|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-569 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 584.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 1 MKARNP-LVFLLKKISWPV-GLIIVAVTIASIGSLTGLLVPLFTGQVVDK-FTFESISPV--FIIALVAVFLVNAVLSGF 75
Cdd:COG1132 1 MSKSPRkLLRRLLRYLRPYrGLLILALLLLLLSALLELLLPLLLGRIIDAlLAGGDLSALllLLLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 76 GYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLD 155
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 156 WQMTLLTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQ 235
Cdd:COG1132 161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 236 AKIAAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHE 315
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 316 PLENIAAPNLQDEIPT-GDLKFDHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYD 393
Cdd:COG1132 321 PPEIPDPPGAVPLPPVrGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 394 GTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSG 473
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG-RPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 474 GQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHE 553
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|....*.
gi 2254949669 554 ELMQTHAMYQQFVETQ 569
Cdd:COG1132 560 ELLARGGLYARLYRLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-570 |
1.19e-157 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 468.16 E-value: 1.19e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASI-GSLTGLLVPLFTGQVVDKFTFESISP---VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLW 96
Cdd:COG2274 157 LLLQVLLASLlINLLALATPLFTQVVIDRVLPNQDLStlwVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFF 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKNESGQLMSRLTDdTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPL 176
Cdd:COG2274 237 RHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 177 GKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGI 256
Cdd:COG2274 316 QPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 257 ILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHEPLENIAAPNLQD-EIPTGDLK 335
Cdd:COG2274 396 LLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSlPRLKGDIE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 336 FDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVM 413
Cdd:COG2274 476 LENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILL 493
Cdd:COG2274 556 QDVFLFSGTIRENITLG-DPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILI 634
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 494 LDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVETQN 570
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-569 |
1.60e-138 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 414.48 E-value: 1.60e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 2 KARNPLVFLLKKIS---WPVGLIIVAVTIASigsLTGLLVPLFTGQVVDK-FTFESISPV--FIIALVAVFLVNAVLSGF 75
Cdd:TIGR02204 1 KRLRPLAALWPFVRpyrGRVLAALVALLITA---AATLSLPYAVRLMIDHgFSKDSSGLLnrYFAFLLVVALVLALGTAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 76 GYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLD 155
Cdd:TIGR02204 78 RFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 156 WQMTLLTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQ 235
Cdd:TIGR02204 158 PKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 236 AKIAAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHE 315
Cdd:TIGR02204 238 IRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 316 PLEnIAAPNLQDEIPT---GDLKFDHVYFGYD---DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGG 389
Cdd:TIGR02204 318 EPD-IKAPAHPKTLPVplrGEIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 390 IYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGVDrEVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGL 469
Cdd:TIGR02204 397 ILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRP-DATDEEVEAAARAAHAHEFISALPEGYDTYLGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 470 KLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGR 549
Cdd:TIGR02204 476 TLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQ 555
|
570 580
....*....|....*....|
gi 2254949669 550 GRHEELMQTHAMYQQFVETQ 569
Cdd:TIGR02204 556 GTHAELIAKGGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-566 |
1.85e-120 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 372.13 E-value: 1.85e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 2 KARNPLVFLLK--KISWPvgLIIVAVTIASIGSLTGLLVPLFTGQVVD----KFTFES-ISPVFIIALVAvfLVNAVLSG 74
Cdd:TIGR00958 144 ETADLLFRLLGlsGRDWP--WLISAFVFLTLSSLGEMFIPFYTGRVIDtlggDKGPPAlASAIFFMCLLS--IASSVSAG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 75 FGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVL 154
Cdd:TIGR00958 220 LRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 155 DWQMTLLTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLK 234
Cdd:TIGR00958 300 SPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKR 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 235 QAKIAAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILH 314
Cdd:TIGR00958 380 KALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLD 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 315 EPlENIAAPNLQDEIP-TGDLKFDHVYFGY---DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGI 390
Cdd:TIGR00958 460 RK-PNIPLTGTLAPLNlEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 391 YYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGVDReVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLK 470
Cdd:TIGR00958 539 LLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD-TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQ 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 471 LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEalDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRG 550
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMG 695
|
570
....*....|....*.
gi 2254949669 551 RHEELMQTHAMYQQFV 566
Cdd:TIGR00958 696 THKQLMEDQGCYKHLV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-570 |
1.17e-112 |
|
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: 347.47 E-value: 1.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 18 VGLIIVAVTIasiGSLTGLLVPL----FTGQVVDKFTFesiSPVFIIALvavFLVNAVLSGFGYYLLNKIGEKIIYAIRS 93
Cdd:TIGR02203 21 VAMILVAATE---STLAALLKPLlddgFGGRDRSVLWW---VPLVVIGL---AVLRGICSFVSTYLLSWVSNKVVRDIRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 94 VLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVI 173
Cdd:TIGR02203 92 RMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 174 VPLGKIMQKISTNTQteiaNFSGLLGRVLTEM----RLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGII 249
Cdd:TIGR02203 172 RRVSKRLRRISKEIQ----NSMGQVTTVAEETlqgyRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 250 MLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHEPLENIAAPNLQDEI 329
Cdd:TIGR02203 248 ASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAIERA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 330 pTGDLKFDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRR 407
Cdd:TIGR02203 328 -RGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRR 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 408 KIGYVMQSNAMMNGTIRDNILYGVDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVK 487
Cdd:TIGR02203 407 QVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLK 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVE 567
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
...
gi 2254949669 568 TQN 570
Cdd:TIGR02203 567 MQF 569
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-559 |
1.28e-111 |
|
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: 344.43 E-value: 1.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 1 MKARNP-LVFLLKKISWPV------GLIIVAVTIASIGSLTGLLVPLFTGQVvdkfTFESISPVFIiALVAVFLVNAVLS 73
Cdd:COG4988 1 QKPLDKrLKRLARGARRWLalavllGLLSGLLIIAQAWLLASLLAGLIIGGA----PLSALLPLLG-LLLAVLLLRALLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 74 GFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFV 153
Cdd:COG4988 76 WLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 154 LDWQMTLLTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSG-LLGRV--LTEMRLVKVANTEKLELDKAHSNLKTIYn 230
Cdd:COG4988 156 LDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGhFLDRLrgLTTLKLFGRAKAEAERIAEASEDFRKRT- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 231 lgLKQAKIA---------------AVVqpisgiimlitigiiLGFGGMRIASGAISAGT-----LVAMIFYvlnlsIPLI 290
Cdd:COG4988 235 --MKVLRVAflssavleffaslsiALV---------------AVYIGFRLLGGSLTLFAalfvlLLAPEFF-----LPLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 291 NLSTLVTDYKKAVGASQRIYEILHEPLENIAAPNLQDEIPTG-DLKFDHVYFGYDD-TPVLKDVSFNVLRGEVTAFVGPS 368
Cdd:COG4988 293 DLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 369 GSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLAN 448
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG-RPDASDEELEAALEAAG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 449 CHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHR 528
Cdd:COG4988 452 LDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR 531
|
570 580 590
....*....|....*....|....*....|.
gi 2254949669 529 LSTIKKAGQIIFLDHGEVTGRGRHEELMQTH 559
Cdd:COG4988 532 LALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
21-309 |
4.76e-109 |
|
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: 328.24 E-value: 4.76e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISPVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHII 100
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 101 HLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIM 180
Cdd:cd18551 81 RLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 181 QKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGF 260
Cdd:cd18551 161 RKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2254949669 261 GGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18551 241 GGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
334-564 |
1.05e-107 |
|
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: 322.64 E-value: 1.05e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGY 411
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDI 491
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 492 LLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQ 564
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-569 |
2.97e-104 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 326.21 E-value: 2.97e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 16 WPV------GLIIVAVTI----ASIGSLTGLLVPLFTgqvvDKF-----TFESISPVFIIALVavfLVNAVLSGFGYYLL 80
Cdd:PRK11176 17 WPTiapfkaGLIVAGVALilnaASDTFMLSLLKPLLD----DGFgkadrSVLKWMPLVVIGLM---ILRGITSFISSYCI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 81 NKIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTL 160
Cdd:PRK11176 90 SWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 161 LTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAA 240
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 241 VVQPISGIimlitigiilgfggmrIASGAI----------------SAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVG 304
Cdd:PRK11176 250 ISDPIIQL----------------IASLALafvlyaasfpsvmdtlTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 305 ASQRIYEILH-EPLENIAApnLQDEIPTGDLKFDHVYFGYD--DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIER 381
Cdd:PRK11176 314 ACQTLFAILDlEQEKDEGK--RVIERAKGDIEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 382 MYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGVDREVSEEELIHYAKLANCHEFIMEFEQGYD 461
Cdd:PRK11176 392 FYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLD 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 462 TIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFL 541
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV 551
|
570 580
....*....|....*....|....*...
gi 2254949669 542 DHGEVTGRGRHEELMQTHAMYQQFVETQ 569
Cdd:PRK11176 552 EDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
336-569 |
3.96e-103 |
|
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: 311.40 E-value: 3.96e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 336 FDHVYFGYD---DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYV 412
Cdd:cd03249 3 FKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDIL 492
Cdd:cd03249 83 SQEPVLFDGTIAENIRYG-KPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 493 LLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVETQ 569
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
259-584 |
5.54e-101 |
|
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: 318.30 E-value: 5.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 259 GFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHEPLENIAAPNLQDEIPT-GDLKFD 337
Cdd:COG5265 282 LMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGgGEVRFE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGYD-DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSN 416
Cdd:COG5265 362 NVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 417 AMMNGTIRDNILYGvdR-EVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLD 495
Cdd:COG5265 442 VLFNDTIAYNIAYG--RpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFD 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 496 EATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVETQnltQHR 575
Cdd:COG5265 520 EATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ---QEE 596
|
....*....
gi 2254949669 576 AVTEQTETE 584
Cdd:COG5265 597 EEAEEALAA 605
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
336-569 |
1.41e-100 |
|
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: 304.54 E-value: 1.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 336 FDHVYFGYDDT-PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQ 414
Cdd:cd03253 3 FENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 SNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLL 494
Cdd:cd03253 83 DTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 495 DEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVETQ 569
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
86-567 |
1.03e-96 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 306.31 E-value: 1.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 86 KIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFIsqkLPGFFPAVITLIGSLIMLFVL---DWQMTLLT 162
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLaffSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 163 FITIpIFILVIVPLgkIMQKISTNTQTEIANFSGLLGRVLTE----MRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKI 238
Cdd:COG4987 162 ALGL-LLAGLLLPL--LAARLGRRAGRRLAAARAALRARLTDllqgAAELAAYGALDRALARLDAAEARLAAAQRRLARL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 239 AAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHEPLE 318
Cdd:COG4987 239 SALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 319 NIAAPNLQDEIPTGDLKFDHVYFGYDDT--PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTS 396
Cdd:COG4987 319 VTEPAEPAPAPGGPSLELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 397 IDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQR 476
Cdd:COG4987 399 LRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLA-RPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGER 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 477 QRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELM 556
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
490
....*....|.
gi 2254949669 557 QTHAMYQQFVE 567
Cdd:COG4987 558 AQNGRYRQLYQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
332-559 |
1.16e-90 |
|
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: 278.73 E-value: 1.16e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 332 GDLKFDHVYFGYD-DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIG 410
Cdd:cd03254 1 GEIEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPD 490
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 491 ILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTH 559
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
33-562 |
2.95e-88 |
|
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: 287.41 E-value: 2.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 33 LTGLLVPLFTGQVVDKF----TFESISpVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFD 108
Cdd:TIGR01846 153 LFALVTPLLFQVVIDKVlvhrGLSTLS-VLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 109 KNESGQLMSRLTDDTKVINDFISQKLPgffpAVITLIGSLIMLFVLDW---QMTLLTFITIPIFILVIVPLGKIMQKIST 185
Cdd:TIGR01846 232 SRRVGDTVARVRELEQIRNFLTGSALT----VVLDLLFVVVFLAVMFFyspTLTGVVIGSLVCYALLSVFVGPILRKRVE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 186 NTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGGMRI 265
Cdd:TIGR01846 308 DKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 266 ASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHEPLENIAAPNLQDEIPTGDLKFDHVYFGYD- 344
Cdd:TIGR01846 388 IGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRYAp 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 345 DTP-VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTI 423
Cdd:TIGR01846 468 DSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSI 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDS 503
Cdd:TIGR01846 548 RDNIALC-NPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDY 626
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 504 ESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMY 562
Cdd:TIGR01846 627 ESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
336-569 |
1.10e-83 |
|
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: 261.27 E-value: 1.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 336 FDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVM 413
Cdd:cd03252 3 FEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILL 493
Cdd:cd03252 83 QENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 494 LDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVETQ 569
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
97-584 |
3.02e-82 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 268.75 E-value: 3.02e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKNESGQLMSRLTDDTkvinDFISQKLPGFFPAVITLIGSLIML----FVLDWQMTLLTFITIPIFILv 172
Cdd:PRK13657 97 ERIIQLPLAWHSQRGSGRALHTLLRGT----DALFGLWLEFMREHLATLVALVVLlplaLFMNWRLSLVLVVLGIVYTL- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 173 ivpLGKIMQKISTNTQTEI-ANFSGLLGRV---LTEMRLVKVANTEKLELDKAHS---NLKTIYNLGLKQAKIAAVVQPI 245
Cdd:PRK13657 172 ---ITTLVMRKTKDGQAAVeEHYHDLFAHVsdaIGNVSVVQSYNRIEAETQALRDiadNLLAAQMPVLSWWALASVLNRA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 246 SGIIMLITIGIIlgfGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEIL------HEPLEN 319
Cdd:PRK13657 249 ASTITMLAILVL---GAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEdavpdvRDPPGA 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 320 IAAPNLQdeiptGDLKFDHVYFGYDDT-PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSID 398
Cdd:PRK13657 326 IDLGRVK-----GAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 399 ALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGvdRE-VSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQ 477
Cdd:PRK13657 401 TVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG--RPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 478 RIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA 558
|
490 500
....*....|....*....|....*..
gi 2254949669 558 THAMYQQFVETQNLTQHRAVTEQTETE 584
Cdd:PRK13657 559 RGGRFAALLRAQGMLQEDERRKQPAAE 585
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-584 |
3.27e-80 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 263.50 E-value: 3.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 17 PVGLIIVAVTIASIGSLTG-LLVPLFTGQVVDKFTFesisPVFIIA-LVAVFLVNAVLSGFGYY----LLNKIGEKIIYA 90
Cdd:PRK10790 24 PLGLAVLMLWVAAAAEVSGpLLISYFIDNMVAKGNL----PLGLVAgLAAAYVGLQLLAAGLHYaqslLFNRAAVGVVQQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 91 IRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAvITLIGS-LIMLFVLDWQMTLLTFITIPIF 169
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRS-AALIGAmLVAMFSLDWRMALVAIMIFPAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 170 ILVIVplgkIMQKIST----NTQTEIANFSGLLGRVLTEMRLVK-----VANTEKL-ELDKAH--SNLKTIYNLGLkqak 237
Cdd:PRK10790 179 LVVMV----IYQRYSTpivrRVRAYLADINDGFNEVINGMSVIQqfrqqARFGERMgEASRSHymARMQTLRLDGF---- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 238 iaaVVQPISGIIMLITI---GIILGFGGmriaSGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILH 314
Cdd:PRK10790 251 ---LLRPLLSLFSALILcglLMLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 315 EPLENIAapnlQDEIP--TGDLKFDHVYFGY-DDTPVLKDVSFNV-LRGEVtAFVGPSGSGKSTLFSLIERMYEIDQGGI 390
Cdd:PRK10790 324 GPRQQYG----NDDRPlqSGRIDIDNVSFAYrDDNLVLQNINLSVpSRGFV-ALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 391 YYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGvdREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLK 470
Cdd:PRK10790 399 RLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 471 LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRG 550
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
|
570 580 590
....*....|....*....|....*....|....
gi 2254949669 551 RHEELMQTHAMYQQFVETQNLTQHRAVTEQTETE 584
Cdd:PRK10790 557 THQQLLAAQGRYWQMYQLQLAGEELAASVREEES 590
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-567 |
2.67e-77 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 258.72 E-value: 2.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 2 KARNPLVFLLKKISWPVGLIIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISP---VFIIALVAVFLVNAVLSGFGYY 78
Cdd:TIGR03796 137 RKPSLLRALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIFVDEILVQGRQDwlrPLLLGMGLTALLQGVLTWLQLY 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 79 LLNKIgeKIIYAIRS---VLWeHIIHLKMPFFDKNESGQLMSRLTDDTKViNDFISQKLPGFFPAVITLIGSLIMLFVLD 155
Cdd:TIGR03796 217 YLRRL--EIKLAVGMsarFLW-HILRLPVRFFAQRHAGDIASRVQLNDQV-AEFLSGQLATTALDAVMLVFYALLMLLYD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 156 WqmtLLTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELD------KAHSN-LKTI 228
Cdd:TIGR03796 293 P---VLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDffsrwaGYQAKlLNAQ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 229 YNLGLKQAKIAAVVQPISGIIMLITIgiilGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQR 308
Cdd:TIGR03796 370 QELGVLTQILGVLPTLLTSLNSALIL----VVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNR 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 309 IYEILHEPL-------ENIAAPNLQDEIPTGDLKFDHVYFGYD--DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLI 379
Cdd:TIGR03796 446 LDDVLRNPVdplleepEGSAATSEPPRRLSGYVELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLV 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 380 ERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNI-LYgvDREVSEEELIHYAKLANCHEFIMEFEQ 458
Cdd:TIGR03796 526 AGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtLW--DPTIPDADLVRACKDAAIHDVITSRPG 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 459 GYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALdilmENR--TTIVIAHRLSTIKKAG 536
Cdd:TIGR03796 604 GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL----RRRgcTCIIVAHRLSTIRDCD 679
|
570 580 590
....*....|....*....|....*....|.
gi 2254949669 537 QIIFLDHGEVTGRGRHEELMQTHAMYQQFVE 567
Cdd:TIGR03796 680 EIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
334-545 |
1.89e-75 |
|
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: 237.28 E-value: 1.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDT--PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGY 411
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQSNAMMNGTIRDNIlygvdrevseeelihyaklanchefimefeqgydtivgerglkLSGGQRQRIDIARSFVKNPDI 491
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 492 LLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGE 545
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-541 |
8.49e-74 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 244.89 E-value: 8.49e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 31 GSLTGLLVPLFT---GQVVDKFTFE-----SISPvFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHL 102
Cdd:TIGR02857 12 GVLGALLIIAQAwllARVVDGLISAgeplaELLP-ALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 103 KMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFIT---IPIFILVIvplGKI 179
Cdd:TIGR02857 91 GPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTaplIPIFMILI---GWA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 180 MQKISTNTQTEIANFSG-LLGRV--LTEMRLVKVANTEKLELDKAHSNLK--TIYNLglkqaKIA----AVVQ---PISG 247
Cdd:TIGR02857 168 AQAAARKQWAALSRLSGhFLDRLrgLPTLKLFGRAKAQAAAIRRSSEEYRerTMRVL-----RIAflssAVLElfaTLSV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 248 IIMLITIGIILGFGGMRIASGaisagtlvamiFYVLNLS----IPLINLSTLVTDYKKAVGASQRIYEILHEPlENIAAP 323
Cdd:TIGR02857 243 ALVAVYIGFRLLAGDLDLATG-----------LFVLLLApefyLPLRQLGAQYHARADGVAAAEALFAVLDAA-PRPLAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 324 nlQDEIPTGD---LKFDHVYFGYDDT-PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDA 399
Cdd:TIGR02857 311 --KAPVTAAPassLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 400 LSLTDWRRKIGYVMQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRI 479
Cdd:TIGR02857 389 ADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 480 DIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFL 541
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-569 |
1.81e-71 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 242.55 E-value: 1.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 2 KARNPLVFLLKKISWPVGLIIVAvtiASIGSLTGLLVPLFTGQVVDKFTFESISPvfIIALVAVFLVNAVLSGFGYYLLN 81
Cdd:TIGR03797 122 GLRDLLRFALRGARRDLLAILAM---GLLGTLLGMLVPIATGILIGTAIPDADRS--LLVQIALALLAAAVGAAAFQLAQ 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 82 -----KIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKvindfISQKLPGffPAVITLIGS------LIM 150
Cdd:TIGR03797 197 slavlRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQ-----IRRILSG--STLTTLLSGifallnLGL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 151 LFVLDWQMTLLTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYN 230
Cdd:TIGR03797 270 MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 231 LGLKQAKIAAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIY 310
Cdd:TIGR03797 350 LELSAQRIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 311 EILHEPLENIAAPNLQDEIpTGDLKFDHVYFGYDDT--PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQG 388
Cdd:TIGR03797 430 PILEALPEVDEAKTDPGKL-SGAIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 389 GIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGVdrEVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERG 468
Cdd:TIGR03797 509 SVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA--PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGG 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 469 LKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILmeNRTTIVIAHRLSTIKKAGQIIFLDHGEVTG 548
Cdd:TIGR03797 587 GTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQ 664
|
570 580
....*....|....*....|.
gi 2254949669 549 RGRHEELMQTHAMYQQFVETQ 569
Cdd:TIGR03797 665 QGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
332-546 |
3.37e-70 |
|
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: 225.81 E-value: 3.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 332 GDLKFDHVYFGY---DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRK 408
Cdd:cd03248 10 GIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 409 IGYVMQSNAMMNGTIRDNILYGVdREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKN 488
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGL-QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 489 PDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEV 546
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-571 |
8.13e-70 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 235.38 E-value: 8.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 20 LIIVAVTiasigsltGLLVPLFTGQVVDKFTFESISPVFIIALVAVFLVNAVLsgfgYYLLNKIGEKIIYA--------I 91
Cdd:PRK10789 4 LIIIAML--------QLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIAVV----VYLLRYVWRVLLFGasyqlaveL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 92 RSVLWEHIIHLKMPFFDKNESGQLMSRLTDDT-KVIndfisqklpgfFPA---VITLIGSLIM----LFV----LDWQMT 159
Cdd:PRK10789 72 REDFYRQLSRQHPEFYLRHRTGDLMARATNDVdRVV-----------FAAgegVLTLVDSLVMgcavLIVmstqISWQLT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 160 LLTFITIPIFILVIVPLGKIMQKISTNTQteiANFSGLLGRV---LTEMRLVKVANTEKL-----ELDKAHSNLKTIYnl 231
Cdd:PRK10789 141 LLALLPMPVMAIMIKRYGDQLHERFKLAQ---AAFSSLNDRTqesLTSIRMIKAFGLEDRqsalfAADAEDTGKKNMR-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 232 glkQAKIAAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYvLNLSI-PLINLSTLVTDYKKAVGASQRIY 310
Cdd:PRK10789 216 ---VARIDARFDPTIYIAIGMANLLAIGGGSWMVVNGSLTLGQLTSFVMY-LGLMIwPMLALAWMFNIVERGSAAYSRIR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 311 EILHE-PLENIAAPNLQDEIPTGDLKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGG 389
Cdd:PRK10789 292 AMLAEaPVVKDGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 390 IYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGL 469
Cdd:PRK10789 372 IRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 470 KLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGR 549
Cdd:PRK10789 451 MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQR 530
|
570 580
....*....|....*....|..
gi 2254949669 550 GRHEELMQTHAMYQQFVETQNL 571
Cdd:PRK10789 531 GNHDQLAQQSGWYRDMYRYQQL 552
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-564 |
1.50e-69 |
|
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: 238.10 E-value: 1.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 6 PLVFLLKKIswpVGLIIVAVTIASIGSLTGllvPLFTGQVVDKF-------TFESISpvfiIALVAVFLVNAVLSGFGYY 78
Cdd:TIGR01193 149 PLITRQKKL---IVNIVIAAIIVTLISIAG---SYYLQKIIDTYiphkmmgTLGIIS----IGLIIAYIIQQILSYIQIF 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 79 LLNKIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFvLDWQM 158
Cdd:TIGR01193 219 LLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVR-QNMLL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 159 TLLTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKI 238
Cdd:TIGR01193 298 FLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 239 AAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLV---AMIFYVLNlsiPLINLSTLVTDYKKAVGASQRIYEILHE 315
Cdd:TIGR01193 378 DQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLItfnALLSYFLT---PLENIINLQPKLQAARVANNRLNEVYLV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 316 PLENIAAPNLQD-EIPTGDLKFDHVYFGYD-DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYD 393
Cdd:TIGR01193 455 DSEFINKKKRTElNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 394 GTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGVDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSG 473
Cdd:TIGR01193 535 GFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISG 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 474 GQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALdILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHE 553
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHD 693
|
570
....*....|.
gi 2254949669 554 ELMQTHAMYQQ 564
Cdd:TIGR01193 694 ELLDRNGFYAS 704
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
332-546 |
1.81e-62 |
|
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: 205.13 E-value: 1.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 332 GDLKFDHVYFGYDD--TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKI 409
Cdd:cd03245 1 GRIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNP 489
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 490 DILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEV 546
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
261-579 |
7.03e-62 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 214.75 E-value: 7.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 261 GGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEiLHEPLENIAAPNLQDEIP--TGDLKFDH 338
Cdd:TIGR01192 261 GTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFD-LEDSVFQREEPADAPELPnvKGAVEFRH 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGYDDTPV-LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNA 417
Cdd:TIGR01192 340 ITFEFANSSQgVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAG 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 418 MMNGTIRDNILYGVDrEVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEA 497
Cdd:TIGR01192 420 LFNRSIRENIRLGRE-GATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 498 TANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVETQNLTQHRAV 577
Cdd:TIGR01192 499 TSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPA 578
|
..
gi 2254949669 578 TE 579
Cdd:TIGR01192 579 TK 580
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-309 |
1.15e-59 |
|
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: 200.02 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 30 IGSLTGLLVPLFTGQVVDKFTFESISP---VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPF 106
Cdd:cd18576 7 LSSAIGLVFPLLAGQLIDAALGGGDTAslnQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 107 FDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIMQKISTN 186
Cdd:cd18576 87 FHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 187 TQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGGMRIA 266
Cdd:cd18576 167 VQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2254949669 267 SGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18576 247 AGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
21-309 |
1.90e-59 |
|
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: 199.70 E-value: 1.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKFTFE---SISPVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWE 97
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAgdlSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 98 HIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLG 177
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 178 KIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGII 257
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 258 LGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
332-546 |
5.74e-58 |
|
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: 193.48 E-value: 5.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 332 GDLKFDHVYFGYDDT--PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKI 409
Cdd:cd03244 1 GDIEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNAMMNGTIRDNI-LYGvdrEVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKN 488
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLdPFG---EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 489 PDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEV 546
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
302-557 |
2.36e-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: 198.82 E-value: 2.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 302 AVGASQRIYEILHEPLENIAAPNLQDeiPTGDLKFDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLI 379
Cdd:COG4618 301 ARQAYRRLNELLAAVPAEPERMPLPR--PKGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 380 ERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNIlygvDR--EVSEEELIHYAKLANCHEFIMEFE 457
Cdd:COG4618 379 VGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI----ARfgDADPEKVVAAAKLAGVHEMILRLP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 458 QGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDIL-MENRTTIVIAHRLSTIKKAG 536
Cdd:COG4618 455 DGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVD 534
|
250 260
....*....|....*....|.
gi 2254949669 537 QIIFLDHGEVTGRGRHEELMQ 557
Cdd:COG4618 535 KLLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-565 |
4.35e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 193.52 E-value: 4.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 19 GLIIVAVT--IASIgsLTGLlvplftgqVVDKFTFESISPVFIiALVAVFLVNAVLS------GFgyyllnKIGEKIIYA 90
Cdd:PRK11174 35 GLLLIAQAwlLATI--LQAL--------IIENIPREALLPPFI-LLILLFVLRALLAwlrervGF------KAGQHIRQQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 91 IRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLP-----GFFPAVItligsLIMLFVLDWQMTLLTFIT 165
Cdd:PRK11174 98 IRQQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPqmalaVLVPLLI-----LIAVFPINWAAGLILLGT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 166 ---IPIFiLVIVPLG---------KIMQKIStntqteiANFSGLLgRVLTEMRLVKVANTEKLELDKAHSNLK--TIYNL 231
Cdd:PRK11174 173 aplIPLF-MALVGMGaadanrrnfLALARLS-------GHFLDRL-RGLETLRLFNRGEAETESIRSASEDFRqrTMEVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 232 glkqaKIA----AVVQpisgiimlitigiilGFGGMRIASGAISAG----------------TLVAMiFYVLNLS----I 287
Cdd:PRK11174 244 -----RMAflssAVLE---------------FFASISIALVAVYFGfsylgelnfghygtgvTLFAG-FFVLILApefyQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 288 PLINLSTLVTDYKKAVGASQRIYEILHEPLEniaapnlqdEIPTGDLKFDH-----------VYFGYDDTPVLKDVSFNV 356
Cdd:PRK11174 303 PLRDLGTFYHAKAQAVGAAESLVTFLETPLA---------HPQQGEKELASndpvtieaedlEILSPDGKTLAGPLNFTL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 357 LRGEVTAFVGPSGSGKSTLFSLIERM--YeidQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGvDRE 434
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-NPD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 435 VSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALD 514
Cdd:PRK11174 450 ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 515 ILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQF 565
Cdd:PRK11174 530 AASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-567 |
8.53e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 192.35 E-value: 8.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 305 ASQRIYEILHEPLENIAAPNLQDEIPTGDLKFDHVYFGYDD--TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERM 382
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 383 YEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGVDrEVSEEELIHYAK---LANchefIMEFEQG 459
Cdd:PRK11160 390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEVLQqvgLEK----LLEDDKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 460 YDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQII 539
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
250 260
....*....|....*....|....*...
