11432 4 KNFVVLKNITKRFG-SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLF-----ADTIKNNL-LHGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSLAR 627
Cdd:PRK11432 81 CMVFQSYALFphmslGENVGYGLkMLGVPKEERKQRVKEALELVDLAGFEDRYVDQ-----------ISGGQQQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIrELQQQFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
492-703 |
7.71e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.11 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD---LRKNIGYVSQNTF------- 561
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 562 LFADTIKNNLLHGSNKYKSD-----EDIVKACQLAESLdfIQKFPDQfntmlekeganLSGGQGQRLSLARTFLKDPDIY 636
Cdd:PRK10419 107 TVREIIREPLRHLLSLDKAErlaraSEMLRAVDLDDSV--LDKRPPQ-----------LSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 637 IFDEATSALDSLTENKImehIDLLT----QHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELIHL 703
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGV---IRLLKklqqQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTF 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
477-701 |
8.21e-15 |
|
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: 77.92 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLN--RYYTASEGNIMIDNYI-------------- 540
Cdd:TIGR03269 1 IEVKNLTKKFDGK-EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIYHVALcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 541 -------------------IDDIDLSDLRKNIGYVSQNTF-LFAD-TIKNNLLHGSNK--YKSDEDIVKACQLAESLDFI 597
Cdd:TIGR03269 80 epcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTFaLYGDdTVLDNVLEALEEigYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 598 QKFpdqfnTMLEKEganLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLST 676
Cdd:TIGR03269 160 HRI-----THIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|....*.
gi 488434717 677 IKN-ADNIYVLNEGQIAENGTHDELI 701
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGTPDEVV 257
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
495-700 |
1.14e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.41 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 495 DINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimidnYIIDDIDLSDL---RKNIGYVSQNTFLFAD-TIKNN 570
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQ-----IMLDGVDLSHVppyQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LLHGSNKYKSDEDIVKAcQLAESL------DFIQKFPDQfntmlekeganLSGGQGQRLSLARTFLKDPDIYIFDEATSA 644
Cdd:PRK11607 112 IAFGLKQDKLPKAEIAS-RVNEMLglvhmqEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 645 LD-SLTENKIMEHIDLLTQHGKTVIIISH-KLSTIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK11607 180 LDkKLRDRMQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
477-698 |
1.50e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfrSVV-LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIG 554
Cdd:COG3845 6 LELRGITKRFG--GVVaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNtFLFAD--TIKNNLLHGSNKYKSD-EDIVKACQLAESLdfIQKFPdqFNTMLEKEGANLSGGQGQRLSLARTFLK 631
Cdd:COG3845 84 MVHQH-FMLVPnlTVAENIVLGLEPTKGGrLDRKAARARIREL--SERYG--LDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 632 DPDIYIFDEATSAL-----DSLtenkiMEHIDLLTQHGKTVIIISHKLSTIK-NADNIYVLNEGQIAenGTHD 698
Cdd:COG3845 159 GARILILDEPTAVLtpqeaDEL-----FEILRRLAAEGKSIIFITHKLREVMaIADRVTVLRRGKVV--GTVD 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
492-672 |
1.85e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGnimidnyiiddidlsdlrKNIGYVSQNTFLFADTIKNNL 571
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV------------------AGCVDVPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 572 LHGSNKYKSDEdIVKACQLAESLDFIQKFpdqfntmlekegANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTEn 651
Cdd:COG2401 107 GRKGDFKDAVE-LLNAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA- 172
|
170 180
....*....|....*....|...
gi 488434717 652 KIMEHI--DLLTQHGKTVIIISH 672
Cdd:COG2401 173 KRVARNlqKLARRAGITLVVATH 195
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
423-693 |
1.86e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.55 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 423 ALTIYYL-DPIERLINIQPTLQSSFVAARRIAEITDLETETELYTSKQPYTFKNnIRIENVNFQYGFRSVVLKDINLNIK 501
Cdd:PRK10522 269 SLTLLFLrTPLLSAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDWQT-LELRNVTFAYQDNGFSVGPINLTIK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 502 KGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFadtikNNLLHGSNKYKSD 581
Cdd:PRK10522 348 RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF-----DQLLGPEGKPANP 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 582 EDIVKacqLAESLDFIQKFPDQFNTMLEkegANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKI-MEHIDLL 660
Cdd:PRK10522 423 ALVEK---WLERLKMAHKLELEDGRISN---LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLL 496
|
250 260 270
....*....|....*....|....*....|...
gi 488434717 661 TQHGKTVIIISHKLSTIKNADNIYVLNEGQIAE 693
Cdd:PRK10522 497 QEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
482-700 |
1.96e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.36 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 482 VNFQYGFR-SVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRY------YTASEGNIMIDNYIIDDIDLSDLRKNIG 554
Cdd:PRK14271 25 VNLTLGFAgKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGGRSIFNYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFADTIKNNLLHGSNKYK----SDEDIVKACQLAESldfiqKFPDQFNTMLEKEGANLSGGQGQRLSLARTFL 630
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKlvprKEFRGVAQARLTEV-----GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 631 KDPDIYIFDEATSALDSLTENKIMEHIDLLTQHgKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
494-702 |
2.42e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 74.74 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 494 KDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLRKNIGYVSQNTF-------LF 563
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgKDLLGMKDDEWRAVRSDIQMIFQDPLaslnprmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 564 ADTIKNNLLHGSNKYKSDE--DIVKACQLAESL--DFIQKFPDQFntmlekeganlSGGQGQRLSLARTFLKDPDIYIFD 639
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEvkDRVKAMMLKVGLlpNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 640 EATSALDSLTENKImehIDLLTQ----HGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELIH 702
Cdd:PRK15079 187 EPVSALDVSIQAQV---VNLLQQlqreMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYH 251
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
477-701 |
2.65e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.48 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:PRK10253 8 LRGEQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLLHGSNKY--------KSDEDIVKACQLAESLdfiqkfpdqfnTMLEKEGAN-LSGGQGQRLSLA 626
Cdd:PRK10253 87 AQNATTPGDiTVQELVARGRYPHqplftrwrKEDEEAVTKAMQATGI-----------THLADQSVDtLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 627 RTFLKDPDIYIFDEATSALDsltenkIMEHIDLLT-------QHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHD 698
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLD------ISHQIDLLEllselnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPK 229
|
...
gi 488434717 699 ELI 701
Cdd:PRK10253 230 EIV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
477-701 |
3.15e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 72.58 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVlKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidLSDL------R 550
Cdd:cd03218 1 LRAENLSKRYGKRKVV-NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD-----ITKLpmhkraR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 551 KNIGYVSQNTFLFAD-TIKNNLL--HGSNKYKSDEDIVKACQLAESLDfIQKFPDQFntmlekeGANLSGGQGQRLSLAR 627
Cdd:cd03218 75 LGIGYLPQEASIFRKlTVEENILavLEIRGLSKKEREEKLEELLEEFH-ITHLRKSK-------ASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
497-701 |
3.61e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.69 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 497 NLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSdlRKNIGYVSQNTFLFAD-TIKNNL---L 572
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 573 HGSNKYKSD-----EDIVKACQLAeslDFIQKFPDQfntmlekeganLSGGQGQRLSLARTFLKDPDIYIFDEATSALDS 647
Cdd:PRK10771 97 NPGLKLNAAqreklHAIARQMGIE---DLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 648 LTENKIMEHID-LLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PRK10771 163 ALRQEMLTLVSqVCQERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| Peptidase_C39D |
cd02420 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
8-128 |
3.67e-14 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239101 [Multi-domain] Cd Length: 125 Bit Score: 69.38 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 8 QYDEKDCGPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYGLVQAGKKIGIELTGVKADsFDDLKQAQLPVMVHiinq 87
Cdd:cd02420 6 QMEATECGAASLAIILAYYGRYVPLSELRIACGVSRDGSNASNLLKAAREYGLTAKGYKKD-LEALREVSLPAIVF---- 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488434717 88 QGYDHYIIIEKIKNNTLYIVDPAKGKYKLSSTEFGKYWTNI 128
Cdd:cd02420 81 WNFNHFLVVEGFDKRKVFLNDPATGRRTVSLEEFDQSFTGV 121
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
202-421 |
3.70e-14 |
|
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: 73.70 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 202 ISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRF-MDTSKIREALSSSTVTL 280
Cdd:cd18573 43 FALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLsSDTSVVGKSLTQNLSDG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 281 LVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDR 360
Cdd:cd18573 123 LRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKE 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 361 fyigTTKFNGIIENLLKLGR---------FSNIQLTVNnflklTISLVILWLGSYLVMTDSMTLGSLLAF 421
Cdd:cd18573 203 ----VERYAKKVDEVFDLAKkealasglfFGSTGFSGN-----LSLLSVLYYGGSLVASGELTVGDLTSF 263
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
162-452 |
4.63e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 73.29 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYTLR 320
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNnDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 321 KPFEKYNQKVAEKDAELSSYLIESFD--GSNTIKSYQSEDDRfyigTTKFNGIIENLLKLG---------RFSNIQLtvn 389
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDE----AARFARRSRELRDLGvrqalagrwFFAALGL--- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 390 nFLKLTISLViLWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18550 234 -FTAIGPALV-YWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
167-452 |
5.01e-14 |
|
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: 73.22 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 167 FISLFINIVGIVGALYFKLLTDHIIPSNVLKN------LHIISFGILLLY-IINALINYLRFQLILHLSLKIDVNLMKDY 239
Cdd:cd18554 6 VIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLdekvykLFTIIGIMFFIFlILRPPVEYYRQYFAQWIANKILYDIRKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 240 FYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSYT 318
Cdd:cd18554 86 FDHLQKLSLRYYANNRSGEIISRVInDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 319 LRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISL 398
Cdd:cd18554 166 FFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488434717 399 VILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18554 246 LVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
488-695 |
5.47e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.98 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 488 FRSVV-LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimidnyiIDDIDLSDLRKNIGYVSQNTFLFADt 566
Cdd:cd03267 31 YREVEaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE-------VRVAGLVPWKRRKKFLRRIGVVFGQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 567 iKNNL---LHGSNKYKSDEDI--VKACQLAESLDfiqKFPD--QFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFD 639
Cdd:cd03267 103 -KTQLwwdLPVIDSFYLLAAIydLPPARFKKRLD---ELSEllDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 640 EATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENG 695
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLkEYNRERGTTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
492-691 |
5.53e-14 |
|
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: 70.54 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGYVSqntflfadtiknn 570
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVP------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 llhgsnkyksdEDivkacQLAESLdfIQKFPDQFNTMLekeGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTE 650
Cdd:cd03215 82 -----------ED-----RKREGL--VLDLSVAENIAL---SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488434717 651 NKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQI 691
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
477-701 |
1.49e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGY 555
Cdd:PRK11614 6 LSFDKVSAHYG-KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFAD-TIKNNLLHG---SNKYKSDEDIVKACQLaesldfiqkFPDQFNTMLEKEGAnLSGGQGQRLSLARTFLK 631
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGgffAERDQFQERIKWVYEL---------FPRLHERRIQRAGT-MSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 632 DPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
492-700 |
1.59e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.23 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRY---YTAS---EGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFAD 565
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 566 -TIKNNLL-----HGSNKYKSDEDIVKACqlAESLDFIQKFPDQFNTmlekEGANLSGGQGQRLSLARTFLKDPDIYIFD 639
Cdd:PRK14246 105 lSIYDNIAyplksHGIKEKREIKKIVEEC--LRKVGLWKEVYDRLNS----PASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 640 EATSALDSLTENKIMEHIDLLTQHgKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
474-695 |
1.63e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 474 KNNIRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTAS-----EGNIMIDNYIIDDIDLS- 547
Cdd:PRK14267 2 KFAIETVNLRVYYG-SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 548 -DLRKNIGYVSQNTFLFAD-TIKNNLLHG---SNKYKSDEDIVKACQLAesldfIQKFP--DQFNTMLEKEGANLSGGQG 620
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHlTIYDNVAIGvklNGLVKSKKELDERVEWA-----LKKAAlwDEVKDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 621 QRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHgKTVIIISHK-LSTIKNADNIYVLNEGQIAENG 695
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-700 |
4.80e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.52 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDidlsDLRKNIGY- 555
Cdd:COG4152 2 LELKGLTKRFG-DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 -----------VSQNTFLFADtiknnlLHGSNKYKSDEDIvkacqlaesLDFIQKF--PDQFNTMLEKeganLSGGQGQR 622
Cdd:COG4152 77 peerglypkmkVGEQLVYLAR------LKGLSKAEAKRRA---------DEWLERLglGDRANKKVEE----LSKGNQQK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 623 LSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDEL 700
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-701 |
6.12e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVlKDINLNIKKGQKVAIVGESGSGKSTIGKLLnRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:PRK13537 8 IDFRNVEKRYGDKLVV-DGLSFHVQRGECFGLLGPNGAGKTTTLRML-LGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD-TIKNNLLHGSNKYKsdediVKACQLAESLDFIQKFPDQFNTMLEKEGAnLSGGQGQRLSLARTFLKDPDI 635
Cdd:PRK13537 86 PQFDNLDPDfTVRENLLVFGRYFG-----LSAAAARALVPPLLEFAKLENKADAKVGE-LSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 636 YIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEG-QIAENGTHdELI 701
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGrKIAEGAPH-ALI 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
466-710 |
1.19e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.98 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 466 TSKQPYTFKNNIRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimidnYIIDDID 545
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR-----IMLDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 546 LSDL---RKNIGYVSQNTFLFAD-TIKNNLLHGSNKYKSDEDIVKAcQLAESLDFIqkfpdQFNTMLEKEGANLSGGQGQ 621
Cdd:PRK09452 78 ITHVpaeNRHVNTVFQSYALFPHmTVFENVAFGLRMQKTPAAEITP-RVMEALRMV-----QLEEFAQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 622 RLSLARTFLKDPDIYIFDEATSALD-SLTENKIMEHIDLLTQHGKTVIIISHK----LSTiknADNIYVLNEGQIAENGT 696
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDyKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM---SDRIVVMRDGRIEQDGT 228
|
250
....*....|....*..