gi 2254949669 540 FLDHGEVTGRGRHEELMQTHAMYQQFVE 567
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
30-309 |
2.61e-53 |
|
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: 183.15 E-value: 2.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 30 IGSLTGLLVPLFTGQVVDKFTFESISPVF---IIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPF 106
Cdd:cd18557 7 ISSAAQLLLPYLIGRLIDTIIKGGDLDVLnelALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 107 FDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIMQKISTN 186
Cdd:cd18557 87 FDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 187 TQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGGMRIA 266
Cdd:cd18557 167 VQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2254949669 267 SGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18557 247 SGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
32-545 |
2.84e-53 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 196.40 E-value: 2.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 32 SLTGLLVPLFT---GQVVDKFTF-ESISPVfIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFF 107
Cdd:PTZ00265 70 TISGGTLPFFVsvfGVIMKNMNLgENVNDI-IFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 108 DKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGKimqKISTNT 187
Cdd:PTZ00265 149 DNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNK---KVKINK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 188 QTEIA---NFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKqakiAAVVQPISGIIMLITIGIILGFG--- 261
Cdd:PTZ00265 226 KTSLLynnNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILK----ANFMESLHIGMINGFILASYAFGfwy 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 262 GMRIASGAIS---------AGTLVAMIFYVL----NLSIPLINlstlVTDYKKAVGASQRIYEILH-EPLeniaAPNLQD 327
Cdd:PTZ00265 302 GTRIIISDLSnqqpnndfhGGSVISILLGVLismfMLTIILPN----ITEYMKSLEATNSLYEIINrKPL----VENNDD 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 328 EIPTGDLK---FDHVYFGYD---DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYY-DGTSIDAL 400
Cdd:PTZ00265 374 GKKLKDIKkiqFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 401 SLTDWRRKIGYVMQSNAMMNGTIRDNILYGV----DREVSEE-------------------------------------E 439
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkDLEALSNyynedgndsqenknkrnscrakcagdlndmsnttdsnE 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 440 LIHYAKLANC---------------HEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSE 504
Cdd:PTZ00265 534 LIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2254949669 505 SERKIQEALDILM--ENRTTIVIAHRLSTIKKAGQIIFLDHGE 545
Cdd:PTZ00265 614 SEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
21-309 |
1.73e-52 |
|
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: 181.08 E-value: 1.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDK-FTFESISPVFIIAL--VAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWE 97
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDiFVEKDLEALLLVPLaiIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 98 HIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLG 177
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 178 KIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGII 257
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 258 LGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
334-546 |
6.53e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 174.23 E-value: 6.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVM 413
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNGTIRDNILYG---VDREVSEEELIHYAKLANCHEFIMefeqgyDTIVGErglkLSGGQRQRIDIARSFVKNPD 490
Cdd:COG4619 81 QEPALWGGTVRDNLPFPfqlRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 491 ILLLDEATANLDSESERKIQEALDILM--ENRTTIVIAHRLSTIKK-AGQIIFLDHGEV 546
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
22-309 |
7.32e-51 |
|
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: 176.85 E-value: 7.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 22 IVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISPVFIIALVAVFLVNAVLSGFGY---YLLNKIGEKIIYAIRSVLWEH 98
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYlqgYLAEKASQKVAYDLRNDLYDH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 99 IIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGK 178
Cdd:cd18542 82 LQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 179 IMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIIL 258
Cdd:cd18542 162 KVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 259 GFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18542 242 WVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
22-309 |
1.88e-50 |
|
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: 175.81 E-value: 1.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 22 IVAVTIASIGSLtglLVPLFTGQVVDKFTFESISPVF---IIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEH 98
Cdd:cd18572 2 FVFLVVAALSEL---AIPHYTGAVIDAVVADGSREAFyraVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 99 IIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGK 178
Cdd:cd18572 79 LLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 179 IMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIIL 258
Cdd:cd18572 159 YYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 259 GFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18572 239 FYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-557 |
3.75e-50 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 181.78 E-value: 3.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 20 LIIVAVTIASIGSLTgLLVPLFTGQVVDK-FTFESISPVFIIALVAVFL--VNAVLSGFGYYLLNKIGEKIIYAIRSVLW 96
Cdd:TIGR01842 8 FIIVGLFSFVINILM-LAPPLYMLQVYDRvLTSGSVPTLLMLTVLALGLylFLGLLDALRSFVLVRIGEKLDGALNQPIF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKnESGQLMSRLTDdtkvINDFI-SQKLPGFFPAVITLIgSLIMLFVLD-WqmtlLTFITIpIFILVIV 174
Cdd:TIGR01842 87 AASFSATLRRGSG-DGLQALRDLDQ----LRQFLtGPGLFAFFDAPWMPI-YLLVCFLLHpW----IGILAL-GGAVVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 175 PLGkIMQKISTNTQTEIAN-FSGLLGRVLTEMRLvkvaNTEKLE----LDKAHSNLKTIYNLGLKQAKIA----AVVQPI 245
Cdd:TIGR01842 156 GLA-LLNNRATKKPLKEATeASIRANNLADSALR----NAEVIEamgmMGNLTKRWGRFHSKYLSAQSAAsdraGMLSNL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 246 SGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHEPLENIAAPNL 325
Cdd:TIGR01842 231 SKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 326 QDeiPTGDLKFDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLT 403
Cdd:TIGR01842 311 PE--PEGHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 404 DWRRKIGYVMQSNAMMNGTIRDNILYgVDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIAR 483
Cdd:TIGR01842 389 TFGKHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALAR 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 484 SFVKNPDILLLDEATANLDSESERKIQEAL-DILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIkALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
86-529 |
1.93e-49 |
|
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: 179.48 E-value: 1.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 86 KIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFIsqkLPGFFP---AVITLIGSLIMLFVLDWQMTLLT 162
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLY---VRVIVPagvALVVGAAAVAAIAVLSVPAALIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 163 FITIPIFiLVIVPL-----GKIMQKISTNTQTEIAN-------------FSGLLGRVLTEMRlvkVANTEKLELDKahsn 224
Cdd:TIGR02868 160 AAGLLLA-GFVAPLvslraARAAEQALARLRGELAAqltdaldgaaelvASGALPAALAQVE---EADRELTRAER---- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 225 lktiynlglKQAKIAAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVG 304
Cdd:TIGR02868 232 ---------RAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 305 ASQRIYEILHEPLEN--IAAPNLQDEIPTG-DLKFDHVYFGYDDTP-VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIE 380
Cdd:TIGR02868 303 AAERIVEVLDAAGPVaeGSAPAAGAVGLGKpTLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 381 RMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGvDREVSEEELIHYAKLANCHEFIMEFEQGY 460
Cdd:TIGR02868 383 GLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGL 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 461 DTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRL 529
Cdd:TIGR02868 462 DTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
21-309 |
6.25e-48 |
|
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: 169.11 E-value: 6.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKF---TFESISPVFIIAL--VAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVL 95
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYivpGQGDLQGLLLLALlyLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 96 WEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVP 175
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 176 LGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIG 255
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 256 IILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-309 |
8.59e-48 |
|
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: 168.84 E-value: 8.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISP-------VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRS 93
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGgntslllLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 94 VLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVI 173
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 174 VPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLIT 253
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 254 IGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
21-309 |
2.60e-46 |
|
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: 164.56 E-value: 2.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISPVFIIALVAVFLVNAVLSGFGY---YLLNKIGEKIIYAIRSVLWE 97
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRlriYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 98 HIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLG 177
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 178 KIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGII 257
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 258 LGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18545 242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-567 |
1.40e-45 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 173.68 E-value: 1.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 2 KARNPLVFLLKKI-SWPVGLIIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESIS------PVFIIALVAVFLVNAVLSG 74
Cdd:PTZ00265 808 KAPNNLRIVYREIfSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEansnkySLYILVIAIAMFISETLKN 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 75 fgyYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFD--KNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLF 152
Cdd:PTZ00265 888 ---YYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSF 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 153 ----VLDWQMTLLTFITIPIFilvivplgKIMQKISTNTQTEI--ANFSGLLGRVLTEMRLVKvanTEKLELDKAHSNLK 226
Cdd:PTZ00265 965 yfcpIVAAVLTGTYFIFMRVF--------AIRARLTANKDVEKkeINQPGTVFAYNSDDEIFK---DPSFLIQEAFYNMN 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 227 TIYNLGL--------------------KQAKIAAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLS 286
Cdd:PTZ00265 1034 TVIIYGLedyfcnliekaidysnkgqkRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTG 1113
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 287 IPLINLSTLVTDYKKAVGASQRIYEILHEPLE-------NIAAPNLQD---EIPTGDLKFDhvYFGYDDTPVLKDVSFNV 356
Cdd:PTZ00265 1114 SYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNidvrdngGIRIKNKNDikgKIEIMDVNFR--YISRPNVPIYKDLTFSC 1191
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 357 LRGEVTAFVGPSGSGKSTLFSLIERMYEI--------------------------------------------------- 385
Cdd:PTZ00265 1192 DSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedst 1271
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 386 ---DQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNILYGVDrEVSEEELIHYAKLANCHEFIMEFEQGYDT 462
Cdd:PTZ00265 1272 vfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATREDVKRACKFAAIDEFIESLPNKYDT 1350
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 463 IVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEAL-DIL-MENRTTIVIAHRLSTIKKAGQIIF 540
Cdd:PTZ00265 1351 NVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvDIKdKADKTIITIAHRIASIKRSDKIVV 1430
|
650 660 670
....*....|....*....|....*....|...
gi 2254949669 541 LDHGEVTG-----RGRHEELMQTH-AMYQQFVE 567
Cdd:PTZ00265 1431 FNNPDRTGsfvqaHGTHEELLSVQdGVYKKYVK 1463
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
30-309 |
1.59e-45 |
|
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: 162.42 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 30 IGSLTGLLVPLFTGQVVDKFTFESISPVF---------IIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHII 100
Cdd:cd18780 7 VSSGTNLALPYFFGQVIDAVTNHSGSGGEealralnqaVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 101 HLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIM 180
Cdd:cd18780 87 AQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 181 QKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGF 260
Cdd:cd18780 167 RKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWY 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2254949669 261 GGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18780 247 GGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
334-555 |
1.31e-44 |
|
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: 157.73 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEI-----DQGGIYYDGTSIDALSLTD--WR 406
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVleLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 407 RKIGYVMQSNAMMNGTIRDNILYGV------DREVSEEELIHYAKLAnchefimefeqGYDTIVGER--GLKLSGGQRQR 478
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLrlhgikLKEELDERVEEALRKA-----------ALWDEVKDRlhALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 479 IDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEEL 555
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
21-309 |
2.73e-44 |
|
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: 159.49 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISPV---------FIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAI 91
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGgvdfsgllrILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 92 RSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFIL 171
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 172 VIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKL---ELDKAHSNLktiYNLGLKQAKIAAVVQPISGI 248
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEaieEFDEINEEL---YKASFKAQFYSGLLMPIMNF 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 249 IMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18547 238 INNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
339-546 |
5.40e-44 |
|
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: 154.30 E-value: 5.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGYDDT--PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSN 416
Cdd:cd03246 6 VSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 417 AMMNGTIRDNILygvdrevseeelihyaklanchefimefeqgydtivgerglklSGGQRQRIDIARSFVKNPDILLLDE 496
Cdd:cd03246 86 ELFSGSIAENIL-------------------------------------------SGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 497 ATANLDSESERKIQEALDIL-MENRTTIVIAHRLSTIKKAGQIIFLDHGEV 546
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
334-559 |
8.07e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.99 E-value: 8.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSlTDWRRKIGYVM 413
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNG-TIRDNI-----LYGVDREVSEEELIHYAKLANCHEFImefeqgyDTIVGerglKLSGGQRQRIDIARSFVK 487
Cdd:COG1131 80 QEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQTH 559
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
24-309 |
1.11e-43 |
|
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: 157.68 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 24 AVTIASIGSLTGLLVPLFTGQVVDKFTFESISP--------VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVL 95
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIeifglslkTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 96 WEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVP 175
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 176 LGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIG 255
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 256 IILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
21-309 |
3.00e-43 |
|
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: 156.48 E-value: 3.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAvTIASIGSltGLLVPLFT---GQVVDKFTFESISPV-----------FIIALVAVFLVNAVLSGFGYYLLNKIGEK 86
Cdd:cd18577 1 LIIG-LLAAIAA--GAALPLMTivfGDLFDAFTDFGSGESspdeflddvnkYALYFVYLGIGSFVLSYIQTACWTITGER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 87 IIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITI 166
Cdd:cd18577 78 QARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 167 PIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPIS 246
Cdd:cd18577 158 PLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 247 GIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18577 238 FFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
334-545 |
1.90e-42 |
|
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: 151.08 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDD-----TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIerMYEIDQ--GGIYYDGTsidalsltdwr 406
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEKlsGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 407 rkIGYVMQSNAMMNGTIRDNILYGvdREVSEEElihYAK-LANC--HEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIAR 483
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFG--KPFDEER---YEKvIKACalEPDLEILPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 484 SFVKNPDILLLDEATANLDSESERKI-QEAL-DILMENRTTIVIAHRLSTIKKAGQIIFLDHGE 545
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIfENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
22-309 |
4.93e-42 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 153.02 E-value: 4.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 22 IVAVTIASigsLTGLLVPLFTGQVVDK-FTFESISPV--FIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEH 98
Cdd:cd18575 2 LIALLIAA---AATLALGQGLRLLIDQgFAAGNTALLnrAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 99 IIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGK 178
Cdd:cd18575 79 LLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 179 IMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIIL 258
Cdd:cd18575 159 RVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 259 GFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18575 239 WLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
334-546 |
5.09e-42 |
|
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: 150.72 E-value: 5.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDD----TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDW---- 405
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 406 RRKIGYVMQSNAMMNG-TIRDNI-----LYGVDREVSEE---ELIHYAKLAN-CHEFIMEfeqgydtivgerglkLSGGQ 475
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVelpllLAGVPKKERREraeELLERVGLGDrLNHYPSE---------------LSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 476 RQRIDIARSFVKNPDILLLDEATANLDSESERKIqeaLDILME-----NRTTIVIAHRLSTIKKAGQIIFLDHGEV 546
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEV---MELLRElnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
334-566 |
6.75e-42 |
|
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: 150.90 E-value: 6.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKIG 410
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQSNAM---MngTIRDNILYGVDR--EVSEEELIHYA--KLANchefimefeqgydtiVGERGLK------LSGGQRQ 477
Cdd:COG1127 86 MLFQGGALfdsL--TVFENVAFPLREhtDLSEAEIRELVleKLEL---------------VGLPGAAdkmpseLSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 478 RIDIARSFVKNPDILLLDEATANLDSESE-------RKIQEALDIlmenrTTIVIAHRLSTIKKAG-QIIFLDHGEVTGR 549
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSavideliRELRDELGL-----TSVVVTHDLDSAFAIAdRVAVLADGKIIAE 223
|
250
....*....|....*...
gi 2254949669 550 GRHEELMQT-HAMYQQFV 566
Cdd:COG1127 224 GTPEELLASdDPWVRQFL 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
334-556 |
7.15e-42 |
|
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: 150.56 E-value: 7.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYV 412
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQS--NAMMNGTIRDNILYG-----VDREVSEE---------ELIHYAKlANCHEfimefeqgydtivgerglkLSGGQR 476
Cdd:COG1122 81 FQNpdDQLFAPTVEEDVAFGpenlgLPREEIRErveealelvGLEHLAD-RPPHE-------------------LSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 477 QRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIA-HRLSTI-KKAGQIIFLDHGEVTGRGRHEE 554
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPRE 220
|
..
gi 2254949669 555 LM 556
Cdd:COG1122 221 VF 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
334-551 |
2.39e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.04 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDD----TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWR 406
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 407 R-KIGYVMQSNAMMNG-TIRDNILY-----GVDREVSEE---ELIHYAKLANC-HEFIMEfeqgydtivgerglkLSGGQ 475
Cdd:COG1136 85 RrHIGFVFQFFNLLPElTALENVALplllaGVSRKERRErarELLERVGLGDRlDHRPSQ---------------LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 476 RQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILM-ENRTTIVIA-HRLSTIKKAGQIIFLDHGEVTGRGR 551
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVtHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
335-545 |
7.72e-41 |
|
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: 147.23 E-value: 7.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 335 KFDHVYFGYDD--TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYV 412
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQsNA---MMNGTIRDNILYG-----VDREVSEEELIHYAKLanchefimefeqgydtiVGERGLK------LSGGQRQR 478
Cdd:cd03225 81 FQ-NPddqFFGPTVEEEVAFGlenlgLPEEEIEERVEEALEL-----------------VGLEGLRdrspftLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 479 IDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGE 545
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
21-289 |
2.92e-40 |
|
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: 147.79 E-value: 2.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISP-----VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVL 95
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqalnVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 96 WEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVP 175
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 176 LGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIG 255
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 2254949669 256 IILGFGGMRIASGAISAGTLVAMIFYVLNLSIPL 289
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
331-546 |
3.24e-40 |
|
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: 145.25 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 331 TGDLKFDH--VYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRK 408
Cdd:cd03369 4 HGEIEVENlsVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 409 IGYVMQSNAMMNGTIRDNilygVDR--EVSEEELihYAKLAnchefimefeqgydtiVGERGLKLSGGQRQRIDIARSFV 486
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSN----LDPfdEYSDEEI--YGALR----------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 487 KNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEV 546
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
334-545 |
4.96e-40 |
|
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: 143.87 E-value: 4.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS--LTDWRRKIGY 411
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQSNAMMNG-TIRDNILYGvdrevseeelihyaklanchefimefeqgydtivgerglkLSGGQRQRIDIARSFVKNPD 490
Cdd:cd03229 81 VFQDFALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 491 ILLLDEATANLDSESERKIQEALDILMEN--RTTIVIAHRLSTIKK-AGQIIFLDHGE 545
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
335-545 |
1.11e-39 |
|
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: 142.00 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 335 KFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQ 414
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 snammngtirdnilygvdrevseeelihyaklanchefimefeqgydtivgerglkLSGGQRQRIDIARSFVKNPDILLL 494
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 495 DEATANLDSESERKIQEAL-DILMENRTTIVIAHRLSTIKKAGQ-IIFLDHGE 545
Cdd:cd00267 105 DEPTSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELAADrVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-556 |
1.18e-39 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.19 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVM 413
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAM-MNGTIRDNILYG-------------VDREVSEEELihyaKLANCHEFImefEQGYDTivgerglkLSGGQRQRI 479
Cdd:COG1120 82 QEPPApFGLTVRELVALGryphlglfgrpsaEDREAVEEAL----ERTGLEHLA---DRPVDE--------LSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 480 DIARSFVKNPDILLLDEATANLDsesERKIQEALDIL-----MENRTTIVIAH------RLSTikkagQIIFLDHGEVTG 548
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLD---LAHQLEVLELLrrlarERGRTVVMVLHdlnlaaRYAD-----RLVLLKDGRIVA 218
|
....*...
gi 2254949669 549 RGRHEELM 556
Cdd:COG1120 219 QGPPEEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
349-499 |
1.40e-39 |
|
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: 141.63 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNG-TIRDNI 427
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 428 -----LYGVDREVSEEELIHYAKLANchefIMEFEqgyDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATA 499
Cdd:pfam00005 81 rlgllLKGLSKREKDARAEEALEKLG----LGDLA---DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
334-546 |
3.05e-39 |
|
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: 142.66 E-value: 3.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIdaLSLTDWRRKIGYVM 413
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMM-NGTIRDNILYG-VDREVSEEELIhyaklANCHEfiMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDI 491
Cdd:cd03259 79 QDYALFpHLTVAENIAFGlKLRGVPKAEIR-----ARVRE--LLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 492 LLLDEATANLDSESERKIQEAL-DILMENR-TTIVIAHRLS-TIKKAGQIIFLDHGEV 546
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELkELQRELGiTTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
334-557 |
3.86e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 143.46 E-value: 3.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTdWRRKIGYVM 413
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNG-TIRDNI-----LYGVDREVSEEELIHYAKLanchefiMEFEQGYDTIVGErglkLSGGQRQRIDIARSFVK 487
Cdd:COG4555 81 DERGLYDRlTVRENIryfaeLYGLFDEELKKRIEELIEL-------LGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-309 |
4.98e-39 |
|
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: 144.60 E-value: 4.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKFT----FESISPVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLW 96
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTigskSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPL 176
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 177 GKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGI 256
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 257 ILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-309 |
1.47e-38 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 143.81 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 16 WPVGLIIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESIspvfiiALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVL 95
Cdd:cd18564 20 WPLKVVIDDVLGDKPLPGLLGLAPLLGPDPLALLLLAAA------ALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 96 WEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVP 175
Cdd:cd18564 94 FAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 176 LGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIG 255
Cdd:cd18564 174 FSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTA 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 256 IILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18564 254 LVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
334-547 |
2.37e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.57 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKI 409
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNA-MMNGTIRDNILY-----GVDREVSEEE---------LIHYAKlANCHEfimefeqgydtivgerglkLSGG 474
Cdd:COG2884 82 GVVFQDFRlLPDRTVYENVALplrvtGKSRKEIRRRvrevldlvgLSDKAK-ALPHE-------------------LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 475 QRQRIDIARSFVKNPDILLLDEATANLDSESERKIqeaLDILME-NR--TTIVIA-HRLSTIKKAGQ-IIFLDHGEVT 547
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEI---MELLEEiNRrgTTVLIAtHDLELVDRMPKrVLELEDGRLV 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
337-550 |
5.19e-38 |
|
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: 138.34 E-value: 5.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 337 DHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSN 416
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 417 AMMngtirdNILYGVDREVSEeelihyaklanchefimefeqgydtivgerglkLSGGQRQRIDIARSFVKNPDILLLDE 496
Cdd:cd03214 83 ELL------GLAHLADRPFNE---------------------------------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 497 ATANLDSESErkiQEALDILME-----NRTTIVIAHRLS-TIKKAGQIIFLDHGEVTGRG 550
Cdd:cd03214 124 PTSHLDIAHQ---IELLELLRRlarerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-575 |
7.12e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.22 E-value: 7.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALsltdwRRKIGYVM 413
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNG---TIRDNILYGVDREV--------SEEELIHYA-KLANCHEFImefeqgyDTIVGErglkLSGGQRQRIDI 481
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVLMGRYGRRglfrrpsrADREAVDEAlERVGLEDLA-------DRPIGE----LSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 482 ARSFVKNPDILLLDEATANLDSESERKIQEALDIL-MENRTTIVIAHRLSTIKK-AGQIIFLDHGeVTGRGRHEELMQTH 559
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPPEEVLTPE 229
|
250
....*....|....*.
gi 2254949669 560 AMYQQFVETQNLTQHR 575
Cdd:COG1121 230 NLSRAYGGPVALLAHG 245
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
75-562 |
1.57e-37 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 149.33 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 75 FGYYLLNKIGEkiIYAIRSV---LWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIML 151
Cdd:TIGR00957 1023 FGYSMAVSIGG--IQASRVLhqdLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVI 1100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 152 FvldwqmtlltfITIPIFILVIVPLGKI---MQKISTNTQTEIANFSGL--------LGRVLTEMRLVKVAN-TEKLELD 219
Cdd:TIGR00957 1101 L-----------LATPIAAVIIPPLGLLyffVQRFYVASSRQLKRLESVsrspvyshFNETLLGVSVIRAFEeQERFIHQ 1169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 220 ---KAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILgfggmrIASGAISAGTLVAMIFYVLNLSIPLINLSTLV 296
Cdd:TIGR00957 1170 sdlKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAV------ISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMS 1243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 297 TDYKKAVGASQRIYEilHEPLENIAAPNLQDEIP------TGDLKFDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPS 368
Cdd:TIGR00957 1244 SEMETNIVAVERLKE--YSETEKEAPWQIQETAPpsgwppRGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRT 1321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 369 GSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNI-LYGvdrEVSEEELIHYAKLA 447
Cdd:TIGR00957 1322 GAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS---QYSDEEVWWALELA 1398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 448 NCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAH 527
Cdd:TIGR00957 1399 HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH 1478
|
490 500 510
....*....|....*....|....*....|....*
gi 2254949669 528 RLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMY 562
Cdd:TIGR00957 1479 RLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
345-555 |
4.42e-37 |
|
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: 137.71 E-value: 4.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 345 DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKIGYVMQS-NAMMN 420
Cdd:cd03258 17 KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKARRRIGMIFQHfNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 GTIRDNILY-----GVDREVSEE---ELIHYAKLANCHEFimefeqgYDTivgerglKLSGGQRQRIDIARSFVKNPDIL 492
Cdd:cd03258 97 RTVFENVALpleiaGVPKAEIEErvlELLELVGLEDKADA-------YPA-------QLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 493 LLDEATANLDSESERKIQEAL-DILMENRTTIV-IAHRLSTIKK-AGQIIFLDHGEVTGRGRHEEL 555
Cdd:cd03258 163 LCDEATSALDPETTQSILALLrDINRELGLTIVlITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
336-565 |
7.36e-37 |
|
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: 136.86 E-value: 7.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 336 FDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKIGYV 412
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQSNAMMNG-TIRDNILYGVdREVSE--EELIhyAKLAnchEFIMEFeqgydtiVGERGLK------LSGGQRQRIDIAR 483
Cdd:cd03261 83 FQSGALFDSlTVFENVAFPL-REHTRlsEEEI--REIV---LEKLEA-------VGLRGAEdlypaeLSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 484 SFVKNPDILLLDEATANLD-------SESERKIQEALDIlmenrTTIVIAHRLSTIKKAG-QIIFLDHGEVTGRGRHEEL 555
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELGL-----TSIMVTHDLDTAFAIAdRIAVLYDGKIVAEGTPEEL 224
|
250
....*....|.
gi 2254949669 556 MQ-THAMYQQF 565
Cdd:cd03261 225 RAsDDPLVRQF 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
334-550 |
8.28e-37 |
|
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: 135.13 E-value: 8.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYD--DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTdWRRKIGY 411
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQSNAMMNGTIRDNIlygvdrevseeelihyaklanchefimefeqgydtivgerGLKLSGGQRQRIDIARSFVKNPDI 491
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 492 LLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRG 550
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
334-527 |
1.00e-36 |
|
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: 136.06 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDD----TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSltdwrRKI 409
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNAMMN-GTIRDNILYGVD-REVSEEELIHYAklancHEFIMEFeqgydtivgerGLK---------LSGGQRQR 478
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElQGVPKAEARERA-----EELLELV-----------GLSgfenayphqLSGGMRQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 479 IDIARSFVKNPDILLLDEATANLDSESERKIQEAL-DILMENRTTIV-IAH 527
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELlDIWRETGKTVLlVTH 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
334-546 |
1.07e-36 |
|
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: 134.45 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSlTDWRRKIGYVM 413
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNG-TIRDNilygvdrevseeelihyaklanchefimefeqgydtivgergLKLSGGQRQRIDIARSFVKNPDIL 492
Cdd:cd03230 80 EEPSLYENlTVREN------------------------------------------LKLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 493 LLDEATANLDSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEV 546
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
20-309 |
1.58e-36 |
|
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: 138.00 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 20 LIIVAVTIAsIGSLTGLLVPLFTGQVVDKFTFESISPVF---IIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLW 96
Cdd:cd18550 1 LALVLLLIL-LSALLGLLPPLLLREIIDDALPQGDLGLLvllALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPL 176
Cdd:cd18550 80 AHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 177 GKIMQKISTNTQTEIANFSGLLGRVLTE--MRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITI 254
Cdd:cd18550 160 GRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 255 GIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18550 240 ALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
334-550 |
2.74e-36 |
|
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: 135.33 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDH--VYF--GYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWR 406
Cdd:cd03257 2 LEVKNlsVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 407 RKIGYVMQS-----NAMMngTIRDNI-----LYGVDREVSEEELIHYAKLanchefiMEFEQGyDTIVGERGLKLSGGQR 476
Cdd:cd03257 82 KEIQMVFQDpmsslNPRM--TIGEQIaeplrIHGKLSKKEARKEAVLLLL-------VGVGLP-EEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 477 QRIDIARSFVKNPDILLLDEATANLDSESERKIqeaLDILME-----NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRG 550
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQI---LDLLKKlqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
334-567 |
3.09e-36 |
|
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: 135.51 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYV 412
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQSNAMM-NGTIRDNI-----LYGVDREVSEE---ELIHYAKLAnchefIMEFEQGYDTivgerglKLSGGQRQRIDIAR 483
Cdd:cd03295 81 IQQIGLFpHMTVEENIalvpkLLKWPKEKIREradELLALVGLD-----PAEFADRYPH-------ELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 484 SFVKNPDILLLDEATANLDSESERKIQEALDILME--NRTTIVIAHRL-STIKKAGQIIFLDHGEVTGRGRHEELMQTHA 560
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
....*..
gi 2254949669 561 myQQFVE 567
Cdd:cd03295 229 --NDFVA 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
334-546 |
5.29e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 134.74 E-value: 5.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDAlSLTDW---RRKIG 410
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDInklRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQS-NAMMNGTIRDNILY------GVDREVSEEELIHY-AKlanchefimefeqgydtiVG--ERGLK----LSGGQR 476
Cdd:COG1126 81 MVFQQfNLFPHLTVLENVTLapikvkKMSKAEAEERAMELlER------------------VGlaDKADAypaqLSGGQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 477 QRIDIARSFVKNPDILLLDEATANLDSESerkIQEALDILM----ENRTTIVIAHRLSTIKK-AGQIIFLDHGEV 546
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPEL---VGEVLDVMRdlakEGMTMVVVTHEMGFAREvADRVVFMDGGRI 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
311-557 |
5.85e-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: 141.19 E-value: 5.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 311 EILHEPLENIAAPNLQDEIPTGD---------LKFDHVYFGY-----DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLF 376
Cdd:COG1123 229 EILAAPQALAAVPRLGAARGRAApaaaaaeplLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 377 SLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKIGYVMQS-----NAMMngTIRDNILYGVD--REVSEEElihyakl 446
Cdd:COG1123 309 RLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDpysslNPRM--TVGDIIAEPLRlhGLLSRAE------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 447 anCHEFIME-FEQgydtiVG-ERGLK------LSGGQRQRIDIARSFVKNPDILLLDEATANLDseseRKIQEA-LDILM 517
Cdd:COG1123 380 --RRERVAElLER-----VGlPPDLAdrypheLSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNLLR 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2254949669 518 E-----NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:COG1123 449 DlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
330-546 |
2.92e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.00 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 330 PTGDLKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLtdWRRKI 409
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP--EKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNA----MmngTIRDNILYG-----VDREVSEE------ELIHYAKLANC--HEfimefeqgydtivgerglkLS 472
Cdd:COG3842 80 GMVFQDYAlfphL---TVAENVAFGlrmrgVPKAEIRArvaellELVGLEGLADRypHQ-------------------LS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 473 GGQRQRIDIARSFVKNPDILLLDEATANLDSE------SE-RKIQEALDIlmenrTTIVIAHRLS---TIkkAGQIIFLD 542
Cdd:COG3842 138 GGQQQRVALARALAPEPRVLLLDEPLSALDAKlreemrEElRRLQRELGI-----TFIYVTHDQEealAL--ADRIAVMN 210
|
....
gi 2254949669 543 HGEV 546
Cdd:COG3842 211 DGRI 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
334-525 |
3.06e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 133.29 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY----DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSltdwrRKI 409
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNAMMN-GTIRDNILYG-----VDREVSEEELIHYAK---LAnchefimEFEQGYdtiVGErglkLSGGQRQRID 480
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelrgVPKAERRERARELLElvgLA-------GFEDAY---PHQ----LSGGMRQRVA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2254949669 481 IARSFVKNPDILLLDEATANLDSESERKIQ-EALDILMENRTTIVI 525
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQdELLRLWQETGKTVLF 194
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
30-309 |
4.86e-35 |
|
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: 133.59 E-value: 4.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 30 IGSLTGLLVPLFTGQVVDKFT----FESIS-PVFIIALVAvfLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKM 104
Cdd:cd18784 7 AAAVGEIFIPYYTGQVIDGIVieksQDKFSrAIIIMGLLA--IASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 105 PFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIMQKIS 184
Cdd:cd18784 85 GFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 185 TNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGGMR 264
Cdd:cd18784 165 KAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2254949669 265 IASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18784 245 VITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
338-546 |
5.32e-35 |
|
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: 131.11 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGydDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDAlSLTDW---RRKIGYVMQ 414
Cdd:cd03262 7 HKSFG--DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNInelRQKVGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 S-NAMMNGTIRDNILY------GVDREVSEEELIHYAKLANchefIMEFEQGYDtivgergLKLSGGQRQRIDIARSFVK 487
Cdd:cd03262 84 QfNLFPHLTVLENITLapikvkGMSKAEAEERALELLEKVG----LADKADAYP-------AQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 488 NPDILLLDEATANLDSESerkIQEALDILM----ENRTTIVIAHRLSTIKK-AGQIIFLDHGEV 546
Cdd:cd03262 153 NPKVMLFDEPTSALDPEL---VGEVLDVMKdlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
334-555 |
1.26e-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: 131.15 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKI 409
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQS-NAMMNGTIRDNILYG----------VDREVSEEElihYAKLANCHEfimefEQGYDTIVGERGLKLSGGQRQR 478
Cdd:cd03256 81 GMIFQQfNLIERLSVLENVLSGrlgrrstwrsLFGLFPKEE---KQRALAALE-----RVGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 479 IDIARSFVKNPDILLLDEATANLDSESERKIQEAL-DILME-NRTTIVIAHRLSTIKKAGQ-IIFLDHGEVTGRGRHEEL 555
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLAREYADrIVGLKDGRIVFDGPPAEL 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-525 |
3.58e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.16 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYE-IDQ----GGIYYDGTSI--DALSLTDWR 406
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPGarveGEILLDGEDIydPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 407 RKIGYVMQ-SN--AMmngTIRDNILYGV------DR----EVSEEELIHYA-------KLanchefimefeqgydtivGE 466
Cdd:COG1117 92 RRVGMVFQkPNpfPK---SIYDNVAYGLrlhgikSKseldEIVEESLRKAAlwdevkdRL------------------KK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 467 RGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRtTIVI 525
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY-TIVI 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
334-546 |
3.72e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.79 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKI 409
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQS-------NAMMN---------GTIRD--NILYGVDREVSEEELihyaklanchefimefEQgydtiVG------ 465
Cdd:COG3638 83 GMIFQQfnlvprlSVLTNvlagrlgrtSTWRSllGLFPPEDRERALEAL----------------ER-----VGladkay 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 466 ERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEAL-DILMENRTTIVIA-HRLSTIKK-AGQIIFLD 542
Cdd:COG3638 142 QRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREDGITVVVNlHQVDLARRyADRIIGLR 221
|
....
gi 2254949669 543 HGEV 546
Cdd:COG3638 222 DGRV 225
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
19-301 |
8.99e-34 |
|
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: 130.26 E-value: 8.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 19 GLIIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISPVFII---ALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVL 95
Cdd:cd18549 2 KLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIigaILLALYILRTLLNYFVTYWGHVMGARIETDMRRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 96 WEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVP 175
Cdd:cd18549 82 FEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 176 LGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIG 255
Cdd:cd18549 162 FNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2254949669 256 IILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKK 301
Cdd:cd18549 242 VVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
21-309 |
3.38e-33 |
|
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: 128.68 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISP----VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLW 96
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTAsqllRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPL 176
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 177 GKIMQKISTNTQteiANFSGLLGRV---LTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLIT 253
Cdd:cd18541 161 GKKIHKRFRKVQ---EAFSDLSDRVqesFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLS 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 254 IGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18541 238 FLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
21-309 |
3.82e-33 |
|
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: 128.37 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDK-FTFESISPV--FIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWE 97
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGpIAHGDRSALwpLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 98 HIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQkLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLG 177
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 178 KIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGII 257
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 258 LGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18543 240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
335-544 |
8.95e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 124.95 E-value: 8.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 335 KFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsidaLSLTDWRRKIGYVMQ 414
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 S---NAMMNGTIRDNILYGVDREVSEEELI---HYAKLANCHEFimefeqgydtiVGERGLK------LSGGQRQRIDIA 482
Cdd:cd03235 76 RrsiDRDFPISVRDVVLMGLYGHKGLFRRLskaDKAKVDEALER-----------VGLSELAdrqigeLSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 483 RSFVKNPDILLLDEATANLDSESERKIQEALDIL-MENRTTIVIAHRLSTIKKAG-QIIFLDHG 544
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFdRVLLLNRT 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-556 |
1.25e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.26 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 335 KFDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYV 412
Cdd:PRK13632 9 KVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQS--NAMMNGTIRDNILYG-----VDREVSEEELIHYAKLANCHEFImEFEQgydtivgergLKLSGGQRQRIDIARSF 485
Cdd:PRK13632 89 FQNpdNQFIGATVEDDIAFGlenkkVPPKKMKDIIDDLAKKVGMEDYL-DKEP----------QNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 486 VKNPDILLLDEATANLDSESERKIQEALDILMENR--TTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELM 556
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
86-567 |
2.41e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 133.18 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 86 KIIYAIRSVLWEHIIHLKMPFFDKNE----SGQLMSRLTDDTKVINDfISQKLPGFFPAVITLIGSLIMLF----VLDWQ 157
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDANALQQ-IAEQLHGLWSAPFRIIVSMVLLYqqlgVASLF 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 158 MTLLTFITIPIFILVIVPLGKIMQKISTNTQTEIanfsGLLGRVLTEMRLVKVANTEKleldKAHSNLKTIYNLGL---K 234
Cdd:PLN03232 446 GSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRV----GIINEILASMDTVKCYAWEK----SFESRIQGIRNEELswfR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 235 QAKI-----AAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLsiplinLSTLVTDYKKAVGASQRI 309
Cdd:PLN03232 518 KAQLlsafnSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNM------LPNLLSQVVNANVSLQRI 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 310 YEILHEPlENIAAPN--LQDEIPTGDLKfdHVYFGYD---DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIerMYE 384
Cdd:PLN03232 592 EELLLSE-ERILAQNppLQPGAPAISIK--NGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGE 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 385 IDQGgiyyDGTSIDAlsltdwRRKIGYVMQSNAMMNGTIRDNILYGVDREVSEeelihYAKL--ANCHEFIMEFEQGYD- 461
Cdd:PLN03232 667 LSHA----ETSSVVI------RGSVAYVPQVSWIFNATVRENILFGSDFESER-----YWRAidVTALQHDLDLLPGRDl 731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 462 TIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKI-QEALDILMENRTTIVIAHRLSTIKKAGQIIF 540
Cdd:PLN03232 732 TEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIIL 811
|
490 500
....*....|....*....|....*..
gi 2254949669 541 LDHGEVTGRGRHEELMQTHAMYQQFVE 567
Cdd:PLN03232 812 VSEGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-559 |
3.91e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 124.15 E-value: 3.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFG--YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQS 415
Cdd:COG1124 8 SVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 416 -----NAMMNgtirdnilygVDREVSEEELIHYaklanchefIMEFEQGYDTIVGERGL----------KLSGGQRQRID 480
Cdd:COG1124 88 pyaslHPRHT----------VDRILAEPLRIHG---------LPDREERIAELLEQVGLppsfldryphQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 481 IARSFVKNPDILLLDEATANLDSESERKIQEALDILMENR--TTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
..
gi 2254949669 558 TH 559
Cdd:COG1124 229 GP 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-555 |
4.99e-32 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 132.34 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 30 IGSLTGLLVPLFTGQVVDKF----TFE-SISPVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKM 104
Cdd:TIGR01271 91 FGEATKAVQPLLLGRIIASYdpfnAPErEIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 105 PFFDKNESGQLMSRLTDDTKVINDFISqkLPGFF---PAVITLIGSLIMLFVLDWQMTLLTFITIpiFILVIVPLGKIMQ 181
Cdd:TIGR01271 171 RVLDKISTGQLVSLLSNNLNKFDEGLA--LAHFVwiaPLQVILLMGLIWELLEVNGFCGLGFLIL--LALFQACLGQKMM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 182 KISTNTQTEIANFSGLLGRVLTEMRLVKVANTEklelDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLitigiilgFG 261
Cdd:TIGR01271 247 PYRDKRAGKISERLAITSEIIENIQSVKAYCWE----EAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFF--------FS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 262 G-----MRIASGAISAGTLVAMIFYVLNLSIPLI-----NLSTLVTDYKKAVGASQRIYEILH----------------- 314
Cdd:TIGR01271 315 GffvvfLSVVPYALIKGIILRRIFTTISYCIVLRmtvtrQFPGAIQTWYDSLGAITKIQDFLCkeeyktleynlttteve 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 315 -------------EPLENIAAPNLQDEIPTGDLKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIER 381
Cdd:TIGR01271 395 mvnvtaswdegigELFEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 382 MYEIDQGGIYYDGtsidalsltdwrrKIGYVMQSNAMMNGTIRDNILYGVdrevSEEELIHYAKLANCH--EFIMEFEQG 459
Cdd:TIGR01271 475 ELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFGL----SYDEYRYTSVIKACQleEDIALFPEK 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 460 YDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEA-LDILMENRTTIVIAHRLSTIKKAGQI 538
Cdd:TIGR01271 538 DKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKI 617
|
570
....*....|....*..
gi 2254949669 539 IFLDHGEVTGRGRHEEL 555
Cdd:TIGR01271 618 LLLHEGVCYFYGTFSEL 634
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-557 |
5.88e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.74 E-value: 5.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDT--PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGY 411
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQS--NAMMNGTIRDNILYGVD-REVSEEELI---HYA-KLANCHEFiMEFEQGydtivgerglKLSGGQRQRIDIARS 484
Cdd:PRK13635 86 VFQNpdNQFVGATVQDDVAFGLEnIGVPREEMVervDQAlRQVGMEDF-LNREPH----------RLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 485 FVKNPDILLLDEATANLDSESERKIQEALDILMENR--TTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
315-555 |
6.95e-32 |
|
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: 124.58 E-value: 6.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 315 EPLENIAAPNLQDEIPTGDLKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDG 394
Cdd:cd03291 19 ELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 395 tsidalsltdwrrKIGYVMQSNAMMNGTIRDNILYGVdrevSEEELIHYAKLANCH--EFIMEFEQGYDTIVGERGLKLS 472
Cdd:cd03291 99 -------------RISFSSQFSWIMPGTIKENIIFGV----SYDEYRYKSVVKACQleEDITKFPEKDNTVLGEGGITLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 473 GGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEA-LDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGR 551
Cdd:cd03291 162 GGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGT 241
|
....
gi 2254949669 552 HEEL 555
Cdd:cd03291 242 FSEL 245
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
21-309 |
8.08e-32 |
|
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: 124.52 E-value: 8.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDK-FTFESISPVFIIAL--VAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWE 97
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSgVRAGDLGVLLLAAAayLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 98 HIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLG 177
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 178 KIMQKISTNTQTEIANFSGLLGRVLTEMRLVKV-----ANTEKL-ELDKAH--SNLKTIYNLG--------LKQAKIAAV 241
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAfrrerRNAERFaELSDDYrdARLRAQRLVAiyfpgvelLGNLATAAV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 242 VqpisgiimlitigiilGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18546 241 L----------------LVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
346-560 |
1.10e-31 |
|
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: 123.52 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 346 TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRK-IGYVMQSNAMM-N 420
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 GTIRDNILY-----GVDREVSEEELIHYAKLANCHEFImefeqgyDTIVGErglkLSGGQRQRIDIARSFVKNPDILLLD 495
Cdd:cd03294 117 RTVLENVAFglevqGVPRAEREERAAEALELVGLEGWE-------HKYPDE----LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 496 EATANLDSESERKIQEALDIL--MENRTTIVIAHRLS-TIKKAGQIIFLDHGEVTGRGRHEELMQTHA 560
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPA 253
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
103-567 |
2.19e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 130.28 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 103 KMPFFDKNESGQLMSRLTDDTkvinDFISQKLPgffpavITLIGSLIMLFVLDWQMtLLTFITIPIFILVIVPLG----K 178
Cdd:PTZ00243 1045 TMSFFDTTPLGRILNRFSRDI----DILDNTLP------MSYLYLLQCLFSICSSI-LVTSASQPFVLVALVPCGylyyR 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 179 IMQKIS-----TNTQTEIAN---FSgLLGRVLT---------EMRLVKVANTEKLELDKAHSNLKTIYN--LGLKQAKIA 239
Cdd:PTZ00243 1114 LMQFYNsanreIRRIKSVAKspvFT-LLEEALQgsatitaygKAHLVMQEALRRLDVVYSCSYLENVANrwLGVRVEFLS 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 240 AVVqpisgiimlITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHEpLEN 319
Cdd:PTZ00243 1193 NIV---------VTVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDE-VPH 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 320 IAAPNLQDEI-----------------------PT---------GDLKFDHVYFGY-DDTP-VLKDVSFNVLRGEVTAFV 365
Cdd:PTZ00243 1263 EDMPELDEEVdalerrtgmaadvtgtvviepasPTsaaphpvqaGSLVFEGVQMRYrEGLPlVLRGVSFRIAPREKVGIV 1342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 366 GPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRDNilygVD--REVSEEELIHY 443
Cdd:PTZ00243 1343 GRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN----VDpfLEASSAEVWAA 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 444 AKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVK-NPDILLLDEATANLDSESERKIQEALDILMENRTT 522
Cdd:PTZ00243 1419 LELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTV 1498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2254949669 523 IVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEEL-MQTHAMYQQFVE 567
Cdd:PTZ00243 1499 ITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVE 1544
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
338-561 |
5.05e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.94 E-value: 5.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIerMYEIDQGG-----IYYDGTSIDALSLTDWRRKIGYV 412
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL--MGLLPHGGrisgeVLLDGRDLLELSEALRGRRIGMV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQS--NAMMNGTIRDNI-----LYGVDREVSEEELIHYAKLAnchefimefeqGYDTIVGERGLKLSGGQRQRIDIARSF 485
Cdd:COG1123 89 FQDpmTQLNPVTVGDQIaealeNLGLSRAEARARVLELLEAV-----------GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 486 VKNPDILLLDEATANLDSESERKIQEALDILMENR--TTIVIAHRLSTI-KKAGQIIFLDHGEVTGRGRHEELMQTHAM 561
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
341-541 |
7.70e-31 |
|
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: 119.92 E-value: 7.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 341 FGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDAlSLTDWRRKIGYVMQSNAMMN 420
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 G-TIRDNI-----LYGVDREVSEEELIHYAKlanchefIMEFEQGYDTIVGErglkLSGGQRQRIDIARSFVKNPDILLL 494
Cdd:cd03263 89 ElTVREHLrfyarLKGLPKSEIKEEVELLLR-------VLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 495 DEATANLDSESERKIQEALDILMENRTTI----------VIAHRLStIKKAGQIIFL 541
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIIltthsmdeaeALCDRIA-IMSDGKLRCI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
345-568 |
1.10e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 122.49 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 345 DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTL---FSLIERMyeiDQGGIYYDGTSIDALS---LTDWRRKIGYVMQS-NA 417
Cdd:COG1135 17 PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLERP---TSGSVLVDGVDLTALSereLRAARRKIGMIFQHfNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 418 MMNGTIRDNILY-----GVDREVSEE---ELIhyaklanchEFImefeqgydtivgerGLK---------LSGGQRQRID 480
Cdd:COG1135 94 LSSRTVAENVALpleiaGVPKAEIRKrvaELL---------ELV--------------GLSdkadaypsqLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 481 IARSFVKNPDILLLDEATANLDSESERKIqeaLDILME-NR----TTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEE 554
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSI---LDLLKDiNRelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLD 227
|
250
....*....|....*.
gi 2254949669 555 LMQT--HAMYQQFVET 568
Cdd:COG1135 228 VFANpqSELTRRFLPT 243
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
332-568 |
5.09e-30 |
|
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: 118.86 E-value: 5.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 332 GDLKFDHVYFGYDDT--PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKI 409
Cdd:cd03288 18 GEIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNAMMNGTIRDNIlyGVDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNP 489
Cdd:cd03288 98 SIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 490 DILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELM-QTHAMYQQFVET 568
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRT 255
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
47-556 |
9.51e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 125.47 E-value: 9.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 47 DKFTFESISPVFIIALVAVFLVNAVLSGF--GYYLLNKIgekiIYAIRSV---LWEHIIHLKMPFFDKNESGQLMSRLTD 121
Cdd:PLN03232 940 DQSTPKSYSPGFYIVVYALLGFGQVAVTFtnSFWLISSS----LHAAKRLhdaMLNSILRAPMLFFHTNPTGRVINRFSK 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 122 DTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDwqmTLLTFITIPIFILVIVPL------GKIMQKISTNTQTEIANFS 195
Cdd:PLN03232 1016 DIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS---TISLWAIMPLLILFYAAYlyyqstSREVRRLDSVTRSPIYAQF 1092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 196 GLLGRVLTEMRLVKVAN-TEKLELDKAHSNLK-TIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGgmRIASGAISAG 273
Cdd:PLN03232 1093 GEALNGLSSIRAYKAYDrMAKINGKSMDNNIRfTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNG--NAENQAGFAS 1170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 274 TLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHEPLEniAAPNLQDEIP------TGDLKFDHVYFGYDD-- 345
Cdd:PLN03232 1171 TMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSE--ATAIIENNRPvsgwpsRGSIKFEDVHLRYRPgl 1248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 346 TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTIRD 425
Cdd:PLN03232 1249 PPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRF 1328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NIlygvD--REVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDS 503
Cdd:PLN03232 1329 NI----DpfSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 504 ESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELM 556
Cdd:PLN03232 1405 RTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-550 |
1.09e-29 |
|
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: 115.73 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 320 IAAPNLQDEIPTGDLKFDhvyfgyddTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLI--ERMYEIDQGGIYYDGTSI 397
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSG--------KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 398 DALSltdWRRKIGYVMQsnammngtirDNILYGvdrEVSEEELIHYAklANChefimefeqgydtivgeRGLklSGGQRQ 477
Cdd:cd03213 76 DKRS---FRKIIGYVPQ----------DDILHP---TLTVRETLMFA--AKL-----------------RGL--SGGERK 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 478 RIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILM-ENRTTIVIAHRLST--IKKAGQIIFLDHGEVTGRG 550
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
334-564 |
1.13e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.36 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDT--PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMY---EIDQGGIYYDGTSIDALSLTDWRRK 408
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 409 IGYVMQS--NAMMNGTIRDNILYGVD-REVSEEELIHYAKLANCHEFIMEFEQGYDTivgerglKLSGGQRQRIDIARSF 485
Cdd:PRK13640 86 VGIVFQNpdNQFVGATVGDDVAFGLEnRAVPRPEMIKIVRDVLADVGMLDYIDSEPA-------NLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 486 VKNPDILLLDEATANLDSESERKIQEALDILME--NRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQ 563
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
.
gi 2254949669 564 Q 564
Cdd:PRK13640 239 E 239
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
21-309 |
1.35e-29 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 118.27 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESISPVFI---IALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWE 97
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILrtgLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 98 HIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLG 177
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 178 KIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDK-AHSNlKTIYNLGLKQAKIAAVVQPISGIIMLITIGI 256
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERfDKAN-DDLTDTSLKAGRLMALLNPLMMLIMNLAIVA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 257 ILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18548 240 ILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
334-546 |
2.30e-29 |
|
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: 117.15 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDT--PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsIDALS---LTDWRRK 408
Cdd:TIGR04520 1 IEVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDeenLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 409 IGYVMQS--NAMMNGTIRDNILYGVD-REVSEEELIH----YAKLANCHEFiMEFEQgydtivgergLKLSGGQRQRIDI 481
Cdd:TIGR04520 79 VGMVFQNpdNQFVGATVEDDVAFGLEnLGVPREEMRKrvdeALKLVGMEDF-RDREP----------HLLSGGQKQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 482 ARSFVKNPDILLLDEATANLDSESERKIQEALDILM--ENRTTIVIAHRLSTIKKAGQIIFLDHGEV 546
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKI 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
332-546 |
4.51e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.25 E-value: 4.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 332 GDLKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLfsLieRM----YEIDQGGIYYDGTsiDALSLTDWRR 407
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL--L--RMiaglEDPTSGEILIGGR--DVTDLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 408 KIGYVMQSNAMM-NGTIRDNILYG----------VDREVSE-------EELIH-YAKlanchefimefeqgydtivgerg 468
Cdd:COG3839 76 NIAMVFQSYALYpHMTVYENIAFPlklrkvpkaeIDRRVREaaellglEDLLDrKPK----------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 469 lKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSE------SE-RKIQEALDIlmenrTTIVIAHRLS---TIkkAGQI 538
Cdd:COG3839 133 -QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRLGT-----TTIYVTHDQVeamTL--ADRI 204
|
....*...
gi 2254949669 539 IFLDHGEV 546
Cdd:COG3839 205 AVMNDGRI 212
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
19-309 |
5.55e-29 |
|
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: 116.78 E-value: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 19 GLIIVAVTIASIGSLTGLLVPLFTGQVVDKFTFESIS---PVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVL 95
Cdd:cd18570 2 KLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDInllNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 96 WEHIIHLKMPFFDKNESGQLMSRLTDDTKvINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVP 175
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFNDANK-IREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 176 LGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIG 255
Cdd:cd18570 161 FNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 256 IILGFGGMRIASGAISAGTLVAmiFYVL--NLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18570 241 LILWIGSYLVIKGQLSLGQLIA--FNALlgYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
13-313 |
9.98e-29 |
|
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: 116.40 E-value: 9.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 13 KISWPVGLIIVAVTIASIGSltGLLVPLF---TGQVVDKFTF----ESISPVFIIALVavFLVNAVLSGFGY----YLLN 81
Cdd:cd18578 2 KLNKPEWPLLLLGLIGAIIA--GAVFPVFailFSKLISVFSLpdddELRSEANFWALM--FLVLAIVAGIAYflqgYLFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 82 KIGEKIIYAIRSVLWEHIIHLKMPFFD--KNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMT 159
Cdd:cd18578 78 IAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 160 LLTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIA 239
Cdd:cd18578 158 LVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALIS 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 240 AVVQPISGIIMLITIGIILGFGGMRIASGAISAG----TLVAMIFYVLNLSipliNLSTLVTDYKKAVGASQRIYEIL 313
Cdd:cd18578 238 GLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEqffiVFMALIFGAQSAG----QAFSFAPDIAKAKAAAARIFRLL 311
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
260-557 |
1.28e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 121.77 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 260 FGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRIYEILHEPLEniAAPNLQDEIP------TGD 333
Cdd:PLN03130 1160 MQNGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSE--APLVIENNRPppgwpsSGS 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGY 411
Cdd:PLN03130 1238 IKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQSNAMMNGTIRDNIlygvD--REVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNP 489
Cdd:PLN03130 1318 IPQAPVLFSGTVRFNL----DpfNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 490 DILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
336-558 |
3.80e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.88 E-value: 3.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 336 FDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSI--DALSLTDWRRKIGYVM 413
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QS-NAMMNGTIRDNILYGVDRevseeelIHYAKLANCHEFIMEfeqgydtIVGERGL---------KLSGGQRQRIDIAR 483
Cdd:PRK09493 84 QQfYLFPHLTALENVMFGPLR-------VRGASKEEAEKQARE-------LLAKVGLaerahhypsELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 484 SFVKNPDILLLDEATANLDSESErkiQEAL----DILMENRTTIVIAHRLSTIKKAG-QIIFLDHGEVTGRGRHEELMQT 558
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELR---HEVLkvmqDLAEEGMTMVIVTHEIGFAEKVAsRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
334-526 |
4.09e-28 |
|
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: 111.80 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLtDWRRKIGYVM 413
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNG-TIRDNI-----LYGVDREVSE-EELIHYAKLAnchefimEFEqgyDTIVGerglKLSGGQRQRIDIARSFV 486
Cdd:COG4133 82 HADGLKPElTVRENLrfwaaLYGLRADREAiDEALEAVGLA-------GLA---DLPVR----QLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2254949669 487 KNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIA 526
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
348-554 |
6.85e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 112.04 E-value: 6.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTdwRRKIGYVMQSNAMM-NGTIRDN 426
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 427 ILYGVDREVSEEELIHyAKLANCHEFImefeqGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESE 506
Cdd:cd03299 92 IAYGLKKRKVDKKEIE-RKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 507 RKIQEAL-DILMENRTTIV-IAHRLSTIKK-AGQIIFLDHGEVTGRGRHEE 554
Cdd:cd03299 166 EKLREELkKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
334-558 |
7.82e-28 |
|
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: 112.10 E-value: 7.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMY------EIDQGGIYYDGTSIDalsltDWRR 407
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygnDVRLFGERRGGEDVW-----ELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 408 KIGYVmqSNAMM-----NGTIRDNIL------YGVDREVSEE---------ELIHYAKLANchefimefeQGYDTivger 467
Cdd:COG1119 79 RIGLV--SPALQlrfprDETVLDVVLsgffdsIGLYREPTDEqrerarellELLGLAHLAD---------RPFGT----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 468 glkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENR-TTIV-IAHRLSTIKKA-GQIIFLDHG 544
Cdd:COG1119 143 ---LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEIPPGiTHVLLLKDG 219
|
250
....*....|....
gi 2254949669 545 EVTGRGRHEELMQT 558
Cdd:COG1119 220 RVVAAGPKEEVLTS 233
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
20-309 |
8.34e-28 |
|
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: 113.34 E-value: 8.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 20 LIIVAVTIASIGSLTGLLVPLFTGQVVDKF----TFESIsPVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVL 95
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFitpgTLDGL-TGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 96 WEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVP 175
Cdd:cd18540 82 FEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 176 LGKIMQKIS-----TNTQTeIANFS-GLLGrvlteMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGII 249
Cdd:cd18540 162 FQKKILKAYrkvrkINSRI-TGAFNeGITG-----AKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 250 MLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18540 236 GSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
334-546 |
8.77e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 110.81 E-value: 8.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIdalslTDWR---RKIG 410
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPpkdRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQSNAMM-NGTIRDNILYG-----VDREVSEEELIHYAKLAnchefimefeqGYDTIVGERGLKLSGGQRQRIDIARS 484
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklrkVPKDEIDERVREVAELL-----------QIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 485 FVKNPDILLLDEATANLDSE------SE-RKIQEALDIlmenrTTIVIAH-RLSTIKKAGQIIFLDHGEV 546
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKlrvqmrAElKRLQQRLGT-----TTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
338-562 |
1.29e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.79 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYfgYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID-----QGGIYYDGTSIDA--LSLTDWRRKIG 410
Cdd:PRK14239 12 SVY--YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSprTDTVDLRKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQSNAMMNGTIRDNILYGV------DREVSEEELIHYAKLANCHEFIMEfeQGYDTIVGerglkLSGGQRQRIDIARS 484
Cdd:PRK14239 90 MVFQQPNPFPMSIYENVVYGLrlkgikDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 485 FVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHrlsTIKKAGQI-----IFLDhGEVTgrgrheELMQTH 559
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRIsdrtgFFLD-GDLI------EYNDTK 232
|
...