gi 488434717 697 HDElihlngIY---KNL 710
Cdd:PRK09452 229 PRE------IYeepKNL 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
491-695 |
1.24e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYyTASEGNIMIDNY---IIDDIDLSDLRKNIGYVSQ------NTF 561
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL-INSQGEIWFDGQplhNLNRRQLLPVRHRIQVVFQdpnsslNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 562 LFADTIKNNLLHGSNKYKS---DEDIVKACQLAESLDFI--QKFPDQFntmlekeganlSGGQGQRLSLARTFLKDPDIY 636
Cdd:PRK15134 379 LNVLQIIEEGLRVHQPTLSaaqREQQVIAVMEEVGLDPEtrHRYPAEF-----------SGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 637 IFDEATSALDSLTENKIMEHIDLLTQ-HGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENG 695
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQkHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
475-700 |
1.65e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.25 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 475 NNIRIENVNFQYGFRSVvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL---RK 551
Cdd:PRK11831 6 NLVDMRGVSFTRGNRCI-FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 552 NIGYVSQNTFLFAD-TIKNNLLHGSNKYKsdedivkacQLAESLDfiqkfpdQFNTMLEKEG-----------ANLSGGQ 619
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPLREHT---------QLPAPLL-------HSTVMMKLEAvglrgaaklmpSELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 620 GQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQH-GKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTH 697
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSA 228
|
...
gi 488434717 698 DEL 700
Cdd:PRK11831 229 QAL 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
496-700 |
1.94e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 496 INLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGniMIDNYIIDDIDLSD---LRKNIGYVSQNTFLFADT------ 566
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGG--TILLRGQHIEGLPGhqiARMGVVRTFQHVRLFREMtvienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 567 -------IKNNLLHGSNK---YKSDEdivkacqlAESLDFIQKFPDQFN--TMLEKEGANLSGGQGQRLSLARTFLKDPD 634
Cdd:PRK11300 102 lvaqhqqLKTGLFSGLLKtpaFRRAE--------SEALDRAATWLERVGllEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 635 IYIFDEATSALDSLTENKIMEHIDLL-TQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
481-702 |
2.01e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 481 NVNFQYGFRSV-VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDN-------------YIIDDIDL 546
Cdd:PRK10261 19 NIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 547 SDLR-KNIGYVSQN-------TFLFADTIKNNL-LH-GSNKyksDEDIVKACQLAESLdfiqKFPDQfNTMLEKEGANLS 616
Cdd:PRK10261 99 RHVRgADMAMIFQEpmtslnpVFTVGEQIAESIrLHqGASR---EEAMVEAKRMLDQV----RIPEA-QTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 617 GGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQH-GKTVIIISHKLSTIKN-ADNIYVLNEGQIAEN 694
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEiADRVLVMYQGEAVET 250
|
....*...
gi 488434717 695 GTHDELIH 702
Cdd:PRK10261 251 GSVEQIFH 258
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
489-700 |
2.16e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.46 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 489 RSVVLKDINLNIKKGQKVAIVGESGSGKST-IGKLLNRYYTASEGNIMIDNYIIDDIdLSDLRKNIGYVSQ-NTFLFADT 566
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTlMNALAFRSPKGVKGSGSVLLNGMPID-AKEMRAISAYVQQdDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 567 IKNNL-------LHGSNKYKSDEDIVKACQLAESLDFIQkfpdqfNTMLEKEGA--NLSGGQGQRLSLARTFLKDPDIYI 637
Cdd:TIGR00955 116 VREHLmfqahlrMPRRVTKKEKRERVDEVLQALGLRKCA------NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 638 FDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLST--IKNADNIYVLNEGQIAENGTHDEL 700
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
493-695 |
2.65e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMID---NYIIDDIDLSDLRKNIGYVSQNTFLFAD---T 566
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqrIDTLSPGKLQALRRDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 567 IK---------NNLLHGSNKYKSDEDIVKACQLAEslDFIQKFPDQFntmlekeganlSGGQGQRLSLARTFLKDPDIYI 637
Cdd:PRK10261 420 VGdsimeplrvHGLLPGKAAAARVAWLLERVGLLP--EHAWRYPHEF-----------SGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 638 FDEATSALD-SLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENG 695
Cdd:PRK10261 487 ADEAVSALDvSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
477-694 |
2.97e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD---LRKNI 553
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 554 GYVSQNTFLFAD-TIKNN-----LLHGSnkykSDEDIVKACQLAES----LDFIQKFPDQfntmlekeganLSGGQGQRL 623
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNvaiplIIAGA----SGDDIRRRVSAALDkvglLDKAKNFPIQ-----------LSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 624 SLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNAD-NIYVLNEGQIAEN 694
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLHGG 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
477-672 |
3.61e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 67.19 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQY---GFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGnimidnyiiddidlsDLRKN- 552
Cdd:COG4525 4 LTVRHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSG---------------EITLDg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 ---------IGYVSQNTFLF-----ADTIKNNL-LHGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekeganLSG 617
Cdd:COG4525 69 vpvtgpgadRGVVFQKDALLpwlnvLDNVAFGLrLRGVPKAERRARAEELLALVGLADFARRRIWQ-----------LSG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 618 GQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISH 672
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLlDVWQRTGKGVFLITH 193
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
507-691 |
4.75e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.98 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 507 AIVGESGSGKSTIGKLLNRYYTASEG----NIMIDNYIIDDIDLSDLRKNIGYVSQNTFLFAD-TIKNNLLHGSNKYKSD 581
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGrivlNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 582 E--DIVKACQLAESLDfiqKFPdqfntmlekegANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDL 659
Cdd:PRK11144 108 QfdKIVALLGIEPLLD---RYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190
....*....|....*....|....*....|....
gi 488434717 660 LTQHGKTVII-ISHKLSTI-KNADNIYVLNEGQI 691
Cdd:PRK11144 174 LAREINIPILyVSHSLDEIlRLADRVVVLEQGKV 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
480-701 |
4.97e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.46 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 480 ENVNFQYGFRSVVlKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGYVSQ 558
Cdd:PRK10895 7 KNLAKAYKGRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 559 NTFLFAD-TIKNNLLhgsNKYKSDEDIVKACQLAESLDFIQKFpdQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYI 637
Cdd:PRK10895 86 EASIFRRlSVYDNLM---AVLQIRDDLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 638 FDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKL-STIKNADNIYVLNEGQIAENGTHDELI 701
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
447-701 |
7.57e-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: 68.29 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 447 VAARRIAEITDLETETELYTSKQPytfknnIRIENVNFQYGF--RSVV--LKDINLNIKKGQKVAIVGESGSGKSTIGKL 522
Cdd:TIGR03269 256 VVAVFMEGVSEVEKECEVEVGEPI------IKVRNVSKRYISvdRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 523 LNRYYTASEGNIMIDN-------YIIDDIDLSDLRKNIGYVSQNTFLFAD-TIKNNLLHGSNKYKSDE-DIVKACQLAES 593
Cdd:TIGR03269 330 IAGVLEPTSGEVNVRVgdewvdmTKPGPDGRGRAKRYIGILHQEYDLYPHrTVLDNLTEAIGLELPDElARMKAVITLKM 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 594 LDFIQKFPDQfntMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISH 672
Cdd:TIGR03269 410 VGFDEEKAEE---ILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlKAREEMEQTFIIVSH 486
|
250 260 270
....*....|....*....|....*....|
gi 488434717 673 KLSTIKN-ADNIYVLNEGQIAENGTHDELI 701
Cdd:TIGR03269 487 DMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
492-696 |
1.10e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.22 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIM---IDNYIIDDIDLSDLRKN-IGYVSQNTFLFAD-T 566
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngQPMSKLSSAAKAELRNQkLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 567 IKNN----LLHGsnKYKSDEDIVKACQLAESLDfiqkfpdqfntmLEKEG----ANLSGGQGQRLSLARTFLKDPDIYIF 638
Cdd:PRK11629 104 ALENvampLLIG--KKKPAEINSRALEMLAAVG------------LEHRAnhrpSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 639 DEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENGT 696
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
491-701 |
1.26e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRK-NIGYVSQNTFLFAD-TIK 568
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 569 NNLLHGSNKYKSDEDIVKA--CQLAESLDfiqkfpdqfntmLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALD 646
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQllAALGCQLD------------LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 647 SLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENG-----THDELI 701
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDII 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
493-689 |
1.52e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKN-IGYVSQNTFLFAD-TIKNN 570
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LLHGSNKYKsdedivKACQLaESLDFiQKFPDQFNTMLEKEG---------ANLSGGQGQRLSLARTFLKDPDIYIFDEA 641
Cdd:PRK09700 101 LYIGRHLTK------KVCGV-NIIDW-REMRVRAAMMLLRVGlkvdldekvANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488434717 642 TSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEG 689
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
499-696 |
1.57e-11 |
|
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: 65.12 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 499 NIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimidnyiiddiDLSDLRKnIGYVSQNTFLFADTIKNNLLHG---- 574
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-----------IEIELDT-VSYKPQYIKADYEGTVRDLLSSitkd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 575 ---SNKYKSdeDIVKacqlaesldfiqkfPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDS---L 648
Cdd:cd03237 89 fytHPYFKT--EIAK--------------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488434717 649 TENKIMEHIDLltQHGKTVIIISHKLSTIKN-ADNIYVLnEGQIAENGT 696
Cdd:cd03237 153 MASKVIRRFAE--NNEKTAFVVEHDIIMIDYlADRLIVF-EGEPSVNGV 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
500-699 |
1.79e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 500 IKKGQKVAIVGESGSGKSTigkLLNRY--YTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQN-TFLFADTIKNNL-LHGS 575
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLtLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 576 NKYKSDEDIVKACQLAESLdfiqKFPDQFNTMLEkegaNLSGGQGQRLSLARTFLK-DPDI------YIFDEATSALDSL 648
Cdd:PRK03695 96 DKTRTEAVASALNEVAEAL----GLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488434717 649 TENKIMEHIDLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDE 699
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
163-452 |
3.46e-11 |
|
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: 64.89 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 163 LFIAFISLFIN---------IVGIV-------GALYFKLLTDHIIPSNVLKNLHIISFGILLLYIINALINYLRFQLILH 226
Cdd:cd18565 1 LVLGLLASILNrlfdlapplLIGVAidavfngEASFLPLVPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 227 LSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEI----------LQRFMDTSkIREALSSSTVTLLvdtfmiiIGAILLYM 296
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLmsvlnndvnqLERFLDDG-ANSIIRVVVTVLG-------IGAILFYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 297 qSPLLLLITIIFIPCFIICSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSED---DRF------YIgTTK 367
Cdd:cd18565 153 -NWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDferERVadaseeYR-DAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 368 FNGIienllklgRFSNIQLTVNNFLKLTISLVILWLGSYLVM------TDSMTLGSLLAFNALTIYYLDPIERLINIQPT 441
Cdd:cd18565 231 WRAI--------RLRAAFFPVIRLVAGAGFVATFVVGGYWVLdgpplfTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQ 302
|
330
....*....|.