gi 2254949669 560 AMY 562
Cdd:PRK14239 233 QMF 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
338-556 |
3.61e-27 |
|
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: 109.83 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGydDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTD-WRRKIGYVMQ-S 415
Cdd:cd03219 7 TKRFG--GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiARLGIGRTFQiP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 416 NAMMNGTIRDNILYGV-----------DREVSEEELIHYAklanchEFIMEF---EQGYDTIVGErglkLSGGQRQRIDI 481
Cdd:cd03219 85 RLFPELTVLENVMVAAqartgsglllaRARREEREARERA------EELLERvglADLADRPAGE----LSYGQQRRLEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 482 ARSFVKNPDILLLDEATANL-DSESERKIQEALDILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELM 556
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
334-555 |
3.76e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY--DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGY 411
Cdd:PRK13648 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQS--NAMMNGTIRDNILYGVdrevsEEELIHYAKLancHEFIMEFEQGYDTI--VGERGLKLSGGQRQRIDIARSFVK 487
Cdd:PRK13648 88 VFQNpdNQFVGSIVKYDVAFGL-----ENHAVPYDEM---HRRVSEALKQVDMLerADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALDILMENR--TTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEEL 555
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
351-569 |
4.64e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 112.51 E-value: 4.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 351 DVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGT----SIDALSLTDWRRKIGYVMQSNAMM-NGTIRD 425
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NILYGVDREVSEEELIHYAKLANChefimefeQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSES 505
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIEL--------LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 506 ERKIQEALDILME--NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVETQ 569
Cdd:TIGR02142 167 KYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQ 233
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-309 |
5.04e-27 |
|
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: 111.50 E-value: 5.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 22 IVAVTIASIGS-LTGLLVPLFTGQVVDKFTF--ESISPVFI----------------IALVAVFLVNAVLSGFGYYLLNK 82
Cdd:cd18565 1 LVLGLLASILNrLFDLAPPLLIGVAIDAVFNgeASFLPLVPaslgpadprgqlwllgGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 83 IGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLT 162
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 163 FITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVV 242
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 243 QPISGIIMLITIGIILGFGGMRI------ASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18565 241 FPVIRLVAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-566 |
6.10e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 109.62 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 326 QDEIPTGDLKfdhVYFGydDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID-----QGGIYYDGTSIDAL 400
Cdd:PRK14247 1 MNKIEIRDLK---VSFG--QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 401 SLTDWRRKIGYVMQ-SNAMMNGTIRDNILYG--VDREV-SEEELIHYAKLAnchefiMEFEQGYDTI---VGERGLKLSG 473
Cdd:PRK14247 76 DVIELRRRVQMVFQiPNPIPNLSIFENVALGlkLNRLVkSKKELQERVRWA------LEKAQLWDEVkdrLDAPAGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 474 GQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQ-IIFLDHGEVTGRGRH 552
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDyVAFLYKGQIVEWGPT 229
|
250
....*....|....*.
gi 2254949669 553 EELMQT--HAMYQQFV 566
Cdd:PRK14247 230 REVFTNprHELTEKYV 245
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
343-555 |
1.23e-26 |
|
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: 107.84 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSI--DAlslTDWRRKIGYVMQSNAMMN 420
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEP---REVRRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 G-TIRDNI-----LYGVDREVSEE---ELIHYAKLanchefiMEFEqgyDTIVGerglKLSGGQRQRIDIARSFVKNPDI 491
Cdd:cd03265 87 ElTGWENLyiharLYGVPGAERREridELLDFVGL-------LEAA---DRLVK----TYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 492 LLLDEATANLDSESERKIQEAL-DILMENRTTIVI-AHRLSTIKK-AGQIIFLDHGEVTGRGRHEEL 555
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIeKLKEEFGMTILLtTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
334-553 |
1.58e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.88 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVM 413
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNGTIRDNIL--YGVDREVSEEelihyAKLAnchEFIMEFEQGyDTIVGERGLKLSGGQRQRIDIARSFVKNPDI 491
Cdd:PRK10247 88 QTPTLFGDTVYDNLIfpWQIRNQQPDP-----AIFL---DDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 492 LLLDEATANLDSESERKIQEALDILMENRTTIVI--AHRLSTIKKAGQIIFLD-HGEVTGRGRHE 553
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
348-551 |
3.25e-26 |
|
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: 107.13 E-value: 3.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLI---ERmyeIDQGGIYYDGTSIDALS---LTDWR-RKIGYVMQS----N 416
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALDedaRARLRaRHVGFVFQSfqllP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 417 AMmngTIRDNI-----LYGVD--REVSEEELIHYAklanchefimefeqgydtiVGERgLK-----LSGGQRQRIDIARS 484
Cdd:COG4181 104 TL---TALENVmlpleLAGRRdaRARARALLERVG-------------------LGHR-LDhypaqLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 485 FVKNPDILLLDEATANLDSESERKIQEAL-DILMENRTTIVIA-HRLSTIKKAGQIIFLDHGEVTGRGR 551
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
112-567 |
4.52e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 114.06 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 112 SGQLMSRLTDDTKVINDfISQKLPGFFPAVITLIGSLIMLF----VLDWQMTLLTFITIPIFILVIVPLGKIMQKISTNT 187
Cdd:PLN03130 397 SGKITNLMTTDAEALQQ-ICQQLHTLWSAPFRIIIAMVLLYqqlgVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRT 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 188 QTEIanfsGLLGRVLTEMRLVKVANTEKleldKAHSNLKTIYNLGL----KQAKIAAVVQPISGIIMLITIGIILG---- 259
Cdd:PLN03130 476 DKRI----GLMNEVLAAMDTVKCYAWEN----SFQSKVQTVRDDELswfrKAQLLSAFNSFILNSIPVLVTVVSFGvftl 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 260 FGGMRIASGAISAGTLVAMifyvlnLSIPLINLSTLVTDYKKAVGASQRIYEILHEPlENIAAPN--LQDEIPTGDLKfd 337
Cdd:PLN03130 548 LGGDLTPARAFTSLSLFAV------LRFPLFMLPNLITQAVNANVSLKRLEELLLAE-ERVLLPNppLEPGLPAISIK-- 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGYD---DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFS-LIERMYEIDQGGIYYDGTsidalsltdwrrkIGYVM 413
Cdd:PLN03130 619 NGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVP 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNGTIRDNILYGVDREVSE-EELIHYAKLAncHEfiMEFEQGYD-TIVGERGLKLSGGQRQRIDIARSFVKNPDI 491
Cdd:PLN03130 686 QVSWIFNATVRDNILFGSPFDPERyERAIDVTALQ--HD--LDLLPGGDlTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 492 LLLDEATANLDSESERKI-QEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVE 567
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
348-558 |
6.81e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 113.34 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDgtsidalsltdwrRKIGYVMQSNAMMNGTIRDNI 427
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 428 LYgvdreVSEEELIHYAKLANCHEFIMEFEQ---GYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSE 504
Cdd:PTZ00243 742 LF-----FDEEDAARLADAVRVSQLEADLAQlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 505 -SERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQT 558
Cdd:PTZ00243 817 vGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT 871
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
339-529 |
8.41e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.79 E-value: 8.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGydDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEI-----DQGGIYYDGTSIDA--LSLTDWRRKIGY 411
Cdd:PRK14243 18 VYYG--SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYApdVDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQSNAMMNGTIRDNILYGV---DREVSEEELIHYAklanchefimeFEQG--YDTI---VGERGLKLSGGQRQRIDIAR 483
Cdd:PRK14243 96 VFQKPNPFPKSIYDNIAYGArinGYKGDMDELVERS-----------LRQAalWDEVkdkLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2254949669 484 SFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRL 529
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
334-546 |
1.12e-25 |
|
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: 105.18 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDAL---SLTDWRRKI 409
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNAMM-NGTIRDNILYGVdrEVSEEELIHYAKLANCHEFIMEFEQGYDTIVGErglkLSGGQRQRIDIARSFVKN 488
Cdd:cd03292 81 GVVFQDFRLLpDRNVYENVAFAL--EVTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 489 PDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQ--IIFLDHGEV 546
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
347-527 |
1.19e-25 |
|
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: 105.21 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYY--DGTSIDALSLTDW------RRKIGYVMQsnam 418
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPReilalrRRTIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 mngtirdnILYGVDReVSEEELihyaklanchefIME--FEQGYDTIVG-ERGLKL------------------SGGQRQ 477
Cdd:COG4778 101 --------FLRVIPR-VSALDV------------VAEplLERGVDREEArARARELlarlnlperlwdlppatfSGGEQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 478 RIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIV-IAH 527
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
337-558 |
1.87e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.55 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 337 DHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQSN 416
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 417 AM-MNGTIRDNILYG-----------VDREVSEEElIHYAKLanchefiMEFEQGY-DTivgerglkLSGGQRQRIDIAR 483
Cdd:COG4604 85 HInSRLTVRELVAFGrfpyskgrltaEDREIIDEA-IAYLDL-------EDLADRYlDE--------LSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 484 SFVKNPDILLLDEATANLDSESERKIQEALDILME--NRTTIVIAHrlsTIKKAG----QIIFLDHGEVTGRGRHEELMQ 557
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLH---DINFAScyadHIVAMKDGRVVAQGTPEEIIT 225
|
.
gi 2254949669 558 T 558
Cdd:COG4604 226 P 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
343-540 |
1.99e-25 |
|
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: 104.93 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIdalslTDW------RRKIGYVMQ-S 415
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-----TKLpmhkraRLGIGYLPQeA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 416 NAMMNGTIRDNILYGVD-REVSEEELIHYAKlanchEFIMEFeqGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLL 494
Cdd:cd03218 85 SIFRKLTVEENILAVLEiRGLSKKEREEKLE-----ELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 495 DEATANLDSESERKIQEALDILMEN-----------RTTIVIAHRlSTIKKAGQIIF 540
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRgigvlitdhnvRETLSITDR-AYIIYEGKVLA 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
351-550 |
2.46e-25 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 103.91 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 351 DVSFnVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGT----SIDALSLTDWRRKIGYVMQSNAMM-NGTIRD 425
Cdd:cd03297 16 KIDF-DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NILYGVDREVSEEELIHYAKLANChefimefeQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSES 505
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDL--------LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2254949669 506 ERKIQEALDILME--NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRG 550
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
337-503 |
2.74e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 107.15 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 337 DHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLI---ERmyeIDQGGIYYDGTsiDALSLTDWR-RKIGYV 412
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGR--DLFTNLPPReRRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQSNAMM-NGTIRDNILYGVD-REVSEEElihyaKLANCHEFImefeqgydTIVGERGLK------LSGGQRQRIDIARS 484
Cdd:COG1118 81 FQHYALFpHMTVAENIAFGLRvRPPSKAE-----IRARVEELL--------ELVQLEGLAdrypsqLSGGQRQRVALARA 147
|
170
....*....|....*....
gi 2254949669 485 FVKNPDILLLDEATANLDS 503
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDA 166
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
338-557 |
2.88e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.58 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGYD---DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQ 414
Cdd:PRK13650 9 NLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 S--NAMMNGTIRDNILYGVDRE-VSEEELIHYAKLANCHEFIMEFEQgydtivgERGLKLSGGQRQRIDIARSFVKNPDI 491
Cdd:PRK13650 89 NpdNQFVGATVEDDVAFGLENKgIPHEEMKERVNEALELVGMQDFKE-------REPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 492 LLLDEATANLDSESERK-IQEALDILMENR-TTIVIAHRLSTIKKAGQIIFLDHGEV----TGR---GRHEELMQ 557
Cdd:PRK13650 162 IILDEATSMLDPEGRLElIKTIKGIRDDYQmTVISITHDLDEVALSDRVLVMKNGQVestsTPRelfSRGNDLLQ 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
337-547 |
3.81e-25 |
|
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: 103.11 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 337 DHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIdalSLTDWRRKIGYVMQ- 414
Cdd:cd03226 3 ENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 --SNAMMNgTIRDNILYGVDR-----EVSEE--ELIHYAKLANCHEFImefeqgydtivgerglkLSGGQRQRIDIARSF 485
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKEldagnEQAETvlKDLDLYALKERHPLS-----------------LSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 486 VKNPDILLLDEATANLDSESERKIQEALDILM-ENRTTIVIAHRLSTIKK-AGQIIFLDHGEVT 547
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-539 |
5.37e-25 |
|
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: 105.91 E-value: 5.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGYDDTPV--LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYE---IDQGGIYYDGTSIDALSLTDWR----RK 408
Cdd:COG0444 8 KVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 409 IGYVMQS-----NAMMngTIRDNIL------YGVDREVSEEELIHYAKLanchefimefeqgydtiVG----ERGLK--- 470
Cdd:COG0444 88 IQMIFQDpmtslNPVM--TVGDQIAeplrihGGLSKAEARERAIELLER-----------------VGlpdpERRLDryp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 471 --LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIqeaLDILM----ENRTTIV-IAHRLSTIKK--------- 534
Cdd:COG0444 149 heLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQI---LNLLKdlqrELGLAILfITHDLGVVAEiadrvavmy 225
|
....*
gi 2254949669 535 AGQII 539
Cdd:COG0444 226 AGRIV 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
285-583 |
5.43e-25 |
|
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: 110.42 E-value: 5.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 285 LSIPLINLSTLVTDYKKAVGASQRIYEIL-HEPLE------NIAAPNLQDEIPTGDLKFDhvyFGYDDTPVLKDVSFNVL 357
Cdd:TIGR00957 586 LRFPLNILPMVISSIVQASVSLKRLRIFLsHEELEpdsierRTIKPGEGNSITVHNATFT---WARDLPPTLNGITFSIP 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 358 RGEVTAFVGPSGSGKSTLFS-LIERMYEIdQGGIYYDGTsidalsltdwrrkIGYVMQSNAMMNGTIRDNILYGVdrevS 436
Cdd:TIGR00957 663 EGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGK----A 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 437 EEELIHYAKLANChEFIMEFE---QGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEAL 513
Cdd:TIGR00957 725 LNEKYYQQVLEAC-ALLPDLEilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV 803
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 514 ---DILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQFVETQNLTQHRAVTEQTET 583
Cdd:TIGR00957 804 igpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWT 876
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
334-516 |
1.25e-24 |
|
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: 102.70 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIdaLSLTDWRRKIGYVM 413
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMM-NGTIRDNILYG----------VDREVseEELIHYAKLAnchefimEFEQGYDTivgerglKLSGGQRQRIDIA 482
Cdd:cd03300 79 QNYALFpHLTVFENIAFGlrlkklpkaeIKERV--AEALDLVQLE-------GYANRKPS-------QLSGGQQQRVAIA 142
|
170 180 190
....*....|....*....|....*....|....
gi 2254949669 483 RSFVKNPDILLLDEATANLDSESERKIQEALDIL 516
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRL 176
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
343-548 |
3.11e-24 |
|
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: 99.43 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTD-WRRKIGYVMQsnammng 421
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 tirdnilygvdrevseeelihyaklanchefimefeqgydtivgerglkLSGGQRQRIDIARSFVKNPDILLLDEATANL 501
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2254949669 502 -DSESERKIQEALDILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTG 548
Cdd:cd03216 114 tPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVG 162
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
348-550 |
3.77e-24 |
|
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: 100.91 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsIDAL-SLTDWRRKIGYVMQSNAMMNG-TIRD 425
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVkEPAEARRRLGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NI-----LYGVDREVSEEELIHYAKLanchefiMEFEQGYDtivgERGLKLSGGQRQRIDIARSFVKNPDILLLDEATAN 500
Cdd:cd03266 98 NLeyfagLYGLKGDELTARLEELADR-------LGMEELLD----RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 501 LDSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEVTGRG 550
Cdd:cd03266 167 LDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
351-530 |
5.41e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.89 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 351 DVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKIGYVMQ----S-NAMMngT 422
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQdpyaSlNPRM--T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 423 IRD---------NILYGVDREVSEEELI--------HYAKLAncHEFimefeqgydtivgerglklSGGQRQRIDIARSF 485
Cdd:COG4608 114 VGDiiaeplrihGLASKAERRERVAELLelvglrpeHADRYP--HEF-------------------SGGQRQRIGIARAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 486 VKNPDILLLDEATANLD-SeserkIQ-EALDILME-----NRTTIVIAHRLS 530
Cdd:COG4608 173 ALNPKLIVCDEPVSALDvS-----IQaQVLNLLEDlqdelGLTYLFISHDLS 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
348-546 |
6.61e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 101.27 E-value: 6.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTD-WRRKIGYVMQSNAMMNG-TIRD 425
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiARLGIARTFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NILYGV---------------------DREVSE--EELIHYAKLANCHefimefeqgyDTIVGErglkLSGGQRQRIDIA 482
Cdd:COG0411 99 NVLVAAharlgrgllaallrlprarreEREAREraEELLERVGLADRA----------DEPAGN----LSYGQQRRLEIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 483 RSFVKNPDILLLDEATANL-DSESE------RKIQEALDIlmenrTTIVIAHRLSTIKK-AGQIIFLDHGEV 546
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLnPEETEelaeliRRLRDERGI-----TILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
21-309 |
7.66e-24 |
|
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: 101.82 E-value: 7.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGS-LTGLLVPLFTGQVVD---KFTFESISPVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLW 96
Cdd:cd18555 3 LLISILLLSLLLqLLTLLIPILTQYVIDnviVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKNESGQLMSRLTDDTkVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPL 176
Cdd:cd18555 83 EHLLKLPYSFFENRSSGDLLFRANSNV-YIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 177 GKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGI 256
Cdd:cd18555 162 RKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 257 ILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18555 242 ILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
342-557 |
1.02e-23 |
|
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: 99.43 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 342 GYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTD-WRRKIGYVMQSNAMM- 419
Cdd:cd03224 9 GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 NGTIRDNIL---YGVDREVSEEELihyaklanchefimefEQGYDT--IVGER----GLKLSGGQRQRIDIARSFVKNPD 490
Cdd:cd03224 89 ELTVEENLLlgaYARRRAKRKARL----------------ERVYELfpRLKERrkqlAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 491 ILLLDEATANLDSESERKIQEALDILMENRTTIV-----------IAHRLstikkagqiIFLDHGEVTGRGRHEELMQ 557
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILlveqnarfaleIADRA---------YVLERGRVVLEGTAAELLA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
334-560 |
1.05e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.83 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPvlKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDwrRKIGYVM 413
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNG-TIRDNILYGV--DREVSEEELIHYAKLAnchefimefEQgydtiVGERGLK------LSGGQRQRIDIARS 484
Cdd:COG3840 78 QENNLFPHlTVAQNIGLGLrpGLKLTAEQRAQVEQAL---------ER-----VGLAGLLdrlpgqLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 485 FVKNPDILLLDEATANLDSeSERkiQEALDILME-----NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQT 558
Cdd:COG3840 144 LVRKRPILLLDEPFSALDP-ALR--QEMLDLVDElcrerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
..
gi 2254949669 559 HA 560
Cdd:COG3840 221 EP 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
349-566 |
1.40e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 102.19 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKIGYVMQS-NAMMNGTIR 424
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQIGMIFQHfNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 425 DNI-----LYGVDREVSE---EELIHYAKLANCHEFimefeqgYDTivgerglKLSGGQRQRIDIARSFVKNPDILLLDE 496
Cdd:PRK11153 101 DNValpleLAGTPKAEIKarvTELLELVGLSDKADR-------YPA-------QLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 497 ATANLDSESERKIqeaLDILME-NRT---TIV-IAHRLSTIKK-AGQIIFLDHGEVTGRGRHEE--LMQTHAMYQQFV 566
Cdd:PRK11153 167 ATSALDPATTRSI---LELLKDiNRElglTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEvfSHPKHPLTREFI 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
334-558 |
1.51e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.55 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYD---DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIG 410
Cdd:PRK13642 5 LEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQS--NAMMNGTIRDNILYGVDRE-VSEEELIHYAKLANCHEFIMEFEQgydtivgERGLKLSGGQRQRIDIARSFVK 487
Cdd:PRK13642 85 MVFQNpdNQFVGATVEDDVAFGMENQgIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 488 NPDILLLDEATANLD----SESERKIQEALDilMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQT 558
Cdd:PRK13642 158 RPEIIILDESTSMLDptgrQEIMRVIHEIKE--KYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
343-555 |
1.89e-23 |
|
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: 99.34 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTsiDALSLTDWRRKIGYVMQSNAMM-NG 421
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGFVFQHYALFrHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDNILYG--------------VDREVSeeELIHYAKLANchefimeFEQGYDTivgerglKLSGGQRQRIDIARSFVK 487
Cdd:cd03296 90 TVFDNVAFGlrvkprserppeaeIRAKVH--ELLKLVQLDW-------LADRYPA-------QLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALDILME--NRTTIVIAHRLS-TIKKAGQIIFLDHGEVTGRGRHEEL 555
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
339-555 |
2.01e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.03 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDwrRKIGYVMQSNAM 418
Cdd:PRK11000 9 VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 ---MNgtIRDNILYG----------VDREVSE-EELIHYAKLAnchefimefeqgydtivgERGLK-LSGGQRQRIDIAR 483
Cdd:PRK11000 87 yphLS--VAENMSFGlklagakkeeINQRVNQvAEVLQLAHLL------------------DRKPKaLSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 484 SFVKNPDILLLDEATANLDSeserkiqeALDILME----------NRTTIVIAH-RLSTIKKAGQIIFLDHGEVTGRGRH 552
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDA--------ALRVQMRieisrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKP 218
|
...
gi 2254949669 553 EEL 555
Cdd:PRK11000 219 LEL 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
344-564 |
2.22e-23 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 99.93 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDqGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMMNGTI 423
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RDNI-LYGvdrEVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLD 502
Cdd:cd03289 94 RKNLdPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 503 SESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELMQTHAMYQQ 564
Cdd:cd03289 171 PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
21-295 |
2.60e-23 |
|
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: 100.33 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIG-SLTGLLVPLFTGQVVDK-FTFESIS--PVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLW 96
Cdd:cd18568 3 LLAEILLASLLlQLLGLALPLFTQIILDRvLVHKNISllNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKNESGQLMSRLTDDTKVINdFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPL 176
Cdd:cd18568 83 KHLLSLPLSFFASRKVGDIITRFQENQKIRR-FLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 177 GKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGI 256
Cdd:cd18568 162 SPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIA 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 2254949669 257 ILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTL 295
Cdd:cd18568 242 VLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL 280
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
320-564 |
2.76e-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: 104.99 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 320 IAAPNLQDEIPTG---DLKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDqGGIYYDGTS 396
Cdd:TIGR01271 1203 IENPHAQKCWPSGgqmDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVS 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 397 IDALSLTDWRRKIGYVMQSNAMMNGTIRDNIlyGVDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQR 476
Cdd:TIGR01271 1282 WNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL--DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHK 1359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 477 QRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEELM 556
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
....*...
gi 2254949669 557 QTHAMYQQ 564
Cdd:TIGR01271 1440 NETSLFKQ 1447
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
24-309 |
2.89e-23 |
|
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: 100.31 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 24 AVTIASIGSLTGLLVPLFTGQVVD---KFTFESISPVFI------IALVAVFLVNAVLSgFGY-YLLNKIGEKIIYAIRS 93
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNvisRSLKETNGDFIEdlkkpaLKLLGLYLLQSLLT-FAYiSLLSVVGERVAARLRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 94 VLWEHIIHLKMPFFDKNESGQLMSRLTDDtkvINDF-------ISQKLpgffPAVITLIGSLIMLFVLDWQMTLLTFITI 166
Cdd:cd18574 80 DLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFkssfkqcVSQGL----RSVTQTVGCVVSLYLISPKLTLLLLVIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 167 PIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDkahsnlktIYNLGLKQAKIAAVV---- 242
Cdd:cd18574 153 PVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE--------LYEEEVEKAAKLNEKlglg 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 243 ----QPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18574 225 igifQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
343-555 |
4.69e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.07 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsIDALSLTDWRRKIGYVMQSNAMM-NG 421
Cdd:PRK11607 29 FDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLSHVPPYQRPINMMFQSYALFpHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDNILYGV--DR----EVSE--EELIhyaKLANCHEFimefeqgydtiVGERGLKLSGGQRQRIDIARSFVKNPDILL 493
Cdd:PRK11607 107 TVEQNIAFGLkqDKlpkaEIASrvNEML---GLVHMQEF-----------AKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 494 LDEATANLDSESERKIQ-EALDILME-NRTTIVIAH-RLSTIKKAGQIIFLDHGEVTGRGRHEEL 555
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
333-565 |
8.19e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 333 DLKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYV 412
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQSNAMMNG-TIRDNILYGVDREVSeeeliHYAKLANCHEFI----MEfEQGYDTIVGERGLKLSGGQRQRIDIARSFVK 487
Cdd:PRK11231 82 PQHHLTPEGiTVRELVAYGRSPWLS-----LWGRLSAEDNARvnqaME-QTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALDIL-MENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQTHAMYQQF 565
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPGLLRTVF 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
348-567 |
1.06e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.51 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDA---LS-----LTDWRRKIGYVMQS-NAM 418
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSqqkglIRQLRQHVGFVFQNfNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 MNGTIRDNILYG---VDREVSEE------ELIHYAKLAnchefimefeqGYDTIVGERglkLSGGQRQRIDIARSFVKNP 489
Cdd:PRK11264 98 PHRTVLENIIEGpviVKGEPKEEatararELLAKVGLA-----------GKETSYPRR---LSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 490 DILLLDEATANLDSESerkIQEALDILM----ENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQ--THAMY 562
Cdd:PRK11264 164 EVILFDEPTSALDPEL---VGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAdpQQPRT 240
|
....*
gi 2254949669 563 QQFVE 567
Cdd:PRK11264 241 RQFLE 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
334-584 |
1.44e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.26 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSltdwRRKIGYV- 412
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 --------MqsnammngTIRDNILY-----GVDREVSEEELIHYAKlanchefimEFEqgydtiVGERGLK----LSGGQ 475
Cdd:COG4152 78 eerglypkM--------KVGEQLVYlarlkGLSKAEAKRRADEWLE---------RLG------LGDRANKkveeLSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 476 RQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEVTGRGRHE 553
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVEElCDRIVIINKGRKVLSGSVD 214
|
250 260 270
....*....|....*....|....*....|....*
gi 2254949669 554 ELMQTHAMYQQFVETQN----LTQHRAVTEQTETE 584
Cdd:COG4152 215 EIRRQFGRNTLRLEADGdagwLRALPGVTVVEEDG 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
346-534 |
1.71e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 346 TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLT---DWR-RKIGYVMQSNAMM-N 420
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQFHHLLpD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 GTIRDNilygvdreVSEEELIHYAKLANCHEFIMEFEQ--GYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEAT 498
Cdd:PRK11629 102 FTALEN--------VAMPLLIGKKKPAEINSRALEMLAavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2254949669 499 ANLDSESERKIQEALDILMENRTT--IVIAHRLSTIKK 534
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKR 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
336-547 |
1.79e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 336 FDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsidalsltDWRrkIGYVMQS 415
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 416 -NAMMNGTIRDNILYGVDR---------------EVSEEELIHYAKLANchefIMEFEQGYD------TIVGERGLK--- 470
Cdd:COG0488 70 pPLDDDLTVLDTVLDGDAElraleaeleeleaklAEPDEDLERLAELQE----EFEALGGWEaearaeEILSGLGFPeed 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 471 -------LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESerkIQ--EalDILMENRTT-IVIAH-R--LSTIkkAGQ 537
Cdd:COG0488 146 ldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlE--EFLKNYPGTvLVVSHdRyfLDRV--ATR 218
|
250
....*....|
gi 2254949669 538 IIFLDHGEVT 547
Cdd:COG0488 219 ILELDRGKLT 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
343-550 |
1.80e-22 |
|
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: 95.75 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSltDWRRKIGYVMQSNAM-MNG 421
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGALIEAPGFyPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDNILYGvdrevseeELIHYAKLANCHEFIMEFeqGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANL 501
Cdd:cd03268 88 TARENLRLL--------ARLLGIRKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 502 DSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEVTGRG 550
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
334-550 |
1.93e-22 |
|
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: 95.64 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNvlRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDwrRKIGYVM 413
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMM-NGTIRDNILYGVDREVSEEElihyaklanchefimEFEQGYDTIVGERGL---------KLSGGQRQRIDIAR 483
Cdd:cd03298 77 QENNLFaHLTVEQNVGLGLSPGLKLTA---------------EDRQAIEVALARVGLaglekrlpgELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 484 SFVKNPDILLLDEATANLDSESErkiQEALDILMENR-----TTIVIAHRLSTIKKAGQ-IIFLDHGEVTGRG 550
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALR---AEMLDLVLDLHaetkmTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
317-514 |
2.13e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 317 LENIAAP--------NLQDEIPTGD--LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID 386
Cdd:COG0488 289 LEREEPPrrdktveiRFPPPERLGKkvLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 387 QGGIYYdGTSIdalsltdwrrKIGYVMQSNAMMNG--TIRDNILYGVDrEVSEEELIHYakLANchefiMEFEqgydtiv 464
Cdd:COG0488 369 SGTVKL-GETV----------KIGYFDQHQEELDPdkTVLDELRDGAP-GGTEQEVRGY--LGR-----FLFS------- 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 465 GERGLK----LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALD 514
Cdd:COG0488 423 GDDAFKpvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD 476
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
348-546 |
2.14e-22 |
|
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: 95.80 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYE---IDQGGIYYDGTsidALSLTDWRRKIGYVMQSNAMMNG-TI 423
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RDNILY------------GVDREVSEEELihyakLANCHefimefeqgyDTIVGERGLK-LSGGQRQRIDIARSFVKNPD 490
Cdd:cd03234 99 RETLTYtailrlprkssdAIRKKRVEDVL-----LRDLA----------LTRIGGNLVKgISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 491 ILLLDEATANLDSESERKIQEAL-DILMENRTTIVIAH--RLSTIKKAGQIIFLDHGEV 546
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
334-550 |
2.64e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 95.34 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGeVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDAlSLTDWRRKIGYVM 413
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMM-NGTIRD-----NILYGVDREVSEEELIHYAKLANCHEFimefeqgYDTIVGerglKLSGGQRQRIDIARSFVK 487
Cdd:cd03264 79 QEFGVYpNFTVREfldyiAWLKGIPSKEVKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRG 550
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
349-560 |
3.21e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.95 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWR----RKIGYVMQSNAMM-NGTI 423
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RDNILYGVDRE-VSEEELIHYAKLANCHEFIMEFEQGYDTivgerglKLSGGQRQRIDIARSFVKNPDILLLDEATANLD 502
Cdd:PRK10070 124 LDNTAFGMELAgINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 503 SESERKIQEALDILM--ENRTTIVIAHRLSTIKKAG-QIIFLDHGEVTGRGRHEELMQTHA 560
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLDEAMRIGdRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
334-556 |
3.24e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 95.82 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSlTD--WRRKIGY 411
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP-PHriARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQSN---AMMngTIRDNILYGV----DREVSEEELihyaklanchEFIME-FEqgydtIVGER----GLKLSGGQRQRI 479
Cdd:COG0410 83 VPEGRrifPSL--TVEENLLLGAyarrDRAEVRADL----------ERVYElFP-----RLKERrrqrAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 480 DIARSFVKNPDILLLDEATANLdseSERKIQEALDILME-NR--TTIVI----AHRLSTIkkAGQIIFLDHGEVTGRGRH 552
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIIRRlNRegVTILLveqnARFALEI--ADRAYVLERGRIVLEGTA 220
|
....
gi 2254949669 553 EELM 556
Cdd:COG0410 221 AELL 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
349-546 |
3.33e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSI--DALSLTDWRRKIGYVMQ--SNAMMNGTIR 424
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 425 DNILYG-VDREVSEEELIHYAKLAnchefiMEFEQ-GYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLD 502
Cdd:PRK13637 103 KDIAFGpINLGLSEEEIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2254949669 503 SESERKIQEALDILME--NRTTIVIAHRLSTIKK-AGQIIFLDHGEV 546
Cdd:PRK13637 177 PKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-569 |
4.12e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.26 E-value: 4.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 329 IPTgdLKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID-----QGGIYYDGTSI--DALS 401
Cdd:PRK14258 5 IPA--IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 402 LTDWRRKIGYVMQSNAMMNGTIRDNILYGVdrevseeELIHY---AKLANCHEFIMEFEQGYDTI---VGERGLKLSGGQ 475
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGV-------KIVGWrpkLEIDDIVESALKDADLWDEIkhkIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 476 RQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALD--ILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHE 553
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLV 235
|
250
....*....|....*.
gi 2254949669 554 ELMQTHAMYQQFVETQ 569
Cdd:PRK14258 236 EFGLTKKIFNSPHDSR 251
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
340-544 |
5.29e-22 |
|
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: 94.71 E-value: 5.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 340 YFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRK----IGYVMQ 414
Cdd:cd03290 7 YFSWgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 SNAMMNGTIRDNILYGVDREVSEEELIHYAKLANCHEFIMEFeqGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLL 494
Cdd:cd03290 87 KPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPF--GDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 495 DEATANLDSE-SERKIQEA-LDILMEN-RTTIVIAHRLSTIKKAGQIIFLDHG 544
Cdd:cd03290 165 DDPFSALDIHlSDHLMQEGiLKFLQDDkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
32-309 |
6.43e-22 |
|
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: 96.00 E-value: 6.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 32 SLTGLLVPLFTGQVVDKFTFESISPVF---IIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFD 108
Cdd:cd18589 9 SLGEMAIPYYTGRMTDWIMNKDAPEAFtaaITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 109 KNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIMQKISTNTQ 188
Cdd:cd18589 89 SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 189 TEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGGMRIASG 268
Cdd:cd18589 169 KSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2254949669 269 AISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18589 249 TVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
267-528 |
1.34e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.73 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 267 SGAISAGTL--VAMIF-YVLNlsipliNLSTLVTDYK-----KAVgaSQRIYEiLHEPLENIAAPNLQDEIPT----GDL 334
Cdd:COG4178 293 AGEITLGGLmqAASAFgQVQG------ALSWFVDNYQslaewRAT--VDRLAG-FEEALEAADALPEAASRIEtsedGAL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 335 KFDHVY-FGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIermyeidqGGI--YYDGTsIDALSLTDwrrkigy 411
Cdd:COG4178 364 ALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI--------AGLwpYGSGR-IARPAGAR------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VM---QSNAMMNGTIRDNILY-GVDREVSEEELIHYAKLANCHEFI--MEFEQGYDTIvgerglkLSGGQRQRIDIARSF 485
Cdd:COG4178 428 VLflpQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAerLDEEADWDQV-------LSLGEQQRLAFARLL 500
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2254949669 486 VKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHR 528
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
343-547 |
1.40e-21 |
|
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: 93.94 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIermyeidQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMM--- 419
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL-------SGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgqk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 -----NGTIRDNI-----LYGVDREVSEEELIHYAKLANCHEFImefeqgyDTIVgeRglKLSGGQRQRIDIARSFVKNP 489
Cdd:cd03267 104 tqlwwDLPVIDSFyllaaIYDLPPARFKKRLDELSELLDLEELL-------DTPV--R--QLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 490 DILLLDEATANLDSESERKIQEALDILMENRTTIVI--AHRLSTIKK-AGQIIFLDHGEVT 547
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-558 |
1.67e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKST----LFSLIErmyeiDQGGIYYDGTSIDALS---LTDWRRKIGYVMQS-NAMM 419
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 NGtiRDNILygvdrEVSEEEL-IHYAKLANCHEfimefEQGYDTIVGERGL----------KLSGGQRQRIDIARSFVKN 488
Cdd:PRK15134 376 NP--RLNVL-----QIIEEGLrVHQPTLSAAQR-----EQQVIAVMEEVGLdpetrhrypaEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 489 PDILLLDEATANLDSESERKIQEALDILMENR--TTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQT 558
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-558 |
1.84e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.96 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGT---------SIDALSLtdwRRKI 409
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKL---RKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQS-NAMMNGTIRDNILYGVDREVSEEELIHYAKLANCHEFIMEFEQGYDTIvGERGLKLSGGQRQRIDIARSFVKN 488
Cdd:PRK14246 93 GMVFQQpNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 489 PDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQT 558
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-566 |
2.35e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.75 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGydDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQ-----GGIYYDGTSI--DALSLTDWRRKIG 410
Cdd:PRK14267 11 RVYYG--SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQ-SNAMMNGTIRDNILYGVDRE---VSEEEL---IHYA-KLANCHEFIMEFEQGYDTivgerglKLSGGQRQRIDIA 482
Cdd:PRK14267 89 MVFQyPNPFPHLTIYDNVAIGVKLNglvKSKKELderVEWAlKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 483 RSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQT--H 559
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFENpeH 241
|
....*..
gi 2254949669 560 AMYQQFV 566
Cdd:PRK14267 242 ELTEKYV 248
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
26-309 |
2.73e-21 |
|
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: 94.33 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 26 TIASIGSLtglLVPLFTGQVVDKFTFESISPVFIIALVAVFLV---NAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHL 102
Cdd:cd18590 6 TLAVICET---FIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFslgSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 103 KMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIMQK 182
Cdd:cd18590 83 DIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 183 ISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGG 262
Cdd:cd18590 163 LSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGR 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2254949669 263 MRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18590 243 QLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
342-541 |
4.41e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 342 GYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTsidalsltdwrRKIGYVMQSNAM--- 418
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 MNGTIRDNILYGV-------------DREVSEEEL--IHYAKLANchefimefeqgydtivgeRGL-KLSGGQRQRIDIA 482
Cdd:NF040873 70 LPLTVRDLVAMGRwarrglwrrltrdDRAAVDDALerVGLADLAG------------------RQLgELSGGQRQRALLA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 483 RSFVKNPDILLLDEATANLDSESERKIQEAL-DILMENRTTIVIAHRLSTIKKAGQIIFL 541
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
334-513 |
9.04e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.07 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSltdwrRKIGYVM 413
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMN-GTIRDNILYGVD-REVSEEELIHYAKLANCHEFIMEFEQgydtivgERGLKLSGGQRQRIDIARSFVKNPDI 491
Cdd:PRK11248 77 QNEGLLPwRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKKVGLEGAEK-------RYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180
....*....|....*....|..
gi 2254949669 492 LLLDEATANLDSESERKIQEAL 513
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLL 171
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
343-502 |
9.18e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 9.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLtdWRRK---IGYVMQSNAMM 419
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM--HKRArlgIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 NG-TIRDNIL-----YGVDREVSEEELihyaklancHEFIMEFeqGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILL 493
Cdd:COG1137 91 RKlTVEDNILavlelRKLSKKEREERL---------EELLEEF--GITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
....*....
gi 2254949669 494 LDEATANLD 502
Cdd:COG1137 160 LDEPFAGVD 168
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-496 |
9.40e-21 |
|
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: 96.02 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 7 LVFLLKKISWPVGLIIVAVTIASIGSlTGLLVplFTGQVVDKFTFESISPVFI-IALVAVFLVNAVLSgfgYYLLNKIGE 85
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLAN-AGLIA--LINQALNATGAALARLLLLfAGLLVLLLLSRLAS---QLLLTRLGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 86 KIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQkLPGFFPAVITLIGSLIMLFVLDWQMTLLTFIT 165
Cdd:COG4615 78 HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 166 IPIFILVIV-PLGKIMQKISTNTQTE---IANFSGLL------------GRVLTEMRLVKVANTEKLELDKAHSNLKTIY 229
Cdd:COG4615 157 LGLGVAGYRlLVRRARRHLRRAREAEdrlFKHFRALLegfkelklnrrrRRAFFDEDLQPTAERYRDLRIRADTIFALAN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 230 NLG--LKQAKIAAVVqpisgiimlitigiilgFggMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQ 307
Cdd:COG4615 237 NWGnlLFFALIGLIL-----------------F--LLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 308 RIYEiLHEPLENIAAPNLQDEIPTGD-----LKFDHVYFGYDDT---------PVlkDVSFNvlRGEVTAFVGPSGSGKS 373
Cdd:COG4615 298 KIEE-LELALAAAEPAAADAAAPPAPadfqtLELRGVTYRYPGEdgdegftlgPI--DLTIR--RGELVFIVGGNGSGKS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 374 TLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIG------YVMQSnammngtirdniLYGVDREVSEE---ELIHYA 444
Cdd:COG4615 373 TLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSavfsdfHLFDR------------LLGLDGEADPArarELLERL 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 445 KLANchefIMEFEQG-YDTivgergLKLSGGQRQRIDIARSFVKNPDILLLDE 496
Cdd:COG4615 441 ELDH----KVSVEDGrFST------TDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
348-547 |
9.96e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 91.05 E-value: 9.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsidalsltdwrrKIGYVMQSNAMMNG--TIRD 425
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------RVSSLLGLGGGFNPelTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NI-----LYGVDREVSEEELihyaklanchEFIMEF---EQGYDTIVGErglkLSGGQRQRIDIARSFVKNPDILLLDEA 497
Cdd:cd03220 104 NIylngrLLGLSRKEIDEKI----------DEIIEFselGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 498 TANLDSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEVT 547
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIR 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
334-534 |
1.21e-20 |
|
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: 90.42 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSltdwRRKIGYVM 413
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMM-NGTIRDNILY-----GVDREVSEEELIHYaklanCHEF-IMEFEQgydtivgERGLKLSGGQRQRIDIARSFV 486
Cdd:cd03269 77 EERGLYpKMKVIDQLVYlaqlkGLKKEEARRRIDEW-----LERLeLSEYAN-------KRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2254949669 487 KNPDILLLDEATANLDSESERKIQEALDILMENRTTIVI-AHRLSTIKK 534
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEE 193
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
343-559 |
1.65e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDwRRKIGYVMQ-SNAMMNG 421
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVVPQfDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDNIL-YG-----VDREVSE--EELIHYAKLanchefimefEQGYDTIVGErglkLSGGQRQRIDIARSFVKNPDILL 493
Cdd:PRK13536 130 TVRENLLvFGryfgmSTREIEAviPSLLEFARL----------ESKADARVSD----LSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 494 LDEATANLDSESERKIQEALDILMENRTTIVI-------AHRLstikkAGQIIFLDHGEVTGRGRHEELMQTH 559
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
340-550 |
1.94e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.34 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 340 YFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVMQ--SNA 417
Cdd:PRK13647 12 FRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQdpDDQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 418 MMNGTIRDNILYG-VDREVSEEELIHYAKLANchefimefeqgydTIVGERGLK------LSGGQRQRIDIARSFVKNPD 490
Cdd:PRK13647 92 VFSSTVWDDVAFGpVNMGLDKDEVERRVEEAL-------------KAVRMWDFRdkppyhLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 491 ILLLDEATANLDSESERKIQEALDILMENRTTIVIA-HRLS-TIKKAGQIIFLDHGEVTGRG 550
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-567 |
2.66e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTL---FSLIE--RMYEIDQGGIYYD-GTSIDALSLTDWRR 407
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLlrvLNLLEtpDSGQLNIAGHQFDfSQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 408 KIGYVMQS-NAMMNGTIRDNIL------YGVDREVSEEELI-HYAKLAnchefIMEFEQGYDtivgergLKLSGGQRQRI 479
Cdd:COG4161 83 KVGMVFQQyNLWPHLTVMENLIeapckvLGLSKEQAREKAMkLLARLR-----LTDKADRFP-------LHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 480 DIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENR-TTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDASHFTQ 230
|
250
....*....|
gi 2254949669 558 THAmyQQFVE 567
Cdd:COG4161 231 PQT--EAFAH 238
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
365-555 |
2.89e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 92.17 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 365 VGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIdaLSLTDWRRKIGYVMQSNAMM-NGTIRDNILYG-----VDREVSEE 438
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV--TNVPPHLRHINMVFQSYALFpHMTVEENVAFGlkmrkVPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 439 ELIHYAKLANCHEFimefeqgydtiVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILME 518
Cdd:TIGR01187 80 RVLEALRLVQLEEF-----------ADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2254949669 519 NR--TTIVIAHRLS-TIKKAGQIIFLDHGEVTGRGRHEEL 555
Cdd:TIGR01187 149 QLgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
334-558 |
3.20e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 89.89 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSlTDWR--RKIGY 411
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP-PHERarAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQsnammnG-------TIRDNILYGVD------REVSEEElihYAKLANCHEFImefeqgydtivGERGLKLSGGQRQR 478
Cdd:TIGR03410 80 VPQ------GreifprlTVEENLLTGLAalprrsRKIPDEI---YELFPVLKEML-----------GRRGGDLSGGQQQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 479 IDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENR--TTIVIAHRLSTIKKAGQ-IIFLDHGEVTGRGRHEEL 555
Cdd:TIGR03410 140 LAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARELADrYYVMERGRVVASGAGDEL 219
|
...
gi 2254949669 556 MQT 558
Cdd:TIGR03410 220 DED 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
327-538 |
3.25e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 327 DEIPTGDLKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSlTDWR 406
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 407 RKIGYVMQ-SNAMMNGTIRDNIL-----YGVDREVSEE---ELIHYAKLanchefimefEQGYDTIVGErglkLSGGQRQ 477
Cdd:PRK13537 80 QRVGVVPQfDNLDPDFTVRENLLvfgryFGLSAAAARAlvpPLLEFAKL----------ENKADAKVGE----LSGGMKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 478 RIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIA-----------HRLSTIKKAGQI 538
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTthfmeeaerlcDRLCVIEEGRKI 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
337-555 |
4.03e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.52 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 337 DHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSI--DALSLTDWRRKIGYVMQ 414
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 S--NAMMNGTIRDNILYG-VDREVSEEELIHYAKLAnCHEFIMEfeqGYDTIVGERglkLSGGQRQRIDIARSFVKNPDI 491
Cdd:PRK13639 86 NpdDQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEA-LKAVGME---GFENKPPHH---LSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 492 LLLDEATANLDSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEVTGRGRHEEL 555
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
334-513 |
4.22e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.31 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYD----DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLtdwRRki 409
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---DR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNAMMNG-TIRDNI-----LYGVDREVSE---EELIHYAKLANCHE-FIMEfeqgydtivgerglkLSGGQRQRI 479
Cdd:COG4525 79 GVVFQKDALLPWlNVLDNVafglrLRGVPKAERRaraEELLALVGLADFARrRIWQ---------------LSGGMRQRV 143
|
170 180 190
....*....|....*....|....*....|....
gi 2254949669 480 DIARSFVKNPDILLLDEATANLDSESERKIQEAL 513
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
334-513 |
4.26e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 92.32 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTdwRRKIGYVM 413
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAM---MngTIRDNILYGVD-REVSEEE----------LIHYAKLANchefimefeqgydtivgERGLKLSGGQRQRI 479
Cdd:PRK09452 93 QSYALfphM--TVFENVAFGLRmQKTPAAEitprvmealrMVQLEEFAQ-----------------RKPHQLSGGQQQRV 153
|
170 180 190
....*....|....*....|....*....|....
gi 2254949669 480 DIARSFVKNPDILLLDEATANLDSESERKIQEAL 513
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNEL 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
351-556 |
4.77e-20 |
|
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: 92.09 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 351 DVSFNVLRGEVTAFVGPSGSGKSTLFSLI---ERmyeIDQGGIYYDGT----SIDALSLTDWRRKIGYVMQSNAM---Mn 420
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLfphL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 gTIRDNILYGVDREVSEEELIHYaklanchefimefeqgyDTIVGERGL---------KLSGGQRQRIDIARSFVKNPDI 491
Cdd:COG4148 93 -SVRGNLLYGRKRAPRAERRISF-----------------DEVVELLGIghlldrrpaTLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 492 LLLDEATANLDSESERKI-------QEALDILMenrttIVIAH------RLstikkAGQIIFLDHGEVTGRGRHEELM 556
Cdd:COG4148 155 LLMDEPLAALDLARKAEIlpylerlRDELDIPI-----LYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVL 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
346-529 |
5.85e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 346 TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTD-WRRKIGYVMQSNAMMNG-TI 423
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RDNILYGvdREVSEEELIHYAKL-ANCHEFIMEFEQGYD--TIVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATAN 500
Cdd:COG1129 97 AENIFLG--REPRRGGLIDWRAMrRRARELLARLGLDIDpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190
....*....|....*....|....*....|.
gi 2254949669 501 L-DSESERkIQEALDILMENRTTIV-IAHRL 529
Cdd:COG1129 171 LtEREVER-LFRIIRRLKAQGVAIIyISHRL 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
340-504 |
7.50e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.30 E-value: 7.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 340 YFGYddTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDwrRKIGYVMQSNAMM 419
Cdd:PRK10851 11 SFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 -NGTIRDNILYG--------------VDREVSE-EELIHYAKLANchefimefeqGYDTivgerglKLSGGQRQRIDIAR 483
Cdd:PRK10851 87 rHMTVFDNIAFGltvlprrerpnaaaIKAKVTQlLEMVQLAHLAD----------RYPA-------QLSGGQKQRVALAR 149
|
170 180
....*....|....*....|.
gi 2254949669 484 SFVKNPDILLLDEATANLDSE 504
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQ 170
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
21-297 |
8.10e-20 |
|
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: 90.17 E-value: 8.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 21 IIVAVTIASIGSLTGLLVPLFTGQVVDKF-------TFESISPVFIIALVAVFLVNAVLSGFGY---YLLNKIGEKIIYA 90
Cdd:cd18554 1 IIITIVIGLVRFGIPLLLPLILKYIVDDViqgssltLDEKVYKLFTIIGIMFFIFLILRPPVEYyrqYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 91 IRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFI 170
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 171 LVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIM 250
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTIT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2254949669 251 LITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIP---LINLSTLVT 297
Cdd:cd18554 241 DLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPlrrLVNSFTTLT 290
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
334-546 |
2.27e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 86.84 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVlkDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsIDALSLTDWRRKIGYVM 413
Cdd:TIGR01277 1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND--QSHTGLAPYQRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNG-TIRDNILYGVDREVS----EEELIHYAKLanchefimefEQGYDTIVGERGLKLSGGQRQRIDIARSFVKN 488
Cdd:TIGR01277 77 QENNLFAHlTVRQNIGLGLHPGLKlnaeQQEKVVDAAQ----------QVGIADYLDRLPEQLSGGQRQRVALARCLVRP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 489 PDILLLDEATANLDSESErkiQEALDILM-----ENRTTIVIAHRLS-TIKKAGQIIFLDHGEV 546
Cdd:TIGR01277 147 NPILLLDEPFSALDPLLR---EEMLALVKqlcseRQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
348-546 |
2.63e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.21 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDW---RRKIGYVMQ-SNAMMN--G 421
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafRRDIQMVFQdSISAVNprK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDNI---------LYGVDREVSEEELIHYAKLAnchefimefeqgyDTIVGERGLKLSGGQRQRIDIARSFVKNPDIL 492
Cdd:PRK10419 107 TVREIIreplrhllsLDKAERLARASEMLRAVDLD-------------DSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 493 LLDEATANLDSESERKIQEALDILMENRTT--IVIAHRLSTIKKAGQ-IIFLDHGEV 546
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQrVMVMDNGQI 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
337-565 |
2.98e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.38 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 337 DHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTL---FSLIE--RMYEIDQGGIYYD-GTSIDALSLTDWRRKIG 410
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvLNLLEmpRSGTLNIAGNHFDfSKTPSDKAIRELRRNVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQS-NAMMNGTIRDNIL------YGVDREVSEE---ELIHYAKLAnchEFIMEFEqgydtivgergLKLSGGQRQRID 480
Cdd:PRK11124 86 MVFQQyNLWPHLTVQQNLIeapcrvLGLSKDQALAraeKLLERLRLK---PYADRFP-----------LHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 481 IARSFVKNPDILLLDEATANLDSESERKIqeaLDILME----NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEEL 555
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQI---VSIIRElaetGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASCF 228
|
250
....*....|
gi 2254949669 556 MQTHAmyQQF 565
Cdd:PRK11124 229 TQPQT--EAF 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-566 |
3.08e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 341 FGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIY-----YDGTSI-DALSLTDWRRKIGYVMQ 414
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIfNYRDVLEFRRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 SNAMMNGTIRDNILYGV--DREVSEEEL--IHYAKLAnchefimefEQGYDTIVGER----GLKLSGGQRQRIDIARSFV 486
Cdd:PRK14271 109 RPNPFPMSIMDNVLAGVraHKLVPRKEFrgVAQARLT---------EVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 487 KNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRLSTIKKAGQ--IIFLDhGEVTGRGRHEELMQT--HAMY 562
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDraALFFD-GRLVEEGPTEQLFSSpkHAET 258
|
....
gi 2254949669 563 QQFV 566
Cdd:PRK14271 259 ARYV 262
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
339-496 |
3.12e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.90 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKIGYVMQS 415
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 416 NAMMNG-TIRDNILYGVdREVSE--EELIHYAKLanchefiMEFEQgydtiVGERGL------KLSGGQRQRIDIARSFV 486
Cdd:PRK11831 93 GALFTDmNVFDNVAYPL-REHTQlpAPLLHSTVM-------MKLEA-----VGLRGAaklmpsELSGGMARRAALARAIA 159
|
170
....*....|
gi 2254949669 487 KNPDILLLDE 496
Cdd:PRK11831 160 LEPDLIMFDE 169
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
35-309 |
3.60e-19 |
|
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: 88.02 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 35 GLLVPLFTGQVVDK-FTFESISP--VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFDKNE 111
Cdd:cd18566 18 ALATPLFILQVYDRvIPNESIPTlqVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 112 SGQLMSRLTDDTKVINDFISQKLPGFF--PAVITLigsLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIMQKISTNTQT 189
Cdd:cd18566 98 SGAHLERLNSLEQIREFLTGQALLALLdlPFVLIF---LGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 190 EIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGGMRIASGA 269
Cdd:cd18566 175 ADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGD 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2254949669 270 ISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18566 255 LTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
343-566 |
4.71e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.95 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSI-------------DALSLTDWRRKI 409
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQS-NAMMNGTIRDNIL------YGVDREVSEEELIHY-AKLAnchefIMEFEQGydtivgERGLKLSGGQRQRIDI 481
Cdd:PRK10619 95 TMVFQHfNLWSHMTVLENVMeapiqvLGLSKQEARERAVKYlAKVG-----IDERAQG------KYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 482 ARSFVKNPDILLLDEATANLDSESerkIQEALDILM----ENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELM 556
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPEL---VGEVLRIMQqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
250
....*....|..
gi 2254949669 557 QT--HAMYQQFV 566
Cdd:PRK10619 241 GNpqSPRLQQFL 252
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
330-578 |
8.20e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 330 PTGDLKFDHVYFGydDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKI 409
Cdd:PRK09536 2 PMIDVSDLSVEFG--DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNAM-MNGTIRDNILYG-------------VDREVSEEELihyaklanchefimefEQGYDTIVGERGL-KLSGG 474
Cdd:PRK09536 80 ASVPQDTSLsFEFDVRQVVEMGrtphrsrfdtwteTDRAAVERAM----------------ERTGVAQFADRPVtSLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 475 QRQRIDIARSFVKNPDILLLDEATANLDSESE-RKIQEALDILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRH 552
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPP 223
|
250 260 270
....*....|....*....|....*....|.
gi 2254949669 553 EELMQTHAMYQQF-----VETQNLTQHRAVT 578
Cdd:PRK09536 224 ADVLTADTLRAAFdartaVGTDPATGAPTVT 254
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
58-309 |
1.38e-18 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 86.95 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 58 FIIALVAVFLVNAVLSGFGYyllNKIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGF 137
Cdd:cd18558 64 YYLIIGAIVLITAYIQGSFW---GLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 138 FPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLE 217
Cdd:cd18558 141 FQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 218 LDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVT 297
Cdd:cd18558 221 ETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIE 300
|
250
....*....|..
gi 2254949669 298 DYKKAVGASQRI 309
Cdd:cd18558 301 AFANARGAAYHI 312
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
334-527 |
2.05e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 82.11 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIyydgTSIDALsltdwrrKIGYvm 413
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----TWGSTV-------KIGY-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 qsnammngtirdnilygvdrevseeelihyaklanchefimeFEQgydtivgerglkLSGGQRQRIDIARSFVKNPDILL 493
Cdd:cd03221 68 ------------------------------------------FEQ------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 2254949669 494 LDEATANLDSESERKIQEALdiLMENRTTIVIAH 527
Cdd:cd03221 94 LDEPTNHLDLESIEALEEAL--KEYPGTVILVSH 125
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
343-502 |
2.41e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.82 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YD-DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDwrRKIGYVMQSNAM--- 418
Cdd:PRK11650 13 YDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNYALyph 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 MngTIRDNILYG-----VDREVSEEELIHYAKlanchefIMEFEQGYDtivgERGLKLSGGQRQRIDIARSFVKNPDILL 493
Cdd:PRK11650 91 M--SVRENMAYGlkirgMPKAEIEERVAEAAR-------ILELEPLLD----RKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
....*....
gi 2254949669 494 LDEATANLD 502
Cdd:PRK11650 158 FDEPLSNLD 166
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
349-557 |
3.09e-18 |
|
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: 87.82 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMyeIDQGG-IYYDGTSIDALS---LTDWRRKIGYVMQ------SNAM 418
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL--IPSEGeIRFDGQDLDGLSrraLRPLRRRMQVVFQdpfgslSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 MNGTIrdnilygvdreVSEEELIHYAKL--ANCHEFIMEfeqgydtIVGERGLK----------LSGGQRQRIDIARSFV 486
Cdd:COG4172 380 TVGQI-----------IAEGLRVHGPGLsaAERRARVAE-------ALEEVGLDpaarhrypheFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 487 KNPDILLLDEATANLDseseRKIQ-EALDILME-----NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:COG4172 442 LEPKLLVLDEPTSALD----VSVQaQILDLLRDlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
334-561 |
3.47e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.90 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDD-TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSID--ALSLTDWRRKIG 410
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQS--NAMMNGTIRDNILYG-VDREVSEEELIHYAklanchEFIMEfEQGYDTIVGERGLKLSGGQRQRIDIARSFVK 487
Cdd:PRK13636 86 MVFQDpdNQLFSASVYQDVSFGaVNLKLPEDEVRKRV------DNALK-RTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEAL-DILMENRTTIVIA-HRLSTIK-KAGQIIFLDHGEVTGRGRHEELMQTHAM 561
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
344-543 |
4.52e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 81.82 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDgtsidalsltdWRRKIGYVMQSNAMMNGTI 423
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-----------EGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RDNILYGVDREvseeelihyaklanchefimefeqgydtivgerglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDS 503
Cdd:cd03223 81 REQLIYPWDDV------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2254949669 504 ESERKIqeaLDILMENRTTIV-IAHRLSTIKKAGQIIFLDH 543
Cdd:cd03223 125 ESEDRL---YQLLKELGITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
344-527 |
5.90e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.58 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIerM----YEIDQGGIYYDGTSIDALSlTDWRRK--IGYVMQsna 417
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MghpkYEVTSGSILLDGEDILELS-PDERARagIFLAFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 418 mmngtirdnilYGVD-REVSEEELIHYAKLANCHEFI--MEFEQ---GYDTIVG------ERGL--KLSGGQRQRIDIAR 483
Cdd:COG0396 85 -----------YPVEiPGVSVSNFLRTALNARRGEELsaREFLKllkEKMKELGldedflDRYVneGFSGGEKKRNEILQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2254949669 484 SFVKNPDILLLDEATANLDSESERKIQEALDILM-ENRTTIVIAH 527
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITH 198
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
20-309 |
6.61e-18 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 84.57 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 20 LIIVAVTIASigSLTGLLVPLFTGQVVDK-FTFESIS--PVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLW 96
Cdd:cd18782 5 IEVLALSFVV--QLLGLANPLLFQVIIDKvLVQQDLAtlYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKNESGQLMSRLTD-DTkvINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVP 175
Cdd:cd18782 83 DHLLRLPLGFFDKRPVGELSTRISElDT--IRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 176 LGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIG 255
Cdd:cd18782 161 FGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 256 IILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18782 241 LVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
344-540 |
6.71e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.60 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSltDWRR--KIGYVMQsNAMM-- 419
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP--EYKRakYIGRVFQ-DPMMgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 --NGTIRDNIL------------YGVDREVSEE--ELIhyAKLAnchefiMEFEQGYDTIVGerglKLSGGQRQridiAR 483
Cdd:COG1101 94 apSMTIEENLAlayrrgkrrglrRGLTKKRRELfrELL--ATLG------LGLENRLDTKVG----LLSGGQRQ----AL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 484 SFV----KNPDILLLDEATANLDSESERKIQEALD--ILMENRTTIVIAHRLS--------TIK-KAGQIIF 540
Cdd:COG1101 158 SLLmatlTKPKLLLLDEHTAALDPKTAALVLELTEkiVEENNLTTLMVTHNMEqaldygnrLIMmHEGRIIL 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
334-502 |
1.01e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.14 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLI----ERMYEIdQGGIYYDGTSIDALSLTdwRRKI 409
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlSPAFSA-SGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQS---NAMMNgtIRDNILYGVDREVSEEELIHYAKLA----NCHEFimeFEQGYDTivgerglkLSGGQRQRIDIA 482
Cdd:COG4136 79 GILFQDdllFPHLS--VGENLAFALPPTIGRAQRRARVEQAleeaGLAGF---ADRDPAT--------LSGGQRARVALL 145
|
170 180
....*....|....*....|
gi 2254949669 483 RSFVKNPDILLLDEATANLD 502
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLD 165
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
334-546 |
1.16e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.73 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYD-DTPV----LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDA----LSLTD 404
Cdd:PRK13641 3 IKFENVDYIYSpGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 405 WRRKIGYVMQ--SNAMMNGTIRDNILYG-----VDREVSEEELIHYAKLANCHEFIME---FEqgydtivgerglkLSGG 474
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpknfgFSEDEAKEKALKWLKKVGLSEDLISkspFE-------------LSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 475 QRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEA-LDILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEV 546
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
348-563 |
1.49e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.75 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFS----LIERMYEIDQGGIYYDGTSIDALSLTDW------------RRKIGY 411
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkelRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQ--SNAMMNGTIRDNILYG-VDREVSEEELihyAKLANCHEFIMefeqGYDTIVGERG-LKLSGGQRQRIDIARSFVK 487
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGpVALGVKKSEA---KKLAKFYLNKM----GLDDSYLERSpFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 488 NPDILLLDEATANLDSESERKIQE-ALDILMENRTTIVIAHRLSTI-KKAGQIIFLDHGEVTGRGRHEELMQTHAMYQ 563
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
342-570 |
2.40e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 342 GYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsidalsltdwrrKIGYVMQSNAMMNG 421
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSALLELGAGFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 --TIRDNI-----LYGVDREVSEEELIHYAKLANCHEFImefeqgyDTIVGerglKLSGGQRQRIDIARSFVKNPDILLL 494
Cdd:COG1134 102 elTGRENIylngrLLGLSRKEIDEKFDEIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 495 DEATANLDSESERKIQEALDILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEVTGRGRHEELMqthAMYQQFVETQN 570
Cdd:COG1134 171 DEVLAVGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVI---AAYEALLAGRE 245
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
343-525 |
5.10e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSL-TDWRRKIGYVMQSNAMMNG 421
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 -TIRDNIL--YGVDREVSEEELIHYAKlanchEFIMEFEQGYdtIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEAT 498
Cdd:PRK10895 93 lSVYDNLMavLQIRDDLSAEQREDRAN-----ELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180
....*....|....*....|....*..