gi 488434717 442 LQSSFVAARRI 452
Cdd:cd18565 303 YQRAMASAKRV 313
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
491-686 |
3.53e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 62.64 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNyiiddidlsdlRKNIGYVSQNTFL-------F 563
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdslpltV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 564 ADTI------KNNLL--HGSNKYKSDEDIVKACQLAEsldfiqkfpdqfntmLEKEG-ANLSGGQGQRLSLARTFLKDPD 634
Cdd:NF040873 75 RDLVamgrwaRRGLWrrLTRDDRAAVDDALERVGLAD---------------LAGRQlGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488434717 635 IYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVL 686
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
477-705 |
4.55e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDnyiiddidlSDLRknIGYV 556
Cdd:PRK09544 5 VSLENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFAD---TIKNNL-LHGSNKyksDEDIVKACQLAESLDFIQkFPDQfntmlekegaNLSGGQGQRLSLARTFLKD 632
Cdd:PRK09544 73 PQKLYLDTTlplTVNRFLrLRPGTK---KEDILPALKRVQAGHLID-APMQ----------KLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 633 PDIYIFDEATSALDSLTENKIMEHID-LLTQHGKTVIIISHKLSTI-KNADNIYVLNEgQIAENGT------HDELIHLN 704
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDqLRRELDCAVLMVSHDLHLVmAKTDEVLCLNH-HICCSGTpevvslHPEFISMF 217
|
.
gi 488434717 705 G 705
Cdd:PRK09544 218 G 218
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
230-452 |
5.19e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 64.10 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 230 KIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIrealsSSTVTLLVDTF-----MIIIGAILLYMQSPLLLL 303
Cdd:cd18572 66 RLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTsDCQKV-----SDPLSTNLNVFlrnlvQLVGGLAFMFSLSWRLTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 304 ITIIFIPCfiicSYTLRKPFEKYNQKVAEKD----AELSSYLIESFDGSNTIKSYQSED---DRFyigttkfNGIIENLL 376
Cdd:cd18572 141 LAFITVPV----IALITKVYGRYYRKLSKEIqdalAEANQVAEEALSNIRTVRSFATEEreaRRY-------ERALDKAL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 377 KLGR----FSNIQLTVNNFLKLTISLVILWLGSYLVMTDSMTLGSLLAFnaltIYYL----DPIERLINIQPTLQSSFVA 448
Cdd:cd18572 210 KLSVrqalAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTF----MLYQqqlgEAFQSLGDVFSSLMQAVGA 285
|
....
gi 488434717 449 ARRI 452
Cdd:cd18572 286 AEKV 289
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-691 |
5.89e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.57 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVN--FQYGFRS--VVLKDINLNIKKGQKVAIVGESGSGKSTigkLLNR---YYTASEGNIMIDNYIIDDidLSDL 549
Cdd:COG1101 2 LELKNLSktFNPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKST---LLNAiagSLPPDSGSILIDGKDVTK--LPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 R--KNIGYVSQNTFL--FAD-TIKNNLLHGSNKYKSDedivkacQLAESLDfiQKFPDQFNTMLEKEG-----------A 613
Cdd:COG1101 77 KraKYIGRVFQDPMMgtAPSmTIEENLALAYRRGKRR-------GLRRGLT--KKRRELFRELLATLGlglenrldtkvG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 614 NLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEhidlLTQ-----HGKTVIIISHKLS-TIKNADNIYVLN 687
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE----LTEkiveeNNLTTLMVTHNMEqALDYGNRLIMMH 223
|
....
gi 488434717 688 EGQI 691
Cdd:COG1101 224 EGRI 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
492-695 |
8.61e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.77 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLL--NRYYTASEGNimidnYIIDDIDLSDL------RKNIGYVSQNTFLF 563
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGE-----ILFKGEDITDLppeeraRLGIFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 564 ADTIKNNLLHGSNkyksdedivkacqlaesldfiqkfpdqfntmlekEGanLSGGQGQRLSLARTFLKDPDIYIFDEATS 643
Cdd:cd03217 90 PGVKNADFLRYVN----------------------------------EG--FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 644 ALD----SLTENKIMEhidLLTQhGKTVIIISH--KLSTIKNADNIYVLNEGQIAENG 695
Cdd:cd03217 134 GLDidalRLVAEVINK---LREE-GKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
476-701 |
1.18e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.39 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIEnVNFQYGFRSVVLKdINLNIKKGQKVAIVGESGSGKSTIGKLLnryytasegnimidnyiiddidlsdlrknIGY 555
Cdd:COG4170 8 NLTIE-IDTPQGRVKAVDR-VSLTLNEGEIRGLVGESGSGKSLIAKAI-----------------------------CGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNTFLFADTIK---NNLLHGSNKYKSD---EDIV------KAC---------QLAESLDFIQ---KFPDQFNT----- 606
Cdd:COG4170 57 TKDNWHVTADRFRwngIDLLKLSPRERRKiigREIAmifqepSSCldpsakigdQLIEAIPSWTfkgKWWQRFKWrkkra 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 607 --MLEKEGA------------NLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQ-HGKTVIIIS 671
Cdd:COG4170 137 ieLLHRVGIkdhkdimnsyphELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLIS 216
|
250 260 270
....*....|....*....|....*....|.
gi 488434717 672 HKLSTIKN-ADNIYVLNEGQIAENGTHDELI 701
Cdd:COG4170 217 HDLESISQwADTITVLYCGQTVESGPTEQIL 247
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
493-701 |
1.37e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMidnyiiddidLSDLRKNIG---YVSQNT-FLFADTik 568
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL----------IDDHPLHFGdysYRSQRIrMIFQDP-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 569 nnllhgSNKYKSDEDIvkacqlAESLDFiqkfPDQFNTMLEKEG------------------AN-----LSGGQGQRLSL 625
Cdd:PRK15112 97 ------STSLNPRQRI------SQILDF----PLRLNTDLEPEQrekqiietlrqvgllpdhASyyphmLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 626 ARTFLKDPDIYIFDEATSALD-SLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELI 701
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
493-701 |
1.62e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTAS--EGNIMIDNYIIDDIDLSDL-RKNIGYVSQNTFLFADT--- 566
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPELsva 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 567 ----IKNNLLHGSNKYKSDEDIVKACQLAESLdfiqKFPDQFNTmleKEGANLSGGQGQRLSLARTFLKDPDIYIFDEAT 642
Cdd:TIGR02633 97 enifLGNEITLPGGRMAYNAMYLRAKNLLREL----QLDADNVT---RPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 643 SaldSLTENKIMEHIDL---LTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQ-----IAENGTHDELI 701
Cdd:TIGR02633 170 S---SLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAvCDTICVIRDGQhvatkDMSTMSEDDII 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
500-677 |
1.92e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 500 IKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNImidnyiiddidLSDLRknIGYVSQntFLFADT----------IKN 569
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----------DPELK--ISYKPQ--YIKPDYdgtvedllrsITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 570 NLlhGSNKYKSDedIVKacqlaesldfiqkfPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDS-- 647
Cdd:PRK13409 427 DL--GSSYYKSE--IIK--------------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeq 488
|
170 180 190
....*....|....*....|....*....|.
gi 488434717 648 -LTENKIMEHIdlLTQHGKTVIIISHKLSTI 677
Cdd:PRK13409 489 rLAVAKAIRRI--AEEREATALVVDHDIYMI 517
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
615-701 |
2.19e-10 |
|
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: 64.26 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 615 LSGGQGQRLSLARTFLKD---PDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVL----- 686
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|....*.