gi 2254949669 499 ANLDSESERKIQEALDILMENRTTIVI 525
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLI 192
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
333-557 |
6.58e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.60 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 333 DLKFDHVYFGYD-DTP----VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDA----LSLT 403
Cdd:PRK13634 2 DITFQKVEHRYQyKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 404 DWRRKIGYVMQ--SNAMMNGTIRDNILYG-VDREVSEEELIHYAKLanchefiMEFEQGYDTIVGERG-LKLSGGQRQRI 479
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEEDAKQKARE-------MIELVGLPEELLARSpFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 480 DIARSFVKNPDILLLDEATANLDSESERKIQEALDILME--NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELM 556
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIF 234
|
.
gi 2254949669 557 Q 557
Cdd:PRK13634 235 A 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
334-556 |
7.16e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYVM 413
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QsNAMMNGTIRDNILYGVDR----------EVSEEELIHYAKLANchefimefeqGYDTIVGERGLKLSGGQRQRIDIAR 483
Cdd:PRK10253 88 Q-NATTPGDITVQELVARGRyphqplftrwRKEDEEAVTKAMQAT----------GITHLADQSVDTLSGGQRQRAWIAM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 484 SFVKNPDILLLDEATANLDSESERKIQEALDILmeNR----TTIVIAHRLS-TIKKAGQIIFLDHGEVTGRGRHEELM 556
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSEL--NRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
334-560 |
1.10e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.63 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDvsFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsIDALSLTDWRRKIGYVM 413
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFD--LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG--QDHTTTPPSRRPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMNG-TIRDNILYGVD-----REVSEEELIHYAKLANCHEFImefeqgyDTIVGErglkLSGGQRQRIDIARSFVK 487
Cdd:PRK10771 78 QENNLFSHlTVAQNIGLGLNpglklNAAQREKLHAIARQMGIEDLL-------ARLPGQ----LSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALDILMENR--TTIVIAHRLS-TIKKAGQIIFLDHGEVTGRGRHEELMQTHA 560
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
349-527 |
1.16e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 79.43 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDA-----------LSLTDWRrkigyvmqsna 417
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrmvvfqnYSLLPWL----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 418 mmngTIRDNILYGVDR---EVSEEElihYAKLANCHEFIMEFEQGYDTIVGErglkLSGGQRQRIDIARSFVKNPDILLL 494
Cdd:TIGR01184 70 ----TVRENIALAVDRvlpDLSKSE---RRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190
....*....|....*....|....*....|....*
gi 2254949669 495 DEATANLDSESERKIQEAL-DILMENR-TTIVIAH 527
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELmQIWEEHRvTVLMVTH 173
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
347-546 |
1.21e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 80.23 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDG---TSIDALSLTDWRRKIGYVMQS-----NAM 418
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlYQLDRKQRRAFRRDVQLVFQDspsavNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 MngTIRDNIlygvdrevsEEELIHY------AKLANCHEFIMEFEQGyDTIVGERGLKLSGGQRQRIDIARSFVKNPDIL 492
Cdd:TIGR02769 105 M--TVRQII---------GEPLRHLtsldesEQKARIAELLDMVGLR-SEDADKLPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 493 LLDEATANLDSESERKIQEALDILMENRTT--IVIAHRLSTIKK-AGQIIFLDHGEV 546
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
349-557 |
1.21e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEiDQGGIYYDGTSIDALSLTDWRRKIGYVMQSN---AMMngtird 425
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQsppFAM------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 nilygvdrEVSEEELIHYAKLANCHEFIMEFEQgydtIVGERGLK---------LSGGQRQRIDIARSFVK-----NPD- 490
Cdd:COG4138 85 --------PVFQYLALHQPAGASSEAVEQLLAQ----LAEALGLEdklsrpltqLSGGEWQRVRLAAVLLQvwptiNPEg 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 491 -ILLLDEATANLDseserkI--QEALD-ILME----NRTTIVIAHRLS-TIKKAGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:COG4138 153 qLLLLDEPMNSLD------VaqQAALDrLLRElcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-546 |
1.21e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.29 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIermyeidQGGIYYDGTSIDALSLTDWR------RKIGYVM-QSNAM--- 418
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKML-------TGILVPTSGEVRVLGYVPFKrrkefaRRIGVVFgQRSQLwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 --------MNGTIrdnilYGVDREVSEEELIHYAKLANCHEFImefeqgyDTIVgeRglKLSGGQRQRIDIARSFVKNPD 490
Cdd:COG4586 111 lpaidsfrLLKAI-----YRIPDAEYKKRLDELVELLDLGELL-------DTPV--R--QLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 491 ILLLDEATANLDSESERKIQEAL-DILMENRTTIVIA-HRLSTIKK-AGQIIFLDHGEV 546
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLkEYNRERGTTILLTsHDMDDIEAlCDRVIVIDHGRI 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
334-556 |
1.73e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSI-DALSLTDWRRKIGY 411
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQS--NAMMNGTIRDNILYGvdrevsEEELihyaklanCHEFImEFEQGYDTIVGERGLK---------LSGGQRQRID 480
Cdd:PRK13644 82 VFQNpeTQFVGRTVEEDLAFG------PENL--------CLPPI-EIRKRVDRALAEIGLEkyrhrspktLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 481 IARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIV-IAHRLSTIKKAGQIIFLDHGEVTGRGRHEELM 556
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
344-553 |
1.87e-16 |
|
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: 77.95 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIerM----YEIDQGGIYYDGTSIDALSLTDWRRK-IGYVMQSNAM 418
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MghpkYEVTEGEILFKGEDITDLPPEERARLgIFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 MNGtirdnilygvdreVSEEELIHYaklanchefimefeqgydtiVGErglKLSGGQRQRIDIARSFVKNPDILLLDEAT 498
Cdd:cd03217 89 IPG-------------VKNADFLRY--------------------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 499 ANLDSESERKIQEALDILM-ENRTTIVIAH--RLSTIKKAGQIIFLDHGEVTGRGRHE 553
Cdd:cd03217 133 SGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
351-502 |
3.44e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.81 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 351 DVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYY---DGTSIDALSL----------TDWrrkiGYVMQsNA 417
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALseaerrrllrTEW----GFVHQ-HP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 418 MMngtirdnilyGVDREVSE-----EELI-----HYAKL-ANCHEFIMEFEQGYDTIvGERGLKLSGGQRQRIDIARSFV 486
Cdd:PRK11701 99 RD----------GLRMQVSAggnigERLMavgarHYGDIrATAGDWLERVEIDAARI-DDLPTTFSGGMQQRLQIARNLV 167
|
170
....*....|....*.
gi 2254949669 487 KNPDILLLDEATANLD 502
Cdd:PRK11701 168 THPRLVFMDEPTGGLD 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
347-557 |
4.36e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 78.63 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS----LTDWRRKIGYVMQ--SNAMMN 420
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 GTIRDNILYGVDR-EVSEEELIHYA--KLANChefimefeqGYDTIVGERG-LKLSGGQRQRIDIARSFVKNPDILLLDE 496
Cdd:PRK13649 101 ETVLKDVAFGPQNfGVSQEEAEALAreKLALV---------GISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 497 ATANLDSESERKIQEALDILMENRTTIV-IAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
334-554 |
5.91e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.22 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGY-DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTD---WRRKI 409
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSN-AMMNGTIRDN-----ILYGVdrevSEEELIHYAKLANCHEFIMEFEQGYDtivgergLKLSGGQRQRIDIAR 483
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNvaiplIIAGA----SGDDIRRRVSAALDKVGLLDKAKNFP-------IQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 484 SFVKNPDILLLDEATANLDSEserkIQEALDILME--NR---TTIVIAHRLSTI-KKAGQIIFLDHGEVTGrGRHEE 554
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDA----LSEGILRLFEefNRvgvTVLMATHDIGLIsRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
334-567 |
7.90e-16 |
|
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: 80.62 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERM--YEIDQGGIYY----------------DGT 395
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 396 S------------IDALSLTDWRRKigYVMQSNAMMngTIRDNILYGVDREV-----SEEELIHYAKLA--NCHEFIMEF 456
Cdd:TIGR03269 81 PcpvcggtlepeeVDFWNLSDKLRR--RIRKRIAIM--LQRTFALYGDDTVLdnvleALEEIGYEGKEAvgRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 457 EQGYDTIVGERglKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILM--ENRTTIVIAHRLSTIKK 534
Cdd:TIGR03269 157 QLSHRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIED 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 2254949669 535 -AGQIIFLDHGEVTGRGRHEEL----MQTHAMYQQFVE 567
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDEVvavfMEGVSEVEKECE 272
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
341-527 |
1.02e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.99 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 341 FGydDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTdwRRKIGYVMQSNAMM- 419
Cdd:PRK11432 16 FG--SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 NGTIRDNILYGVDRE-VSEEELIHYAKLANCHEFIMEFEQGY-DTIvgerglklSGGQRQRIDIARSFVKNPDILLLDEA 497
Cdd:PRK11432 92 HMSLGENVGYGLKMLgVPKEERKQRVKEALELVDLAGFEDRYvDQI--------SGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 2254949669 498 TANLDS-------ESERKIQEALDIlmenrTTIVIAH 527
Cdd:PRK11432 164 LSNLDAnlrrsmrEKIRELQQQFNI-----TSLYVTH 195
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
334-555 |
1.28e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.51 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDD-TP----VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS----LTD 404
Cdd:PRK13646 3 IRFDNVSYTYQKgTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 405 WRRKIGYVMQ--SNAMMNGTIRDNILYGVDR-EVSEEELIHYAklancHEFIMEFEQGYDtIVGERGLKLSGGQRQRIDI 481
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfKMNLDEVKNYA-----HRLLMDLGFSRD-VMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 482 ARSFVKNPDILLLDEATANLDSESERKIQEALDILM--ENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEEL 555
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
329-514 |
1.83e-15 |
|
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: 79.21 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 329 IPTGD------LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSidalsl 402
Cdd:TIGR03719 312 IPPGPrlgdkvIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 403 tdwrrKIGYVMQSNAMMNG--TIRDNILYGVD------REVSEEelihyaklANCHEFimEFeQGYD--TIVGErglkLS 472
Cdd:TIGR03719 386 -----KLAYVDQSRDALDPnkTVWEEISGGLDiiklgkREIPSR--------AYVGRF--NF-KGSDqqKKVGQ----LS 445
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2254949669 473 GGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALD 514
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
313-543 |
2.23e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.90 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 313 LHEPLENIAAPNLQDEIPTGDLKfdHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIErmyeidqgGIYY 392
Cdd:PRK10938 242 LPEPDEPSARHALPANEPRIVLN--NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT--------GDHP 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 393 DGTSIDaLSL---------TDW--RRKIGYVMQSNAM---MNGTIRDNIL------YGVDREVSEEElihyAKLANCHEF 452
Cdd:PRK10938 312 QGYSND-LTLfgrrrgsgeTIWdiKKHIGYVSSSLHLdyrVSTSVRNVILsgffdsIGIYQAVSDRQ----QKLAQQWLD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 453 IMefeqGYDTIVGERGLK-LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTiviahrlst 531
Cdd:PRK10938 387 IL----GIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGET--------- 453
|
250
....*....|..
gi 2254949669 532 ikkagQIIFLDH 543
Cdd:PRK10938 454 -----QLLFVSH 460
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
349-551 |
2.28e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDG------TSIDALSLtdwrrKIGYV----MQSNAM 418
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvrirSPRDAIAL-----GIGMVhqhfMLVPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 mngTIRDNILYGvdREVSEEELIHYAKLAnchEFIMEFEQGY------DTIVGErglkLSGGQRQRIDIARSFVKNPDIL 492
Cdd:COG3845 96 ---TVAENIVLG--LEPTKGGRLDRKAAR---ARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 493 LLDEATANLDSeserkiQEAlDILM--------ENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGR 551
Cdd:COG3845 164 ILDEPTAVLTP------QEA-DELFeilrrlaaEGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVD 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
334-533 |
2.44e-15 |
|
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: 79.41 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGyddTP----VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIermyeidqGGIY--YDGT-SIDAlsltdwR 406
Cdd:TIGR00954 452 IKFENIPLV---TPngdvLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELWpvYGGRlTKPA------K 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 407 RKIGYVMQSNAMMNGTIRDNILYG------VDREVSEEELIHYakLANCH-EFIMEFEQGYDTIVGERGLkLSGGQRQRI 479
Cdd:TIGR00954 515 GKLFYVPQRPYMTLGTLRDQIIYPdssedmKRRGLSDKDLEQI--LDNVQlTHILEREGGWSAVQDWMDV-LSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 480 DIARSFVKNPDILLLDEATANLDSESERKIQEALDILmeNRTTIVIAHRLSTIK 533
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
348-525 |
2.70e-15 |
|
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: 74.01 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRK-IGYV----MQSNAMMNGT 422
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 423 IRDNILYGVDrevseeelihyaklanchefimefeqgydtivgerglkLSGGQRQRIDIARSFVKNPDILLLDEATANLD 502
Cdd:cd03215 95 VAENIALSSL--------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180
....*....|....*....|...
gi 2254949669 503 SESERKIQEALDILMENRTTIVI 525
Cdd:cd03215 137 VGAKAEIYRLIRELADAGKAVLL 159
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
338-502 |
3.34e-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: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGYDD--TPVLKDVSFNVLRGEVTAFVGPSGSGKS----TLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRR---- 407
Cdd:COG4172 13 SVAFGQGGgtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 408 KIGYVMQ--SNAMmngtirdNILYGVDREVSEEELIHyAKL--ANCHEFIME-FEQgydtiVG----ERGLK-----LSG 473
Cdd:COG4172 93 RIAMIFQepMTSL-------NPLHTIGKQIAEVLRLH-RGLsgAAARARALElLER-----VGipdpERRLDayphqLSG 159
|
170 180
....*....|....*....|....*....
gi 2254949669 474 GQRQRIDIARSFVKNPDILLLDEATANLD 502
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-573 |
6.06e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSID--ALSLTDWRRKIGYVMQ-- 414
Cdd:PRK13638 7 LWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFQdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 SNAMMNGTIRDNILYGV-DREVSEEELIHYAKLANchefimefeqgydTIVGERGLK------LSGGQRQRIDIARSFVK 487
Cdd:PRK13638 87 EQQIFYTDIDSDIAFSLrNLGVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALD-ILMENRTTIVIAHRLSTIKKAGQIIF-LDHGEVTGRGRHEELMQThamyQQF 565
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRrIVAQGNHVIISSHDIDLIYEISDAVYvLRQGQILTHGAPGEVFAC----TEA 229
|
....*...
gi 2254949669 566 VETQNLTQ 573
Cdd:PRK13638 230 MEQAGLTQ 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
361-561 |
6.11e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.45 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 361 VTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDG-TSIDA---LSLTDWRRKIGYVMQSNAMM-NGTIRDNILYGVDREV 435
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAekgICLPPEKRRIGYVFQDARLFpHYKVRGNLRYGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 436 SEEelihyaklanchefimefeqgYDTIVGERGLK---------LSGGQRQRIDIARSFVKNPDILLLDEATANLDseSE 506
Cdd:PRK11144 106 VAQ---------------------FDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLD--LP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 507 RKiQEALDIL----MENRTTIV-IAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQTHAM 561
Cdd:PRK11144 163 RK-RELLPYLerlaREINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLEEVWASSAM 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
325-563 |
1.21e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 325 LQDEIPTGDLKF--DHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSL 402
Cdd:PRK10575 1 MQEYTNHSDTTFalRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 403 TDWRRKIGYVMQSNAMMNG-TIRDNILYG-------------VDREVSEEELihyaklanchefimefeqgydTIVGERG 468
Cdd:PRK10575 81 KAFARKVAYLPQQLPAAEGmTVRELVAIGrypwhgalgrfgaADREKVEEAI---------------------SLVGLKP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 469 L------KLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAhRLSTIKKAGQ----I 538
Cdd:PRK10575 140 LahrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAARycdyL 218
|
250 260
....*....|....*....|....*
gi 2254949669 539 IFLDHGEVTGRGRHEELMQTHAMYQ 563
Cdd:PRK10575 219 VALRGGEMIAQGTPAELMRGETLEQ 243
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
349-546 |
1.40e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGgiyyDGTSIDALSLT---------DWRR---KIGYVMQSN 416
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKS----AGSHIELLGRTvqregrlarDIRKsraNTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 417 AMMNG-TIRDNILYGV--DREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILL 493
Cdd:PRK09984 96 NLVNRlSVLENVLIGAlgSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 494 LDEATANLDSESERKIQEALDILMENR--TTIVIAHRLS-TIKKAGQIIFLDHGEV 546
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
343-533 |
1.74e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.12 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID--QGGIYYDGTSIDALSLTDWRRK-IGYVMQSNAMM 419
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 -NGTIRDNILYGvdREVSEEELIHYAKL-ANCHEFIMEFeqGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEA 497
Cdd:PRK13549 95 kELSVLENIFLG--NEITPGGIMDYDAMyLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2254949669 498 TANLdSESERKIqeALDILMENR----TTIVIAHRLSTIK 533
Cdd:PRK13549 171 TASL-TESETAV--LLDIIRDLKahgiACIYISHKLNEVK 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
334-555 |
1.89e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDD------TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDG--TSiDALSLTDW 405
Cdd:PRK13633 5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTS-DEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 406 RRKIGYVMQS--NAMMNGTIRDNILYGVDREVSEEELIHyAKLANCHEFIMEFEqgYDTIVGERglkLSGGQRQRIDIAR 483
Cdd:PRK13633 84 RNKAGMVFQNpdNQIVATIVEEDVAFGPENLGIPPEEIR-ERVDESLKKVGMYE--YRRHAPHL---LSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 484 SFVKNPDILLLDEATANLDSeSERKiqEALDILME-----NRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRGRHEEL 555
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDP-SGRR--EVVNTIKElnkkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
342-566 |
3.03e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.92 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 342 GYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDAL---SLTDWRRK-IGYVMQSNA 417
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 418 MMNG-TIRDN-----ILYGVDREvseeelihyAKLANCHEFIMEFeqGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDI 491
Cdd:PRK10535 97 LLSHlTAAQNvevpaVYAGLERK---------QRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 492 LLLDEATANLDSESERKIQEALDILMEN-RTTIVIAHRLSTIKKAGQIIFLDHGEVT----------GRGRHEELMQTHA 560
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIVrnppaqekvnVAGGTEPVVNTAS 245
|
....*.
gi 2254949669 561 MYQQFV 566
Cdd:PRK10535 246 GWRQFV 251
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
344-540 |
4.32e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.92 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFS-LIER--MYEIDQGGIYYDGTSIDAlsltDWRRKIGYVMQSNAMM- 419
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERvtTGVITGGDRLVNGRPLDS----SFQRSIGYVQQQDLHLp 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 NGTIRDNILYGV----DREVSEEELIHYAklanchEFIM---EFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDIL 492
Cdd:TIGR00956 850 TSTVRESLRFSAylrqPKSVSKSEKMEYV------EEVIkllEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2254949669 493 L-LDEATANLDSESERKIQEALDILMENRTTIviahrLSTIKKAGQIIF 540
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADHGQAI-----LCTIHQPSAILF 967
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
347-526 |
4.87e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.06 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDalsLTDWRRKIGYVMQSNAMMNG-TIRD 425
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHRNAMKPAlTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NI-----LYGvDREVSEEELIHYAKLANchefIMEFEQGYdtivgerglkLSGGQRQRIDIARSFVKNPDILLLDEATAN 500
Cdd:PRK13539 93 NLefwaaFLG-GEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*.
gi 2254949669 501 LDSESERKIQEALDILMENRTTIVIA 526
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
341-554 |
8.32e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 341 FGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDAlSLTDWRRKIGYVMQSNAMM- 419
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGINp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 NGTIRDNILYGVDREVSEEELIHYAKLANCHEFImEFEQGYdtivgerglkLSGGQRQRIDIARSFVKNPDILLLDEATA 499
Cdd:PRK13540 88 YLTLRENCLYDIHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 500 NLDseserkiQEALDILMenrtTIVIAHRlstiKKAGQIIFLDHGEVT-GRGRHEE 554
Cdd:PRK13540 157 ALD-------ELSLLTII----TKIQEHR----AKGGAVLLTSHQDLPlNKADYEE 197
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
349-557 |
9.17e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID---QGGIYYDGTSIDALSLtdwRRKIGYVMQSNaMMNG--TI 423
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEM---RAISAYVQQDD-LFIPtlTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RDNILYG----VDREVSE-------EELIHYAKLANCHefimefeqgyDTIVGERGLK--LSGGQRQRIDIARSFVKNPD 490
Cdd:TIGR00955 117 REHLMFQahlrMPRRVTKkekrervDEVLQALGLRKCA----------NTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 491 ILLLDEATANLDSESERKIQEALDILMENRTTIVIA-HRLST--IKKAGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
348-546 |
1.28e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLfslIERMYEI---DQGGIYY---------------DGTSIDALSLT------ 403
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTF---IEHLNALllpDTGTIEWifkdeknkkktkekeKVLEKLVIQKTrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 404 ---DWRRKIGYVMQ--SNAMMNGTIRDNIL-----YGVDREVSEEELIHYAKLANCHEFIME---FEqgydtivgerglk 470
Cdd:PRK13651 99 kikEIRRRVGVVFQfaEYQLFEQTIEKDIIfgpvsMGVSKEEAKKRAAKYIELVGLDESYLQrspFE------------- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 471 LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIA-HRL-STIKKAGQIIFLDHGEV 546
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLdNVLEWTKRTIFFKDGKI 243
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
329-555 |
1.41e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.37 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 329 IPTGDLKfdHVYFGydDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRK 408
Cdd:PRK13652 4 IETRDLC--YSYSG--SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 409 IGYVMQS--NAMMNGTIRDNILYGVDREVSEEELIHYAKLANCHEFimefeqGYDTIVGERGLKLSGGQRQRIDIARSFV 486
Cdd:PRK13652 80 VGLVFQNpdDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 487 KNPDILLLDEATANLDSESERKIQEALDILMEN--RTTIVIAHRLSTIKKAGQIIF-LDHGEVTGRGRHEEL 555
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYvMDKGRIVAYGTVEEI 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
349-530 |
1.70e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 71.92 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTL---FSLIErmyEIDQGGIYYDGTSI---DALSLTDWRRKIGYVMQSN-AMMN- 420
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIE---TPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPyGSLNp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 -GTIRDnILygvdrevsEEELIHYAKL--ANCHEFIMEfeqgydtIVGERGLK----------LSGGQRQRIDIARSFVK 487
Cdd:PRK11308 108 rKKVGQ-IL--------EEPLLINTSLsaAERREKALA-------MMAKVGLRpehydryphmFSGGQRQRIAIARALML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2254949669 488 NPDILLLDEATANLDSEserkIQ-EALDILM----ENRTTIV-IAHRLS 530
Cdd:PRK11308 172 DPDVVVADEPVSALDVS----VQaQVLNLMMdlqqELGLSYVfISHDLS 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
334-557 |
1.97e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYD-DTP----VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS----LTD 404
Cdd:PRK13643 2 IKFEKVNYTYQpNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 405 WRRKIGYVMQ--SNAMMNGTIRDNILYGVDR-EVSEEELIHYAklANCHEFIMEFEQGYDtivgERGLKLSGGQRQRIDI 481
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNfGIPKEKAEKIA--AEKLEMVGLADEFWE----KSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 482 ARSFVKNPDILLLDEATANLDSESERKIQEALD-ILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQ 557
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFEsIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
352-556 |
2.26e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 352 VSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEiDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNammngtirdNILYGV 431
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLSQQQ---------TPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 432 DrevseeeLIHYAKL---ANCHEFIMEFEQGYdtIVGERGL---------KLSGGQRQRIDIARSFVK-----NPD--IL 492
Cdd:PRK03695 85 P-------VFQYLTLhqpDKTRTEAVASALNE--VAEALGLddklgrsvnQLSGGEWQRVRLAAVVLQvwpdiNPAgqLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 493 LLDEATANLDSESerkiQEALDILME-----NRTTIVIAHRLS-TIKKAGQIIFLDHGEVTGRGRHEELM 556
Cdd:PRK03695 156 LLDEPMNSLDVAQ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
331-555 |
2.41e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.81 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 331 TGDLKFDHVYFGY-DDTP----VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQG----GIYYDGTSIDAL- 400
Cdd:PRK13645 4 SKDIILDNVSYTYaKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivGDYAIPANLKKIk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 401 SLTDWRRKIGYVMQ--SNAMMNGTIRDNILYG-VDREVSEEELihYAKLANchefIMEFEQGYDTIVGERGLKLSGGQRQ 477
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpVNLGENKQEA--YKKVPE----LLKLVQLPEDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 478 RIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMEN--RTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEE 554
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237
|
.
gi 2254949669 555 L 555
Cdd:PRK13645 238 I 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
347-545 |
8.24e-13 |
|
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: 71.12 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLierMYEIDQGgiyYDGTSIDALSLtdwrrKIGYVMQSNAM-MNGTIRD 425
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDKD---FNGEARPQPGI-----KVGYLPQEPQLdPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NILYGV-------DR--EVSE---EELIHYAKLA-------------NCHEFIMEFEQG--------YDTIVGerglKLS 472
Cdd:TIGR03719 88 NVEEGVaeikdalDRfnEISAkyaEPDADFDKLAaeqaelqeiidaaDAWDLDSQLEIAmdalrcppWDADVT----KLS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 473 GGQRQRIDIARSFVKNPDILLLDEATANLDSES----ERKIQEAldilmeNRTTIVIAH-RLSTIKKAGQIIFLDHGE 545
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQEY------PGTVVAVTHdRYFLDNVAGWILELDRGR 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
334-555 |
1.50e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDwRRKIG-YV 412
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGiYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQSNAMM--NGTIRDNILYGVDR-EVSEEELIHYAKLANCHeFIMEFEQGydtivgerglKLSGGQRQRIDIARSFVKNP 489
Cdd:PRK15439 91 VPQEPLLfpNLSVKENILFGLPKrQASMQKMKQLLAALGCQ-LDLDSSAG----------SLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 490 DILLLDEATANLD-SESERKIQEALDILMENRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEEL 555
Cdd:PRK15439 160 RILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
342-521 |
1.58e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.52 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 342 GYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLF----SLIERMYEIDqGGIYYDGTSIDALSLTdWRRKIGYVMQSna 417
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSVE-GDIHYNGIPYKEFAEK-YPGEIIYVSEE-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 418 mmngtirdnilygvDREVSE---EELIHYAKLANCHEFImefeqgydtivgeRGLklSGGQRQRIDIARSFVKNPDILLL 494
Cdd:cd03233 92 --------------DVHFPTltvRETLDFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCW 142
|
170 180
....*....|....*....|....*..