gi 488434717 687 -NEGQIAENGTHDELI 701
Cdd:TIGR00630 910 dGGGTVVASGTPEEVA 925
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
478-707 |
2.35e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 478 RIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVS 557
Cdd:PRK10575 13 ALRNVSFRVPGR-TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 QN-------TFLFADTIKNNLLHGSNKYKSDED---IVKACQLAESLDFIQKFPDqfntmlekegaNLSGGQGQRLSLAR 627
Cdd:PRK10575 92 QQlpaaegmTVRELVAIGRYPWHGALGRFGAADrekVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQ-HGKTVIIISHKLS-TIKNADNIYVLNEGQIAENGTHDELIH--- 702
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRget 240
|
....*
gi 488434717 703 LNGIY 707
Cdd:PRK10575 241 LEQIY 245
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
480-689 |
2.41e-10 |
|
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: 60.33 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 480 ENVNFQ---YGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTigkLLNryytasegnimidnyiiddiDLSDlRKNIGYV 556
Cdd:cd03232 7 KNLNYTvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLD--------------------VLAG-RKTAGVI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFADTIKNNLLHGSNkYKSDEDIVKACQ-LAESLDFiqkfpdqfntmlekeGANLSG---GQGQRLSLARTFLKD 632
Cdd:cd03232 63 TGEILINGRPLDKNFQRSTG-YVEQQDVHSPNLtVREALRF---------------SALLRGlsvEQRKRLTIGVELAAK 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 633 PDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLS--TIKNADNIYVLNEG 689
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
495-702 |
2.63e-10 |
|
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: 62.81 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 495 DINLNIKKGQKVAIVGESGSGKSTI------------------GKLL----NRYYTASEgnimidnyiiddidlsdlRKN 552
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLlraiaglerpdsgrirlgGEVLqdsaRGIFLPPH------------------RRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 IGYVSQNTFLFAD-TIKNNLLHG------SNKYKSDEDIVKACQLAESLDfiqKFPDQfntmlekeganLSGGQGQRLSL 625
Cdd:COG4148 79 IGYVFQEARLFPHlSVRGNLLYGrkraprAERRISFDEVVELLGIGHLLD---RRPAT-----------LSGGERQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 626 ARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKT-VIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELIH 702
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
493-683 |
3.10e-10 |
|
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: 61.48 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKS-----TIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL----RKNIG--------- 554
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSslindTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVividQSPIGrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTF---LFADTIK-----NNLLHGSNKYKSDEDIVkACQLAESLDFIQKFPDQFNTM------------LEKEGAN 614
Cdd:cd03271 91 YTGVFDEireLFCEVCKgkrynRETLEVRYKGKSIADVL-DMTVEEALEFFENIPKIARKLqtlcdvglgyikLGQPATT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 615 LSGGQGQRLSLARTFLK---DPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNI 683
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWI 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
607-686 |
3.10e-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: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 607 MLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYV 685
Cdd:COG1245 205 ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILdYLADYVHI 284
|
.
gi 488434717 686 L 686
Cdd:COG1245 285 L 285
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
493-701 |
3.17e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTAS--EGNIMIDNYIIDDIDLSDL-RKNIGYVSQ----------- 558
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTeRAGIAIIHQelalvkelsvl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 559 -NTFLFADTIKNNLLHGSNKYKSDEDIVKACQLAESLDfiqkfpdqfntmlEKEGaNLSGGQGQRLSLARTFLKDPDIYI 637
Cdd:PRK13549 101 eNIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPA-------------TPVG-NLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 638 FDEATSaldSLTENKIMEHIDL---LTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI-----AENGTHDELI 701
Cdd:PRK13549 167 LDEPTA---SLTESETAVLLDIirdLKAHGIACIYISHKLNEVKAiSDTICVIRDGRHigtrpAAGMTEDDII 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
500-677 |
3.29e-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: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 500 IKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNImidnyiiddidlsDLRKNIGYVSQ----------NTFLFaDTIKN 569
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyispdydgtvEEFLR-SANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 570 NLlhGSNKYKsdEDIVKacqlaesldfiqkfPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDS-- 647
Cdd:COG1245 429 DF--GSSYYK--TEIIK--------------PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeq 490
|
170 180 190
....*....|....*....|....*....|.
gi 488434717 648 -LTENKIMEHIdlLTQHGKTVIIISHKLSTI 677
Cdd:COG1245 491 rLAVAKAIRRF--AENRGKTAMVVDHDIYLI 519
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
493-683 |
4.52e-10 |
|
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: 59.26 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIgkLLNRYYTASEgnimidnyiiddIDLSDLRKNIGYvsqNTFLFADTIKNNLL 572
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGK------------ARLISFLPKFSR---NKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 573 HGsnkyksdedivkacqlaesLDFIQkfpdqfntmLEKEGANLSGGQGQRLSLArTFL---KDPDIYIFDEATSALDSLT 649
Cdd:cd03238 74 VG-------------------LGYLT---------LGQKLSTLSGGELQRVKLA-SELfsePPGTLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....
gi 488434717 650 ENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNI 683
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVLSSADWI 158
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
162-420 |
5.56e-10 |
|
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: 60.95 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTdhiiPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18577 13 AALPLMTIVFGDLFDAFTDFGSGESS----PDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPllllitiifipcfiicSYTL- 319
Cdd:cd18577 89 ALLRQDIAWFDKNGAGELTSRLTsDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSW----------------KLTLv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 320 ---------------RKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSED---DRF--YIGTTKFNGIienllKLG 379
Cdd:cd18577 153 llatlpliaivggimGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEkeiKRYskALEKARKAGI-----KKG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 488434717 380 RFSNIQLTVNNFLKLTISLVILWLGSYLVMTDSMTLGSLLA 420
Cdd:cd18577 228 LVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLT 268
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
479-672 |
5.88e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 479 IENVNFQYGFRSVVlKDINLNIKKGQKVAIVGESGSGKSTIGKLLnryytasegnimidnyiiddidLSDLRKNIGYVSQ 558
Cdd:PRK11147 322 MENVNYQIDGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLM----------------------LGQLQADSGRIHC 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 559 NTFL---FAD----------TIKNNLLHGSnkyksdEDIVKACQLAESLDFIQKF---PDQFNTMLEKeganLSGGQGQR 622
Cdd:PRK11147 379 GTKLevaYFDqhraeldpekTVMDNLAEGK------QEVMVNGRPRHVLGYLQDFlfhPKRAMTPVKA----LSGGERNR 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488434717 623 LSLARTFLKDPDIYIFDEATSALDSLTEnKIMEhiDLLTQHGKTVIIISH 672
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDVETL-ELLE--ELLDSYQGTVLLVSH 495
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
477-672 |
6.43e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidLSDLRKNIGYV 556
Cdd:PRK11248 2 LQISHLYADYGGKPA-LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFLFA-----DTIKNNL-LHGSNKyksDEDIVKACQLAESLD---FIQKFPDQfntmlekeganLSGGQGQRLSLAR 627
Cdd:PRK11248 76 FQNEGLLPwrnvqDNVAFGLqLAGVEK---MQRLEIAHQMLKKVGlegAEKRYIWQ-----------LSGGQRQRVGIAR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488434717 628 TFLKDPDIYIFDEATSALDSLTENKIMEhidLLTQ----HGKTVIIISH 672
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFTREQMQT---LLLKlwqeTGKQVLLITH 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
478-698 |
7.24e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 478 RIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDL-------- 549
Cdd:PRK11701 8 SVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 550 -RKNIGYVSQNTflfADTIKNNLLHGSN-----------KYksdEDIvkacqLAESLDFIQK----------FPDQFntm 607
Cdd:PRK11701 87 lRTEWGFVHQHP---RDGLRMQVSAGGNigerlmavgarHY---GDI-----RATAGDWLERveidaariddLPTTF--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 608 lekeganlSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMehiDLL----TQHGKTVIIISHKLSTIKN-ADN 682
Cdd:PRK11701 153 --------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLL---DLLrglvRELGLAVVIVTHDLAVARLlAHR 221
|
250
....*....|....*.
gi 488434717 683 IYVLNEGQIAENGTHD 698
Cdd:PRK11701 222 LLVMKQGRVVESGLTD 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
483-702 |
9.12e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 483 NFQYGFRS-----VVLKDINLNIKKGQKVAIVGESGSGKS----TIGKLLNR---YYTASE----GNIMIDNYIIDdidL 546
Cdd:PRK15134 10 NLSVAFRQqqtvrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYPSGDirfhGESLLHASEQT---L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 547 SDLRKN-IGYVSQNTFLFAD---TIKNNL-----LHGSNKYKSDEDIVKAC-------QLAESLdfiQKFPDQfntmlek 610
Cdd:PRK15134 87 RGVRGNkIAMIFQEPMVSLNplhTLEKQLyevlsLHRGMRREAARGEILNCldrvgirQAAKRL---TDYPHQ------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 611 eganLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQH-GKTVIIISHKLSTIKN-ADNIYVLNE 688
Cdd:PRK15134 157 ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQN 232
|
250
....*....|....
gi 488434717 689 GQIAENGTHDELIH 702
Cdd:PRK15134 233 GRCVEQNRAATLFS 246
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
477-695 |
9.53e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIdlsdLRKN-IGY 555
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 556 VSQNT---FLFADTIKNNLLHGSNKY--------KSDEDIVKACqLAESldfiqkfpdqfnTMLE---KEGANLSGGQGQ 621
Cdd:PRK15056 83 VPQSEevdWSFPVLVEDVVMMGRYGHmgwlrrakKRDRQIVTAA-LARV------------DMVEfrhRQIGELSGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 622 RLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGQIAENG 695
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
166-427 |
1.24e-09 |
|
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: 59.96 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 166 AFISLFINIVGIVGA-LYFKLLTDHIIPSNV------LKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKD 238
Cdd:cd18780 1 GTIALLVSSGTNLALpYFFGQVIDAVTNHSGsggeeaLRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 239 YFYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSPLLLLITIIFIPCFIICSY 317
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSsDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 318 TLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKLGR--------FSNIqltVN 389
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKE----VSRYSEKINESYLLGKklarasggFNGF---MG 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 488434717 390 NFLKLTISLViLWLGSYLVMTDSMTLGSLLAFNALTIY 427
Cdd:cd18780 234 AAAQLAIVLV-LWYGGRLVIDGELTTGLLTSFLLYTLT 270
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
166-424 |
1.76e-09 |
|
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: 59.43 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 166 AFISLFINIVGIVGA-LYFKLLTDHIipSNVLKNLHIISFGILLLY----IINALINYLRFQLILHLSLKIDVNLMKDYF 240
Cdd:cd18582 1 ALLLLVLAKLLNVAVpFLLKYAVDAL--SAPASALLAVPLLLLLAYglarILSSLFNELRDALFARVSQRAVRRLALRVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 241 YHVLHLPMNFFDTRKSGEiLQRFMD--TSKIREALSSSTVTLLVDTF-MIIIGAILLYMQSPLLLLITIIFIPCFIICSY 317
Cdd:cd18582 79 RHLHSLSLRFHLSRKTGA-LSRAIErgTRGIEFLLRFLLFNILPTILeLLLVCGILWYLYGWSYALITLVTVALYVAFTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 318 TLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDdrfYIgTTKFNGIIENLLKLGRFSNIQLTVNNF---LKL 394
Cdd:cd18582 158 KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEE---YE-AERYDKALAKYEKAAVKSQTSLALLNIgqaLII 233
|
250 260 270
....*....|....*....|....*....|.
gi 488434717 395 TISL-VILWLGSYLVMTDSMTLGSLLAFNAL 424
Cdd:cd18582 234 SLGLtAIMLLAAQGVVAGTLTVGDFVLVNTY 264
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
492-690 |
1.99e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTigkLLNRYYTASEGNIMIDNYIIDDIDLS-DLRKNIGYVSQNTFLFAD-TIKN 569
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKST---LLNALAGRIQGNNFTGTILANNRKPTkQILKRTGFVTQDDILYPHlTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 570 NLLHGS-----NKYKSDEDIVkacqLAESLDFIQKFPDQFNTMLEKEGA-NLSGGQGQRLSLARTFLKDPDIYIFDEATS 643
Cdd:PLN03211 160 TLVFCSllrlpKSLTKQEKIL----VAESVISELGLTKCENTIIGNSFIrGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488434717 644 ALDSLTENKIMEHIDLLTQHGKTVIIISHKLST--IKNADNIYVLNEGQ 690
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
477-703 |
2.64e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTA-----SEGNIMIDNYIIDDIDLSDLRK 551
Cdd:PRK09984 5 IRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdksagSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 552 N---IGYVSQNTFLFAD-TIKNNLLHGS----------NKYKSDEDIVKACQLAESLDFIQkFPDQfntmlekEGANLSG 617
Cdd:PRK09984 84 SranTGYIFQQFNLVNRlSVLENVLIGAlgstpfwrtcFSWFTREQKQRALQALTRVGMVH-FAHQ-------RVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 618 GQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENG 695
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrDINQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
|
250
....*....|...