gi 2254949669 495 DEATANLDSESerkiqeALDILMENRT 521
Cdd:cd03233 143 DNSTRGLDSST------ALEILKCIRT 163
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
18-294 |
1.61e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 68.46 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 18 VGLIIVAVTIASIGSLTGLLVPLFTGQVVDKFTfesispVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWE 97
Cdd:cd18561 4 LGLLITALYIAQAWLLARALARIFAGGPWEDIM------PPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 98 HIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLG 177
Cdd:cd18561 78 KLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 178 KIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGII 257
Cdd:cd18561 158 RLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALA 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 2254949669 258 LGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLST 294
Cdd:cd18561 238 LGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGA 274
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
25-305 |
1.67e-12 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 68.31 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 25 VTIAS-IGSLTGLLVPLFTGQVVDK-FTFESISP--VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHII 100
Cdd:cd18783 7 VAIASlILHVLALAPPIFFQIVIDKvLVHQSYSTlyVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 101 HLKMPFFDKNESGQLMSRLTdDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTF---ITIPIFILVIVPlg 177
Cdd:cd18783 87 SLPIDFFERTPAGVLTKHMQ-QIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLafsALIALIILAFLP-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 178 kIMQKISTNTQTEIANFSGLLGRVLTEMRLVK---VANTEKLELDKAHSnlKTIyNLGLKQAKIAAVVQPISGIIMLITI 254
Cdd:cd18783 164 -PFRRRLQALYRAEGERQAFLVETVHGIRTVKslaLEPRQRREWDERVA--RAI-RARFAVGRLSNWPQTLTGPLEKLMT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 255 GIILGFGGMRIASGAISAGTLVAmiFYVL--NLSIPLINLSTLVTDYKKAVGA 305
Cdd:cd18783 240 VGVIWVGAYLVFAGSLTVGALIA--FNMLagRVAGPLVQLAGLVQEYQEARLS 290
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
347-502 |
1.71e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGyVM-QSNAM------- 418
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA-VLpQHSSLsfpftve 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 ----M------NGTIRDNILygVDREVSEEELIHYAklanchefimefeqgydtivGERGLKLSGGQRQRIDIAR----- 483
Cdd:PRK13548 95 evvaMgraphgLSRAEDDAL--VAAALAQVDLAHLA--------------------GRDYPQLSGGEQQRVQLARvlaql 152
|
170 180
....*....|....*....|
gi 2254949669 484 -SFVKNPDILLLDEATANLD 502
Cdd:PRK13548 153 wEPDGPPRWLLLDEPTSALD 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
334-533 |
1.82e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID--QGGIYYDGTSIDALSLTDWRRK-IG 410
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMQSNAMM-NGTIRDNILYGvdREVSEE-ELIHYAKLA-NCHEFIMEFEQGYDTI---VGERGlklsGGQRQRIDIARS 484
Cdd:TIGR02633 82 IIHQELTLVpELSVAENIFLG--NEITLPgGRMAYNAMYlRAKNLLRELQLDADNVtrpVGDYG----GGQQQLVEIAKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 485 FVKNPDILLLDEATANLdseSERKIQEALDILME----NRTTIVIAHRLSTIK 533
Cdd:TIGR02633 156 LNKQARLLILDEPSSSL---TEKETEILLDIIRDlkahGVACVYISHKLNEVK 205
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
33-309 |
2.51e-12 |
|
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: 67.91 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 33 LTGLLVPLFTGQVVDK-FTFESISP--VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFDK 109
Cdd:cd18588 16 LFALVTPLFFQVIIDKvLVHRSLSTldVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 110 NESGQLMSRLTD-DTkvINDFISQKlpgFFPAVITLIGS---LIMLFVLDWQMTLLTFITIPIFILVIVPLGKIMQKIST 185
Cdd:cd18588 96 RQVGDTVARVRElES--IRQFLTGS---ALTLVLDLVFSvvfLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 186 NTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGGMRI 265
Cdd:cd18588 171 EKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2254949669 266 ASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAVGASQRI 309
Cdd:cd18588 251 MDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
349-544 |
2.52e-12 |
|
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: 65.73 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID--QGGIYYDGTSIDAlsltDWRRKIGYVMQSNAMM-NGTIRD 425
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----NFQRSTGYVEQQDVHSpNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NILYGvdrevseeelihyAKLanchefimefeqgydtivgeRGLKLSggQRQRIDIARSFVKNPDILLLDEATANLDSES 505
Cdd:cd03232 99 ALRFS-------------ALL--------------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2254949669 506 ERKIQEAL-DILMENRTTIVIAHRLS--TIKKAGQIIFLDHG 544
Cdd:cd03232 144 AYNIVRFLkKLADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
347-502 |
3.02e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTD-WRRKIGYV----MQSNAMMNG 421
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVpedrKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDNILYGVDREVSEEELIHYAKL-ANCHEFIMEFE---QGYDTIVGErglkLSGGQRQRIDIARSFVKNPDILLLDEA 497
Cdd:COG1129 346 SIRENITLASLDRLSRGGLLDRRRErALAEEYIKRLRiktPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEP 421
|
....*
gi 2254949669 498 TANLD 502
Cdd:COG1129 422 TRGID 426
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
349-532 |
3.38e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSID-ALSltdwRRKIGYVMQSN----------- 416
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQ----KNLVAYVPQSEevdwsfpvlve 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 417 --AMMN-----GTIRdnILYGVDREVSEEELIHYAKLANCHEFIMEfeqgydtivgerglkLSGGQRQRIDIARSFVKNP 489
Cdd:PRK15056 99 dvVMMGryghmGWLR--RAKKRDRQIVTAALARVDMVEFRHRQIGE---------------LSGGQKKRVFLARAIAQQG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2254949669 490 DILLLDEATANLDSESERKIQEALDILM-ENRTTIVIAHRLSTI 532
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
340-547 |
3.44e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 340 YFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIG-----YVMQ 414
Cdd:PRK11147 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEgtvydFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 SNAMMNGTIRD--NILYGVDREVSEEELIHYAKLANC--HEFIMEFEQGYDTIVGERGL-------KLSGGQRQRIDIAR 483
Cdd:PRK11147 90 GIEEQAEYLKRyhDISHLVETDPSEKNLNELAKLQEQldHHNLWQLENRINEVLAQLGLdpdaalsSLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 484 SFVKNPDILLLDEATANLDSESerkIQEALDILMENRTTIV-IAHRLSTIKK-AGQIIFLDHGEVT 547
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
329-514 |
4.17e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 329 IPTGD------LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYdGTSIdalsl 402
Cdd:PRK11819 314 IPPGPrlgdkvIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 403 tdwrrKIGYVMQSNAMMNG--TI-------RDNILYGvDREVSEEelihyaklANCHEFimEFeQGYD--TIVGErglkL 471
Cdd:PRK11819 388 -----KLAYVDQSRDALDPnkTVweeisggLDIIKVG-NREIPSR--------AYVGRF--NF-KGGDqqKKVGV----L 446
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2254949669 472 SGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALD 514
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
349-502 |
4.51e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS---LTDWRRKIGYVMQsNAMMNGTIRD 425
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQ-DPYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NILYGVDREVSEEELIHYAKLANCHEFIMEfeqgydtivgERGLK----------LSGGQRQRIDIARSFVKNPDILLLD 495
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAARVAWLLE----------RVGLLpehawrypheFSGGQRQRICIARALALNPKVIIAD 488
|
....*..
gi 2254949669 496 EATANLD 502
Cdd:PRK10261 489 EAVSALD 495
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
349-536 |
9.43e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 9.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTD-WRRKIGYVMQSNAMMNG-TIRDN 426
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 427 ILYG--VDREVSEEELIHYAKL---ANCHEFIMEFEQGYDTIVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANL 501
Cdd:PRK09700 101 LYIGrhLTKKVCGVNIIDWREMrvrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 2254949669 502 DSESERKIQEALDILMENRTTIV-IAHRLSTIKKAG 536
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRIC 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
338-527 |
1.02e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.80 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 338 HVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSlTDWR-----RKIGYV 412
Cdd:PRK10584 15 SVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD-EEARaklraKHVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQS-------NAMMNGTIrDNILYGVDREVSEEELIHYAKLANchefimefeqgydtiVGER----GLKLSGGQRQRIDI 481
Cdd:PRK10584 94 FQSfmliptlNALENVEL-PALLRGESSRQSRNGAKALLEQLG---------------LGKRldhlPAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2254949669 482 ARSFVKNPDILLLDEATANLDSESERKIQEALDILmeNR----TTIVIAH 527
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL--NRehgtTLILVTH 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-527 |
1.09e-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: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 358 RGEVTAFVGPSGSGKSTLFSLIermyeidQGGIYYDGTSIDALsltdwRRKIGYVMQS-NAMMNGTIRDnILYGVDREVS 436
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIE-----LDTVSYKPQYiKADYEGTVRD-LLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 437 EE-----ELIHYAKLanchefimefEQGYDTIVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQE 511
Cdd:cd03237 91 THpyfktEIAKPLQI----------EQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170
....*....|....*...
gi 2254949669 512 ALD--ILMENRTTIVIAH 527
Cdd:cd03237 157 VIRrfAENNEKTAFVVEH 174
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
346-547 |
1.53e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 346 TPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMY---------EIDQGGIYYDGTSIDALSltdwrrkigyvmqsn 416
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgtpvagcvDVPDNQFGREASLIDAIG--------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 417 ammngtIRDNILYGVdrevseeELIHYAKLANCHEFIMEFEQgydtivgerglkLSGGQRQRIDIARSFVKNPDILLLDE 496
Cdd:COG2401 108 ------RKGDFKDAV-------ELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 497 ATANLDSESERKIQEAL-DILMENRTTIVIA-HRlSTIKKAGQ---IIFLDHGEVT 547
Cdd:COG2401 163 FCSHLDRQTAKRVARNLqKLARRAGITLVVAtHH-YDVIDDLQpdlLIFVGYGGVP 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
347-502 |
2.98e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRK-IGYV----MQSNAMMNG 421
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIpedrLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDN-ILYGVDRE-VSEEELIHYAKL-ANCHEFIMEFE---QGYDTIVGerglKLSGGQRQRIDIARSFVKNPDILLLD 495
Cdd:COG3845 352 SVAENlILGRYRRPpFSRGGFLDRKAIrAFAEELIEEFDvrtPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
....*..
gi 2254949669 496 EATANLD 502
Cdd:COG3845 428 QPTRGLD 434
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
352-555 |
3.71e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.86 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 352 VSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKiGYV--MQSNAMMNG-TIRDNIL 428
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVrtFQHVRLFREmTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 429 YGVDREV----------------SEEELIHYAklANCHEFImefeqGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDIL 492
Cdd:PRK11300 103 VAQHQQLktglfsgllktpafrrAESEALDRA--ATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 493 LLDEATANLDSESERKIQEALDILME--NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEEL 555
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
344-514 |
7.57e-11 |
|
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: 61.61 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSlTDWRRKIGYVMQSNAMMNgti 423
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKP--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 rdnilygvdrEVSEEELIHyaklancheFIMEFEQGYD-------TIVGERGLK------LSGGQRQRIDIARSFVKNPD 490
Cdd:TIGR01189 87 ----------ELSALENLH---------FWAAIHGGAQrtiedalAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRP 147
|
170 180
....*....|....*....|....
gi 2254949669 491 ILLLDEATANLDSESERKIQEALD 514
Cdd:TIGR01189 148 LWILDEPTTALDKAGVALLAGLLR 171
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
344-513 |
8.22e-11 |
|
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: 61.74 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSiDALSLTDWRRKIGYVMQSNammngti 423
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-LDFQRDSIARGLLYLGHAP------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 rdnilyGVDREVSEEELIHYAKLANCHEFImefEQGYDTiVGERGLK------LSGGQRQRIDIARSFVKNPDILLLDEA 497
Cdd:cd03231 83 ------GIKTTLSVLENLRFWHADHSDEQV---EEALAR-VGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170
....*....|....*.
gi 2254949669 498 TANLDSESERKIQEAL 513
Cdd:cd03231 153 TTALDKAGVARFAEAM 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
345-505 |
8.74e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 345 DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLierMYEIDQGgiyYDGTSIDALSLTdwrrkIGYVMQS---NAmmNG 421
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDKE---FEGEARPAPGIK-----VGYLPQEpqlDP--EK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDNILYGV-------DR--EVSEE---------ELI-HYAKL------ANCHEFIMEFEQG--------YDTIVGerg 468
Cdd:PRK11819 86 TVRENVEEGVaevkaalDRfnEIYAAyaepdadfdALAaEQGELqeiidaADAWDLDSQLEIAmdalrcppWDAKVT--- 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 2254949669 469 lKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSES 505
Cdd:PRK11819 163 -KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
347-529 |
9.52e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.03 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDAlSLTDWRRKIGYVMQSNAMMNG-TIRD 425
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 426 NIL-YGVDREVSEEElihyAKLAncHEFIMEfEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSE 504
Cdd:TIGR01257 1023 HILfYAQLKGRSWEE----AQLE--MEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180
....*....|....*....|....*
gi 2254949669 505 SERKIQEALDILMENRTTIVIAHRL 529
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
20-281 |
1.05e-10 |
|
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: 62.86 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 20 LIIVAVTIasigSLTGLLVPLFTGQVVDkftfESISP-------VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIR 92
Cdd:cd18567 7 ILLLSLAL----ELFALASPLYLQLVID----EVIVSgdrdlltVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 93 SVLWEHIIHLKMPFFDKNESGQLMSRLtDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILV 172
Cdd:cd18567 79 SNLFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 173 IVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLI 252
Cdd:cd18567 158 RLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGL 237
|
250 260
....*....|....*....|....*....
gi 2254949669 253 TIGIILGFGGMRIASGAISAGTLVAMIFY 281
Cdd:cd18567 238 ENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
334-551 |
1.10e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIdalslTDW------RR 407
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-----TDWqtakimRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 408 KIGYVMQSNAMMNG-TIRDNILYG---VDREVSEEELIHYAKLancheFIMEFEQGYdtivgERGLKLSGGQRQRIDIAR 483
Cdd:PRK11614 81 AVAIVPEGRRVFSRmTVEENLAMGgffAERDQFQERIKWVYEL-----FPRLHERRI-----QRAGTMSGGEQQMLAIGR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 484 SFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHrlstiKKAGQIIFL-DHGEVTGRGR 551
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVE-----QNANQALKLaDRGYVLENGH 214
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
359-524 |
1.47e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 359 GEVTAFVGPSGSGKSTLFSLIERMYEID--QGGIYYDGTSIDALSLtdwrRKIGYVMQSNAMM-NGTIRDNILY----GV 431
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL----KRTGFVTQDDILYpHLTVRETLVFcsllRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 432 DREVSEEELIHYAK-------LANCHefimefeqgyDTIVGERGLK-LSGGQRQRIDIARSFVKNPDILLLDEATANLDS 503
Cdd:PLN03211 170 PKSLTKQEKILVAEsviselgLTKCE----------NTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180
....*....|....*....|.
gi 2254949669 504 ESERKIQEALDILMENRTTIV 524
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIV 260
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
339-502 |
3.04e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGydDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGtsidalsltdwRRKIGYVMQ---- 414
Cdd:PRK09544 12 VSFG--QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQklyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 415 --------SNAMM--NGTIRDNILYGVDRevseeelihyAKLANCHEFIMEfeqgydtivgerglKLSGGQRQRIDIARS 484
Cdd:PRK09544 79 dttlpltvNRFLRlrPGTKKEDILPALKR----------VQAGHLIDAPMQ--------------KLSGGETQRVLLARA 134
|
170
....*....|....*...
gi 2254949669 485 FVKNPDILLLDEATANLD 502
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVD 152
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
332-514 |
3.99e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 332 GDLKFD--HVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYdGTSIDalsltdwrrkI 409
Cdd:PRK11147 316 GKIVFEmeNVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE----------V 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 410 GYVMQSNAMMN--GTIRDNI--------LYGVDREVseeelihyakLANCHEFI------MefeqgydTIVGerglKLSG 473
Cdd:PRK11147 385 AYFDQHRAELDpeKTVMDNLaegkqevmVNGRPRHV----------LGYLQDFLfhpkraM-------TPVK----ALSG 443
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2254949669 474 GQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALD 514
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
345-576 |
5.16e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 345 DTPVLKDVSFNVLRGEVTAFVGPSGSGKS----TLFSLIERMYEIDQGGIYYDGTSIDALSLTDwrRKIGYVMQS----- 415
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRG--RKIATIMQNprsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 416 NAMMngTIRDN---ILYGVDREVSEEELIHyaklanchefIMEfEQGYDTIvgERGLKL-----SGGQRQRIDIARSFVK 487
Cdd:PRK10418 93 NPLH--TMHTHareTCLALGKPADDATLTA----------ALE-AVGLENA--ARVLKLypfemSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 488 NPDILLLDEATANLDSESERKIQEALDILMENRT--TIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQT--HAmy 562
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNApkHA-- 235
|
250
....*....|....*
gi 2254949669 563 qqfvETQNLTQ-HRA 576
Cdd:PRK10418 236 ----VTRSLVSaHLA 246
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
339-558 |
6.15e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.91 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGYDDTP--VLKDVSFNVLRGEVTAFVGPSGSGKSTlfSLIERMYEIDQGG------IYYDGTSIDALSLTDWRRKIG 410
Cdd:PRK11022 11 VHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSV--SSLAIMGLIDYPGrvmaekLEFNGQDLQRISEKERRNLVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 411 YVMqsnAMMngtIRD-----NILYGVDREVSEEELIHYA-KLANCHEFIMEFEqgydTIVG----ERGL-----KLSGGQ 475
Cdd:PRK11022 89 AEV---AMI---FQDpmtslNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLL----NQVGipdpASRLdvyphQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 476 RQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILM--ENRTTIVIAHRLSTIKKAGQ-IIFLDHGEVTGRGRH 552
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEAAHkIIVMYAGQVVETGKA 238
|
....*.
gi 2254949669 553 EELMQT 558
Cdd:PRK11022 239 HDIFRA 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
352-527 |
6.73e-10 |
|
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: 61.74 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 352 VSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYY-------DGTSIDALSLTDWRRKIGYVMQSNAMM-NGTI 423
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RDNILYGVDREVSEEelihYAKLANCHEFIME-FEQGY-DTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANL 501
Cdd:TIGR03269 383 LDNLTEAIGLELPDE----LARMKAVITLKMVgFDEEKaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180
....*....|....*....|....*...
gi 2254949669 502 DSESERKIQEALDILME--NRTTIVIAH 527
Cdd:TIGR03269 459 DPITKVDVTHSILKAREemEQTFIIVSH 486
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
341-504 |
1.24e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 341 FGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIdalSLTDWRRKIGYVMQsnammn 420
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDRSRFMAYLGH------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 gtirdniLYGVDREVSEEELIHY-AKLANCHEFIMefEQGYDTIVGERGL------KLSGGQRQRIDIARSFVKNPDILL 493
Cdd:PRK13543 90 -------LPGLKADLSTLENLHFlCGLHGRRAKQM--PGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWL 160
|
170
....*....|.
gi 2254949669 494 LDEATANLDSE 504
Cdd:PRK13543 161 LDEPYANLDLE 171
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
350-533 |
1.39e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.72 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 350 KDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRK---IGYVMQS-----NAMMng 421
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDplaslNPRM-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDNIlygvdrevSEEELIHYAKLANchefiMEFEQGYDTIVGERGL----------KLSGGQRQRIDIARSFVKNPDI 491
Cdd:PRK15079 116 TIGEII--------AEPLRTYHPKLSR-----QEVKDRVKAMMLKVGLlpnlinryphEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2254949669 492 LLLDEATANLDSESE-------RKIQEALDIlmenrTTIVIAHRLSTIK 533
Cdd:PRK15079 183 IICDEPVSALDVSIQaqvvnllQQLQREMGL-----SLIFIAHDLAVVK 226
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
19-198 |
1.46e-09 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 59.35 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 19 GLIIVAVTIASIGSLTGLLVPLFTGQVvdkfTFESISPvFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEH 98
Cdd:cd18584 5 GLLAALLIIAQAWLLARIIAGVFLEGA----GLAALLP-LLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 99 IIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGK 178
Cdd:cd18584 80 LLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGK 159
|
170 180
....*....|....*....|
gi 2254949669 179 IMQKISTNTQTEIANFSGLL 198
Cdd:cd18584 160 AAQAASRRQWAALSRLSGHF 179
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
358-532 |
2.07e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.18 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 358 RGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIyydgtsidalsltDWRRKIGYVMQS-NAMMNGTIRDNI--LYGVDRE 434
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQYiSPDYDGTVEEFLrsANTDDFG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 435 VS--EEELIHYAKLanchEFIMEFEqgydtiVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEA 512
Cdd:COG1245 432 SSyyKTEIIKPLGL----EKLLDKN------VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170 180
....*....|....*....|..
gi 2254949669 513 LDILMENR--TTIVIAHRLSTI 532
Cdd:COG1245 498 IRRFAENRgkTAMVVDHDIYLI 519
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
346-555 |
2.28e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 346 TPVLKDVSFNVLRGEVTAFVGPSGSGKS-TLFSLierMYEIDQGGiyyDGTSIDALSLTDWRRKIGYVM-QSNAMMNGtI 423
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALAL---MRLLEQAG---GLVQCDKMLLRRRSRQVIELSeQSAAQMRH-V 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RD--------------NILYGVDREVSEEELIHYAklANCHEFIMEFEQGYD--------TIVGERGLKLSGGQRQRIDI 481
Cdd:PRK10261 102 RGadmamifqepmtslNPVFTVGEQIAESIRLHQG--ASREEAMVEAKRMLDqvripeaqTILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 482 ARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRT--TIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEEL 555
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
347-564 |
2.65e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKS-TLFSLIERM----YEIDQGGIYYDGTSI---DALSLTDWR-RKIGYVMQSnA 417
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpsppVVYPSGDIRFHGESLlhaSEQTLRGVRgNKIAMIFQE-P 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 418 MmngtIRDNILYGVDREVSEEELIHYA--KLANCHEFIMEFEQgydtiVGERGLK---------LSGGQRQRIDIARSFV 486
Cdd:PRK15134 102 M----VSLNPLHTLEKQLYEVLSLHRGmrREAARGEILNCLDR-----VGIRQAAkrltdyphqLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 487 KNPDILLLDEATANLDSESERKIqeaLDILME-----NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQT-- 558
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQI---LQLLRElqqelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSApt 249
|
....*.
gi 2254949669 559 HAMYQQ 564
Cdd:PRK15134 250 HPYTQK 255
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
334-551 |
5.46e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.83 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPV-LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIGYV 412
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQSNAMMNGtirdniLYGVDREVSEEELIHY--AKLANCHEfiMEFEQGYDTivgerGLKLSGGQRQRIDIARSFVKNPD 490
Cdd:PRK10522 403 FTDFHLFDQ------LLGPEGKPANPALVEKwlERLKMAHK--LELEDGRIS-----NLKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 491 ILLLDEATANLDSESERKI-QEALDILMENRTTIV-IAHRLSTIKKAGQIIFLDHG---EVTGRGR 551
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFaISHDDHYFIHADRLLEMRNGqlsELTGEER 535
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
349-570 |
5.76e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.75 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGT-SIDALSltdwrrkIGYVMQSNAMMNGTIRdNI 427
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAIS-------SGLNGQLTGIENIELK-GL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 428 LYGVDREVSEEELIHYAKLANCHEFIMEFEQGYdtivgerglklSGGQRQRIDIARSFVKNPDILLLDEATANLDSESER 507
Cdd:PRK13545 112 MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 508 KIQEALDILMENRTTI-VIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMqthAMYQQFVETQN 570
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIfFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVV---DHYDEFLKKYN 242
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
334-558 |
6.06e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 334 LKFDHVYFGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDwrrkigyvm 413
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 qsnAMMNG--------------TIRDNILYG--------VDRevseEELIHYAKLanchefimEFEQGYDTIVGERGLK- 470
Cdd:PRK11288 76 ---ALAAGvaiiyqelhlvpemTVAENLYLGqlphkggiVNR----RLLNYEARE--------QLEHLGVDIDPDTPLKy 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 471 LSGGQRQRIDIARSFVKNPDILLLDEATANLdseSERKIqealDILM--------ENRTTIVIAHRLS---------TIK 533
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSL---SAREI----EQLFrvirelraEGRVILYVSHRMEeifalcdaiTVF 213
|
250 260
....*....|....*....|....*..
gi 2254949669 534 KAGQII--FLDHGEVTgrgrHEELMQT 558
Cdd:PRK11288 214 KDGRYVatFDDMAQVD----RDQLVQA 236
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
344-527 |
6.14e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLI--ERMYEIDQGGIYYDGTSIDALSLTDwRRKIG------YVMQS 415
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPED-RAGEGifmafqYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 416 NAMMNGTIRDNILYGVDREVSEEELIHYAKLANCHEFIMEFEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLD 495
Cdd:PRK09580 91 PGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190
....*....|....*....|....*....|...
gi 2254949669 496 EATANLDSESERKIQEALDILM-ENRTTIVIAH 527
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRdGKRSFIIVTH 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
358-543 |
6.40e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 358 RGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRKIgyvmqsnammngtirdnilygvdrevse 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 438 eelihyaklanchefimefeqgydtIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALD--- 514
Cdd:smart00382 53 -------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|...
gi 2254949669 515 ----ILMENRTTIVIAHRLSTIKKAGQIIFLDH 543
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
339-529 |
7.40e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.87 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 339 VYFGyDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIdALSLTDWRRKIGYVMQSNAM 418
Cdd:TIGR01257 1946 VYSG-TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 mngtirDNILYGvdrevsEEELIHYAKLANCHEfiMEFEQGYDTIVGERGLKL---------SGGQRQRIDIARSFVKNP 489
Cdd:TIGR01257 2024 ------DDLLTG------REHLYLYARLRGVPA--EEIEKVANWSIQSLGLSLyadrlagtySGGNKRKLSTAIALIGCP 2089
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2254949669 490 DILLLDEATANLDSESERKIQEAL-DILMENRTTIVIAHRL 529
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSM 2130
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
348-541 |
8.01e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.70 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMyeidQGGIYYDG-TSIDALSLTD--WRRKIGYVMQSNAMM-NGTI 423
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR----KTGGYIEGdIRISGFPKKQetFARISGYCEQNDIHSpQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 RDNILYG----VDREVSEEElihyaKLANCHEF--IMEFEQGYDTIVGERGLK-LSGGQRQRIDIARSFVKNPDILLLDE 496
Cdd:PLN03140 971 RESLIYSaflrLPKEVSKEE-----KMMFVDEVmeLVELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 497 ATANLDSESE----RKIQEALDIlmeNRTTIVIAHRLST-----------IKKAGQIIFL 541
Cdd:PLN03140 1046 PTSGLDARAAaivmRTVRNTVDT---GRTVVCTIHQPSIdifeafdelllMKRGGQVIYS 1102
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
343-546 |
1.58e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.84 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMyEIDQGGIYYDGTSidalSLTDWRRKIGYVMQSNAMMN-G 421
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAGTA----PLAEAREDTRLMFQDARLLPwK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 422 TIRDNI---LYGVDREVSEEEL--IHYAKLANchefimefeqgydtivgERGLKLSGGQRQRIDIARSFVKNPDILLLDE 496
Cdd:PRK11247 97 KVIDNVglgLKGQWRDAALQALaaVGLADRAN-----------------EWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2254949669 497 ATANLDSESERKIQEALDILMENR--TTIVIAHRLS-TIKKAGQIIFLDHGEV 546
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
349-556 |
2.16e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSI-----------------DALSLTDWRRKIGY 411
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyrsqrirmifqDPSTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 412 VMQS----NAMMNGTIRDNILYGVDREVS--EEELIHYAKLanchefimefeqgydtivgerglkLSGGQRQRIDIARSF 485
Cdd:PRK15112 109 ILDFplrlNTDLEPEQREKQIIETLRQVGllPDHASYYPHM------------------------LAPGQKQRLGLARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949669 486 VKNPDILLLDEATANLDSESERKIQEALDILMENR--TTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELM 556
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-534 |
2.78e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTD-WRRKIGYVMQS-NAMMNGTIRDN 426
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 427 ILYGvdREVSEEELIHYAKLANCHEFIMEfEQGYDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLdseSE 506
Cdd:PRK10982 94 MWLG--RYPTKGMFVDQDKMYRDTKAIFD-ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TE 167
|
170 180 190
....*....|....*....|....*....|..