gi 488434717 696 T-----HDELIHL 703
Cdd:PRK09984 236 SsqqfdNERFDHL 248
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
495-700 |
2.89e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.35 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 495 DINLNIKKGQKVAIVGESGSGKS----TIGKLL--NRYYTASEGNIMIDNYIIDDIDLSDLRknigyVSQNTFLFAD--- 565
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGRIGGSATFNGREILNLPEKELNKLR-----AEQISMIFQDpmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 566 ------TIKNNL-----LH-GSNKYKSDEDIVK---ACQLAESLDFIQKFPDQFntmlekeganlSGGQGQRLSLARTFL 630
Cdd:PRK09473 109 slnpymRVGEQLmevlmLHkGMSKAEAFEESVRmldAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 631 KDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVII-ISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
492-703 |
3.00e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGYVSQN---TFLFAD-T 566
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPEDrkgEGLVLDlS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 567 IKNNLL------HGSNKYKSDEDIVKACQ-LAESLDfIqKFPDqfntmLEKEGANLSGGQGQRLSLARTFLKDPDIYIFD 639
Cdd:COG1129 347 IRENITlasldrLSRGGLLDRRRERALAEeYIKRLR-I-KTPS-----PEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 640 EATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIA-----ENGTHDELIHL 703
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELlGLSDRILVMREGRIVgeldrEEATEEAIMAA 489
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
477-695 |
3.76e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.47 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFRSVvLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYV 556
Cdd:PRK09536 4 IDVSDLSVEFGDTTV-LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 557 SQNTFL-FADTIKNNLLHGSNKYKS-----DEDIVKACQLAESLDFIQKFPDQFNTmlekegaNLSGGQGQRLSLARTFL 630
Cdd:PRK09536 83 PQDTSLsFEFDVRQVVEMGRTPHRSrfdtwTETDRAAVERAMERTGVAQFADRPVT-------SLSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 631 KDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLS-TIKNADNIYVLNEGQIAENG 695
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
477-691 |
3.78e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGFrSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIG-- 554
Cdd:PRK11147 4 ISIHGAWLSFSD-APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEgt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 ---YVSQNTFLFADTIKN--NLLHGSNKYKSDEDIVKACQLAESLDF--IQKFPDQFNTMLEKEG-------ANLSGGQG 620
Cdd:PRK11147 83 vydFVAEGIEEQAEYLKRyhDISHLVETDPSEKNLNELAKLQEQLDHhnLWQLENRINEVLAQLGldpdaalSSLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 621 QRLSLARTFLKDPDIYIFDEATSALDsltenkiMEHIDLLTQHGKT----VIIISHKLSTIKN-ADNIYVLNEGQI 691
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLD-------IETIEWLEGFLKTfqgsIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
500-686 |
5.20e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 500 IKKGQKVAIVGESGSGKSTIGKLLN--------------------RYYTASEgnimidnyiiDDIDLSDLRKN------- 552
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgelipnlgdyeeepswdevlKRFRGTE----------LQNYFKKLYNGeikvvhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 IGYVSQNTFLFADTIKNnLLHGSNKYKSDEDIVKACQLAESLDfiqkfpdqfntmleKEGANLSGGQGQRLSLARTFLKD 632
Cdd:PRK13409 166 PQYVDLIPKVFKGKVRE-LLKKVDERGKLDEVVERLGLENILD--------------RDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 633 PDIYIFDEATSALDsltenkIMEHIDL------LTQhGKTVIIISHKLSTIKN-ADNIYVL 686
Cdd:PRK13409 231 ADFYFFDEPTSYLD------IRQRLNVarlireLAE-GKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
493-716 |
6.83e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.13 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVsQNTFLfadtikNNLL 572
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI-ENIEL------KGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 573 HGSNKYKSDEDIVKACQLAEsldfIQKFPDQfntmlekEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENK 652
Cdd:PRK13545 113 MGLTKEKIKEIIPEIIEFAD----IGKFIYQ-------PVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 653 IMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELI-HLNGIYKNLWQLQMK 716
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVdHYDEFLKKYNQMSVE 247
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
615-704 |
8.08e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 59.46 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 615 LSGGQGQRLSLARTFL---KDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADniYVLNEGqi 691
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVAD--YVLELG-- 885
|
90 100
....*....|....*....|...
gi 488434717 692 AENG----------THDELIHLN 704
Cdd:PRK00635 886 PEGGnlggyllascSPEELIHLH 908
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
475-678 |
8.39e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.99 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 475 NNIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIdnyiiddidlsDLRKNIG 554
Cdd:TIGR00954 450 NGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK-----------PAKGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFADTIKNNLLH--GSNKYK----SDEDIVKACQLAesldfiqkfpdQFNTMLEKEGA---------NLSGGQ 619
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIIYpdSSEDMKrrglSDKDLEQILDNV-----------QLTHILEREGGwsavqdwmdVLSGGE 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 620 GQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHidlLTQHGKTVIIISHKLSTIK 678
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL---CREFGITLFSVSHRKSLWK 643
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
607-686 |
1.09e-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: 56.61 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 607 MLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYV 685
Cdd:cd03236 132 VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYIHC 211
|
.
gi 488434717 686 L 686
Cdd:cd03236 212 L 212
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
608-683 |
1.15e-08 |
|
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: 56.11 E-value: 1.15e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 608 LEKEGANLSGGQGQRLSLARTFLKDPD--IYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNI 683
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHV 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
491-691 |
1.33e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGK-----STIGKLLNRYYTAS---EGNIMIdnyiiddidLSDLRKNIG----YVS- 557
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRtelamSVFGRSYGRNISGTvfkDGKEVD---------VSTVSDAIDaglaYVTe 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 ---QNTFLFADTIKNNL----LHG-SNKYKSDEDivKACQLAEslDFIQKFPDQFNTMLEKEGaNLSGGQGQRLSLARTF 629
Cdd:NF040905 345 drkGYGLNLIDDIKRNItlanLGKvSRRGVIDEN--EEIKVAE--EYRKKMNIKTPSVFQKVG-NLSGGNQQKVVLSKWL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 630 LKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKL-STIKNADNIYVLNEGQI 691
Cdd:NF040905 420 FTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELpELLGMCDRIYVMNEGRI 482
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
614-696 |
1.90e-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: 54.50 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 614 NLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHG-KTVIIISHKLSTIKNADNIYVLNEGQIA 692
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
....
gi 488434717 693 ENGT 696
Cdd:cd03222 151 VYGI 154
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
161-461 |
2.38e-08 |
|
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: 56.31 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 161 KLLFIAFISLFINivgivGALY--FKLLTDHII-------PSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKI 231
Cdd:cd18578 9 PLLLLGLIGAIIA-----GAVFpvFAILFSKLIsvfslpdDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 232 DVNLMKDYFYHVLHLPMNFFD--TRKSGEILQRFM-DTSKIREALSSSTVTLLVDTFMIIIGAIL--------------- 293
Cdd:cd18578 84 TRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLStDASDVRGLVGDRLGLILQAIVTLVAGLIIafvygwklalvglat 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 294 --LYMqspllllitiifipcfiICSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDrFYigtTKFNGI 371
Cdd:cd18578 164 vpLLL-----------------LAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDY-FL---EKYEEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 372 IENLLKLGR----FSNIQLTVNNFLKLTISLVILWLGSYLVMTDSMTLGSLL-AFNALtIYYLDPIERLINIQPTLQSSF 446
Cdd:cd18578 223 LEEPLKKGLrralISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFiVFMAL-IFGAQSAGQAFSFAPDIAKAK 301
|
330
....*....|....*
gi 488434717 447 VAARRIAEITDLETE 461
Cdd:cd18578 302 AAAARIFRLLDRKPE 316
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
473-672 |
2.58e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 473 FKNNIRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGnimidnyiidDIDLSDlRKN 552
Cdd:PRK15064 316 HRNALEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSE-NAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 IGYVSQ-NTFLFADTIknNLLHGSNKYKS---DEDIVKAC--QLAESLDFIQKFPDqfntmlekegaNLSGGQGQRLSLA 626
Cdd:PRK15064 384 IGYYAQdHAYDFENDL--TLFDWMSQWRQegdDEQAVRGTlgRLLFSQDDIKKSVK-----------VLSGGEKGRMLFG 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488434717 627 RTFLKDPDIYIFDEATSALDsltenkiMEHIDLLT----QHGKTVIIISH 672
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD-------MESIESLNmaleKYEGTLIFVSH 493
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
496-696 |
2.83e-08 |
|
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: 57.72 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 496 INLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIdLSDLRKNIGYVSQNTFLFAD-TIKNNLL-H 573
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN-LDAVRQSLGMCPQHNILFHHlTVAEHILfY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 574 GSNKYKSDEDivkaCQLaesldfiqkfpdQFNTMLE---------KEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSA 644
Cdd:TIGR01257 1028 AQLKGRSWEE----AQL------------EMEAMLEdtglhhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 645 LDSLTENKIMehiDLLTQH--GKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGT 696
Cdd:TIGR01257 1092 VDPYSRRSIW---DLLLKYrsGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
475-672 |
3.95e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 475 NNIRIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMID--NYIIDDIDLSDLRKN 552
Cdd:PRK10938 259 PRIVLNNGVVSYNDR-PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLfgRRRGSGETIWDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 IGYVSQNTFL---FADTIKNNLLHGsnkYKSDEDIVKACQlaeslDFIQKFPDQFNTML--EKEGAN-----LSGGQgQR 622
Cdd:PRK10938 338 IGYVSSSLHLdyrVSTSVRNVILSG---FFDSIGIYQAVS-----DRQQKLAQQWLDILgiDKRTADapfhsLSWGQ-QR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488434717 623 LSL-ARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKT-VIIISH 672
Cdd:PRK10938 409 LALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
492-672 |
4.08e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidlsdlrkNIGYVSQNTFLFAD-TIKNN 570
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI-----------KVGYLPQEPQLDPTkTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LLHGsnkyksdedivkacqLAESLDFIQKF----------PDQFNTMLEKEG---------------------------- 612
Cdd:TIGR03719 89 VEEG---------------VAEIKDALDRFneisakyaepDADFDKLAAEQAelqeiidaadawdldsqleiamdalrcp 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 613 ------ANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSltenkimEHIDLLTQHGK----TVIIISH 672
Cdd:TIGR03719 154 pwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERHLQeypgTVVAVTH 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
491-672 |
5.52e-08 |
|
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: 53.65 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGnimidnyiiddidlsDLRKNIGYVSQNTflfaDTIKNN 570
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG---------------RVLLNGGPLDFQR----DSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LLhgsnkYKSDEDIVKACQLA-ESLDFIQKF--PDQFNTMLEKEG---------ANLSGGQGQRLSLARTFLKDPDIYIF 638
Cdd:cd03231 75 LL-----YLGHAPGIKTTLSVlENLRFWHADhsDEQVEEALARVGlngfedrpvAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....
gi 488434717 639 DEATSALDSLTENKIMEHIDLLTQHGKTVIIISH 672
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
476-702 |
5.56e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimidnyiiddIDLSDLRKN--- 552
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE----------IWIGGRVVNele 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 553 -----IGYVSQNTFLFAD-TIKNNL-----LHGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekeganLSGGQGQ 621
Cdd:PRK11650 73 padrdIAMVFQNYALYPHmSVRENMayglkIRGMPKAEIEERVAEAARILELEPLLDRKPRE-----------LSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 622 RLSLARTFLKDPDIYIFDEATSALDSltenKIMEHIDLLTQH-----GKTVIIISH-KLSTIKNADNIYVLNEGQIAENG 695
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDA----KLRVQMRLEIQRlhrrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIG 217
|
....*..
gi 488434717 696 THDELIH 702
Cdd:PRK11650 218 TPVEVYE 224
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
162-299 |
6.21e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 54.82 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 162 LLFIAFISLFINIVGIVGALYFKLLTDHIIPSNVLKNLH--IISFGILLLYIInaLINYLRFQLILHLSLKIDVNLMKDY 239
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYylGVYAALLVLASV--LLVLLRWLLFVLAGLRASRRLHDKL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488434717 240 FYHVLHLPMNFFDTRKSGEILQRF-MDTSKIREALSSSTVTLLVDTFMIIIGAILLYMQSP 299
Cdd:cd18580 79 LRSVLRAPMSFFDTTPSGRILNRFsKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP 139
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
491-672 |
7.62e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 53.13 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRkNIGYVSQntflfADTIKNN 570
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGH-----LPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LlhgsnkyksdedivkacQLAESLDFIQKF--PDQFN--TMLEKEG---------ANLSGGQGQRLSLARTFLKDPDIYI 637
Cdd:TIGR01189 88 L-----------------SALENLHFWAAIhgGAQRTieDALAAVGltgfedlpaAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 488434717 638 FDEATSALDSLTENKIMEHIDLLTQHGKTVIIISH 672
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
240-452 |
8.29e-08 |
|
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: 54.40 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 240 FYHVLHLPMNFFDTRKSGEILQRFM-DTSKIREALSSStVTLLVDTFM-IIIGAILLYMQSPLLLLITIIFIPCFIICSY 317
Cdd:cd18589 76 FAAVLRQEIAFFDSNQTGDIVSRVTtDTEDMSESLSEN-LSLLMWYLArGLFLFIFMLWLSPKLALLTALGLPLLLLVPK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 318 TLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKLGRFSNIQLTVN----NFLK 393
Cdd:cd18589 155 FVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGE----AQRYRQRLQKTYRLNKKEAAAYAVSmwtsSFSG 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 394 LTISLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18589 231 LALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
488-702 |
9.04e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 9.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 488 FRSVvlKDINLNIKKGQKVAIVGESGSGKS----TIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGyvSQNTFLF 563
Cdd:PRK11022 20 FRAV--DRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVG--AEVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 564 AD---------TIKNNLLH-------GSNKYKSDE--DIVKACQLAESLDFIQKFPDQfntmlekeganLSGGQGQRLSL 625
Cdd:PRK11022 96 QDpmtslnpcyTVGFQIMEaikvhqgGNKKTRRQRaiDLLNQVGIPDPASRLDVYPHQ-----------LSGGMSQRVMI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 626 ARTFLKDPDIYIFDEATSALDSLTENKIME-HIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDELIH 702
Cdd:PRK11022 165 AMAIACRPKLLIADEPTTALDVTIQAQIIElLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
613-700 |
1.03e-07 |
|
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: 55.22 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 613 ANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI 691
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
....*....
gi 488434717 692 AENGTHDEL 700
Cdd:TIGR02633 482 KGDFVNHAL 490
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
491-672 |
1.25e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.57 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNimiDNYIIDDIDLSDLRKNIGYVSQntflfADTIKNN 570
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGT---IKLDGGDIDDPDVAEACHYLGH-----RNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LlhgsnkyksdedivkacQLAESLDFIQKFPDQFNTMLEK-------------EGANLSGGQGQRLSLARTFLKDPDIYI 637
Cdd:PRK13539 88 L-----------------TVAENLEFWAAFLGGEELDIAAaleavglaplahlPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 488434717 638 FDEATSALDS----LTENKIMEHidlLTQHGkTVIIISH 672
Cdd:PRK13539 151 LDEPTAALDAaavaLFAELIRAH---LAQGG-IVIAATH 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
493-701 |
1.37e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGYVSQNTFLFAD-TIKNN 570
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVPEmTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LLHGsnkyksdedivkacQLAESLDFIQKFPDQFNTMLEKEG-----------ANLSGGQGQRLSLARTFLKDPDIYIFD 639
Cdd:PRK11288 100 LYLG--------------QLPHKGGIVNRRLLNYEAREQLEHlgvdidpdtplKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 640 EATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAE------NGTHDELI 701
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRDQLV 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
492-700 |
2.53e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNI--MIDNYIIDDIDLSDLRKNIGYVSQN---TFLFADT 566
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwQGKPLDYSKRGLLALRQQVATVFQDpeqQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 567 IKNNLLHGSNKYKSDEDIVKACQLAESLDFIQKFPDQfntmlekEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALD 646
Cdd:PRK13638 96 DSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQ-------PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 647 SLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
493-690 |
2.73e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGYVSQNTFLFAD-TIKNN 570
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LLHGSNKYKS---DEDIV----KAcqLAESLDfIQKFPdqfntmlEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATS 643
Cdd:PRK10982 94 MWLGRYPTKGmfvDQDKMyrdtKA--IFDELD-IDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488434717 644 aldSLTEnKIMEH----IDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQ 690
Cdd:PRK10982 164 ---SLTE-KEVNHlftiIRKLKERGCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
477-702 |
2.76e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.39 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 477 IRIENVNFQYGfrSVVLKDINLNIKKGQKVAIVGESGSGKS-TIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLR-KNIG 554
Cdd:PRK10418 5 IELRNIALQAA--QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRgRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 555 YVSQNTFLFADTIKNNLLHGSNKYK-----SDEDIVKACQLAESLD----FIQKFPDQfntmlekeganLSGGQGQRLSL 625
Cdd:PRK10418 83 TIMQNPRSAFNPLHTMHTHARETCLalgkpADDATLTAALEAVGLEnaarVLKLYPFE-----------MSGGMLQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 626 ARTFLKDPDIYIFDEATSALDSLTENKIMEHI-DLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIAENGTHDELIH 702
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLeSIVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
615-684 |
2.99e-07 |
|
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: 50.82 E-value: 2.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 615 LSGGQGQRLSLARTF----LKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNIY 684
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
615-701 |
3.02e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 615 LSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVI-IISHKLSTI-KNADNIYVLNEGQIA 692
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDLQMLsQWADKINVLYCGQTV 238
|
....*....
gi 488434717 693 ENGTHDELI 701
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
481-681 |
4.49e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.10 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 481 NVNFQYGfRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIdLSDLRKNIGYVSQNT 560
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD-LCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 561 FLFAD-TIKNNLLHGSNKYKSDEDIVKACQLAeSLDFIQKFPDQFntmlekeganLSGGQGQRLSLARTFLKDPDIYIFD 639
Cdd:PRK13540 84 GINPYlTLRENCLYDIHFSPGAVGITELCRLF-SLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488434717 640 EATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNAD 681
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
502-677 |
6.40e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 502 KGQKVAIVGESGSGKSTIGKLLNRYYTASegnimidnyiiddidlsdlrknigyvsqntflfadtiknnllHGSNKYKSD 581
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP------------------------------------------GGGVIYIDG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 582 EDIvkacqlaesldFIQKFPDQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLT 661
Cdd:smart00382 39 EDI-----------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180
....*....|....*....|..
gi 488434717 662 ------QHGKTVIIISHKLSTI 677
Cdd:smart00382 108 llllksEKNLTVILTTNDEKDL 129
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
610-700 |
6.95e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 610 KEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNE 688
Cdd:NF000106 140 RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDR 219
|
90
....*....|..
gi 488434717 689 GQIAENGTHDEL 700
Cdd:NF000106 220 GRVIADGKVDEL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
613-700 |
6.97e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 613 ANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI 691
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
....*....
gi 488434717 692 AENGTHDEL 700
Cdd:PRK13549 484 KGDLINHNL 492
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
165-452 |
7.51e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 51.34 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 165 IAFISLFInIVGIVGALYFKLLTDHIIPSNVLKN----LHIISFGILLLYIINALINYLRF--------QLILHLSLKId 232
Cdd:cd18546 1 LALALLLV-VVDTAASLAGPLLVRYGIDSGVRAGdlgvLLLAAAAYLAVVLAGWVAQRAQTrltgrtgeRLLYDLRLRV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 233 vnlmkdyFYHVLHLPMNFFDTRKSGEILQRfMdTSKIrEALSS----STVTLLVDTF-MIIIGAILLYMqSPLLLLITII 307
Cdd:cd18546 79 -------FAHLQRLSLDFHERETSGRIMTR-M-TSDI-DALSEllqtGLVQLVVSLLtLVGIAVVLLVL-DPRLALVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 308 FIPCFIICSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLlklgRFSNIQLT 387
Cdd:cd18546 148 ALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRN----AERFAELSDDY----RDARLRAQ 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 388 VNN-----FLKLTISL---VILWLGSYLVMTDSMTLGSLLAFnaltIYYL----DPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18546 220 RLVaiyfpGVELLGNLataAVLLVGAWRVAAGTLTVGVLVAF----LLYLrrffAPIQQLSQVFDSYQQARAALEKI 292
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
615-683 |
8.30e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.72 E-value: 8.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 615 LSGGQGQRLSLARtFLKDPD----IYIFDEATSAL---DsltENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNI 683
Cdd:COG0178 827 LSGGEAQRVKLAS-ELSKRStgktLYILDEPTTGLhfhD---IRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWI 898
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
493-691 |
8.65e-07 |
|
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: 50.34 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNryytasegnimidnyiiddidlSDLRKNI---GYVSQNTFLFADTikN 569
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA----------------------NRTEGNVsveGDIHYNGIPYKEF--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 570 NLLHGSNKYKSDEDI-VKACQLAESLDFIQKFpdQFNTMLEKeganLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSL 648
Cdd:cd03233 79 EKYPGEIIYVSEEDVhFPTLTVRETLDFALRC--KGNEFVRG----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488434717 649 TENKIMEHIDLLTQHGKTVIIIShkLS-----TIKNADNIYVLNEGQI 691
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTFVS--LYqasdeIYDLFDKVLVLYEGRQ 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
465-691 |
9.49e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 465 YTSKQPYTFKNNI-RIENVNFQYGFRsVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNImidnyiidd 543
Cdd:PRK10636 300 FSFRAPESLPNPLlKMEKVSAGYGDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 544 idlsDLRKNI--GYVSQNT--FLFADtiKNNLLHGSNkyksdediVKACQLAESL-DFIQKFPDQFNTMLEkEGANLSGG 618
Cdd:PRK10636 370 ----GLAKGIklGYFAQHQleFLRAD--ESPLQHLAR--------LAPQELEQKLrDYLGGFGFQGDKVTE-ETRRFSGG 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 619 QGQRLSLARTFLKDPDIYIFDEATSALD-----SLTEnkimehidLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI 691
Cdd:PRK10636 435 EKARLVLALIVWQRPNLLLLDEPTNHLDldmrqALTE--------ALIDFEGALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
492-696 |
1.04e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRY--YTASEGNIMIDNYIIDDIDlSDLRKNIGY------------VS 557
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIflafqypieipgVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 QNTFLfadtiknNLLHGSNKYKSDEDIVKACQLAESLDFIQKFPDQFNTMLEK---EGanLSGGQGQRLSLARTFLKDPD 634
Cdd:CHL00131 101 NADFL-------RLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRnvnEG--FSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 635 IYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHK---LSTIKnADNIYVLNEGQIAENGT 696
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYIK-PDYVHVMQNGKIIKTGD 235
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
615-683 |
1.51e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 51.61 E-value: 1.51e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 615 LSGGQGQRLSLARTFLKDPD---IYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNADNI 683
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWI 902
|
|
| Peptidase_C39A |
cd02549 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
14-126 |
2.21e-06 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.