gi 2254949669 507 RKIQEALDI---LMENRTTIV-IAHRLSTIKK 534
Cdd:PRK10982 168 KEVNHLFTIirkLKERGCGIVyISHKMEEIFQ 199
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
348-542 |
2.81e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.11 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSltdwRRKIGYVMQSNAM-MNGTIRDN 426
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHNLGLkLEMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 427 ILYGVDREVSEEEL---IHYAKLanchefimefeqgyDTIVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDS 503
Cdd:PRK13541 91 LKFWSEIYNSAETLyaaIHYFKL--------------HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2254949669 504 ESeRKIQEALDILMENRTTIVI--AHRLSTIKKAgQIIFLD 542
Cdd:PRK13541 157 EN-RDLLNNLIVMKANSGGIVLlsSHLESSIKSA-QILQLD 195
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
23-209 |
3.13e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 55.18 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 23 VAVTIASIGSLTGLLVPLFTGQVVDKFTFESISP-----VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWE 97
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlsegyLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 98 HIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQkLPGFFPAVITLIGSLIMLFvldWQMTLLTFITIpIFILVIVPLG 177
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLF-LHYLWSAPLQIIVALYLLY---RLLGWAALAGL-GVLLLLIPLQ 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 2254949669 178 KIMQKISTNTQTEIANFS----GLLGRVLTEMRLVK 209
Cdd:cd18579 156 AFLAKLISKLRKKLMKATdervKLTNEILSGIKVIK 191
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
344-525 |
4.88e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 344 DDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLI--ERMYEIDQGGIYYDGTSIdaLSLT-DWRRKIGYVM--QSNAM 418
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESI--LDLEpEERAHLGIFLafQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 MNGTIRDNIL---YGVDR---EVSEEELIHYaklancHEFIMEFEQ--GYDTIVGERGLK--LSGGQRQRIDIARSFVKN 488
Cdd:CHL00131 96 IPGVSNADFLrlaYNSKRkfqGLPELDPLEF------LEIINEKLKlvGMDPSFLSRNVNegFSGGEKKRNEILQMALLD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2254949669 489 PDILLLDEATANLDSESERKIQEALDILMENRTTIVI 525
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSENSIIL 206
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
349-534 |
5.01e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID--QGGIYYDGTSIDALSLTDW-RRKIGYVMQSNAMMNG-TIR 424
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSeALGIVIIHQELALIPYlSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 425 DNILYGvdREVSEEELIHYAKLANCHEFIME---FEQGYDTIVGERGLklsgGQRQRIDIARSFVKNPDILLLDEATANL 501
Cdd:NF040905 97 ENIFLG--NERAKRGVIDWNETNRRARELLAkvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 2254949669 502 -DSESERkiqeALDILMENR----TTIVIAHRLSTIKK 534
Cdd:NF040905 171 nEEDSAA----LLDLLLELKaqgiTSIIISHKLNEIRR 204
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
20-173 |
5.01e-08 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 54.79 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 20 LIIVAVTIASIgsLTGLLVPLFTGQVVDKF---TFESISPVFIIALVAVFLVNAVLSGFGYYLLNKIGEKI-IYAIRSVL 95
Cdd:cd18569 5 LFVVLAGLLLV--IPGLVIPVFSRIFIDDIlvgGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLaLSSSSRFF 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 96 WeHIIHLKMPFFDKNESGQLMSRL-TDDTkvINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVI 173
Cdd:cd18569 83 W-HVLRLPVEFFSQRYAGDIASRVqSNDR--VANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVL 158
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
341-572 |
8.38e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 341 FGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSL--------TDWRRkigyv 412
Cdd:PRK10938 11 FRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFeqlqklvsDEWQR----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 mqsnammNGTirDNILYGVD---REVSEEELIHYAKLANCHEFIMEFeqGYDTIVGERGLKLSGGQRQRIDIARSFVKNP 489
Cdd:PRK10938 86 -------NNT--DMLSPGEDdtgRTTAEIIQDEVKDPARCEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 490 DILLLDEATANLDSESERKIQEALDILMENRTTIV-IAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQtHAMYQQFVE 567
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ-QALVAQLAH 233
|
....*
gi 2254949669 568 TQNLT 572
Cdd:PRK10938 234 SEQLE 238
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
30-295 |
1.10e-07 |
|
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: 53.77 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 30 IGSLTGLLVPLFTGQVVDKFTFESISPV-----FIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKM 104
Cdd:cd18560 7 LGKACNVLAPLFLGRAVNALTLAKVKDLesavtLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 105 PFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIG-SLIMLFVLDWQMTLLTFITIPIFILVIVPLGKIMQKI 183
Cdd:cd18560 87 DWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVvSVVFAFHFGAWLALIVFLSVLLYGVFTIKVTEWRTKF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 184 ST------NTQTEIANFSgllgrvLTEMRLVKVANTEKLELDK--------AHSNLKTIYNLGL---KQAKIAAVVQPIS 246
Cdd:cd18560 167 RRaankkdNEAHDIAVDS------LLNFETVKYFTNEKYEVDRygeavkeyQKSSVKVQASLSLlnvGQQLIIQLGLTLG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2254949669 247 GIimlitigiilgFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLSTL 295
Cdd:cd18560 241 LL-----------LAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTI 278
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
15-172 |
1.19e-07 |
|
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: 53.66 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 15 SWPVGLIIVAVTIASIGSLTGLLvpLFTGQVVDKFTFESISPVFIIALVAVFLVnAVLSGFGYYLLNKIGEKIIYAIRSV 94
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLD--WWSSDWSSSPNSSSGYYLGVYAALLVLAS-VLLVLLRWLLFVLAGLRASRRLHDK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 95 LWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILV 172
Cdd:cd18580 78 LLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
340-526 |
1.27e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 340 YFGYDDTP---VLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIE---RMYEIDQGG-IYYDGTSIDALSltdwRRKIGYV 412
Cdd:TIGR00956 65 LKKFRDTKtfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntDGFHIGVEGvITYDGITPEEIK----KHYRGDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 413 MQS----NAMMNGTIRDNILY------------GVDREVSEEELIHYAkLAnchefIMEFEQGYDTIVGE---RGLklSG 473
Cdd:TIGR00956 141 VYNaetdVHFPHLTVGETLDFaarcktpqnrpdGVSREEYAKHIADVY-MA-----TYGLSHTRNTKVGNdfvRGV--SG 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 474 GQRQRIDIARSFVKNPDILLLDEATANLDS----ESERKIQEALDILmenRTTIVIA 526
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSatalEFIRALKTSANIL---DTTPLVA 266
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-532 |
1.65e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 358 RGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIyydgtsidalsltDWRRKIGYVMQS-NAMMNGTIRDnILYGVDREVS 436
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQYiKPDYDGTVED-LLRSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 437 ----EEELIHYAKLANchefIMEFEqgydtiVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEA 512
Cdd:PRK13409 430 ssyyKSEIIKPLQLER----LLDKN------VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170 180
....*....|....*....|..
gi 2254949669 513 LDILMENR--TTIVIAHRLSTI 532
Cdd:PRK13409 496 IRRIAEEReaTALVVDHDIYMI 517
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
36-295 |
1.87e-07 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 52.92 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 36 LLVPLFTGQVVDKFT-FESISPVFIIALVAVflvnavlsgfgYYLLNKIGekIIYAIRSVLW----------------EH 98
Cdd:cd18583 13 VLVPRQLGIIVDSLSgGSGKSPWKEIGLYVL-----------LRFLQSGG--GLGLLRSWLWipveqysyralstaafNH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 99 IIHLKMPFFDKNESGQLMSRLtDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVL-DWQMTLLTFITIPIFILVIVPLG 177
Cdd:cd18583 80 VMNLSMDFHDSKKSGEVLKAI-EQGSSINDLLEQILFQIVPMIIDLVIAIVYLYYLfDPYMGLIVAVVMVLYVWSTIKLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 178 KIMQKIstntQTEIANFSGLLGRVLTEMRL----VKVANTEKLELDKAHSNLKTiynlglKQAKIAAVVQPISGIIMLIT 253
Cdd:cd18583 159 SWRTKL----RRDMIDADREERSILTESLLnwetVKYFNREPYEKERYREAVKN------YQKAERKYLFSLNLLNAVQS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2254949669 254 IGIILGF-GGM-----RIASGAISAGTLVAMIFYVLNLSIPLINLSTL 295
Cdd:cd18583 229 LILTLGLlAGCflaayQVSQGQATVGDFVTLLTYWAQLSGPLNFFATL 276
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
19-294 |
2.10e-07 |
|
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: 52.93 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 19 GLIIVAVTIASIGSLTGLLVPLFTGQVVDK---FTFESISPVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVL 95
Cdd:cd18779 2 GLLGQILLASLLLQLLGLALPLLTGVLVDRvipRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 96 WEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVItLIGSLIMLFVLDWQMTLLTFITIPIFILVIVP 175
Cdd:cd18779 82 LEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTL-VLGYLALLFAQSPLLGLVVLGLAALQVALLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 176 LGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIG 255
Cdd:cd18779 161 TRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 2254949669 256 IILGFGGMRIASGAISAGTLVAMIFYVLNLSIPLINLST 294
Cdd:cd18779 241 VLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVG 279
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
349-568 |
2.71e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSidalsltdwrrkigYVMQSNAMMNGTIR--DN 426
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV--------------SVIAISAGLSGQLTgiEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 427 I-----LYGVDREVSEE---ELIHYAKLAnchEFIMEFEQGYdtivgerglklSGGQRQRIDIARSFVKNPDILLLDEAt 498
Cdd:PRK13546 106 IefkmlCMGFKRKEIKAmtpKIIEFSELG---EFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEA- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 499 anLDSESERKIQEALDILME----NRTTIVIAHRLSTIKK-AGQIIFLDHGEVTGRGRHEELMQThamYQQFVET 568
Cdd:PRK13546 171 --LSVGDQTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAFLND 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
349-532 |
3.06e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRK-IGYVMQS-NAMMNGTIRDN 426
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQElNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 427 ILYGvdRE-VSEEELIHYAK--------LANchefiMEFEQGYDTIVGErglkLSGGQRQRIDIARSFVKNPDILLLDEA 497
Cdd:PRK10762 100 IFLG--REfVNRFGRIDWKKmyaeadklLAR-----LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2254949669 498 TANL-DSESE---RKIQEaldiLMENRTTIV-IAHRLSTI 532
Cdd:PRK10762 169 TDALtDTETEslfRVIRE----LKSQGRGIVyISHRLKEI 204
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
60-184 |
3.88e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 52.15 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 60 IALVAVFLVNAVLSGFGYYLLNKIGEKIIYairSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFP 139
Cdd:cd18605 49 GFLAGLNSLFTLLRAFLFAYGGLRAARRLH---NKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLA 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2254949669 140 AVITLIGSLIMLfvldwqmtlltFITIPIFILVIVPLGKIMQKIS 184
Cdd:cd18605 126 QLFGLLGYLVVI-----------CYQLPWLLLLLLPLAFIYYRIQ 159
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
30-303 |
7.42e-07 |
|
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: 50.96 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 30 IGSLTGLLVPLFTGQVVDKFT-FESISPVFIIALVAVF----LVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKM 104
Cdd:cd18582 7 LAKLLNVAVPFLLKYAVDALSaPASALLAVPLLLLLAYglarILSSLFNELRDALFARVSQRAVRRLALRVFRHLHSLSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 105 PFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLIMLFVL-DWQMTLLTFITIPIFILVIVPLGKIMQKI 183
Cdd:cd18582 87 RFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFTIKVTEWRTKF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 184 STNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGIIMLITIGIILGFGGM 263
Cdd:cd18582 167 RREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQ 246
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2254949669 264 RIASGAISAGTLVAMIFYVLNLSIPLINLSTLVTDYKKAV 303
Cdd:cd18582 247 GVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
51-176 |
9.33e-07 |
|
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: 50.94 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 51 FESISPVFIIALVAVF-LVNAVLSGFGYYLLNKIGekiIYAIRSVL---WEHIIHLKMPFFDKNESGQLMSRLTDDTKVI 126
Cdd:cd18606 29 FFGLSQGFYIGIYAGLgVLQAIFLFLFGLLLAYLG---IRASKRLHnkaLKRVLRAPMSFFDTTPLGRILNRFSKDTDVL 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2254949669 127 NDFISQKLPGFFPAVITLIGSLImlfvldwqmtlLTFITIPIFILVIVPL 176
Cdd:cd18606 106 DNELPDSLRMFLYTLSSIIGTFI-----------LIIIYLPWFAIALPPL 144
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
347-517 |
1.04e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDwrrkigyvmqsnAMMNGTI--- 423
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD------------GLANGIVyis 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 424 ----RDNILYGVD----------REVSEE--ELIHYAKLANCHEFIMEFE---QGYDTIVGErglkLSGGQRQRIDIARS 484
Cdd:PRK10762 334 edrkRDGLVLGMSvkenmsltalRYFSRAggSLKHADEQQAVSDFIRLFNiktPSMEQAIGL----LSGGNQQKVAIARG 409
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2254949669 485 FVKNPDILLLDEATANLDSESERKI--------QEALDILM 517
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIyqlinqfkAEGLSIIL 450
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
465-555 |
1.16e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 465 GERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVIAHRL--STIKKAGQIIFLD 542
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVID 218
|
90
....*....|...
gi 2254949669 543 HGEVTGRGRHEEL 555
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
97-188 |
1.82e-06 |
|
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: 49.78 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 97 EHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLPGFFPAVITLIGSLImlfvldwqmtlLTFITIPIFILVIVPL 176
Cdd:cd18603 82 HNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLV-----------VISISTPIFLVVIIPL 150
|
90
....*....|....*..
gi 2254949669 177 GKI---MQK--ISTNTQ 188
Cdd:cd18603 151 AILyffIQRfyVATSRQ 167
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
349-539 |
2.10e-06 |
|
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: 49.54 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKS-----TLFSLIERMYEIDQG--GIYydgTSIDALSLTDW-----RRKIGYVMQSN 416
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSslindTLYPALARRLHLKKEqpGNH---DRIEGLEHIDKvividQSPIGRTPRSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 417 -AMMNG---TIRD----------------NILY---------GVDREVSEEELIHYAKLANCHEFIMEFEQGYDTIvGER 467
Cdd:cd03271 88 pATYTGvfdEIRElfcevckgkrynretlEVRYkgksiadvlDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKL-GQP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 468 GLKLSGGQRQRIDIARSFVK---NPDILLLDEATANLDSESERKIQEALDILMEN-RTTIVIAHRLSTIKKAGQII 539
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCADWII 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
345-525 |
3.95e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 345 DTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALSLTDWRRK-IGYVMQSNA----MM 419
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITESRRdngfFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 420 NGTIRDNI-------------LYGVDREVSEEELIHYAK--LA-NCHefimEFEQGydtiVGErglkLSGGQRQRIDIAR 483
Cdd:PRK09700 355 NFSIAQNMaisrslkdggykgAMGLFHEVDEQRTAENQRelLAlKCH----SVNQN----ITE----LSGGNQQKVLISK 422
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2254949669 484 SFVKNPDILLLDEATANLDSESERKIQEALDILMENRTTIVI 525
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM 464
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
323-510 |
4.42e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 323 PNLQDEIPTGD-------LKFDHVYFGYDDTPVL-KDVSFNVLRGEVTAFVGPSGSGKSTLFSLIErmyeidqggiyydg 394
Cdd:PLN03073 491 PDYKFEFPTPDdrpgppiISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIS-------------- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 395 tsidalslTDWRRKIGYVMQSNAMMNGTIRDNILYGVDreVSEEELIHYAKlanCHEFIMefEQGYDTIVGERGLK---- 470
Cdd:PLN03073 557 --------GELQPSSGTVFRSAKVRMAVFSQHHVDGLD--LSSNPLLYMMR---CFPGVP--EQKLRAHLGSFGVTgnla 621
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2254949669 471 ------LSGGQRQRIDIARSFVKNPDILLLDEATANLDSES-ERKIQ 510
Cdd:PLN03073 622 lqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
469-545 |
5.53e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.18 E-value: 5.53e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 469 LKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILMEN--RTTIVIAHRLSTIKKAGQIIFLDHGE 545
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
347-529 |
6.07e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDvsfnvlrGEVTAFVGPSGSGKST---------------------------------LFSLIERMYE--------- 384
Cdd:PRK13409 94 PIPKE-------GKVTGILGPNGIGKTTavkilsgelipnlgdyeeepswdevlkrfrgteLQNYFKKLYNgeikvvhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 385 --IDQGGIYYDGTSIDALSLTDWRRKIGYVMQSNAMmngtirDNILygvDREVSEeelihyaklanchefimefeqgydt 462
Cdd:PRK13409 167 qyVDLIPKVFKGKVRELLKKVDERGKLDEVVERLGL------ENIL---DRDISE------------------------- 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 463 ivgerglkLSGGQRQRIDIARSFVKNPDILLLDEATANLD----SESERKIQEaldiLMENRTTIVIAHRL 529
Cdd:PRK13409 213 --------LSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIRE----LAEGKYVLVVEHDL 271
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
343-507 |
6.74e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 343 YDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSI-DALSLTDWRRKIGYVMQ---SNAM 418
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMaDARHRRAVCPRIAYMPQglgKNLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 419 MNGTIRDNI-----LYGVDREVSE---EELIHYAKLAnchefimEFEqgyDTIVGerglKLSGGQRQRIDIARSFVKNPD 490
Cdd:NF033858 91 PTLSVFENLdffgrLFGQDAAERRrriDELLRATGLA-------PFA---DRPAG----KLSGGMKQKLGLCCALIHDPD 156
|
170
....*....|....*..
gi 2254949669 491 ILLLDEATANLDSESER 507
Cdd:NF033858 157 LLILDEPTTGVDPLSRR 173
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
314-561 |
9.11e-06 |
|
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: 48.28 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 314 HEPLEniaapnLQDEIptgdLKFDHVYFGYDDTPVLK---DVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEID-QGG 389
Cdd:TIGR02633 248 HEPHE------IGDVI----LEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGN 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 390 IYYDGTSIDALSLTDW-RRKIGYVMQSNAmmngtiRDNIL--YGVDREVSEEELIHYAKLANCHEfimEFEQG-YDTIVG 465
Cdd:TIGR02633 318 VFINGKPVDIRNPAQAiRAGIAMVPEDRK------RHGIVpiLGVGKNITLSVLKSFCFKMRIDA---AAELQiIGSAIQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 466 ERGLK----------LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILM-ENRTTIVIAHRLSTIKK 534
Cdd:TIGR02633 389 RLKVKtaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLG 468
|
250 260
....*....|....*....|....*...
gi 2254949669 535 -AGQIIFLDHGEVTGRGRHEELMQTHAM 561
Cdd:TIGR02633 469 lSDRVLVIGEGKLKGDFVNHALTQEQVL 496
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
341-527 |
9.70e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 341 FGYDDTPVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGI---------YY--DGTS--IDALSLTDWRR 407
Cdd:PRK15064 327 KGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigYYaqDHAYdfENDLTLFDWMS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 408 KIGYVMQSNAMMNGTIrDNILYgvdrevSEEELIHYAKLanchefimefeqgydtivgerglkLSGGQRQRIDIARSFVK 487
Cdd:PRK15064 407 QWRQEGDDEQAVRGTL-GRLLF------SQDDIKKSVKV------------------------LSGGEKGRMLFGKLMMQ 455
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2254949669 488 NPDILLLDEATANLDSESerkIqEALDILMENR--TTIVIAH 527
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMES---I-ESLNMALEKYegTLIFVSH 493
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
57-204 |
1.27e-05 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 47.16 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 57 VFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTKVINDFISQKLpG 136
Cdd:cd18553 55 FFGIILIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVIQSFL-F 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 137 FFPAVITLIGSLIMLFVLDWQMTLltFITIpIFILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTE 204
Cdd:cd18553 134 ILSEIFVILFIYSLLLYVNWKITL--VLTL-FLGLNVFFITKIVSKKIKKQGKKREESQKKFYKILSE 198
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
25-305 |
1.36e-05 |
|
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: 47.05 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 25 VTIAS-IGSLTGLLVPLFTGQVVDK----FTFESISpVFIIALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHI 99
Cdd:cd18587 7 VLLAAlLINLFALASPLFVMNVYDRvvpnNAIETLW-VLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSRLFERV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 100 IHLKMPFfDKNESGQLMSRLTD-DTkvINDFISQK-------LP--GFFPAVITLIGslimlfvldWQMTLLTFITIPIF 169
Cdd:cd18587 86 LGLRLEA-RPASVGSFANNLREfES--VRDFFTSAtltalidLPfvLLFLAVIALIG---------GPLALVPLVAIPLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 170 ILVIVPLGKIMQKISTNTQTEIANFSGLLGRVLTEMRLVKVANTEKLELDKAHSNLKTIYNLGLKQAKIAAVVQPISGII 249
Cdd:cd18587 154 LLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949669 250 MLITIGIILGFGGMRIASGAISAGTLVAMifYVLN---LSiPLINLSTLVTDYKKAVGA 305
Cdd:cd18587 234 QQLVTVAIVIVGVYLISDGELTMGGLIAC--VILSgraLA-PLGQIAGLLTRYQQARTA 289
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
349-544 |
1.38e-05 |
|
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: 45.78 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTLFsliermyeidQGGIYYDGTSIDALSLTDWrrkigyvmqsnammngtirdnil 428
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV----------NEGLYASGKARLISFLPKF----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 429 ygvdrevSEEELIHYAKLanchEFIMEFEQGYDTIvGERGLKLSGGQRQRIDIARSFVKNPD--ILLLDEATANLDSESE 506
Cdd:cd03238 58 -------SRNKLIFIDQL----QFLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 2254949669 507 RKIQEALD-ILMENRTTIVIAHRLSTIKKAGQIIFLDHG 544
Cdd:cd03238 126 NQLLEVIKgLIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
348-502 |
3.66e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 348 VLKDVSFNVLRGEVTAFVGPSGSGKSTL-FSLIERMYEID-QGGIYYDGTSIDALSLTDW-RRKIGYVM----QSNAMMN 420
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKEVDVSTVSDAiDAGLAYVTedrkGYGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 GTIRDNILYGVDREVSEEELIhyaklaNCHEFIMEFEQGYDTI------VGERGLKLSGGQRQRIDIARSFVKNPDILLL 494
Cdd:NF040905 355 DDIKRNITLANLGKVSRRGVI------DENEEIKVAEEYRKKMniktpsVFQKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
....*...
gi 2254949669 495 DEATANLD 502
Cdd:NF040905 429 DEPTRGID 436
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
451-555 |
3.88e-05 |
|
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: 46.93 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 451 EFIMEFEQGYDTIvGERGLKLSGGQRQRIDIARSFVK---NPDILLLDEATANLDSESERKIQEALDILMEN-RTTIVIA 526
Cdd:TIGR00630 811 QTLCDVGLGYIRL-GQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIE 889
|
90 100 110
....*....|....*....|....*....|....*
gi 2254949669 527 HRLSTIKKAGQIIFL-----DH-GEVTGRGRHEEL 555
Cdd:TIGR00630 890 HNLDVIKTADYIIDLgpeggDGgGTVVASGTPEEV 924
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
358-531 |
4.54e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.32 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 358 RGEVTAFVGPSGSGKSTL-----------FSLIERMYEIDQGGIYYDGTSI----DALSLTDWR--RKIGYVMQSNAMMN 420
Cdd:COG1245 98 KGKVTGILGPNGIGKSTAlkilsgelkpnLGDYDEEPSWDEVLKRFRGTELqdyfKKLANGEIKvaHKPQYVDLIPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 GTIRDnILYGVDREVSEEELIHYAKLANchefimefeqgydtiVGERGLK-LSGGQRQRIDIARSFVKNPDILLLDEATA 499
Cdd:COG1245 178 GTVRE-LLEKVDERGKLDELAEKLGLEN---------------ILDRDISeLSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|....*.
gi 2254949669 500 NLD----SESERKIQEALDilmENRTTIVIAHRLST 531
Cdd:COG1245 242 YLDiyqrLNVARLIRELAE---EGKYVLVVEHDLAI 274
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
30-173 |
5.25e-05 |
|
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: 45.51 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 30 IGSLTGLLVPLFTGQVVDK-FTFESISPVFII--ALVAVFLVNAVLSGFGYYLLNKIGEKIIYAIRSVLWEHIIHLKMPF 106
Cdd:cd18571 13 LGSLLQLIFPFLTQSIVDKgINNKDLNFIYLIliAQLVLFLGSTSIEFIRSWILLHISSRINISIISDFLIKLMRLPISF 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 107 FDKNESGQLMSRLTDDTKvINDFISQKLPGFFPAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVI 173
Cdd:cd18571 93 FDTKMTGDILQRINDHSR-IESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILWI 158
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
333-529 |
1.23e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 333 DLKFDHVYFGYDDTPV--LKDVSFNVLRGEVTAFVGPSGSGKS-TLFSLIERMYE--IDQGGIYYDGTSIDALSLTDWRR 407
Cdd:PRK09473 14 DVKDLRVTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 408 ----KIGYVMQsNAM--MNGTIRdnilygVDREVSEEELIHyaKLANCHEFIMEFEQGYDTIVGERGLK--------LSG 473
Cdd:PRK09473 94 lraeQISMIFQ-DPMtsLNPYMR------VGEQLMEVLMLH--KGMSKAEAFEESVRMLDAVKMPEARKrmkmypheFSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 474 GQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALDILME--NRTTIVIAHRL 529
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDL 222
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
349-552 |
2.75e-04 |
|
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: 42.63 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 349 LKDVSFNVLRGEVTAFVGPSGSGKSTL-FSLI----ERMYeIDQGGIYY----------DGTSIDALSLTdwrrkIGyVM 413
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIyaegQRRY-VESLSAYArqflgqmdkpDVDSIEGLSPA-----IA-ID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 414 QSNAMMN-----GTIRDniLYGVDRevseeelIHYAK--LANCHEFIMEFEQGYDTiVGERGLKLSGGQRQRIDIARSFV 486
Cdd:cd03270 84 QKTTSRNprstvGTVTE--IYDYLR-------LLFARvgIRERLGFLVDVGLGYLT-LSRSAPTLSGGEAQRIRLATQIG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2254949669 487 KNPD--ILLLDEATANLdseSERKIQEALDILMENR----TTIVIAHRLSTIKKAGQIIflDHGevTGRGRH 552
Cdd:cd03270 154 SGLTgvLYVLDEPSIGL---HPRDNDRLIETLKRLRdlgnTVLVVEHDEDTIRAADHVI--DIG--PGAGVH 218
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
471-539 |
3.27e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 471 LSGGQRQ------RIDIARSFVKNPDILLLDEATANLDSESerkIQEALDILME------NRTTIVIAHRLSTIKKAGQI 538
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEESLAEIIEerksqkNFQLIVITHDEELVDAADHI 192
|
.
gi 2254949669 539 I 539
Cdd:cd03240 193 Y 193
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
468-527 |
3.50e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 3.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949669 468 GLKLsggqrqRIDIARSFVKNPDILLLDEATANLDSESERKIQealDILME-NRTTIVIAH 527
Cdd:PRK15064 159 GWKL------RVLLAQALFSNPDILLLDEPTNNLDINTIRWLE---DVLNErNSTMIIISH 210
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
57-180 |
4.08e-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: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 57 VFIIALVAVFLVNAVLSgfgyYLLNKIGEKIIYAIRSVLWEHIIHLKMPFFDKNESGQLMSRLTDDTkvinDFISQKLPg 136
Cdd:cd18599 63 VYGGSILVILLLSLIRG----FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDL----DEVDVRLP- 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2254949669 137 fFPAVITLIGSLIMLFVLdwqmtLLTFITIPIFILVIVPLGKIM 180
Cdd:cd18599 134 -FTLENFLQNVLLVVFSL-----IIIAIVFPWFLIALIPLAIIF 171
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
30-216 |
6.01e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 42.15 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 30 IGSLTGLLVPLFTGQVVDKF--TFESISPVFIIA--LVAVFLVNAVL-SGFGYYLlNKIGEKIIYAIRSVLWEHIIHLKM 104
Cdd:cd18598 8 LADVLGFAGPLLLNKLVEFLedSSEPLSDGYLYAlgLVLSSLLGALLsSHYNFQM-NKVSLKVRAALVTAVYRKALRVRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 105 PFFDKNESGQLMSRLTDDTKVINDFisqkLPGFFpAVITLIGSLIMLFVLDWQMTLLTFITIPIFILVIVPLGK-IMQKI 183
Cdd:cd18598 87 SSLSKFSTGEIVNLMSTDADRIVNF----CPSFH-DLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKwIAKRI 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 2254949669 184 STNTqTEIANFS----GLLGRVLTEMRLVKVANTEKL 216
Cdd:cd18598 162 GALS-EKMMKHKdarvKLMTEILSGIRVIKLLAWERI 197
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
347-562 |
6.15e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 347 PVLKDVSFNVLRGEVTAFVGPSGSGKSTLFSLIERMYEIDQGGIYYDGTSIDALS-----------LTDWRRKIGYVMQS 415
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 416 NAMMNGTIRDnilygVDREVSEEELIHYAKLANCHEFIMEFEQ----GYDTIVGErglkLSGGQRQRIDIARSFVKNPDI 491
Cdd:PRK10982 342 DIGFNSLISN-----IRNYKNKVGLLDNSRMKSDTQWVIDSMRvktpGHRTQIGS----LSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2254949669 492 LLLDEATANLDSESERKI-QEALDILMENRTTIVIAHRL-STIKKAGQIIFLDHGEVTG-----RGRHEELMQTHAMY 562
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLVAGivdtkTTTQNEILRLASLH 490
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|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
472-527 |
6.67e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 6.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949669 472 SGGQRQRIDIARSFVKNPDILLLDEATANLDSESERKIQEALdiLMENRTTIVIAH 527
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
359-550 |
1.05e-03 |
|
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: 41.20 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 359 GEVTAFVGPSGSGKSTLFSLIERMYEIDQGGI-----------YYDGTSIDALsLTDWR-------RKIGYVMQSNAMMN 420
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNY-FTKLLegdvkviVKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 421 GTIRDnILYGVDREVSEEELIHyaklanchefIMEFEQgydtiVGERGL-KLSGGQRQRIDIARSFVKNPDILLLDEATA 499
Cdd:cd03236 105 GKVGE-LLKKKDERGKLDELVD----------QLELRH-----VLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2254949669 500 NLDS----ESERKIQEaldILMENRTTIVIAHRLSTIKKAGQIIFLDHGEVTGRG 550
Cdd:cd03236 169 YLDIkqrlNAARLIRE---LAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYG 220
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|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
355-375 |
2.41e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 2.41e-03
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
351-539 |
3.28e-03 |
|
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: 38.49 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 351 DVSFNvlRGEVTAFVGPSGSGKSTLFsliermyeidqggiyydgtsidalsltdwrRKIGYVMqSNAMMNGTIRDNILYG 430
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTIL------------------------------DAIGLAL-GGAQSATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 431 VdrEVSEEELihyaklanchEFIMEFEQgydtivgerglkLSGGQRQRIDIARSF----VKNPDILLLDEATANLDSESE 506
Cdd:cd03227 62 C--IVAAVSA----------ELIFTRLQ------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|....
gi 2254949669 507 RKIQEAL-DILMENRTTIVIAHRLSTIKKAGQII 539
Cdd:cd03227 118 QALAEAIlEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
450-516 |
3.87e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.83 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949669 450 HEFIMEF--EQGYDTIVGERGLKLSGGQRQ-------------RIDIARSFVKNPDILLLDEATANLDsesERKIQEALD 514
Cdd:pfam13558 10 LSFEVEVrdEDGSEVETYRRSGGLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLD---EENIRTALE 86
|
..
gi 2254949669 515 IL 516
Cdd:pfam13558 87 LL 88
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
357-389 |
4.34e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 39.42 E-value: 4.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2254949669 357 LRGEVTAFVGPSGSGKSTLFSLIE------------------------RMYEIDQGG 389
Cdd:PRK00098 162 LAGKVTVLAGQSGVGKSTLLNALApdlelktgeisealgrgkhttthvELYDLPGGG 218
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