Pssm-ID: 239109 [Multi-domain] Cd Length: 141 Bit Score: 47.79 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 14 CGPTCLAMISQFYGKRVSIPRLREYAKTDKLGTNLYG-----LVQAG-KKIGieLTGVKADSFDDLKQaQL----PVMVH 83
Cdd:cd02549 7 CGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKDGYGtypkpIVSAAaRKYG--LVVRPLTGLLALLR-QLaaghPVIVS 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488434717 84 IINQQGYD---HYIIIEKI-KNNTLYIVDPAKGK-YKLSSTEFGKYWT 126
Cdd:cd02549 84 VNLGVSITpsgHAMVVIGYdRKGNVYVNDPGGGRrLVVSFDEFEKAWK 131
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
206-421 |
2.70e-06 |
|
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: 49.85 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 206 ILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRFmdTSKIREALSS--STVTLLVD 283
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRL--TADVQEFKSSfkQCVSQGLR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 284 TFMIIIGAIL-LYMQSPLLLLITIIFIPCFIICSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSED---D 359
Cdd:cd18574 126 SVTQTVGCVVsLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDrelE 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 360 RFYIGTTKFNGIIENL-LKLGRF---SNiqLTVNNflkltISLVILWLGSYLVMTDSMTLGSLLAF 421
Cdd:cd18574 206 LYEEEVEKAAKLNEKLgLGIGIFqglSN--LALNG-----IVLGVLYYGGSLVSRGELTAGDLMSF 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
614-699 |
3.32e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 614 NLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKL-STIKNADNIYVLNEGQIA 692
Cdd:PRK11288 396 NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIA 475
|
....*..
gi 488434717 693 ENGTHDE 699
Cdd:PRK11288 476 GELAREQ 482
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
493-690 |
3.43e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTAS--EGNIMIDNYIIDDIDLSDLRKN-----------IGYVS-- 557
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALgiviihqelalIPYLSia 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 QNTFLFADTIKNNLLHGSNKYKSDEDIVKACQLAESldfiqkfPDqfnTMLEKEGAnlsgGQGQRLSLARTFLKDPDIYI 637
Cdd:NF040905 97 ENIFLGNERAKRGVIDWNETNRRARELLAKVGLDES-------PD---TLVTDIGV----GKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 638 FDEATSAL---DSlteNKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQ 690
Cdd:NF040905 163 LDEPTAALneeDS---AALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGR 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
493-701 |
6.55e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSD-LRKNIGYVSQNT----FLFADTI 567
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 568 KNNLLHGSNKYKSDedivKACQL---AESL---DFIQKFPDQFNTMlEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEA 641
Cdd:PRK10762 348 KENMSLTALRYFSR----AGGSLkhaDEQQavsDFIRLFNIKTPSM-EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 642 TSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQI-----AENGTHDELI 701
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
486-672 |
7.56e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 486 YGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIiddidlsdlrkNIGYVSQNTFLFAD 565
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI-----------KVGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 566 -TIKNNLLHGsnkyksdedivkacqLAESLDFIQKF----------PDQFNTMLEKEG---------------------- 612
Cdd:PRK11819 85 kTVRENVEEG---------------VAEVKAALDRFneiyaayaepDADFDALAAEQGelqeiidaadawdldsqleiam 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488434717 613 ------------ANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSltenkimEHIDLLTQHGK----TVIIISH 672
Cdd:PRK11819 150 dalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLEQFLHdypgTVVAVTH 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
615-692 |
1.42e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 1.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 615 LSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQIA 692
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEIS 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
481-677 |
1.93e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 481 NVNFQYGFRS---VVLKDINLNIKKGQKVAIVGESGSGKSTigkLLN----RYYTA--SEGNIMIDNYIIDdidlSDLRK 551
Cdd:TIGR00956 764 NLTYEVKIKKekrVILNNVDGWVKPGTLTALMGASGAGKTT---LLNvlaeRVTTGviTGGDRLVNGRPLD----SSFQR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 552 NIGYVSQNTF-LFADTIKNNLlhgsnKYKSDEDIVKACQLAESLDFIQKFPDqfntMLEKE----------GANLSGGQG 620
Cdd:TIGR00956 837 SIGYVQQQDLhLPTSTVRESL-----RFSAYLRQPKSVSKSEKMEYVEEVIK----LLEMEsyadavvgvpGEGLNVEQR 907
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 621 QRLSLARTFLKDPDIYIF-DEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTI 677
Cdd:TIGR00956 908 KRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAI 965
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
492-697 |
1.94e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLL--NRYYTASEGNIMIDNYIIDDIDLSDlRKNIGY------------VS 557
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPED-RAGEGIfmafqypveipgVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 558 QNTFLfadtikNNLLHGSNKYKSDEDIVKAcqlaESLDFIQ------KFPDQFNTMLEKEGanLSGGQGQRLSLARTFLK 631
Cdd:PRK09580 95 NQFFL------QTALNAVRSYRGQEPLDRF----DFQDLMEekiallKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488434717 632 DPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHK---LSTIKnADNIYVLNEGQIAENGTH 697
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDF 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
615-693 |
2.72e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 615 LSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNA-DNIYVLNEGQIAE 693
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| Peptidase_C39_2 |
pfam13529 |
Peptidase_C39 like family; |
3-109 |
5.30e-05 |
|
Peptidase_C39 like family;
Pssm-ID: 379241 [Multi-domain] Cd Length: 139 Bit Score: 43.59 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 3 IKFIRQYDEKD--CGPTCLAMISQFYGKRVS-----------------IPRLREYAKTDKLGTNLYGLVQAGKKIGIELT 63
Cdd:pfam13529 2 VPYYNQLDELPngCGPTSLAMVLSYLGITVTqdelakeigtnpdgnpnTGFVGNPYDKSGYGVYNPPIVALAEKYGLKVT 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 64 GVKADSFDDLKQ---AQLPVMVHIINQQGYD-------HYIIIE--KIKNNTLYIVDP 109
Cdd:pfam13529 82 DITGSSFDEVIRlldAGIPVVVSTTTFGPLNyyftssgHLVVIVgyDDKGDYVYVNDP 139
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
447-700 |
6.21e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.17 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 447 VAARRIAEITDLE-------TETELYTSKQPYTFKNNI-RIENVNFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKST 518
Cdd:COG3845 220 VGTVDTAETSEEElaelmvgREVLLRVEKAPAEPGEVVlEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 519 IGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKN-IGYVS---QNTFLFAD-TIKNNLL---HGSNKYKS----DEDIVK 586
Cdd:COG3845 300 LAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPedrLGRGLVPDmSVAENLIlgrYRRPPFSRggflDRKAIR 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 587 AcqLAESLdfIQKF----PDQFNTMlekegANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQ 662
Cdd:COG3845 380 A--FAEEL--IEEFdvrtPGPDTPA-----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD 450
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488434717 663 HGKTVIIISHKLSTIKN-ADNIYVLNEGQI-----AENGTHDEL 700
Cdd:COG3845 451 AGAAVLLISEDLDEILAlSDRIAVMYEGRIvgevpAAEATREEI 494
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
615-707 |
7.34e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 615 LSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIA- 692
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAg 471
|
90
....*....|....*....
gi 488434717 693 ----ENGTHDELIHLNGIY 707
Cdd:PRK10982 472 ivdtKTTTQNEILRLASLH 490
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
491-696 |
7.76e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 491 VVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNY-----------IIDDIDLSDLRKNIGYVSQN 559
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTgdvtlngeplaAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 560 TFLF-ADTIKnnLL----H----GSNKYKSDEDIVKACQLAESldfiqkfpdqfNTMLEKEGANLSGGQGQRLSLARTFL 630
Cdd:PRK13547 95 AFAFsAREIV--LLgrypHarraGALTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 631 K---------DPDIYIFDEATSALDSLTENKIMEHIDLLTQHGKT-VIIISHKLS-TIKNADNIYVLNEGQIAENGT 696
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
216-358 |
1.20e-04 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; 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: 350044 [Multi-domain] Cd Length: 324 Bit Score: 44.79 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 216 INYLRFQLILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRFMDTSKIREALSSSTVTLLVDTFMIIIGAILLY 295
Cdd:cd18600 86 MGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVV 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488434717 296 --MQSPLLLLITIIFIPCFIICSYTLRKpFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSED 358
Cdd:cd18600 166 siLQPYIFLATVPVIIAFIVLRAYFLRT-SQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQP 229
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
192-294 |
2.32e-04 |
|
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: 43.85 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 192 PSNVLKNLHIISFGILLLYIInaLINYLRFQLILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRF-MDTSKIR 270
Cdd:cd18601 53 IEDLDRDFNLGIYAGLTAATF--VFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFsKDIGHLD 130
|
90 100
....*....|....*....|....
gi 488434717 271 EALsSSTVTLLVDTFMIIIGAILL 294
Cdd:cd18601 131 DLL-PLTFLDFLQLLLQVVGVVLL 153
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
493-703 |
2.50e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRK-NIGYVSQNTFLFAD-TIKNN 570
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEaGIGIIHQELNLIPQlTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 571 LLHGSNKYKSDEDIVKACQLAESLDFIQKFPDQFNTmlEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSAL-DSLT 649
Cdd:PRK10762 100 IFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSS--DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 650 E---NKIMEhidlLTQHGKTVIIISHKLSTI-KNADNIYVLNEGQ-IAENG----THDELIHL 703
Cdd:PRK10762 178 EslfRVIRE----LKSQGRGIVYISHRLKEIfEICDDVTVFRDGQfIAEREvadlTEDSLIEM 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
497-700 |
3.68e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 497 NLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQ--NTFLF----------- 563
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQrnNTDMLspgeddtgrtt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 564 ADTIKNNLlhgsnkyksdEDIVKACQLAESLdfiqkfpdQFNTMLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATS 643
Cdd:PRK10938 103 AEIIQDEV----------KDPARCEQLAQQF--------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 644 ALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDEL 700
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
166-421 |
3.88e-04 |
|
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: 43.07 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 166 AFISLFInivGIVGALYFKLLTDHIIPSNVL-KNLHIISFGIL---LLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18784 1 AFFFLLA---AAVGEIFIPYYTGQVIDGIVIeKSQDKFSRAIIimgLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRFM-DTSKIrealsSSTVTLLVDTF---MIIIGAILLYM--QSPLLLLITIIFIPCFIIC 315
Cdd:cd18784 78 SIVSQEIGFFDTVKTGDITSRLTsDTTTM-----SDTVSLNLNIFlrsLVKAIGVIVFMfkLSWQLSLVTLIGLPLIAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 316 SYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLT 395
Cdd:cd18784 153 SKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELA 232
|
250 260
....*....|....*....|....*.
gi 488434717 396 ISLVILWLGSYLVMTDSMTLGSLLAF 421
Cdd:cd18784 233 LTVSTLYYGGHLVITGQISGGNLISF 258
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
613-672 |
4.74e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.10 E-value: 4.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488434717 613 ANLSGGQGQRLSLARTFLKDPDIYIFDEATSALD----SLTENKIMEHidllTQHGKTVIIISH 672
Cdd:PRK13538 128 RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvARLEALLAQH----AEQGGMVILTTH 187
|
|
| Peptidase_C70 |
pfam12385 |
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ... |
14-121 |
5.08e-04 |
|
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.
Pssm-ID: 403550 [Multi-domain] Cd Length: 143 Bit Score: 40.91 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 14 CGPTCLAMI-SQFYGKRVSIPRL-REYAKTDKLGTNLYG--LVQAGKKIGIELTGVKADSFDDLKQAQL-----PVMVHI 84
Cdd:pfam12385 18 CWAASASMIaGYRGQKPIDPSEIaALVPGWSQYDTGLNGpeDIALAEKWGLGNVPEPPQSYSIDALVKLlraygPLWCAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488434717 85 INQQGYD-HYIIIEKIKNN--TLYIVDPAKG-KYKLSSTEF 121
Cdd:pfam12385 98 AWPGGFVgHAIVLTGIDEDgtPVYYHDPWSGpRREVSLASF 138
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
160-288 |
5.65e-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: 42.55 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 160 GKLLFIAFISLFINIVGIV---------------GALYFKLLTDHIIPSNVLKNLHI-----ISFGILLLYIINALINYL 219
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTvfsdwwlsywlkqgsGNTTNNVDNSTVDSGNISDNPDLnfyqlVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488434717 220 RFQLIlhlSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRF---MDTSKIReaLSSSTVTLLVDTFMII 288
Cdd:cd18599 81 VFVKV---TLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFskdLDEVDVR--LPFTLENFLQNVLLVV 147
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
202-294 |
7.46e-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: 42.08 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 202 ISFGILllyiiNALINYLRFQLILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRFmdtSKIREALSSS---TV 278
Cdd:cd18606 42 AGLGVL-----QAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRF---SKDTDVLDNElpdSL 113
|
90
....*....|....*.
gi 488434717 279 TLLVDTFMIIIGAILL 294
Cdd:cd18606 114 RMFLYTLSSIIGTFIL 129
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
493-701 |
8.78e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 493 LKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDLSDLRKNIGYVSQNTFlfadtikNNLL 572
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIEF-------KMLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 573 HGSNKYKSDEDIVKACQLAESLDFIQKFPDQFntmlekeganlSGGQGQRLSLARTFLKDPDIYIFDEATSALDSLTENK 652
Cdd:PRK13546 113 MGFKRKEIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488434717 653 IMEHIDLLTQHGKTVIIISHKLSTIKN-ADNIYVLNEGQIAENGTHDELI 701
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
483-680 |
1.13e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 483 NFQYGFRSVVLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDIDlsdlRKNIGYVSQNTFL 562
Cdd:PRK13541 6 QLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHNLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 563 FAD-TIKNNLLHGSNKYKSDEDIVKACQLAESLDFiqkfpdqfntmLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEA 641
Cdd:PRK13541 82 KLEmTVFENLKFWSEIYNSAETLYAAIHYFKLHDL-----------LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 488434717 642 TSALDSLTENKIMEHIDLLTQHGKTVIIISHKLSTIKNA 680
Cdd:PRK13541 151 ETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKSA 189
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
240-447 |
2.20e-03 |
|
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: 40.67 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 240 FYHVLHLPMNFFDTRKSGEILqRFMD--TSKIREALSSSTVTL---LVDTFMIIIgaILLYMQSPLLLLITIIFIPCFII 314
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVV-RIMDrgTESANTLLSYLVFYLvptLLELIVVSV--VFAFHFGAWLALIVFLSVLLYGV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 315 CSYTLRKPFEKYNQKVAEKDAELSSYLIESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKLGRFSNIQLTVNNFLKL 394
Cdd:cd18560 155 FTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYE----VDRYGEAVKEYQKSSVKVQASLSLLNVGQQ 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 395 TI----SLVILWLGSYLVMTDSMTLGSLLAFNALTIYYLDPIERLINIQPTLQSSFV 447
Cdd:cd18560 231 LIiqlgLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLT 287
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
343-452 |
2.38e-03 |
|
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: 40.46 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 343 ESFDGSNTIKSYQSEDDRfyigTTKFNGIIENLLKLGRFSN---------IQLTVNnflklTISLVILWLGSYLVMTDSM 413
Cdd:cd18548 183 ENLTGIRVIRAFNREDYE----EERFDKANDDLTDTSLKAGrlmallnplMMLIMN-----LAIVAILWFGGHLINAGSL 253
|
90 100 110
....*....|....*....|....*....|....*....
gi 488434717 414 TLGSLLAFNALTIYYLDPIERLINIQPTLQSSFVAARRI 452
Cdd:cd18548 254 QVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
492-664 |
2.47e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.83 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 492 VLKDINLNIKKGQKVAIVGESGSGKSTIGKLLNRYYTASEGNIMIDNYIIDDidlSDLRKNIGYVSQNTFLFAD--TIKN 569
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLPGLKADlsTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 570 ----NLLHGSnkyksdedivKACQLAESLDFIQKFPDQFNTMLEKeganLSGGQGQRLSLARTFLKDPDIYIFDEATSAL 645
Cdd:PRK13543 103 lhflCGLHGR----------RAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170 180
....*....|....*....|....*...
gi 488434717 646 D----SLTENKIMEHID-----LLTQHG 664
Cdd:PRK13543 169 DlegiTLVNRMISAHLRgggaaLVTTHG 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
476-672 |
3.08e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 476 NIRIENVNFQYGFRSVVlKDINLNIKKGQKVAIVGESGSGKSTIGKLL----------NRYYTASEGNIMIDNYIIDDID 545
Cdd:PLN03073 177 DIHMENFSISVGGRDLI-VDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkNCQILHVEQEVVGDDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 546 LSD-------LRKNIGYVSQNTFLFADTIKNNLlHGSNKYKSDEDIVKA--CQLAESLDFIQKFPDQFNT---------- 606
Cdd:PLN03073 256 LNTdiertqlLEEEAQLVAQQRELEFETETGKG-KGANKDGVDKDAVSQrlEEIYKRLELIDAYTAEARAasilaglsft 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488434717 607 --MLEKEGANLSGGQGQRLSLARTFLKDPDIYIFDEATSALDSlteNKIMEHIDLLTQHGKTVIIISH 672
Cdd:PLN03073 335 peMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKWPKTFIVVSH 399
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
205-421 |
3.25e-03 |
|
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: 40.01 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 205 GILLLYIINALINYLRFQLilhlslkidvnlmkdyFYHVLHLPMNFFDTRKSGEILQRF-MDTSKIREA--------LSS 275
Cdd:cd18590 57 GGLFMCTLSRLNLRLRHQL----------------FSSLVQQDIGFFEKTKTGDLTSRLsTDTTLMSRSvalnanvlLRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 276 STVTLLVDTFMIIIG---AILLYMQSPLLLlitiifipcfiicsyTLRKPFEKYNQKVAEK----DAELSSYLIESFDGS 348
Cdd:cd18590 121 LVKTLGMLGFMLSLSwqlTLLTLIEMPLTA---------------IAQKVYNTYHQKLSQAvqdsIAKAGELAREAVSSI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488434717 349 NTIKSYQSEDDRFYIGTTKFNGIIENLLKLGRFSNIQLTVNNFLKLTISLVILWLGSYLVMTDSMTLGSLLAF 421
Cdd:cd18590 186 RTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSF 258
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
589-710 |
5.48e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 589 QLAESLDFIQKFPDQFNTMLEKEGANLSGGQG-QRLSLART-------FL----KDPDIYIFDEATSALDSLTENKIMEH 656
Cdd:PRK00635 1665 EVAETFPFLKKIQKPLQALIDNGLGYLPLGQNlSSLSLSEKiaikiakFLylppKHPTLFLLDEIATSLDNQQKSALLVQ 1744
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488434717 657 IDLLTQHGKTVIIISHKLSTIKNADNIYVLNEGqiaeNGTHDELIHLNGIYKNL 710
Cdd:PRK00635 1745 LRTLVSLGHSVIYIDHDPALLKQADYLIEMGPG----SGKTGGKILFSGPPKDI 1794
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
243-293 |
5.51e-03 |
|
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: 39.51 E-value: 5.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488434717 243 VLHLPMNFFDTRKSGEILQRFM-DTSKIREALsSSTVTLLVDTFMIIIGAIL 293
Cdd:cd18602 93 IVRAPMRFFDTTPIGRILNRFSsDTNVIDQKL-PTTLERLLRFLLLCLSAII 143
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
202-294 |
6.93e-03 |
|
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: 39.00 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 202 ISFGIL--LLYIINALINYLRFQL---ILHLSLkidvnlmkdyFYHVLHLPMNFFDTRKSGEILQRF---MDTskIREAL 273
Cdd:cd18603 48 GALGLGqaIFVFLGSLALALGCVRasrNLHNKL----------LHNILRAPMSFFDTTPLGRILNRFskdIDT--VDNTL 115
|
90 100
....*....|....*....|.
gi 488434717 274 sSSTVTLLVDTFMIIIGAILL 294
Cdd:cd18603 116 -PQNIRSFLNCLFQVISTLVV 135
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
207-296 |
7.52e-03 |
|
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: 38.99 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 207 LLLYIINALINYLRFQLILHLSLKIDVNLMKDYFYHVLHLPMNFFDTRKSGEILQRF-MDTSKIREALSSSTVTLLVDTF 285
Cdd:cd18604 50 ALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFsKDIETIDSELADSLSSLLESTL 129
|
90
....*....|...
gi 488434717 286 MI--IIGAILLYM 296
Cdd:cd18604 130 SLlvILIAIVVVS 142
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
164-297 |
8.19e-03 |
|
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: 39.01 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488434717 164 FIAFISLFINIVGIVGALYFKLLTDHI--IPSNVLKNLHIISFGILLLYIINALINYLRFQLILHLSLKIDVNLMKDYFY 241
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLssYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488434717 242 HVLHLPMNFFDTRKSGEILQRF-MDTSKIREALSSStVTLLVDTFMIIIGAILLYMQ 297
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMsVDVQRIEDFFLFL-HYLWSAPLQIIVALYLLYRL 136
|
|
| |
